Matrix metalloproteinase interactions with collagen and elastin

Matrix Biology - Tập 44-46 - Trang 224-231 - 2015
Steven R. Van Doren1
1Department of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, USA

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Shoulders, 2009, Collagen structure and stability, Annu Rev Biochem, 78, 929, 10.1146/annurev.biochem.77.032207.120833

Wagenseil, 2007, New insights into elastic fiber assembly, Birth Defects Res C Embryo Today, 81, 229, 10.1002/bdrc.20111

Tamburro, 2005, The dissection of human tropoelastin: from the molecular structure to the self-assembly to the elasticity mechanism, Pathol Biol (Paris), 53, 383, 10.1016/j.patbio.2004.12.014

Houghton, 2011, Consequences of elastolysis, 217

Baldock, 2011, Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity, Proc Natl Acad Sci U S A, 108, 4322, 10.1073/pnas.1014280108

Yeo, 2012, Tropoelastin bridge region positions the cell-interactive C terminus and contributes to elastic fiber assembly, Proc Natl Acad Sci U S A, 109, 2878, 10.1073/pnas.1111615108

Antonicelli, 2007, Elastin-elastases and inflamm-aging, Curr Top Dev Biol, 79, 99, 10.1016/S0070-2153(06)79005-6

Fields, 2013, Interstitial collagen catabolism, J Biol Chem, 288, 8785, 10.1074/jbc.R113.451211

Filippov, 2003, Matrilysin-dependent elastolysis by human macrophages, J Exp Med, 198, 925, 10.1084/jem.20030626

Dean, 2008, Macrophage-specific metalloelastase (MMP-12) truncates and inactivates ELR+ CXC chemokines and generates CCL2, -7, -8, and -13 antagonists: potential role of the macrophage in terminating polymorphonuclear leukocyte influx, Blood, 112, 3455, 10.1182/blood-2007-12-129080

Marchant, 2014, A new transcriptional role for matrix metalloproteinase-12 in antiviral immunity, Nat Med, 20, 493, 10.1038/nm.3508

Bellac, 2014, Macrophage matrix metalloproteinase-12 dampens inflammation and neutrophil influx in arthritis, Cell Rep, 9, 618, 10.1016/j.celrep.2014.09.006

Aimes, 1995, Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments, J Biol Chem, 270, 5872, 10.1074/jbc.270.11.5872

Patterson, 2001, Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain, FEBS Lett, 503, 158, 10.1016/S0014-5793(01)02723-5

Konttinen, 1998, New collagenolytic enzymes/cascade identified at the pannus-hard tissue junction in rheumatoid arthritis: destruction from above, Matrix Biol, 17, 585, 10.1016/S0945-053X(98)90110-X

Bigg, 2007, Activity of matrix metalloproteinase-9 against native collagen types I and III, FEBS J, 274, 1246, 10.1111/j.1742-4658.2007.05669.x

Collier, 2011, Diffusion of MMPs on the surface of collagen fibrils: the mobile cell surface–collagen substratum interface, PLoS One, 6, e24029, 10.1371/journal.pone.0024029

Rosenblum, 2010, Direct visualization of protease action on collagen triple helical structure, PLoS One, 5, e11043, 10.1371/journal.pone.0011043

Atkinson, 2001, Membrane type 1 matrix metalloproteinase and gelatinase A synergistically degrade type 1 collagen in a cell model, FEBS Lett, 491, 222, 10.1016/S0014-5793(01)02204-9

Saffarian, 2004, Interstitial collagenase is a Brownian ratchet driven by proteolysis of collagen, Science, 306, 108, 10.1126/science.1099179

Perumal, 2008, Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis, Proc Natl Acad Sci U S A, 105, 2824, 10.1073/pnas.0710588105

Sarkar Susanta, 2012, Single-molecule tracking of collagenase on native type I collagen fibrils reveals degradation mechanism, Curr Biol, 22, 1047, 10.1016/j.cub.2012.04.012

Welgus, 1981, Human skin fibroblast collagenase. Assessment of activation energy and deuterium isotope effect with collagenous substrates, J Biol Chem, 256, 9516, 10.1016/S0021-9258(19)68793-4

Pilcher, 1997, The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix, J Cell Biol, 137, 1445, 10.1083/jcb.137.6.1445

Lin, 2008, Matrix metalloproteinase-8 facilitates neutrophil migration through the corneal stromal matrix by collagen degradation and production of the chemotactic peptide Pro–Gly–Pro, Am J Pathol, 173, 144, 10.2353/ajpath.2008.080081

Rosenblum, 2007, Insights into the structure and domain flexibility of full-length pro-matrix metalloproteinase-9/gelatinase B, Structure, 15, 1227, 10.1016/j.str.2007.07.019

Overall, 2007, Protease yoga: extreme flexibility of a matrix metalloproteinase, Structure, 15, 1159, 10.1016/j.str.2007.10.001

Sun, 2000, Atomic force microscopy-based detection of binding and cleavage site of matrix metalloproteinase on individual type II collagen helices, Anal Biochem, 283, 153, 10.1006/abio.2000.4629

Fields, 1991, A model for interstitial collagen catabolism by mammalian collagenases, J Theor Biol, 153, 585, 10.1016/S0022-5193(05)80157-2

Minond, 2006, The roles of substrate thermal stability and P2 and P1′ subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity, J Biol Chem, 281, 38302, 10.1074/jbc.M606004200

Minond, 2007, Differentiation of secreted and membrane-type matrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences, Biochemistry, 46, 3724, 10.1021/bi062199j

Lauer-Fields, 2009, Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity, J Biol Chem, 284, 24017, 10.1074/jbc.M109.016873

Robichaud, 2011, Exosite interactions impact matrix metalloproteinase collagen specificities, J Biol Chem, 286, 37535, 10.1074/jbc.M111.273391

Makareeva, 2008, Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta, J Biol Chem, 283, 4787, 10.1074/jbc.M705773200

Leikina, 2002, Type I collagen is thermally unstable at body temperature, Proc Natl Acad Sci U S A, 99, 1314, 10.1073/pnas.032307099

Arnold, 1998, Recombinant procollagen II: deletion of D period segments identifies sequences that are required for helix stabilization and generates a temperature-sensitive N-proteinase cleavage site, J Biol Chem, 273, 31822, 10.1074/jbc.273.48.31822

Bächinger, 1991, Sequence specific thermal stability of the collagen triple helix, Int J Biol Macromol, 13, 152, 10.1016/0141-8130(91)90040-2

Persikov, 2005, Prediction of collagen stability from amino acid sequence, J Biol Chem, 280, 19343, 10.1074/jbc.M501657200

Xiao, 2010, Local conformation and dynamics of isoleucine in the collagenase cleavage site provide a recognition signal for matrix metalloproteinases, J Biol Chem, 285, 34181, 10.1074/jbc.M110.128355

Stultz, 2002, Localized unfolding of collagen explains collagenase cleavage near imino-poor sites, J Mol Biol, 319, 997, 10.1016/S0022-2836(02)00421-7

Nerenberg, 2008, Differential unfolding of α1 and α2 chains in type I collagen and collagenolysis, J Mol Biol, 382, 246, 10.1016/j.jmb.2008.07.009

Salsas-Escat, 2010, Cleavage site specificity and conformational selection in type I collagen degradation, Biochemistry, 49, 4147, 10.1021/bi9021473

Bode, 1994, The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity, EMBO J, 13, 1263, 10.1002/j.1460-2075.1994.tb06378.x

Overall, 2002, Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites, Mol Biotechnol, 22, 51, 10.1385/MB:22:1:051

Chung, 2004, Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis, EMBO J, 23, 3020, 10.1038/sj.emboj.7600318

Han, 2010, Molecular mechanism of type I collagen homotrimer resistance to mammalian collagenases, J Biol Chem, 285, 22276, 10.1074/jbc.M110.102079

Bertini, 2012, Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis, J Am Chem Soc, 134, 2100, 10.1021/ja208338j

Arnold, 2011, The interface between catalytic and hemopexin domains in matrix metalloproteinase-1 conceals a collagen binding exosite, J Biol Chem, 286, 45073, 10.1074/jbc.M111.285213

Manka, 2012, Structural insights into triple-helical collagen cleavage by matrix metalloproteinase 1, Proc Natl Acad Sci U S A, 109, 12461, 10.1073/pnas.1204991109

Cerofolini, 2013, Examination of matrix metalloproteinase-1 in solution: a preference for the pre-collagenolysis state, J Biol Chem, 288, 30659, 10.1074/jbc.M113.477240

Bertini, 2009, Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1), J Biol Chem, 284, 12821, 10.1074/jbc.M809627200

Jozic, 2005, X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding, J Biol Chem, 280, 9578, 10.1074/jbc.M411084200

Bertini, 2006, Snapshots of the reaction mechanism of matrix metalloproteinases, Angew Chem Int Ed, 45, 7952, 10.1002/anie.200603100

Díaz, 2013, Unraveling the molecular structure of the catalytic domain of matrix metalloproteinase-2 in complex with a triple-helical peptide by means of molecular dynamics simulations, Biochemistry, 52, 8556, 10.1021/bi401144p

Maskos, 2005, Crystal structures of MMPs in complex with physiological and pharmacological inhibitors, Biochimie, 87, 249, 10.1016/j.biochi.2004.11.019

Chung, 2000, Identification of the (183)RWTNNFREY(191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity, J Biol Chem, 275, 29610, 10.1074/jbc.M004039200

Pelman, 2005, Pivotal molecular determinants of peptidic and collagen triple helicase activities reside in the S3′ subsite of matrix metalloproteinase 8 (MMP-8): the role of hydrogen bonding potential of ASN188 and TYR189 and the connecting cis bond, J Biol Chem, 280, 2370, 10.1074/jbc.M409603200

Palmier, 2010, NMR and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices, J Biol Chem, 285, 30918, 10.1074/jbc.M110.136903

Bode, 1995, A helping hand for collagenases: the haemopexin-like domain, Structure, 3, 527, 10.1016/S0969-2126(01)00185-X

Zhao, 2015, Transient collagen triple helix binding to a key metalloproteinase in invasion and development, Structure, 23, 257, 10.1016/j.str.2014.11.021

Tam, 2004, J Biol Chem, 279, 43336, 10.1074/jbc.M407186200

Xu, 2009, Nuclear magnetic resonance mapping and functional confirmation of the collagen binding sites of matrix metalloproteinase-2, Biochemistry, 48, 5822, 10.1021/bi900513h

Gioia, 2009, The collagen binding domain of gelatinase A modulates degradation of collagen IV by gelatinase B, J Mol Biol, 386, 419, 10.1016/j.jmb.2008.12.021

O'Farrell, 1998, The fibronectin-like domain is required for the type V and XI collagenolytic activity of gelatinase B, Arch Biochem Biophys, 354, 24, 10.1006/abbi.1998.0662

O'Farrell, 2000, Identification of structural elements important for matrix metalloproteinase type V collagenolytic activity as revealed by chimeric enzymes. Role of fibronectin-like domain and active site of gelatinase B, J Biol Chem, 275, 27964, 10.1074/jbc.M003936200

Morgunova, 1999, Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed, Science, 284, 1667, 10.1126/science.284.5420.1667

Briknarova, 1999, The second type II module from human matrix metalloproteinase 2: structure, function and dynamics, Structure, 7, 1235, 10.1016/S0969-2126(00)80057-X

Xu, 2004, Contributions of the MMP-2 collagen binding domain to gelatin cleavage. Substrate binding via the collagen binding domain is required for hydrolysis of gelatin but not short peptides, Matrix Biol, 23, 171, 10.1016/j.matbio.2004.05.002

Van Doren, 2011, Structural basis of extracellular matrix interactions with matrix metalloproteinases, 123

Gehrmann, 2002, The col-1 module of human matrix metalloproteinase-2 (MMP-2): structural/functional relatedness between gelatin-binding fibronectin type II modules and lysine-binding kringle domains, Biol Chem, 383, 137, 10.1515/BC.2002.014

Azhagiya Singam, 2014, Molecular dynamics simulation study on the interaction of collagen-like peptides with gelatinase-A (MMP-2), Biopolymers, 101, 779, 10.1002/bip.22457

Shipley, 1996, The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases. Role of the fibronectin type II-like repeats, J Biol Chem, 271, 4335, 10.1074/jbc.271.8.4335

Curci, 1998, Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms, J Clin Invest, 102, 1900, 10.1172/JCI2182

Taddese, 2008, Mapping of macrophage elastase cleavage sites in insoluble human skin elastin, Matrix Biol, 27, 420, 10.1016/j.matbio.2008.02.001

Bertini, 2009, Characterisation of the MMP-12-elastin adduct, Chem Eur J, 15, 7842, 10.1002/chem.200901009

Fulcher, 2011, Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation, Biochemistry, 50, 9488, 10.1021/bi2009807

Bhaskaran, 2007, Solution structure of inhibitor-free human metalloelastase (MMP-12) indicates an internal conformational adjustment, J Mol Biol, 374, 1333, 10.1016/j.jmb.2007.10.028

Stura, 2013, Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain, FASEB J, 27, 4395, 10.1096/fj.13-233601