The extracellular matrix in tumor progression and metastasis

Hanahan D, Weinberg RA (2000) The hallmarks of cancer. Cell 100(1):57–70

Hanahan D, Weinberg RA (2011) Hallmarks of cancer: the next generation. Cell 144(5):646–674. https://doi.org/10.1016/j.cell.2011.02.013

Paul CD, Mistriotis P, Konstantopoulos K (2017) Cancer cell motility: lessons from migration in confined spaces. Nat Rev Cancer 17(2):131–140. https://doi.org/10.1038/nrc.2016.123

Theocharis AD, Skandalis SS, Gialeli C, Karamanos NK (2016) Extracellular matrix structure. Adv Drug Deliv Rev 97:4–27. https://doi.org/10.1016/j.addr.2015.11.001

Chang TT, Thakar D, Weaver VM (2017) Force-dependent breaching of the basement membrane. Matrix Biol 57–58:178–189. https://doi.org/10.1016/j.matbio.2016.12.005

Walker C, Mojares E, Del Rio Hernandez A (2018) Role of extracellular matrix in development and cancer progression. Int J Mol Sci 19(10):3028. https://doi.org/10.3390/ijms19103028

Kalluri R (2016) The biology and function of fibroblasts in cancer. Nat Rev Cancer 16(9):582–598. https://doi.org/10.1038/nrc.2016.73

Rozario T, DeSimone DW (2010) The extracellular matrix in development and morphogenesis: a dynamic view. Dev Biol 341(1):126–140. https://doi.org/10.1016/j.ydbio.2009.10.026

Halper J, Kjaer M (2014) Basic components of connective tissues and extracellular matrix: elastin, fibrillin, fibulins, fibrinogen, fibronectin, laminin, tenascins and thrombospondins. Adv Exp Med Biol 802:31–47. https://doi.org/10.1007/978-94-007-7893-1_3

Singh B, Fleury C, Jalalvand F, Riesbeck K (2012) Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host. FEMS Microbiol Rev 36(6):1122–1180. https://doi.org/10.1111/j.1574-6976.2012.00340.x

Halfter W, Oertle P, Monnier CA, Camenzind L, Reyes-Lua M, Hu H, Candiello J, Labilloy A, Balasubramani M, Henrich PB, Plodinec M (2015) New concepts in basement membrane biology. FEBS J 282(23):4466–4479. https://doi.org/10.1111/febs.13495

Mak KM, Mei R (2017) Basement membrane type IV collagen and laminin: an overview of their biology and value as fibrosis biomarkers of liver disease. Anat Rec (Hoboken) 300(8):1371–1390. https://doi.org/10.1002/ar.23567

McCarthy KJ (2015) The basement membrane proteoglycans perlecan and agrin: something old, something new. Curr Top Membr 76:255–303. https://doi.org/10.1016/bs.ctm.2015.09.001

Miller RT (2017) Mechanical properties of basement membrane in health and disease. Matrix Biol 57–58:366–373. https://doi.org/10.1016/j.matbio.2016.07.001

Randles MJ, Humphries MJ, Lennon R (2017) Proteomic definitions of basement membrane composition in health and disease. Matrix Biol 57–58:12–28. https://doi.org/10.1016/j.matbio.2016.08.006

Liang J, Jiang D, Noble PW (2016) Hyaluronan as a therapeutic target in human diseases. Adv Drug Deliv Rev 97:186–203. https://doi.org/10.1016/j.addr.2015.10.017

Iozzo RV, Schaefer L (2015) Proteoglycan form and function: a comprehensive nomenclature of proteoglycans. Matrix Biol 42:11–55. https://doi.org/10.1016/j.matbio.2015.02.003

Schaefer L, Tredup C, Gubbiotti MA, Iozzo RV (2017) Proteoglycan neofunctions: regulation of inflammation and autophagy in cancer biology. FEBS J 284(1):10–26. https://doi.org/10.1111/febs.13963

Ricard-Blum S (2011) The collagen family. Cold Spring Harb Perspect Biol 3(1):a004978. https://doi.org/10.1101/cshperspect.a004978

An B, Lin YS, Brodsky B (2016) Collagen interactions: drug design and delivery. Adv Drug Deliv Rev 97:69–84. https://doi.org/10.1016/j.addr.2015.11.013

Mao M, Alavi MV, Labelle-Dumais C, Gould DB (2015) Type IV collagens and basement membrane diseases: cell biology and pathogenic mechanisms. Curr Top Membr 76:61–116. https://doi.org/10.1016/bs.ctm.2015.09.002

Bhattacharjee A, Bansal M (2005) Collagen structure: the Madras triple helix and the current scenario. IUBMB Life 57(3):161–172. https://doi.org/10.1080/15216540500090710

Brodsky B, Persikov AV (2005) Molecular structure of the collagen triple helix. Adv Protein Chem 70:301–339. https://doi.org/10.1016/S0065-3233(05)70009-7

Beck K, Brodsky B (1998) Supercoiled protein motifs: the collagen triple-helix and the α-helical coiled coil. J Struct Biol 122(1–2):17–29. https://doi.org/10.1006/jsbi.1998.3965

Provenzano PP, Vanderby R Jr (2006) Collagen fibril morphology and organization: implications for force transmission in ligament and tendon. Matrix Biol 25(2):71–84. https://doi.org/10.1016/j.matbio.2005.09.005

Boudko SP, Danylevych N, Hudson BG, Pedchenko VK (2018) Basement membrane collagen IV: isolation of functional domains. Methods Cell Biol 143:171–185. https://doi.org/10.1016/bs.mcb.2017.08.010

Cummings CF, Pedchenko V, Brown KL, Colon S, Rafi M, Jones-Paris C, Pokydeshava E, Liu M, Pastor-Pareja JC, Stothers C, Ero-Tolliver IA, McCall AS, Vanacore R, Bhave G, Santoro S, Blackwell TS, Zent R, Pozzi A, Hudson BG (2016) Extracellular chloride signals collagen IV network assembly during basement membrane formation. J Cell Biol 213(4):479–494. https://doi.org/10.1083/jcb.201510065

Vanacore RM, Friedman DB, Ham AJ, Sundaramoorthy M, Hudson BG (2005) Identification of S-hydroxylysyl-methionine as the covalent cross-link of the noncollagenous (NC1) hexamer of the α1α1α2 collagen IV network: a role for the post-translational modification of lysine 211 to hydroxylysine 211 in hexamer assembly. J Biol Chem 280(32):29300–29310. https://doi.org/10.1074/jbc.M502752200

Heljasvaara R, Aikio M, Ruotsalainen H, Pihlajaniemi T (2017) Collagen XVIII in tissue homeostasis and dysregulation—lessons learned from model organisms and human patients. Matrix Biol 57–58:55–75. https://doi.org/10.1016/j.matbio.2016.10.002

Shaw LM, Olsen BR (1991) FACIT collagens: diverse molecular bridges in extracellular matrices. Trends Biochem Sci 16(5):191–194

Has C, Bruckner-Tuderman L (2006) Molecular and diagnostic aspects of genetic skin fragility. J Dermatol Sci 44(3):129–144. https://doi.org/10.1016/j.jdermsci.2006.08.003

Barker HE, Cox TR, Erler JT (2012) The rationale for targeting the LOX family in cancer. Nat Rev Cancer 12(8):540–552. https://doi.org/10.1038/nrc3319

Eckert RL, Fisher ML, Grun D, Adhikary G, Xu W, Kerr C (2015) Transglutaminase is a tumor cell and cancer stem cell survival factor. Mol Carcinog 54(10):947–958. https://doi.org/10.1002/mc.22375

Li B, Cerione RA, Antonyak M (2011) Tissue transglutaminase and its role in human cancer progression. Adv Enzymol Relat Areas Mol Biol 78:247–293

Saitow CB, Wise SG, Weiss AS, Castellot JJ, Kaplan DL (2013) Elastin biology and tissue engineering with adult cells. Biomol Concepts 4(2):173–185. https://doi.org/10.1515/bmc-2012-0040

Kim YM, Kim EC, Kim Y (2011) The human lysyl oxidase-like 2 protein functions as an amine oxidase toward collagen and elastin. Mol Biol Rep 38(1):145–149. https://doi.org/10.1007/s11033-010-0088-0

Mezzenga R, Mitsi M (2018) The molecular dance of fibronectin: conformational flexibility leads to functional versatility. Biomacromol. https://doi.org/10.1021/acs.biomac.8b01258

White ES, Muro AF (2011) Fibronectin splice variants: understanding their multiple roles in health and disease using engineered mouse models. IUBMB Life 63(7):538–546. https://doi.org/10.1002/iub.493

Kumra H, Reinhardt DP (2016) Fibronectin-targeted drug delivery in cancer. Adv Drug Deliv Rev 97:101–110. https://doi.org/10.1016/j.addr.2015.11.014

Woods A, Longley RL, Tumova S, Couchman JR (2000) Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts. Arch Biochem Biophys 374(1):66–72. https://doi.org/10.1006/abbi.1999.1607

Prasad A, Clark RA (2018) Fibronectin interaction with growth factors in the context of general ways extracellular matrix molecules regulate growth factor signaling. G Ital Dermatol Venereol 153(3):361–374. https://doi.org/10.23736/S0392-0488.18.05952-7

Dosio F, Arpicco S, Stella B, Fattal E (2016) Hyaluronic acid for anticancer drug and nucleic acid delivery. Adv Drug Deliv Rev 97:204–236. https://doi.org/10.1016/j.addr.2015.11.011

Neill T, Schaefer L, Iozzo RV (2016) Decorin as a multivalent therapeutic agent against cancer. Adv Drug Deliv Rev 97:174–185. https://doi.org/10.1016/j.addr.2015.10.016

Gubbiotti MA, Neill T, Iozzo RV (2017) A current view of perlecan in physiology and pathology: a mosaic of functions. Matrix Biol 57–58:285–298. https://doi.org/10.1016/j.matbio.2016.09.003

Harvey SJ, Miner JH (2008) Revisiting the glomerular charge barrier in the molecular era. Curr Opin Nephrol Hypertens 17(4):393–398. https://doi.org/10.1097/MNH.0b013e32830464de

Aumailley M (2013) The laminin family. Cell Adhes Migr 7(1):48–55. https://doi.org/10.4161/cam.22826

Hohenester E, Engel J (2002) Domain structure and organisation in extracellular matrix proteins. Matrix Biol 21(2):115–128

Rousselle P, Beck K (2013) Laminin 332 processing impacts cellular behavior. Cell Adhes Migr 7(1):122–134. https://doi.org/10.4161/cam.23132

Hohenester E, Yurchenco PD (2013) Laminins in basement membrane assembly. Cell Adhes Migr 7(1):56–63. https://doi.org/10.4161/cam.21831

Thakur R, Mishra DP (2016) Matrix reloaded: CCN, tenascin and SIBLING group of matricellular proteins in orchestrating cancer hallmark capabilities. Pharmacol Ther 168:61–74. https://doi.org/10.1016/j.pharmthera.2016.09.002

Viloria K, Hill NJ (2016) Embracing the complexity of matricellular proteins: the functional and clinical significance of splice variation. Biomol Concepts 7(2):117–132. https://doi.org/10.1515/bmc-2016-0004

Sawyer AJ, Kyriakides TR (2016) Matricellular proteins in drug delivery: therapeutic targets, active agents, and therapeutic localization. Adv Drug Deliv Rev 97:56–68. https://doi.org/10.1016/j.addr.2015.12.016

Sofeu Feugaing DD, Gotte M, Viola M (2013) More than matrix: the multifaceted role of decorin in cancer. Eur J Cell Biol 92(1):1–11. https://doi.org/10.1016/j.ejcb.2012.08.004

Yoshida T, Akatsuka T, Imanaka-Yoshida K (2015) Tenascin-C and integrins in cancer. Cell Adhes Migr 9(1–2):96–104. https://doi.org/10.1080/19336918.2015.1008332

Brellier F, Martina E, Degen M, Heuze-Vourc’h N, Petit A, Kryza T, Courty Y, Terracciano L, Ruiz C, Chiquet-Ehrismann R (2012) Tenascin-W is a better cancer biomarker than tenascin-C for most human solid tumors. BMC Clin Pathol 12:14. https://doi.org/10.1186/1472-6890-12-14

Chiquet-Ehrismann R, Hagios C, Matsumoto K (1994) The tenascin gene family. Perspect Dev Neurobiol 2(1):3–7

Bellahcene A, Castronovo V, Ogbureke KU, Fisher LW, Fedarko NS (2008) Small integrin-binding ligand N-linked glycoproteins (SIBLINGs): multifunctional proteins in cancer. Nat Rev Cancer 8(3):212–226. https://doi.org/10.1038/nrc2345

Kamili NA, Arthur CM, Gerner-Smidt C, Tafesse E, Blenda A, Dias-Baruffi M, Stowell SR (2016) Key regulators of galectin-glycan interactions. Proteomics 16(24):3111–3125. https://doi.org/10.1002/pmic.201600116

Naschberger E, Liebl A, Schellerer VS, Schutz M, Britzen-Laurent N, Kolbel P, Schaal U, Haep L, Regensburger D, Wittmann T, Klein-Hitpass L, Rau TT, Dietel B, Meniel VS, Clarke AR, Merkel S, Croner RS, Hohenberger W, Sturzl M (2016) Matricellular protein SPARCL1 regulates tumor microenvironment-dependent endothelial cell heterogeneity in colorectal carcinoma. J Clin Invest 126(11):4187–4204. https://doi.org/10.1172/JCI78260

Roberts DD, Kaur S, Isenberg JS (2017) Regulation of cellular redox signaling by matricellular proteins in vascular biology, immunology, and cancer. Antioxid Redox Signal 27(12):874–911. https://doi.org/10.1089/ars.2017.7140

Gonzalez-Gonzalez L, Alonso J (2018) Periostin: a matricellular protein with multiple functions in cancer development and progression. Front Oncol 8:225. https://doi.org/10.3389/fonc.2018.00225

Vincent KM, Postovit LM (2018) Matricellular proteins in cancer: a focus on secreted Frizzled-related proteins. J Cell Commun Signal 12(1):103–112. https://doi.org/10.1007/s12079-017-0398-2

Grosche J, Meissner J, Eble JA (2018) More than a syllable in fib-ROS-is: the role of ROS on the fibrotic extracellular matrix and on cellular contacts. Mol Aspects Med 63:30–46. https://doi.org/10.1016/j.mam.2018.03.005

Holle AW, Young JL, Van Vliet KJ, Kamm RD, Discher D, Janmey P, Spatz JP, Saif T (2018) Cell-extracellular matrix mechanobiology: forceful tools and emerging needs for basic and translational research. Nano Lett 18(1):1–8. https://doi.org/10.1021/acs.nanolett.7b04982

Stroka KM, Konstantopoulos K (2014) Physical biology in cancer. 4. Physical cues guide tumor cell adhesion and migration. Am J Physiol Cell Physiol 306(2):C98–C109. https://doi.org/10.1152/ajpcell.00289.2013

Barczyk M, Carracedo S, Gullberg D (2010) Integrins. Cell Tissue Res 339(1):269–280. https://doi.org/10.1007/s00441-009-0834-6

Campbell ID, Humphries MJ (2011) Integrin structure, activation, and interactions. Cold Spring Harb Perspect Biol 3(3):a004994. https://doi.org/10.1101/cshperspect.a004994

Humphries JD, Chastney MR, Askari JA, Humphries MJ (2018) Signal transduction via integrin adhesion complexes. Curr Opin Cell Biol 56:14–21. https://doi.org/10.1016/j.ceb.2018.08.004

Horton ER, Humphries JD, James J, Jones MC, Askari JA, Humphries MJ (2016) The integrin adhesome network at a glance. J Cell Sci 129(22):4159–4163. https://doi.org/10.1242/jcs.192054

Kanchanawong P, Shtengel G, Pasapera AM, Ramko EB, Davidson MW, Hess HF, Waterman CM (2010) Nanoscale architecture of integrin-based cell adhesions. Nature 468(7323):580–584. https://doi.org/10.1038/nature09621

Winograd-Katz SE, Fassler R, Geiger B, Legate KR (2014) The integrin adhesome: from genes and proteins to human disease. Nat Rev Mol Cell Biol 15(4):273–288. https://doi.org/10.1038/nrm3769

Geiger B, Yamada KM (2011) Molecular architecture and function of matrix adhesions. Cold Spring Harb Perspect Biol 3(5):a005033. https://doi.org/10.1101/cshperspect.a005033

Zaidel-Bar R, Geiger B (2010) The switchable integrin adhesome. J Cell Sci 123(Pt 9):1385–1388. https://doi.org/10.1242/jcs.066183

Carulli S, Beck K, Dayan G, Boulesteix S, Lortat-Jacob H, Rousselle P (2012) Cell surface proteoglycans syndecan-1 and -4 bind overlapping but distinct sites in laminin α3 LG45 protein domain. J Biol Chem 287(15):12204–12216. https://doi.org/10.1074/jbc.M111.300061

Bachy S, Letourneur F, Rousselle P (2008) Syndecan-1 interaction with the LG4/5 domain in laminin-332 is essential for keratinocyte migration. J Cell Physiol 214(1):238–249. https://doi.org/10.1002/jcp.21184

Soares MA, Teixeira FC, Fontes M, Areas AL, Leal MG, Pavao MS, Stelling MP (2015) Heparan sulfate proteoglycans may promote or inhibit cancer progression by interacting with integrins and affecting cell migration. Biomed Res Int 2015:453801. https://doi.org/10.1155/2015/453801

Pantazaka E, Papadimitriou E (2014) Chondroitin sulfate-cell membrane effectors as regulators of growth factor-mediated vascular and cancer cell migration. Biochim Biophys Acta 1840(8):2643–2650. https://doi.org/10.1016/j.bbagen.2014.01.009

Hinz B, Phan SH, Thannickal VJ, Prunotto M, Desmouliere A, Varga J, De Wever O, Mareel M, Gabbiani G (2012) Recent developments in myofibroblast biology: paradigms for connective tissue remodeling. Am J Pathol 180(4):1340–1355. https://doi.org/10.1016/j.ajpath.2012.02.004

Otranto M, Sarrazy V, Bonte F, Hinz B, Gabbiani G, Desmouliere A (2012) The role of the myofibroblast in tumor stroma remodeling. Cell Adh Migr 6(3):203–219. https://doi.org/10.4161/cam.20377

Dvorak HF (1986) Tumors: wounds that do not heal. Similarities between tumor stroma generation and wound healing. N Engl J Med 315(26):1650–1659. https://doi.org/10.1056/nejm198612253152606

Dvorak HF (2015) Tumors: wounds that do not heal-redux. Cancer Immunol Res 3(1):1–11. https://doi.org/10.1158/2326-6066.Cir-14-0209

Kuzet SE, Gaggioli C (2016) Fibroblast activation in cancer: when seed fertilizes soil. Cell Tissue Res 365(3):607–619. https://doi.org/10.1007/s00441-016-2467-x

Desmouliere A, Guyot C, Gabbiani G (2004) The stroma reaction myofibroblast: a key player in the control of tumor cell behavior. Int J Dev Biol 48(5–6):509–517. https://doi.org/10.1387/ijdb.041802ad

Caja L, Dituri F, Mancarella S, Caballero-Diaz D, Moustakas A, Giannelli G, Fabregat I (2018) TGF-β and the tissue microenvironment: relevance in fibrosis and cancer. Int J Mol Sci 19(5):1294. https://doi.org/10.3390/ijms19051294

Khan Z, Marshall JF (2016) The role of integrins in TGFβ activation in the tumour stroma. Cell Tissue Res 365(3):657–673. https://doi.org/10.1007/s00441-016-2474-y

Wang M, Zhao J, Zhang L, Wei F, Lian Y, Wu Y, Gong Z, Zhang S, Zhou J, Cao K, Li X, Xiong W, Li G, Zeng Z, Guo C (2017) Role of tumor microenvironment in tumorigenesis. J Cancer 8(5):761–773. https://doi.org/10.7150/jca.17648

Crotti S, Piccoli M, Rizzolio F, Giordano A, Nitti D, Agostini M (2017) Extracellular matrix and colorectal cancer: how surrounding microenvironment affects cancer cell behavior? J Cell Physiol 232(5):967–975. https://doi.org/10.1002/jcp.25658

Erdogan B, Webb DJ (2017) Cancer-associated fibroblasts modulate growth factor signaling and extracellular matrix remodeling to regulate tumor metastasis. Biochem Soc Trans 45(1):229–236. https://doi.org/10.1042/BST20160387

Cunderlikova B (2016) Clinical significance of immunohistochemically detected extracellular matrix proteins and their spatial distribution in primary cancer. Crit Rev Oncol Hematol 105:127–144. https://doi.org/10.1016/j.critrevonc.2016.04.017

Rizzacasa B, Morini E, Pucci S, Murdocca M, Novelli G, Amati F (2017) LOX-1 and its splice variants: a new challenge for atherosclerosis and cancer-targeted therapies. Int J Mol Sci 18(2):290. https://doi.org/10.3390/ijms18020290

Huang L, Xu AM, Liu W (2015) Transglutaminase 2 in cancer. Am J Cancer Res 5(9):2756–2776

Rojas A, Anazco C, Gonzalez I, Araya P (2018) Extracellular matrix glycation and receptor for advanced glycation end-products activation: a missing piece in the puzzle of the association between diabetes and cancer. Carcinogenesis 39(4):515–521. https://doi.org/10.1093/carcin/bgy012

Malik R, Lelkes PI, Cukierman E (2015) Biomechanical and biochemical remodeling of stromal extracellular matrix in cancer. Trends Biotechnol 33(4):230–236. https://doi.org/10.1016/j.tibtech.2015.01.004

Malik R, Luong T, Cao X, Han B, Shah N, Franco-Barraza J, Han L, Shenoy VB, Lelkes PI, Cukierman E (2018) Rigidity controls human desmoplastic matrix anisotropy to enable pancreatic cancer cell spread via extracellular signal-regulated kinase 2. Matrix Biol 1:2. https://doi.org/10.1016/j.matbio.2018.11.001

Tolle RC, Gaggioli C, Dengjel J (2018) Three-dimensional cell culture conditions affect the proteome of cancer-associated fibroblasts. J Proteome Res 17(8):2780–2789. https://doi.org/10.1021/acs.jproteome.8b00237

Ronca R, Sozzani S, Presta M, Alessi P (2009) Delivering cytokines at tumor site: the immunocytokine-conjugated anti-EDB-fibronectin antibody case. Immunobiology 214(9–10):800–810. https://doi.org/10.1016/j.imbio.2009.06.005

Ramamonjisoa N, Ackerstaff E (2017) Characterization of the tumor microenvironment and tumor-stroma interaction by non-invasive preclinical imaging. Front Oncol 7:3. https://doi.org/10.3389/fonc.2017.00003

Micke P, Ostman A (2004) Tumour-stroma interaction: cancer-associated fibroblasts as novel targets in anti-cancer therapy? Lung Cancer 45(Suppl 2):S163–S175. https://doi.org/10.1016/j.lungcan.2004.07.977

Hirata E, Sahai E (2017) Tumor microenvironment and differential responses to therapy. Cold Spring Harb Perspect Med 7(7):a026781. https://doi.org/10.1101/cshperspect.a026781

Topalovski M, Brekken RA (2016) Matrix control of pancreatic cancer: new insights into fibronectin signaling. Cancer Lett 381(1):252–258. https://doi.org/10.1016/j.canlet.2015.12.027

Zollinger AJ, Smith ML (2017) Fibronectin, the extracellular glue. Matrix Biol 60–61:27–37. https://doi.org/10.1016/j.matbio.2016.07.011

Han Z, Lu ZR (2017) Targeting fibronectin for cancer imaging and therapy. J Mater Chem B 5(4):639–654. https://doi.org/10.1039/C6TB02008A

Wang K, Seo BR, Fischbach C, Gourdon D (2016) Fibronectin mechanobiology regulates tumorigenesis. Cell Mol Bioeng 9:1–11. https://doi.org/10.1007/s12195-015-0417-4

Bachman H, Nicosia J, Dysart M, Barker TH (2015) Utilizing fibronectin integrin-binding specificity to control cellular responses. Adv Wound Care (New Rochelle) 4(8):501–511. https://doi.org/10.1089/wound.2014.0621

Kanchanawong P, Waterman CM (2012) Advances in light-based imaging of three-dimensional cellular ultrastructure. Curr Opin Cell Biol 24(1):125–133. https://doi.org/10.1016/j.ceb.2011.11.010

Chiovaro F, Martina E, Bottos A, Scherberich A, Hynes NE, Chiquet-Ehrismann R (2015) Transcriptional regulation of tenascin-W by TGF-β signaling in the bone metastatic niche of breast cancer cells. Int J Cancer 137(8):1842–1854. https://doi.org/10.1002/ijc.29565

Adams JC, Chiquet-Ehrismann R, Tucker RP (2015) The evolution of tenascins and fibronectin. Cell Adhes Migr 9(1–2):22–33. https://doi.org/10.4161/19336918.2014.970030

Martina E, Chiquet-Ehrismann R, Brellier F (2010) Tenascin-W: an extracellular matrix protein associated with osteogenesis and cancer. Int J Biochem Cell Biol 42(9):1412–1415. https://doi.org/10.1016/j.biocel.2010.06.004

Degen M, Brellier F, Schenk S, Driscoll R, Zaman K, Stupp R, Tornillo L, Terracciano L, Chiquet-Ehrismann R, Ruegg C, Seelentag W (2008) Tenascin-W, a new marker of cancer stroma, is elevated in sera of colon and breast cancer patients. Int J Cancer 122(11):2454–2461. https://doi.org/10.1002/ijc.23417

Degen M, Brellier F, Kain R, Ruiz C, Terracciano L, Orend G, Chiquet-Ehrismann R (2007) Tenascin-W is a novel marker for activated tumor stroma in low-grade human breast cancer and influences cell behavior. Cancer Res 67(19):9169–9179. https://doi.org/10.1158/0008-5472.CAN-07-0666

Kim BG, An HJ, Kang S, Choi YP, Gao MQ, Park H, Cho NH (2011) Laminin-332-rich tumor microenvironment for tumor invasion in the interface zone of breast cancer. Am J Pathol 178(1):373–381. https://doi.org/10.1016/j.ajpath.2010.11.028

Tsuruta D, Kobayashi H, Imanishi H, Sugawara K, Ishii M, Jones JC (2008) Laminin-332-integrin interaction: a target for cancer therapy? Curr Med Chem 15(20):1968–1975

Marinkovich MP (2007) Tumour microenvironment: laminin 332 in squamous-cell carcinoma. Nat Rev Cancer 7(5):370–380. https://doi.org/10.1038/nrc2089

Guess CM, Lafleur BJ, Weidow BL, Quaranta V (2009) A decreased ratio of laminin-332 β3 to gamma2 subunit mRNA is associated with poor prognosis in colon cancer. Cancer Epidemiol Biomark Prev 18(5):1584–1590. https://doi.org/10.1158/1055-9965.EPI-08-1027

Guess CM, Quaranta V (2009) Defining the role of laminin-332 in carcinoma. Matrix Biol 28(8):445–455. https://doi.org/10.1016/j.matbio.2009.07.008

Chen J, Wang W, Wei J, Zhou D, Zhao X, Song W, Sun Q, Huang P, Zheng S (2015) Overexpression of β3 chains of laminin-332 is associated with clinicopathologic features and decreased survival in patients with pancreatic adenocarcinoma. Appl Immunohistochem Mol Morphol 23(7):516–521. https://doi.org/10.1097/PAI.0000000000000115

Katayama M, Funakoshi A, Sumii T, Sanzen N, Sekiguchi K (2005) Laminin gamma2-chain fragment circulating level increases in patients with metastatic pancreatic ductal cell adenocarcinomas. Cancer Lett 225(1):167–176. https://doi.org/10.1016/j.canlet.2004.11.052

Ramovs V, Te Molder L, Sonnenberg A (2017) The opposing roles of laminin-binding integrins in cancer. Matrix Biol 57–58:213–243. https://doi.org/10.1016/j.matbio.2016.08.007

Yamada M, Sekiguchi K (2015) Molecular basis of laminin-integrin interactions. Curr Top Membr 76:197–229. https://doi.org/10.1016/bs.ctm.2015.07.002

Tripathi M, Nandana S, Yamashita H, Ganesan R, Kirchhofer D, Quaranta V (2008) Laminin-332 is a substrate for hepsin, a protease associated with prostate cancer progression. J Biol Chem 283(45):30576–30584. https://doi.org/10.1074/jbc.M802312200

Tripathi M, Potdar AA, Yamashita H, Weidow B, Cummings PT, Kirchhofer D, Quaranta V (2011) Laminin-332 cleavage by matriptase alters motility parameters of prostate cancer cells. Prostate 71(2):184–196. https://doi.org/10.1002/pros.21233

Cavaco ACM, Rezaei M, Caliandro MF, Lima AM, Stehling M, Dhayat SA, Haier J, Brakebusch C, Eble JA (2018) The interaction between laminin-332 and α3β1 integrin determines differentiation and maintenance of CAFs, and supports invasion of pancreatic duct adenocarcinoma cells. Cancers (Basel) 11(1):14. https://doi.org/10.3390/cancers11010014

Luo Z, Wang Q, Lau WB, Lau B, Xu L, Zhao L, Yang H, Feng M, Xuan Y, Yang Y, Lei L, Wang C, Yi T, Zhao X, Wei Y, Zhou S (2016) Tumor microenvironment: the culprit for ovarian cancer metastasis? Cancer Lett 377(2):174–182. https://doi.org/10.1016/j.canlet.2016.04.038

Paszek MJ, Zahir N, Johnson KR, Lakins JN, Rozenberg GI, Gefen A, Reinhart-King CA, Margulies SS, Dembo M, Boettiger D, Hammer DA, Weaver VM (2005) Tensional homeostasis and the malignant phenotype. Cancer Cell 8(3):241–254. https://doi.org/10.1016/j.ccr.2005.08.010

Giussani M, Merlino G, Cappelletti V, Tagliabue E, Daidone MG (2015) Tumor-extracellular matrix interactions: identification of tools associated with breast cancer progression. Semin Cancer Biol 35:3–10. https://doi.org/10.1016/j.semcancer.2015.09.012

Sundquist E, Renko O, Salo S, Magga J, Cervigne NK, Nyberg P, Risteli J, Sormunen R, Vuolteenaho O, Zandonadi F, Paes Leme AF, Coletta RD, Ruskoaho H, Salo T (2016) Neoplastic extracellular matrix environment promotes cancer invasion in vitro. Exp Cell Res 344(2):229–240. https://doi.org/10.1016/j.yexcr.2016.04.003

Te Boekhorst V, Friedl P (2016) plasticity of cancer cell invasion-mechanisms and implications for therapy. Adv Cancer Res 132:209–264. https://doi.org/10.1016/bs.acr.2016.07.005

Bhowmick NA, Neilson EG, Moses HL (2004) Stromal fibroblasts in cancer initiation and progression. Nature 432(7015):332–337. https://doi.org/10.1038/nature03096

Cavaco A, Rezaei M, Niland S, Eble JA (2017) Collateral damage intended: cancer-associated fibroblasts and vasculature are potential targets in cancer therapy. Int J Mol Sci 18(11):2355. https://doi.org/10.3390/ijms18112355

Marchiq I, Pouyssegur J (2016) Hypoxia, cancer metabolism and the therapeutic benefit of targeting lactate/H(+) symporters. J Mol Med (Berl) 94(2):155–171. https://doi.org/10.1007/s00109-015-1307-x

Nielsen N, Lindemann O, Schwab A (2014) TRP channels and STIM/ORAI proteins: sensors and effectors of cancer and stroma cell migration. Br J Pharmacol 171(24):5524–5540. https://doi.org/10.1111/bph.12721

Tochhawng L, Deng S, Pervaiz S, Yap CT (2013) Redox regulation of cancer cell migration and invasion. Mitochondrion 13(3):246–253. https://doi.org/10.1016/j.mito.2012.08.002

Xing Y, Zhao S, Zhou BP, Mi J (2015) Metabolic reprogramming of the tumour microenvironment. FEBS J 282(20):3892–3898. https://doi.org/10.1111/febs.13402

Baluna RG, Eng TY, Thomas CR (2006) Adhesion molecules in radiotherapy. Radiat Res 166(6):819–831. https://doi.org/10.1667/RR0380.1

Borek C (2004) Dietary antioxidants and human cancer. Integr Cancer Ther 3(4):333–341. https://doi.org/10.1177/1534735404270578

Westbury CB, Yarnold JR (2012) Radiation fibrosis–current clinical and therapeutic perspectives. Clin Oncol (R Coll Radiol) 24(10):657–672. https://doi.org/10.1016/j.clon.2012.04.001

Yahyapour R, Motevaseli E, Rezaeyan A, Abdollahi H, Farhood B, Cheki M, Rezapoor S, Shabeeb D, Musa AE, Najafi M, Villa V (2018) Reduction-oxidation (redox) system in radiation-induced normal tissue injury: molecular mechanisms and implications in radiation therapeutics. Clin Transl Oncol 20(8):975–988. https://doi.org/10.1007/s12094-017-1828-6

Polanska UM, Orimo A (2013) Carcinoma-associated fibroblasts: non-neoplastic tumour-promoting mesenchymal cells. J Cell Physiol 228(8):1651–1657. https://doi.org/10.1002/jcp.24347

Koch S, Claesson-Welsh L (2012) Signal transduction by vascular endothelial growth factor receptors. Cold Spring Harb Perspect Med 2(7):a006502. https://doi.org/10.1101/cshperspect.a006502

Melincovici CS, Bosca AB, Susman S, Marginean M, Mihu C, Istrate M, Moldovan IM, Roman AL, Mihu CM (2018) Vascular endothelial growth factor (VEGF) - key factor in normal and pathological angiogenesis. Rom J Morphol Embryol 59(2):455–467

Miyazono K, Katsuno Y, Koinuma D, Ehata S, Morikawa M (2018) Intracellular and extracellular TGF-β signaling in cancer: some recent topics. Front Med 12(4):387–411. https://doi.org/10.1007/s11684-018-0646-8

Crafts TD, Jensen AR, Blocher-Smith EC, Markel TA (2015) Vascular endothelial growth factor: therapeutic possibilities and challenges for the treatment of ischemia. Cytokine 71(2):385–393. https://doi.org/10.1016/j.cyto.2014.08.005

Iozzo RV, Sanderson RD (2011) Proteoglycans in cancer biology, tumour microenvironment and angiogenesis. J Cell Mol Med 15(5):1013–1031. https://doi.org/10.1111/j.1582-4934.2010.01236.x

Zanotelli MR, Reinhart-King CA (2018) Mechanical forces in tumor angiogenesis. Adv Exp Med Biol 1092:91–112. https://doi.org/10.1007/978-3-319-95294-9_6

Edgar LT, Maas SA, Guilkey JE, Weiss JA (2015) A coupled model of neovessel growth and matrix mechanics describes and predicts angiogenesis in vitro. Biomech Model Mechanobiol 14(4):767–782. https://doi.org/10.1007/s10237-014-0635-z

Sund M, Xie L, Kalluri R (2004) The contribution of vascular basement membranes and extracellular matrix to the mechanics of tumor angiogenesis. APMIS 112(7–8):450–462. https://doi.org/10.1111/j.1600-0463.2004.t01-1-apm11207-0806.x

Knopik-Skrocka A, Kręplewska P, Jarmołowska-Jurczyszyn D (2017) Tumor blood vessels and vasculogenic mimicry – Current knowledge and searching for new cellular/molecular targets of anti-angiogenic therapy. Adv Cell Biol 5(1):50–71. https://doi.org/10.1515/acb-2017-0005

Zuazo-Gaztelu I, Casanovas O (2018) Unraveling the role of angiogenesis in cancer ecosystems. Front Oncol 8:248. https://doi.org/10.3389/fonc.2018.00248

Dudley AC (2012) Tumor endothelial cells. Cold Spring Harb Perspect Med 2(3):a006536. https://doi.org/10.1101/cshperspect.a006536

Angara K, Borin TF, Arbab AS (2017) Vascular mimicry: a novel neovascularization mechanism driving anti-angiogenic therapy (AAT) resistance in glioblastoma. Transl Oncol 10(4):650–660. https://doi.org/10.1016/j.tranon.2017.04.007

Dunleavey JM, Dudley AC (2012) Vascular mimicry: concepts and implications for anti-angiogenic therapy. Curr Angiogenes 1(2):133–138. https://doi.org/10.2174/2211552811201020133

Seftor RE, Hess AR, Seftor EA, Kirschmann DA, Hardy KM, Margaryan NV, Hendrix MJ (2012) Tumor cell vasculogenic mimicry: from controversy to therapeutic promise. Am J Pathol 181(4):1115–1125. https://doi.org/10.1016/j.ajpath.2012.07.013

Reid SE, Kay EJ, Neilson LJ, Henze AT, Serneels J, McGhee EJ, Dhayade S, Nixon C, Mackey JB, Santi A, Swaminathan K, Athineos D, Papalazarou V, Patella F, Roman-Fernandez A, ElMaghloob Y, Hernandez-Fernaud JR, Adams RH, Ismail S, Bryant DM, Salmeron-Sanchez M, Machesky LM, Carlin LM, Blyth K, Mazzone M, Zanivan S (2017) Tumor matrix stiffness promotes metastatic cancer cell interaction with the endothelium. EMBO J 36(16):2373–2389. https://doi.org/10.15252/embj.201694912

Folberg R, Maniotis AJ (2004) Vasculogenic mimicry. APMIS 112(7–8):508–525. https://doi.org/10.1111/j.1600-0463.2004.apm11207-0810.x

Cao Z, Bao M, Miele L, Sarkar FH, Wang Z, Zhou Q (2013) Tumour vasculogenic mimicry is associated with poor prognosis of human cancer patients: a systemic review and meta-analysis. Eur J Cancer 49(18):3914–3923. https://doi.org/10.1016/j.ejca.2013.07.148

Hutchenreuther J, Vincent K, Norley C, Racanelli M, Gruber SB, Johnson TM, Fullen DR, Raskin L, Perbal B, Holdsworth DW, Postovit LM, Leask A (2018) Activation of cancer-associated fibroblasts is required for tumor neovascularization in a murine model of melanoma. Matrix Biol. https://doi.org/10.1016/j.matbio.2018.06.003

Seftor RE, Seftor EA, Kirschmann DA, Hendrix MJ (2002) Targeting the tumor microenvironment with chemically modified tetracyclines: inhibition of laminin 5 gamma2 chain promigratory fragments and vasculogenic mimicry. Mol Cancer Ther 1(13):1173–1179

Qiao L, Liang N, Zhang J, Xie J, Liu F, Xu D, Yu X, Tian Y (2015) Advanced research on vasculogenic mimicry in cancer. J Cell Mol Med 19(2):315–326. https://doi.org/10.1111/jcmm.12496

Velez DO, Tsui B, Goshia T, Chute CL, Han A, Carter H, Fraley SI (2017) 3D collagen architecture induces a conserved migratory and transcriptional response linked to vasculogenic mimicry. Nat Commun 8(1):1651. https://doi.org/10.1038/s41467-017-01556-7

Labelle M, Hynes RO (2012) The initial hours of metastasis: the importance of cooperative host-tumor cell interactions during hematogenous dissemination. Cancer Discov 2(12):1091–1099. https://doi.org/10.1158/2159-8290.CD-12-0329

Sleeman JP, Cady B, Pantel K (2012) The connectivity of lymphogenous and hematogenous tumor cell dissemination: biological insights and clinical implications. Clin Exp Metastasis 29(7):737–746. https://doi.org/10.1007/s10585-012-9489-x

Zhu T, Hu X, Wei P, Shan G (2018) Molecular background of the regional lymph node metastasis of gastric cancer. Oncol Lett 15(3):3409–3414. https://doi.org/10.3892/ol.2018.7813

Jones D, Pereira ER, Padera TP (2018) Growth and immune evasion of lymph node metastasis. Front Oncol 8:36. https://doi.org/10.3389/fonc.2018.00036

Pircher A, Wolf D, Heidenreich A, Hilbe W, Pichler R, Heidegger I (2017) Synergies of targeting tumor angiogenesis and immune checkpoints in non-small cell lung cancer and renal cell cancer: from basic concepts to clinical reality. Int J Mol Sci 18(11):2291. https://doi.org/10.3390/ijms18112291

Schito L (2018) Bridging angiogenesis and immune evasion in the hypoxic tumor microenvironment. Am J Physiol Regul Integr Comp Physiol 1:4. https://doi.org/10.1152/ajpregu.00209.2018

Cimpean AM, Tamma R, Ruggieri S, Nico B, Toma A, Ribatti D (2017) Mast cells in breast cancer angiogenesis. Crit Rev Oncol Hematol 115:23–26. https://doi.org/10.1016/j.critrevonc.2017.04.009

Gajewski TF, Schreiber H, Fu YX (2013) Innate and adaptive immune cells in the tumor microenvironment. Nat Immunol 14(10):1014–1022. https://doi.org/10.1038/ni.2703

Quail DF, Joyce JA (2013) Microenvironmental regulation of tumor progression and metastasis. Nat Med 19(11):1423–1437. https://doi.org/10.1038/nm.3394

Sangaletti S, Chiodoni C, Tripodo C, Colombo MP (2017) The good and bad of targeting cancer-associated extracellular matrix. Curr Opin Pharmacol 35:75–82. https://doi.org/10.1016/j.coph.2017.06.003

Hao NB, Lu MH, Fan YH, Cao YL, Zhang ZR, Yang SM (2012) Macrophages in tumor microenvironments and the progression of tumors. Clin Dev Immunol 2012:948098. https://doi.org/10.1155/2012/948098

Shevach EM (2009) Mechanisms of foxp3 + T regulatory cell-mediated suppression. Immunity 30(5):636–645. https://doi.org/10.1016/j.immuni.2009.04.010

Sica A, Massarotti M (2017) Myeloid suppressor cells in cancer and autoimmunity. J Autoimmun 85:117–125. https://doi.org/10.1016/j.jaut.2017.07.010

Zhao H, Liao X, Kang Y (2017) Tregs: where we are and what comes next? Front Immunol 8:1578. https://doi.org/10.3389/fimmu.2017.01578

Dermani FK, Samadi P, Rahmani G, Kohlan AK, Najafi R (2019) PD-1/PD-L1 immune checkpoint: potential target for cancer therapy. J Cell Physiol 234(2):1313–1325. https://doi.org/10.1002/jcp.27172

Hahn AW, Gill DM, Pal SK, Agarwal N (2017) The future of immune checkpoint cancer therapy after PD-1 and CTLA-4. Immunotherapy 9(8):681–692. https://doi.org/10.2217/imt-2017-0024

Hatae R, Chamoto K (2016) Immune checkpoint inhibitors targeting programmed cell death-1 (PD-1) in cancer therapy. Rinsho Ketsueki 57(10):2224–2231. https://doi.org/10.11406/rinketsu.57.2224

Chakravarthy A, Khan L, Bensler NP, Bose P, De Carvalho DD (2018) TGF-β-associated extracellular matrix genes link cancer-associated fibroblasts to immune evasion and immunotherapy failure. Nat Commun 9(1):4692. https://doi.org/10.1038/s41467-018-06654-8

Rhee I (2016) Diverse macrophages polarization in tumor microenvironment. Arch Pharm Res 39(11):1588–1596. https://doi.org/10.1007/s12272-016-0820-y

Torcellan T, Stolp J, Chtanova T (2017) In vivo imaging sheds light on immune cell migration and function in cancer. Front Immunol 8:309. https://doi.org/10.3389/fimmu.2017.00309

Jacquemet G, Hamidi H, Ivaska J (2015) Filopodia in cell adhesion, 3D migration and cancer cell invasion. Curr Opin Cell Biol 36:23–31. https://doi.org/10.1016/j.ceb.2015.06.007

Angst BD, Marcozzi C, Magee AI (2001) The cadherin superfamily. J Cell Sci 114(Pt 4):625–626

Bertocchi C, Wang Y, Ravasio A, Hara Y, Wu Y, Sailov T, Baird MA, Davidson MW, Zaidel-Bar R, Toyama Y, Ladoux B, Mege RM, Kanchanawong P (2017) Nanoscale architecture of cadherin-based cell adhesions. Nat Cell Biol 19(1):28–37. https://doi.org/10.1038/ncb3456

Gloushankova NA, Rubtsova SN, Zhitnyak IY (2017) Cadherin-mediated cell-cell interactions in normal and cancer cells. Tissue Barriers 5(3):e1356900. https://doi.org/10.1080/21688370.2017.1356900

Harrison OJ, Jin X, Hong S, Bahna F, Ahlsen G, Brasch J, Wu Y, Vendome J, Felsovalyi K, Hampton CM, Troyanovsky RB, Ben-Shaul A, Frank J, Troyanovsky SM, Shapiro L, Honig B (2011) The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure 19(2):244–256. https://doi.org/10.1016/j.str.2010.11.016

Leckband DE, de Rooij J (2014) Cadherin adhesion and mechanotransduction. Annu Rev Cell Dev Biol 30:291–315. https://doi.org/10.1146/annurev-cellbio-100913-013212

Cichon MA, Radisky DC (2014) Extracellular matrix as a contextual determinant of transforming growth factor-β signaling in epithelial-mesenchymal transition and in cancer. Cell Adhes Migr 8(6):588–594. https://doi.org/10.4161/19336918.2014.972788

Pietila M, Ivaska J, Mani SA (2016) Whom to blame for metastasis, the epithelial-mesenchymal transition or the tumor microenvironment? Cancer Lett 380(1):359–368. https://doi.org/10.1016/j.canlet.2015.12.033

Yu Y, Xiao CH, Tan LD, Wang QS, Li XQ, Feng YM (2014) Cancer-associated fibroblasts induce epithelial-mesenchymal transition of breast cancer cells through paracrine TGF-β signalling. Br J Cancer 110(3):724–732. https://doi.org/10.1038/bjc.2013.768

Eatemadi A, Aiyelabegan HT, Negahdari B, Mazlomi MA, Daraee H, Daraee N, Eatemadi R, Sadroddiny E (2017) Role of protease and protease inhibitors in cancer pathogenesis and treatment. Biomed Pharmacother 86:221–231. https://doi.org/10.1016/j.biopha.2016.12.021

Wolf K, Friedl P (2011) Extracellular matrix determinants of proteolytic and non-proteolytic cell migration. Trends Cell Biol 21(12):736–744. https://doi.org/10.1016/j.tcb.2011.09.006

Stefanidakis M, Koivunen E (2006) Cell-surface association between matrix metalloproteinases and integrins: role of the complexes in leukocyte migration and cancer progression. Blood 108(5):1441–1450. https://doi.org/10.1182/blood-2006-02-005363

Nagase H, Visse R, Murphy G (2006) Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 69(3):562–573. https://doi.org/10.1016/j.cardiores.2005.12.002

Jacob A, Prekeris R (2015) The regulation of MMP targeting to invadopodia during cancer metastasis. Front Cell Dev Biol 3:4. https://doi.org/10.3389/fcell.2015.00004

Ren F, Tang R, Zhang X, Madushi WM, Luo D, Dang Y, Li Z, Wei K, Chen G (2015) Overexpression of MMP family members functions as prognostic biomarker for breast cancer patients: a systematic review and meta-analysis. PLoS ONE 10(8):e0135544. https://doi.org/10.1371/journal.pone.0135544

Vandooren J, Van den Steen PE, Opdenakker G (2013) Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decade. Crit Rev Biochem Mol Biol 48(3):222–272. https://doi.org/10.3109/10409238.2013.770819

Huang H (2018) Matrix metalloproteinase-9 (MMP-9) as a cancer biomarker and MMP-9 biosensors: recent advances. Sensors (Basel) 18(10):3249. https://doi.org/10.3390/s18103249

Zhang X, Huang S, Guo J, Zhou L, You L, Zhang T, Zhao Y (2016) Insights into the distinct roles of MMP-11 in tumor biology and future therapeutics (review). Int J Oncol 48(5):1783–1793. https://doi.org/10.3892/ijo.2016.3400

Castro-Castro A, Marchesin V, Monteiro P, Lodillinsky C, Rosse C, Chavrier P (2016) Cellular and molecular mechanisms of MT1-MMP-dependent cancer cell invasion. Annu Rev Cell Dev Biol 32:555–576. https://doi.org/10.1146/annurev-cellbio-111315-125227

Pahwa S, Stawikowski MJ, Fields GB (2014) Monitoring and inhibiting MT1-MMP during cancer initiation and progression. Cancers (Basel) 6(1):416–435. https://doi.org/10.3390/cancers6010416

Alcantara MB, Dass CR (2013) Regulation of MT1-MMP and MMP-2 by the serpin PEDF: a promising new target for metastatic cancer. Cell Physiol Biochem 31(4–5):487–494. https://doi.org/10.1159/000350069

Poincloux R, Lizarraga F, Chavrier P (2009) Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia. J Cell Sci 122(Pt 17):3015–3024. https://doi.org/10.1242/jcs.034561

Radisky ES, Radisky DC (2015) Matrix metalloproteinases as breast cancer drivers and therapeutic targets. Front Biosci 20:1144–1163. https://doi.org/10.2741/4364

Parvanescu V, Georgescu M, Georgescu I, Surlin V, Patrascu S, Picleanu AM, Georgescu E (2015) The role of matrix metalloproteinase-9 (MMP-9) as a prognostic factor in epithelial and lymphatic neoplasia. Chirurgia (Bucur) 110(6):506–510

Tam EM, Moore TR, Butler GS, Overall CM (2004) Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities. J Biol Chem 279(41):43336–43344. https://doi.org/10.1074/jbc.M407186200

Farina AR, Mackay AR (2014) Gelatinase B/MMP-9 in tumour pathogenesis and progression. Cancers (Basel) 6(1):240–296. https://doi.org/10.3390/cancers6010240

Overall CM (2001) Matrix metalloproteinase substrate binding domains, modules and exosites. Overview and experimental strategies. Methods Mol Biol 151:79–120

Thakur V, Bedogni B (2016) The membrane tethered matrix metalloproteinase MT1-MMP at the forefront of melanoma cell invasion and metastasis. Pharmacol Res 111:17–22. https://doi.org/10.1016/j.phrs.2016.05.019

Sato H, Takino T (2010) Coordinate action of membrane-type matrix metalloproteinase-1 (MT1-MMP) and MMP-2 enhances pericellular proteolysis and invasion. Cancer Sci 101(4):843–847. https://doi.org/10.1111/j.1349-7006.2010.01498.x

Saad S, Gottlieb DJ, Bradstock KF, Overall CM, Bendall LJ (2002) Cancer cell-associated fibronectin induces release of matrix metalloproteinase-2 from normal fibroblasts. Cancer Res 62(1):283–289

Itoh Y (2006) MT1-MMP: a key regulator of cell migration in tissue. IUBMB Life 58(10):589–596. https://doi.org/10.1080/15216540600962818

Itoh Y, Seiki M (2006) MT1-MMP: a potent modifier of pericellular microenvironment. J Cell Physiol 206(1):1–8. https://doi.org/10.1002/jcp.20431

Eddy RJ, Weidmann MD, Sharma VP, Condeelis JS (2017) Tumor cell invadopodia: invasive protrusions that orchestrate metastasis. Trends Cell Biol 27(8):595–607. https://doi.org/10.1016/j.tcb.2017.03.003

Revach OY, Geiger B (2014) The interplay between the proteolytic, invasive, and adhesive domains of invadopodia and their roles in cancer invasion. Cell Adhes Migr 8(3):215–225

Bagnato A, Rosano L (2018) Endothelin-1 receptor drives invadopodia: exploiting how β-arrestin-1 guides the way. Small GTPases 9(5):394–398. https://doi.org/10.1080/21541248.2016.1235526

Alekhina O, Burstein E, Billadeau DD (2017) Cellular functions of WASP family proteins at a glance. J Cell Sci 130(14):2235–2241. https://doi.org/10.1242/jcs.199570

Frugtniet B, Jiang WG, Martin TA (2015) Role of the WASP and WAVE family proteins in breast cancer invasion and metastasis. Breast Cancer (Dove Med Press) 7:99–109. https://doi.org/10.2147/BCTT.S59006

Parekh A, Weaver AM (2016) Regulation of invadopodia by mechanical signaling. Exp Cell Res 343(1):89–95. https://doi.org/10.1016/j.yexcr.2015.10.038

Jeannot P, Besson A (2017) Cortactin function in invadopodia. Small GTPases. https://doi.org/10.1080/21541248.2017.1405773

Linder S (2007) The matrix corroded: podosomes and invadopodia in extracellular matrix degradation. Trends Cell Biol 17(3):107–117. https://doi.org/10.1016/j.tcb.2007.01.002

Nicholas NS, Pipili A, Lesjak MS, Wells CM (2017) Differential role for PAK1 and PAK4 during the invadopodia lifecycle. Small GTPases. https://doi.org/10.1080/21541248.2017.1295830

Seano G, Primo L (2015) Podosomes and invadopodia: tools to breach vascular basement membrane. Cell Cycle 14(9):1370–1374. https://doi.org/10.1080/15384101.2015.1026523

Deryugina EI, Quigley JP (2015) Tumor angiogenesis: MMP-mediated induction of intravasation- and metastasis-sustaining neovasculature. Matrix Biol 44–46:94–112. https://doi.org/10.1016/j.matbio.2015.04.004

Genis L, Galvez BG, Gonzalo P, Arroyo AG (2006) MT1-MMP: universal or particular player in angiogenesis? Cancer Metastasis Rev 25(1):77–86. https://doi.org/10.1007/s10555-006-7891-z

Binder MJ, McCoombe S, Williams ED, McCulloch DR, Ward AC (2017) The extracellular matrix in cancer progression: role of hyalectan proteoglycans and ADAMTS enzymes. Cancer Lett 385:55–64. https://doi.org/10.1016/j.canlet.2016.11.001

Branch KM, Hoshino D, Weaver AM (2012) Adhesion rings surround invadopodia and promote maturation. Biol Open 1(8):711–722. https://doi.org/10.1242/bio.20121867

Zara M, Canobbio I, Visconte C, Canino J, Torti M, Guidetti GF (2018) Molecular mechanisms of platelet activation and aggregation induced by breast cancer cells. Cell Signal 48:45–53. https://doi.org/10.1016/j.cellsig.2018.04.008

Covic L, Kuliopulos A (2018) Protease-activated receptor 1 as therapeutic target in breast, lung, and ovarian cancer: pepducin approach. Int J Mol Sci 19(8):2237. https://doi.org/10.3390/ijms19082237

Liu X, Yu J, Song S, Yue X, Li Q (2017) Protease-activated receptor-1 (PAR-1): a promising molecular target for cancer. Oncotarget 8(63):107334–107345. https://doi.org/10.18632/oncotarget.21015

Monboisse JC, Oudart JB, Ramont L, Brassart-Pasco S (1840) Maquart FX (2014) Matrikines from basement membrane collagens: a new anti-cancer strategy. Biochim Biophys Acta 8:2589–2598. https://doi.org/10.1016/j.bbagen.2013.12.029

Tran KT, Lamb P, Deng JS (2005) Matrikines and matricryptins: implications for cutaneous cancers and skin repair. J Dermatol Sci 40(1):11–20. https://doi.org/10.1016/j.jdermsci.2005.05.001

Hornebeck W, Maquart FX (2003) Proteolyzed matrix as a template for the regulation of tumor progression. Biomed Pharmacother 57(5–6):223–230

Ramont L, Brassart-Pasco S, Thevenard J, Deshorgue A, Venteo L, Laronze JY, Pluot M, Monboisse JC, Maquart FX (2007) The NC1 domain of type XIX collagen inhibits in vivo melanoma growth. Mol Cancer Ther 6(2):506–514. https://doi.org/10.1158/1535-7163.MCT-06-0207

Brassart-Pasco S, Senechal K, Thevenard J, Ramont L, Devy J, Di Stefano L, Dupont-Deshorgue A, Brezillon S, Feru J, Jazeron JF, Diebold MD, Ricard-Blum S, Maquart FX, Monboisse JC (2012) Tetrastatin, the NC1 domain of the α4(IV) collagen chain: a novel potent anti-tumor matrikine. PLoS ONE 7(4):e29587. https://doi.org/10.1371/journal.pone.0029587

Folkman J (2006) Antiangiogenesis in cancer therapy–endostatin and its mechanisms of action. Exp Cell Res 312(5):594–607. https://doi.org/10.1016/j.yexcr.2005.11.015

Liu X, Nie W, Xie Q, Chen G, Li X, Jia Y, Yin B, Qu X, Li Y, Liang J (2018) Endostatin reverses immunosuppression of the tumor microenvironment in lung carcinoma. Oncol Lett 15(2):1874–1880. https://doi.org/10.3892/ol.2017.7455

Hope C, Emmerich PB, Papadas A, Pagenkopf A, Matkowskyj KA, Van De Hey DR, Payne SN, Clipson L, Callander NS, Hematti P, Miyamoto S, Johnson MG, Deming DA, Asimakopoulos F (2017) Versican-derived matrikines regulate Batf3-dendritic cell differentiation and promote T cell infiltration in colorectal cancer. J Immunol 199(5):1933–1941. https://doi.org/10.4049/jimmunol.1700529

Poluzzi C, Iozzo RV, Schaefer L (2016) Endostatin and endorepellin: a common route of action for similar angiostatic cancer avengers. Adv Drug Deliv Rev 97:156–173. https://doi.org/10.1016/j.addr.2015.10.012

Woodall BP, Nystrom A, Iozzo RA, Eble JA, Niland S, Krieg T, Eckes B, Pozzi A, Iozzo RV (2008) Integrin α2β1 is the required receptor for endorepellin angiostatic activity. J Biol Chem 283(4):2335–2343. https://doi.org/10.1074/jbc.M708364200

Grahovac J, Wells A (2014) Matrikine and matricellular regulators of EGF receptor signaling on cancer cell migration and invasion. Lab Invest 94(1):31–40. https://doi.org/10.1038/labinvest.2013.132

Da Silva J, Lameiras P, Beljebbar A, Berquand A, Villemin M, Ramont L, Dukic S, Nuzillard JM, Molinari M, Gautier M, Brassart-Pasco S, Brassart B (2018) Structural characterization and in vivo pro-tumor properties of a highly conserved matrikine. Oncotarget 9(25):17839–17857. https://doi.org/10.18632/oncotarget.24894

Scandolera A, Odoul L, Salesse S, Guillot A, Blaise S, Kawecki C, Maurice P, El Btaouri H, Romier-Crouzet B, Martiny L, Debelle L, Duca L (2016) The elastin receptor complex: a unique matricellular receptor with high anti-tumoral potential. Front Pharmacol 7:32. https://doi.org/10.3389/fphar.2016.00032

Duca L, Floquet N, Alix AJ, Haye B, Debelle L (2004) Elastin as a matrikine. Crit Rev Oncol Hematol 49(3):235–244. https://doi.org/10.1016/j.critrevonc.2003.09.007

Alexander S, Friedl P (2012) Cancer invasion and resistance: interconnected processes of disease progression and therapy failure. Trends Mol Med 18(1):13–26. https://doi.org/10.1016/j.molmed.2011.11.003

Devreotes P, Horwitz AR (2015) Signaling networks that regulate cell migration. Cold Spring Harb Perspect Biol 7(8):a005959. https://doi.org/10.1101/cshperspect.a005959

Ridley AJ, Schwartz MA, Burridge K, Firtel RA, Ginsberg MH, Borisy G, Parsons JT, Horwitz AR (2003) Cell migration: integrating signals from front to back. Science 302(5651):1704–1709. https://doi.org/10.1126/science.1092053

Schwartz MA, Horwitz AR (2006) Integrating adhesion, protrusion, and contraction during cell migration. Cell 125(7):1223–1225. https://doi.org/10.1016/j.cell.2006.06.015

Vicente-Manzanares M, Horwitz AR (2011) Cell migration: an overview. Methods Mol Biol 769:1–24. https://doi.org/10.1007/978-1-61779-207-6_1

Vicente-Manzanares M, Webb DJ, Horwitz AR (2005) Cell migration at a glance. J Cell Sci 118(Pt 21):4917–4919. https://doi.org/10.1242/jcs.02662

Aguilar-Cuenca R, Juanes-Garcia A, Vicente-Manzanares M (2014) Myosin II in mechanotransduction: master and commander of cell migration, morphogenesis, and cancer. Cell Mol Life Sci 71(3):479–492. https://doi.org/10.1007/s00018-013-1439-5

Vicente-Manzanares M, Ma X, Adelstein RS, Horwitz AR (2009) Non-muscle myosin II takes centre stage in cell adhesion and migration. Nat Rev Mol Cell Biol 10(11):778–790. https://doi.org/10.1038/nrm2786

Vicente-Manzanares M, Choi CK, Horwitz AR (2009) Integrins in cell migration–the actin connection. J Cell Sci 122(Pt 2):199–206. https://doi.org/10.1242/jcs.018564

Yamaguchi H, Condeelis J (2007) Regulation of the actin cytoskeleton in cancer cell migration and invasion. Biochim Biophys Acta 1773(5):642–652. https://doi.org/10.1016/j.bbamcr.2006.07.001

Ungefroren H, Witte D, Lehnert H (2018) The role of small GTPases of the Rho/Rac family in TGF-β-induced EMT and cell motility in cancer. Dev Dyn 247(3):451–461. https://doi.org/10.1002/dvdy.24505

Lawson CD, Ridley AJ (2018) Rho GTPase signaling complexes in cell migration and invasion. J Cell Biol 217(2):447–457. https://doi.org/10.1083/jcb.201612069

Casalou C, Faustino A, Barral DC (2016) Arf proteins in cancer cell migration. Small GTPases 7(4):270–282. https://doi.org/10.1080/21541248.2016.1228792

Kale VP, Hengst JA, Desai DH, Amin SG, Yun JK (2015) The regulatory roles of ROCK and MRCK kinases in the plasticity of cancer cell migration. Cancer Lett 361(2):185–196. https://doi.org/10.1016/j.canlet.2015.03.017

Huttenlocher A, Horwitz AR (2011) Integrins in cell migration. Cold Spring Harb Perspect Biol 3(9):a005074. https://doi.org/10.1101/cshperspect.a005074

Bays JL, DeMali KA (2017) Vinculin in cell-cell and cell-matrix adhesions. Cell Mol Life Sci 74(16):2999–3009. https://doi.org/10.1007/s00018-017-2511-3

Goldmann WH (2016) Role of vinculin in cellular mechanotransduction. Cell Biol Int 40(3):241–256. https://doi.org/10.1002/cbin.10563

Grashoff C, Hoffman BD, Brenner MD, Zhou R, Parsons M, Yang MT, McLean MA, Sligar SG, Chen CS, Ha T, Schwartz MA (2010) Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics. Nature 466(7303):263–266. https://doi.org/10.1038/nature09198

Ehrlicher AJ, Krishnan R, Guo M, Bidan CM, Weitz DA, Pollak MR (2015) Α-actinin binding kinetics modulate cellular dynamics and force generation. Proc Natl Acad Sci U S A 112(21):6619–6624. https://doi.org/10.1073/pnas.1505652112

Roca-Cusachs P, del Rio A, Puklin-Faucher E, Gauthier NC, Biais N, Sheetz MP (2013) Integrin-dependent force transmission to the extracellular matrix by α-actinin triggers adhesion maturation. Proc Natl Acad Sci USA 110(15):E1361–E1370. https://doi.org/10.1073/pnas.1220723110

Carisey A, Tsang R, Greiner AM, Nijenhuis N, Heath N, Nazgiewicz A, Kemkemer R, Derby B, Spatz J, Ballestrem C (2013) Vinculin regulates the recruitment and release of core focal adhesion proteins in a force-dependent manner. Curr Biol 23(4):271–281. https://doi.org/10.1016/j.cub.2013.01.009

Zaidel-Bar R, Milo R, Kam Z, Geiger B (2007) A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J Cell Sci 120(Pt 1):137–148. https://doi.org/10.1242/jcs.03314

Bays JL, Peng X, Tolbert CE, Guilluy C, Angell AE, Pan Y, Superfine R, Burridge K, DeMali KA (2014) Vinculin phosphorylation differentially regulates mechanotransduction at cell-cell and cell-matrix adhesions. J Cell Biol 205(2):251–263. https://doi.org/10.1083/jcb.201309092

Dobrokhotov O, Samsonov M, Sokabe M, Hirata H (2018) Mechanoregulation and pathology of YAP/TAZ via Hippo and non-Hippo mechanisms. Clin Transl Med 7(1):23. https://doi.org/10.1186/s40169-018-0202-9

Noguchi S, Saito A, Nagase T (2018) YAP/TAZ signaling as a molecular link between fibrosis and cancer. Int J Mol Sci 19(11):3674. https://doi.org/10.3390/ijms19113674

Zanconato F, Cordenonsi M, Piccolo S (2016) YAP/TAZ at the roots of cancer. Cancer Cell 29(6):783–803. https://doi.org/10.1016/j.ccell.2016.05.005

Palecek SP, Loftus JC, Ginsberg MH, Lauffenburger DA, Horwitz AF (1997) Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature 385(6616):537–540. https://doi.org/10.1038/385537a0

Gritsenko PG, Ilina O, Friedl P (2012) Interstitial guidance of cancer invasion. J Pathol 226(2):185–199. https://doi.org/10.1002/path.3031

Wolf K, Alexander S, Schacht V, Coussens LM, von Andrian UH, van Rheenen J, Deryugina E, Friedl P (2009) Collagen-based cell migration models in vitro and in vivo. Semin Cell Dev Biol 20(8):931–941. https://doi.org/10.1016/j.semcdb.2009.08.005

Deng J, Zhao C, Spatz JP, Wei Q (2017) Nanopatterned adhesive, stretchable hydrogel to control ligand spacing and regulate cell spreading and migration. ACS Nano 11(8):8282–8291. https://doi.org/10.1021/acsnano.7b03449

Arnold M, Hirschfeld-Warneken VC, Lohmuller T, Heil P, Blummel J, Cavalcanti-Adam EA, Lopez-Garcia M, Walther P, Kessler H, Geiger B, Spatz JP (2008) Induction of cell polarization and migration by a gradient of nanoscale variations in adhesive ligand spacing. Nano Lett 8(7):2063–2069. https://doi.org/10.1021/nl801483w

Alfano M, Nebuloni M, Allevi R, Zerbi P, Longhi E, Luciano R, Locatelli I, Pecoraro A, Indrieri M, Speziali C, Doglioni C, Milani P, Montorsi F, Salonia A (2016) Linearized texture of three-dimensional extracellular matrix is mandatory for bladder cancer cell invasion. Sci Rep 6:36128. https://doi.org/10.1038/srep36128

Krause M, Wolf K (2015) Cancer cell migration in 3D tissue: negotiating space by proteolysis and nuclear deformability. Cell Adh Migr 9(5):357–366. https://doi.org/10.1080/19336918.2015.1061173

Wolf K, Te Lindert M, Krause M, Alexander S, Te Riet J, Willis AL, Hoffman RM, Figdor CG, Weiss SJ, Friedl P (2013) Physical limits of cell migration: control by ECM space and nuclear deformation and tuning by proteolysis and traction force. J Cell Biol 201(7):1069–1084. https://doi.org/10.1083/jcb.201210152

Denais CM, Gilbert RM, Isermann P, McGregor AL, te Lindert M, Weigelin B, Davidson PM, Friedl P, Wolf K, Lammerding J (2016) Nuclear envelope rupture and repair during cancer cell migration. Science 352(6283):353–358. https://doi.org/10.1126/science.aad7297

Petrie RJ, Yamada KM (2016) Multiple mechanisms of 3D migration: the origins of plasticity. Curr Opin Cell Biol 42:7–12. https://doi.org/10.1016/j.ceb.2016.03.025

Doyle AD, Petrie RJ, Kutys ML, Yamada KM (2013) Dimensions in cell migration. Curr Opin Cell Biol 25(5):642–649. https://doi.org/10.1016/j.ceb.2013.06.004

Petrie RJ, Harlin HM, Korsak LI, Yamada KM (2017) Activating the nuclear piston mechanism of 3D migration in tumor cells. J Cell Biol 216(1):93–100. https://doi.org/10.1083/jcb.201605097

Friedl P, Locker J, Sahai E, Segall JE (2012) Classifying collective cancer cell invasion. Nat Cell Biol 14(8):777–783. https://doi.org/10.1038/ncb2548

Friedl P, Gilmour D (2009) Collective cell migration in morphogenesis, regeneration and cancer. Nat Rev Mol Cell Biol 10(7):445–457. https://doi.org/10.1038/nrm2720

Khalil AA, Ilina O, Gritsenko PG, Bult P, Span PN, Friedl P (2017) Collective invasion in ductal and lobular breast cancer associates with distant metastasis. Clin Exp Metastasis 34(6–7):421–429. https://doi.org/10.1007/s10585-017-9858-6

Das T, Spatz JP (2016) Getting a grip on collective cell migration. Nat Cell Biol 18(12):1265–1267. https://doi.org/10.1038/ncb3447

Park JA, Atia L, Mitchel JA, Fredberg JJ, Butler JP (2016) Collective migration and cell jamming in asthma, cancer and development. J Cell Sci 129(18):3375–3383. https://doi.org/10.1242/jcs.187922

Ramos Gde O, Bernardi L, Lauxen I, Sant’Ana Filho M, Horwitz AR, Lamers ML (2016) Fibronectin modulates cell adhesion and signaling to promote single cell migration of highly invasive oral squamous cell carcinoma. PLoS ONE 11(3):e0151338. https://doi.org/10.1371/journal.pone.0151338

Wolf K, Wu YI, Liu Y, Geiger J, Tam E, Overall C, Stack MS, Friedl P (2007) Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat Cell Biol 9(8):893–904. https://doi.org/10.1038/ncb1616

Han T, Kang D, Ji D, Wang X, Zhan W, Fu M, Xin HB, Wang JB (2013) How does cancer cell metabolism affect tumor migration and invasion? Cell Adh Migr 7(5):395–403. https://doi.org/10.4161/cam.26345

Lehmann S, Te Boekhorst V, Odenthal J, Bianchi R, van Helvert S, Ikenberg K, Ilina O, Stoma S, Xandry J, Jiang L, Grenman R, Rudin M, Friedl P (2017) Hypoxia induces a HIF-1-dependent transition from collective-to-amoeboid dissemination in epithelial cancer cells. Curr Biol 27(3):392–400. https://doi.org/10.1016/j.cub.2016.11.057

Gaggioli C, Hooper S, Hidalgo-Carcedo C, Grosse R, Marshall JF, Harrington K, Sahai E (2007) Fibroblast-led collective invasion of carcinoma cells with differing roles for RhoGTPases in leading and following cells. Nat Cell Biol 9(12):1392–1400. https://doi.org/10.1038/ncb1658

Erpenbeck L, Schön MP (2010) Deadly allies: the fatal interplay between platelets and metastizing cancer cells. Blood 115(17):3427–3436

Camerer E (2004) Platelets, protease-activated receptors, and fibrinogen in hematogenous metastasis. Blood 104:397–401

Weisel JW, Litvinov RI (2017) Fibrin formation, structure and properties. Subcell Biochem 82:405–456. https://doi.org/10.1007/978-3-319-49674-0_13

O’Sullivan JM, Preston RJS, Robson T, O’Donnell JS (2018) Emerging Roles for von Willebrand Factor in Cancer Cell Biology. Semin Thromb Hemost 44(2):159–166. https://doi.org/10.1055/s-0037-1607352

Bauer AT, Suckau J, Frank K, Desch A, Goertz L, Wagner AH, Hecker M, Goerge T, Umansky L, Beckhove P, Utikal J, Gorzelanny C, Diaz-Valdes N, Umansky V, Schneider SW (2015) von Willebrand factor fibers promote cancer-associated platelet aggregation in malignant melanoma of mice and humans. Blood 125(20):3153–3163. https://doi.org/10.1182/blood-2014-08-595686

Peinado H, Zhang H, Matei IR, Costa-Silva B, Hoshino A, Rodrigues G, Psaila B, Kaplan RN, Bromberg JF, Kang Y, Bissell MJ, Cox TR, Giaccia AJ, Erler JT, Hiratsuka S, Ghajar CM, Lyden D (2017) Pre-metastatic niches: organ-specific homes for metastases. Nat Rev Cancer 17(5):302–317. https://doi.org/10.1038/nrc.2017.6

Psaila B, Lyden D (2009) The metastatic niche: adapting the foreign soil. Nat Rev Cancer 9(4):285–293. https://doi.org/10.1038/nrc2621

Hoshino A, Costa-Silva B, Shen TL, Rodrigues G, Hashimoto A, Tesic Mark M, Molina H, Kohsaka S, Di Giannatale A, Ceder S, Singh S, Williams C, Soplop N, Uryu K, Pharmer L, King T, Bojmar L, Davies AE, Ararso Y, Zhang T, Zhang H, Hernandez J, Weiss JM, Dumont-Cole VD, Kramer K, Wexler LH, Narendran A, Schwartz GK, Healey JH, Sandstrom P, Labori KJ, Kure EH, Grandgenett PM, Hollingsworth MA, de Sousa M, Kaur S, Jain M, Mallya K, Batra SK, Jarnagin WR, Brady MS, Fodstad O, Muller V, Pantel K, Minn AJ, Bissell MJ, Garcia BA, Kang Y, Rajasekhar VK, Ghajar CM, Matei I, Peinado H, Bromberg J, Lyden D (2015) Tumour exosome integrins determine organotropic metastasis. Nature 527(7578):329–335. https://doi.org/10.1038/nature15756

Geraud C, Koch PS, Damm F, Schledzewski K, Goerdt S (2014) The metastatic cycle: metastatic niches and cancer cell dissemination. J Dtsch Dermatol Ges 12(11):1012–1019. https://doi.org/10.1111/ddg.12451

Aguado BA, Bushnell GG, Rao SS, Jeruss JS, Shea LD (2017) Engineering the pre-metastatic niche. Nat Biomed Eng 1. https://doi.org/10.1038/s41551-017-0077

Liu Y, Cao X (2016) Characteristics and significance of the pre-metastatic niche. Cancer Cell 30(5):668–681. https://doi.org/10.1016/j.ccell.2016.09.011

Rezaeeyan H, Shirzad R, McKee TD, Saki N (2018) Role of chemokines in metastatic niche: new insights along with a diagnostic and prognostic approach. APMIS 126(5):359–370. https://doi.org/10.1111/apm.12818

Nogues L, Benito-Martin A, Hergueta-Redondo M, Peinado H (2018) The influence of tumour-derived extracellular vesicles on local and distal metastatic dissemination. Mol Aspects Med 60:15–26. https://doi.org/10.1016/j.mam.2017.11.012

Lobb RJ, Lima LG, Moller A (2017) Exosomes: key mediators of metastasis and pre-metastatic niche formation. Semin Cell Dev Biol 67:3–10. https://doi.org/10.1016/j.semcdb.2017.01.004

Gartland A, Erler JT, Cox TR (2016) The role of lysyl oxidase, the extracellular matrix and the pre-metastatic niche in bone metastasis. J Bone Oncol 5(3):100–103. https://doi.org/10.1016/j.jbo.2016.04.001

Peinado H, Lavotshkin S, Lyden D (2011) The secreted factors responsible for pre-metastatic niche formation: old sayings and new thoughts. Semin Cancer Biol 21(2):139–146. https://doi.org/10.1016/j.semcancer.2011.01.002

Hoye AM, Erler JT (2016) Structural ECM components in the premetastatic and metastatic niche. Am J Physiol Cell Physiol 310(11):C955–C967. https://doi.org/10.1152/ajpcell.00326.2015

Descot A, Oskarsson T (2013) The molecular composition of the metastatic niche. Exp Cell Res 319(11):1679–1686. https://doi.org/10.1016/j.yexcr.2013.04.017

Cox TR, Rumney RMH, Schoof EM, Perryman L, Hoye AM, Agrawal A, Bird D, Latif NA, Forrest H, Evans HR, Huggins ID, Lang G, Linding R, Gartland A, Erler JT (2015) The hypoxic cancer secretome induces pre-metastatic bone lesions through lysyl oxidase. Nature 522(7554):106–110. https://doi.org/10.1038/nature14492

El-Haibi CP, Bell GW, Zhang J, Collmann AY, Wood D, Scherber CM, Csizmadia E, Mariani O, Zhu C, Campagne A, Toner M, Bhatia SN, Irimia D, Vincent-Salomon A, Karnoub AE (2012) Critical role for lysyl oxidase in mesenchymal stem cell-driven breast cancer malignancy. Proc Natl Acad Sci USA 109(43):17460–17465. https://doi.org/10.1073/pnas.1206653109

Pickup MW, Laklai H, Acerbi I, Owens P, Gorska AE, Chytil A, Aakre M, Weaver VM, Moses HL (2013) Stromally derived lysyl oxidase promotes metastasis of transforming growth factor-β-deficient mouse mammary carcinomas. Cancer Res 73(17):5336–5346. https://doi.org/10.1158/0008-5472.CAN-13-0012

Jablonska J, Lang S, Sionov RV, Granot Z (2017) The regulation of pre-metastatic niche formation by neutrophils. Oncotarget 8(67):112132–112144. https://doi.org/10.18632/oncotarget.22792

Yumoto K, Eber MR, Berry JE, Taichman RS, Shiozawa Y (2014) Molecular pathways: niches in metastatic dormancy. Clin Cancer Res 20(13):3384–3389. https://doi.org/10.1158/1078-0432.CCR-13-0897

Oskarsson T, Batlle E, Massague J (2014) Metastatic stem cells: sources, niches, and vital pathways. Cell Stem Cell 14(3):306–321. https://doi.org/10.1016/j.stem.2014.02.002

Leprini A, Querze G, Zardi L (1994) Tenascin isoforms: possible targets for diagnosis and therapy of cancer and mechanisms regulating their expression. Perspect Dev Neurobiol 2(1):117–123

Nicolo G, Salvi S, Oliveri G, Borsi L, Castellani P, Zardi L (1990) Expression of tenascin and of the ED-B containing oncofetal fibronectin isoform in human cancer. Cell Differ Dev 32(3):401–408

Vandooren J, Opdenakker G, Loadman PM, Edwards DR (2016) Proteases in cancer drug delivery. Adv Drug Deliv Rev 97:144–155. https://doi.org/10.1016/j.addr.2015.12.020

Piperigkou Z, Manou D, Karamanou K, Theocharis AD (2018) Strategies to target matrix metalloproteinases as therapeutic approach in cancer. Methods Mol Biol 1731:325–348. https://doi.org/10.1007/978-1-4939-7595-2_27

Gingras D, Batist G, Beliveau R (2001) AE-941 (Neovastat): a novel multifunctional antiangiogenic compound. Expert Rev Anticancer Ther 1(3):341–347. https://doi.org/10.1586/14737140.1.3.341

Gingras D, Boivin D, Deckers C, Gendron S, Barthomeuf C, Beliveau R (2003) Neovastat–a novel antiangiogenic drug for cancer therapy. Anticancer Drugs 14(2):91–96. https://doi.org/10.1097/01.cad.0000054520.85618.3f

Lu C, Lee JJ, Komaki R, Herbst RS, Feng L, Evans WK, Choy H, Desjardins P, Esparaz BT, Truong MT, Saxman S, Kelaghan J, Bleyer A, Fisch MJ (2010) Chemoradiotherapy with or without AE-941 in stage III non-small cell lung cancer: a randomized phase III trial. J Natl Cancer Inst 102(12):859–865. https://doi.org/10.1093/jnci/djq179

Rizvi NA, Humphrey JS, Ness EA, Johnson MD, Gupta E, Williams K, Daly DJ, Sonnichsen D, Conway D, Marshall J, Hurwitz H (2004) A phase I study of oral BMS-275291, a novel nonhydroxamate sheddase-sparing matrix metalloproteinase inhibitor, in patients with advanced or metastatic cancer. Clin Cancer Res 10(6):1963–1970

Leighl NB, Paz-Ares L, Douillard JY, Peschel C, Arnold A, Depierre A, Santoro A, Betticher DC, Gatzemeier U, Jassem J, Crawford J, Tu D, Bezjak A, Humphrey JS, Voi M, Galbraith S, Hann K, Seymour L, Shepherd FA (2005) Randomized phase III study of matrix metalloproteinase inhibitor BMS-275291 in combination with paclitaxel and carboplatin in advanced non-small-cell lung cancer: National Cancer Institute of Canada-Clinical Trials Group Study BR.18. J Clin Oncol 23(12):2831–2839. https://doi.org/10.1200/JCO.2005.04.044

Hirte H, Vergote IB, Jeffrey JR, Grimshaw RN, Coppieters S, Schwartz B, Tu D, Sadura A, Brundage M, Seymour L (2006) A phase III randomized trial of BAY 12-9566 (tanomastat) as maintenance therapy in patients with advanced ovarian cancer responsive to primary surgery and paclitaxel/platinum containing chemotherapy: a National Cancer Institute of Canada Clinical Trials Group Study. Gynecol Oncol 102(2):300–308. https://doi.org/10.1016/j.ygyno.2005.12.020

Hande KR, Collier M, Paradiso L, Stuart-Smith J, Dixon M, Clendeninn N, Yeun G, Alberti D, Binger K, Wilding G (2004) Phase I and pharmacokinetic study of prinomastat, a matrix metalloprotease inhibitor. Clin Cancer Res 10(3):909–915

Bissett D, O’Byrne KJ, von Pawel J, Gatzemeier U, Price A, Nicolson M, Mercier R, Mazabel E, Penning C, Zhang MH, Collier MA, Shepherd FA (2005) Phase III study of matrix metalloproteinase inhibitor prinomastat in non-small-cell lung cancer. J Clin Oncol 23(4):842–849. https://doi.org/10.1200/JCO.2005.03.170

Paemen L, Martens E, Masure S, Opdenakker G (1995) Monoclonal antibodies specific for natural human neutrophil gelatinase B used for affinity purification, quantitation by two-site ELISA and inhibition of enzymatic activity. Eur J Biochem 234(3):759–765

Martens E, Leyssen A, Van Aelst I, Fiten P, Piccard H, Hu J, Descamps FJ, Van den Steen PE, Proost P, Van Damme J, Liuzzi GM, Riccio P, Polverini E, Opdenakker G (2007) A monoclonal antibody inhibits gelatinase B/MMP-9 by selective binding to part of the catalytic domain and not to the fibronectin or zinc binding domains. Biochim Biophys Acta 1770(2):178–186. https://doi.org/10.1016/j.bbagen.2006.10.012

Devy L, Huang L, Naa L, Yanamandra N, Pieters H, Frans N, Chang E, Tao Q, Vanhove M, Lejeune A, van Gool R, Sexton DJ, Kuang G, Rank D, Hogan S, Pazmany C, Ma YL, Schoonbroodt S, Nixon AE, Ladner RC, Hoet R, Henderikx P, Tenhoor C, Rabbani SA, Valentino ML, Wood CR, Dransfield DT (2009) Selective inhibition of matrix metalloproteinase-14 blocks tumor growth, invasion, and angiogenesis. Cancer Res 69(4):1517–1526. https://doi.org/10.1158/0008-5472.CAN-08-3255

Lemaitre V, D’Armiento J (2006) Matrix metalloproteinases in development and disease. Birth Defects Res C 78(1):1–10. https://doi.org/10.1002/bdrc.20065

Li L, Li H (2013) Role of microRNA-mediated MMP regulation in the treatment and diagnosis of malignant tumors. Cancer Biol Ther 14(9):796–805. https://doi.org/10.4161/cbt.25936

Gabriely G, Wurdinger T, Kesari S, Esau CC, Burchard J, Linsley PS, Krichevsky AM (2008) MicroRNA 21 promotes glioma invasion by targeting matrix metalloproteinase regulators. Mol Cell Biol 28(17):5369–5380. https://doi.org/10.1128/MCB.00479-08

Costa PM, Cardoso AL, Custodia C, Cunha P, Pereira de Almeida L, Pedroso de Lima MC (2015) MiRNA-21 silencing mediated by tumor-targeted nanoparticles combined with sunitinib: a new multimodal gene therapy approach for glioblastoma. J Control Release 207:31–39. https://doi.org/10.1016/j.jconrel.2015.04.002

Chan N, Willis A, Kornhauser N, Ward MM, Lee SB, Nackos E, Seo BR, Chuang E, Cigler T, Moore A, Donovan D, Vallee Cobham M, Fitzpatrick V, Schneider S, Wiener A, Guillaume-Abraham J, Aljom E, Zelkowitz R, Warren JD, Lane ME, Fischbach C, Mittal V, Vahdat L (2017) Influencing the tumor microenvironment: a phase II study of copper depletion using tetrathiomolybdate in patients with breast cancer at high risk for recurrence and in preclinical models of lung metastases. Clin Cancer Res 23(3):666–676. https://doi.org/10.1158/1078-0432.CCR-16-1326

Hecht JR, Benson AB 3rd, Vyushkov D, Yang Y, Bendell J, Verma U (2017) A phase II, randomized, double-blind, placebo-controlled study of simtuzumab in combination with FOLFIRI for the second-line treatment of metastatic KRAS mutant colorectal adenocarcinoma. Oncologist 22(3):243-e223. https://doi.org/10.1634/theoncologist.2016-0479

Benson AB 3rd, Wainberg ZA, Hecht JR, Vyushkov D, Dong H, Bendell J, Kudrik F (2017) A phase II randomized, double-blind, placebo-controlled study of simtuzumab or placebo in combination with gemcitabine for the first-line treatment of pancreatic adenocarcinoma. Oncologist 22(3):241-e215. https://doi.org/10.1634/theoncologist.2017-0024

Barry-Hamilton V, Spangler R, Marshall D, McCauley S, Rodriguez HM, Oyasu M, Mikels A, Vaysberg M, Ghermazien H, Wai C, Garcia CA, Velayo AC, Jorgensen B, Biermann D, Tsai D, Green J, Zaffryar-Eilot S, Holzer A, Ogg S, Thai D, Neufeld G, Van Vlasselaer P, Smith V (2010) Allosteric inhibition of lysyl oxidase-like-2 impedes the development of a pathologic microenvironment. Nat Med 16(9):1009–1017. https://doi.org/10.1038/nm.2208

Rodriguez HM, Vaysberg M, Mikels A, McCauley S, Velayo AC, Garcia C, Smith V (2010) Modulation of lysyl oxidase-like 2 enzymatic activity by an allosteric antibody inhibitor. J Biol Chem 285(27):20964–20974. https://doi.org/10.1074/jbc.M109.094136

Rasmussen HS, McCann PP (1997) Matrix metalloproteinase inhibition as a novel anticancer strategy: a review with special focus on batimastat and marimastat. Pharmacol Ther 75(1):69–75

Cathcart J, Pulkoski-Gross A, Cao J (2015) Targeting matrix metalloproteinases in cancer: bringing new life to old ideas. Genes Dis 2(1):26–34. https://doi.org/10.1016/j.gendis.2014.12.002

Rao BG (2005) Recent developments in the design of specific matrix metalloproteinase inhibitors aided by structural and computational studies. Curr Pharm Des 11(3):295–322

Au JL, Yeung BZ, Wientjes MG, Lu Z, Wientjes MG (2016) Delivery of cancer therapeutics to extracellular and intracellular targets: determinants, barriers, challenges and opportunities. Adv Drug Deliv Rev 97:280–301. https://doi.org/10.1016/j.addr.2015.12.002

Rodriguez-Cabello JC, Arias FJ, Rodrigo MA, Girotti A (2016) Elastin-like polypeptides in drug delivery. Adv Drug Deliv Rev 97:85–100. https://doi.org/10.1016/j.addr.2015.12.007

Arosio D, Casagrande C (2016) Advancement in integrin facilitated drug delivery. Adv Drug Deliv Rev 97:111–143. https://doi.org/10.1016/j.addr.2015.12.001

Multhaupt HA, Leitinger B, Gullberg D, Couchman JR (2016) Extracellular matrix component signaling in cancer. Adv Drug Deliv Rev 97:28–40. https://doi.org/10.1016/j.addr.2015.10.013

Hinderer S, Layland SL, Schenke-Layland K (2016) ECM and ECM-like materials—biomaterials for applications in regenerative medicine and cancer therapy. Adv Drug Deliv Rev 97:260–269. https://doi.org/10.1016/j.addr.2015.11.019

Celia-Terrassa T, Kang Y (2018) Metastatic niche functions and therapeutic opportunities. Nat Cell Biol 20(8):868–877. https://doi.org/10.1038/s41556-018-0145-9

Ordonez-Moran P, Huelsken J (2014) Complex metastatic niches: already a target for therapy? Curr Opin Cell Biol 31:29–38. https://doi.org/10.1016/j.ceb.2014.06.012

Horton ER, Astudillo P, Humphries MJ, Humphries JD (2016) Mechanosensitivity of integrin adhesion complexes: role of the consensus adhesome. Exp Cell Res 343(1):7–13. https://doi.org/10.1016/j.yexcr.2015.10.025

Murphy DA, Courtneidge SA (2011) The ‘ins’ and ‘outs’ of podosomes and invadopodia: characteristics, formation and function. Nat Rev Mol Cell Biol 12(7):413–426. https://doi.org/10.1038/nrm3141

Leitinger B, Hohenester E (2007) Mammalian collagen receptors. Matrix Biol 26(3):146–155. https://doi.org/10.1016/j.matbio.2006.10.007

Torres PH, Sousa GL, Pascutti PG (2011) Structural analysis of the N-terminal fragment of the antiangiogenic protein endostatin: a molecular dynamics study. Proteins 79(9):2684–2692. https://doi.org/10.1002/prot.23096

Oudart JB, Monboisse JC, Maquart FX, Brassart B, Brassart-Pasco S, Ramont L (2017) Type XIX collagen: a new partner in the interactions between tumor cells and their microenvironment. Matrix Biol 57–58:169–177. https://doi.org/10.1016/j.matbio.2016.07.010

Nagase H, Fields GB (1996) Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides. Biopolymers 40(4):399–416. https://doi.org/10.1002/(SICI)1097-0282(1996)40:4%3C399:AID-BIP5%3E3.0.CO;2-R

Mithieux SM, Weiss AS (2005) Elastin. Adv Protein Chem 70:437–461. https://doi.org/10.1016/S0065-3233(05)70013-9

Wells JM, Gaggar A, Blalock JE (2015) MMP generated matrikines. Matrix Biol 44–46:122–129. https://doi.org/10.1016/j.matbio.2015.01.016

Cain SA, Mularczyk EJ, Singh M, Massam-Wu T, Kielty CM (2016) ADAMTS-10 and -6 differentially regulate cell-cell junctions and focal adhesions. Sci Rep 6:35956. https://doi.org/10.1038/srep35956

Bax DV, Mahalingam Y, Cain S, Mellody K, Freeman L, Younger K, Shuttleworth CA, Humphries MJ, Couchman JR, Kielty CM (2007) Cell adhesion to fibrillin-1: identification of an Arg-Gly-Asp-dependent synergy region and a heparin-binding site that regulates focal adhesion formation. J Cell Sci 120(Pt 8):1383–1392. https://doi.org/10.1242/jcs.003954

Jovanovic J, Iqbal S, Jensen S, Mardon H, Handford P (2008) Fibrillin-integrin interactions in health and disease. Biochem Soc Trans 36(Pt 2):257–262. https://doi.org/10.1042/BST0360257

Joshi R, Goihberg E, Ren W, Pilichowska M, Mathew P (2017) Proteolytic fragments of fibronectin function as matrikines driving the chemotactic affinity of prostate cancer cells to human bone marrow mesenchymal stromal cells via the α5β1 integrin. Cell Adh Migr 11(4):305–315. https://doi.org/10.1080/19336918.2016.1212139

White ES, Baralle FE, Muro AF (2008) New insights into form and function of fibronectin splice variants. J Pathol 216(1):1–14. https://doi.org/10.1002/path.2388

Faron G, Balepa L, Parra J, Fils JF, Gucciardo L (2018) The fetal fibronectin test: 25 years after its development, what is the evidence regarding its clinical utility? A systematic review and meta-analysis. J Matern Fetal Neonatal Med. https://doi.org/10.1080/14767058.2018.1491031

Sawicka KM, Seeliger M, Musaev T, Macri LK, Clark RA (2015) Fibronectin interaction and enhancement of growth factors: importance for wound healing. Adv Wound Care (New Rochelle) 4(8):469–478. https://doi.org/10.1089/wound.2014.0616

Wang Y, Ni H (2016) Fibronectin maintains the balance between hemostasis and thrombosis. Cell Mol Life Sci 73(17):3265–3277. https://doi.org/10.1007/s00018-016-2225-y

Mercuri FA, Maciewicz RA, Tart J, Last K, Fosang AJ (2000) Mutations in the interglobular domain of aggrecan alter matrix metalloproteinase and aggrecanase cleavage patterns Evidence that matrix metalloproteinase cleavage interferes with aggrecanase activity. J Biol Chem 275(42):33038–33045

Viapiano MS, Hockfield S, Matthews RT (2008) BEHAB/brevican requires ADAMTS-mediated proteolytic cleavage to promote glioma invasion. J Neurooncol 88(3):261–272. https://doi.org/10.1007/s11060-008-9575-8

Demircan K, Topcu V, Takigawa T, Akyol S, Yonezawa T, Ozturk G, Ugurcu V, Hasgul R, Yigitoglu MR, Akyol O, McCulloch DR, Hirohata S (2014) ADAMTS4 and ADAMTS5 knockout mice are protected from versican but not aggrecan or brevican proteolysis during spinal cord injury. Biomed Res Int 2014:693746. https://doi.org/10.1155/2014/693746

Li H, Leung TC, Hoffman S, Balsamo J, Lilien J (2000) Coordinate regulation of cadherin and integrin function by the chondroitin sulfate proteoglycan neurocan. J Cell Biol 149(6):1275–1288

Mohan V, Wyatt EV, Gotthard I, Phend KD, Diestel S, Duncan BW, Weinberg RJ, Tripathy A, Maness PF (2018) Neurocan inhibits semaphorin 3F induced dendritic spine remodeling through NrCAM in cortical neurons. Front Cell Neurosci 12:346. https://doi.org/10.3389/fncel.2018.00346

Wu Y, Chen L, Zheng PS, Yang BB (2002) β 1-Integrin-mediated glioma cell adhesion and free radical-induced apoptosis are regulated by binding to a C-terminal domain of PG-M/versican. J Biol Chem 277(14):12294–12301. https://doi.org/10.1074/jbc.M110748200

Overall CM (2002) Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites. Mol Biotechnol 22(1):51–86. https://doi.org/10.1385/MB:22:1:051

Iozzo RV, Moscatello DK, McQuillan DJ, Eichstetter I (1999) Decorin is a biological ligand for the epidermal growth factor receptor. J Biol Chem 274(8):4489–4492

Moreth K, Iozzo RV, Schaefer L (2012) Small leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation. Cell Cycle 11(11):2084–2091. https://doi.org/10.4161/cc.20316

Goldoni S, Humphries A, Nystrom A, Sattar S, Owens RT, McQuillan DJ, Ireton K, Iozzo RV (2009) Decorin is a novel antagonistic ligand of the Met receptor. J Cell Biol 185(4):743–754. https://doi.org/10.1083/jcb.200901129

Khan GA, Girish GV, Lala N, Di Guglielmo GM, Lala PK (2011) Decorin is a novel VEGFR-2-binding antagonist for the human extravillous trophoblast. Mol Endocrinol 25(8):1431–1443. https://doi.org/10.1210/me.2010-0426

Hausser H, Wedekind P, Sperber T, Peters R, Hasilik A, Kresse H (1996) Isolation and cellular localization of the decorin endocytosis receptor. Eur J Cell Biol 71(4):325–331

Nastase MV, Young MF, Schaefer L (2012) Biglycan: a multivalent proteoglycan providing structure and signals. J Histochem Cytochem 60(12):963–975. https://doi.org/10.1369/0022155412456380

Grindel B, Li Q, Arnold R, Petros J, Zayzafoon M, Muldoon M, Stave J, Chung LW, Farach-Carson MC (2016) Perlecan/HSPG2 and matrilysin/MMP-7 as indices of tissue invasion: tissue localization and circulating perlecan fragments in a cohort of 288 radical prostatectomy patients. Oncotarget 7(9):10433–10447. https://doi.org/10.18632/oncotarget.7197

Eble JA, Wucherpfennig KW, Gauthier L, Dersch P, Krukonis E, Isberg RR, Hemler ME (1998) Recombinant soluble human α3β1 integrin: purification, processing, regulation, and specific binding to laminin-5 and invasin in a mutually exclusive manner. Biochemistry 37(31):10945–10955. https://doi.org/10.1021/bi980175+

Kaasboll OJ, Gadicherla AK, Wang JH, Monsen VT, Hagelin EMV, Dong MQ, Attramadal H (2018) Connective tissue growth factor (CCN2) is a matricellular preproprotein controlled by proteolytic activation. J Biol Chem 293(46):17953–17970. https://doi.org/10.1074/jbc.RA118.004559

Su JL, Chiou J, Tang CH, Zhao M, Tsai CH, Chen PS, Chang YW, Chien MH, Peng CY, Hsiao M, Kuo ML, Yen ML (2010) CYR61 regulates BMP-2-dependent osteoblast differentiation through the αvβ3 integrin/integrin-linked kinase/ERK pathway. J Biol Chem 285(41):31325–31336. https://doi.org/10.1074/jbc.M109.087122

Crockett JC, Schutze N, Tosh D, Jatzke S, Duthie A, Jakob F, Rogers MJ (2007) The matricellular protein CYR61 inhibits osteoclastogenesis by a mechanism independent of αvβ3 and αvβ5. Endocrinology 148(12):5761–5768. https://doi.org/10.1210/en.2007-0473

Chen CC, Young JL, Monzon RI, Chen N, Todorovic V, Lau LF (2007) Cytotoxicity of TNFα is regulated by integrin-mediated matrix signaling. EMBO J 26(5):1257–1267. https://doi.org/10.1038/sj.emboj.7601596

Tsai HC, Chang AC, Tsai CH, Huang YL, Gan L, Chen CK, Liu SC, Huang TY, Fong YC, Tang CH (2019) CCN2 promotes drug resistance in osteosarcoma by enhancing ABCG2 expression. J Cell Physiol 234(6):9297–9307. https://doi.org/10.1002/jcp.27611

Babic AM, Chen CC, Lau LF (1999) Fisp12/mouse connective tissue growth factor mediates endothelial cell adhesion and migration through integrin αvβ3, promotes endothelial cell survival, and induces angiogenesis in vivo. Mol Cell Biol 19(4):2958–2966

Scherberich A, Tucker RP, Degen M, Brown-Luedi M, Andres AC, Chiquet-Ehrismann R (2005) Tenascin-W is found in malignant mammary tumors, promotes α8 integrin-dependent motility and requires p38MAPK activity for BMP-2 and TNF-α induced expression in vitro. Oncogene 24(9):1525–1532. https://doi.org/10.1038/sj.onc.1208342

Martina E, Degen M, Ruegg C, Merlo A, Lino MM, Chiquet-Ehrismann R, Brellier F (2010) Tenascin-W is a specific marker of glioma-associated blood vessels and stimulates angiogenesis in vitro. FASEB J 24(3):778–787. https://doi.org/10.1096/fj.09-140491

Gillan L, Matei D, Fishman DA, Gerbin CS, Karlan BY, Chang DD (2002) Periostin secreted by epithelial ovarian carcinoma is a ligand for αVβ3 and αVβ5 integrins and promotes cell motility. Cancer Res 62(18):5358–5364

Kakizaki Y, Makino N, Tozawa T, Honda T, Matsuda A, Ikeda Y, Ito M, Saito Y, Kimura W, Ueno Y (2016) Stromal fibrosis and expression of matricellular proteins correlate with histological grade of intraductal papillary mucinous neoplasm of the pancreas. Pancreas 45(8):1145–1152. https://doi.org/10.1097/MPA.0000000000000617

Thijssen VL, Rabinovich GA, Griffioen AW (2013) Vascular galectins: regulators of tumor progression and targets for cancer therapy. Cytokine Growth Factor Rev 24(6):547–558. https://doi.org/10.1016/j.cytogfr.2013.07.003

Mendez-Huergo SP, Blidner AG, Rabinovich GA (2017) Galectins: emerging regulatory checkpoints linking tumor immunity and angiogenesis. Curr Opin Immunol 45:8–15. https://doi.org/10.1016/j.coi.2016.12.003

Agnihotri R, Crawford HC, Haro H, Matrisian LM, Havrda MC, Liaw L (2001) Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin). J Biol Chem 276(30):28261–28267. https://doi.org/10.1074/jbc.M103608200

Takafuji V, Forgues M, Unsworth E, Goldsmith P, Wang XW (2007) An osteopontin fragment is essential for tumor cell invasion in hepatocellular carcinoma. Oncogene 26(44):6361–6371. https://doi.org/10.1038/sj.onc.1210463

Furger KA, Allan AL, Wilson SM, Hota C, Vantyghem SA, Postenka CO, Al-Katib W, Chambers AF, Tuck AB (2003) Β3 integrin expression increases breast carcinoma cell responsiveness to the malignancy-enhancing effects of osteopontin. Mol Cancer Res 1(11):810–819

Rangaswami H, Bulbule A, Kundu GC (2006) Osteopontin: role in cell signaling and cancer progression. Trends Cell Biol 16(2):79–87. https://doi.org/10.1016/j.tcb.2005.12.005

Teramoto H, Castellone MD, Malek RL, Letwin N, Frank B, Gutkind JS, Lee NH (2005) Autocrine activation of an osteopontin-CD44-Rac pathway enhances invasion and transformation by H-RasV12. Oncogene 24(3):489–501. https://doi.org/10.1038/sj.onc.1208209

Ye QH, Qin LX, Forgues M, He P, Kim JW, Peng AC, Simon R, Li Y, Robles AI, Chen Y, Ma ZC, Wu ZQ, Ye SL, Liu YK, Tang ZY, Wang XW (2003) Predicting hepatitis B virus-positive metastatic hepatocellular carcinomas using gene expression profiling and supervised machine learning. Nat Med 9(4):416–423. https://doi.org/10.1038/nm843