Tissue Inhibitors of Metalloproteinases in Cell Signaling: Metalloproteinase-Independent Biological Activities

Science Signaling - Tập 1 Số 27 - 2008
William G. Stetler‐Stevenson1
1Chief, Extracellular Matrix Pathology Section, Cell and Cancer Biology Branch, Vascular Biology Faculty, Center for Cancer Research, National Cancer Institute (NCI), NIH, Advanced Technology Center, 8717 Grovemont Circle, Room 115, Bethesda, MD 20892–4605, USA.

Tóm tắt

Over the past 20 years, the tissue inhibitors of metalloproteinases (TIMPs) have been implicated in direct regulation of cell growth and apoptosis. However, the mechanisms of these effects have been controversial. Recent work by several laboratories has identified specific signaling pathways and cell surface binding partners for members of the TIMP family. TIMP-2 binding to the integrin α 3 β 1 is the first description of a cell surface receptor for a TIMP family member. TIMP-2 has been shown to induce gene expression, to promote G 1 cell cycle arrest, and to inhibit cell migration. TIMP-1 binding to CD63 inhibits cell growth and apoptosis. These new findings suggest that TIMPs are multifunctional and can act either directly through cell surface receptors or indirectly through modulation of protease activity to direct cell fate. The emerging concept is that TIMPs function in a contextual fashion so that the mechanism of action depends on the tissue microenvironment.

Từ khóa


Tài liệu tham khảo

10.1126/science.2465572

10.1093/jnci/83.11.775

10.1093/jnci/82.7.589

Y. A. DeClerck, N. Perez, H. Shimada, T. C. Boone, K. E. Langley, S. M. Taylor, Inhibition of invasion and metastasis in cells transfected with an inhibitor of metalloproteinases. Cancer Res. 52, 701–708 (1992).1732058

A. M. Montgomery, B. M. Mueller, R. A. Reisfeld, S. M. Taylor, Y. A. DeClerck, Effect of tissue inhibitor of the matrix metalloproteinases-2 expression on the growth and spontaneous metastasis of a human melanoma cell line. Cancer Res. 54, 5467–5473 (1994).7923181

P. D. Brown, Matrix metalloproteinase inhibitors. Angiogenesis 1, 142–154 (1998).14517381

10.1126/science.1067100

10.1038/nrc745

10.1016/j.critrevonc.2003.09.008

10.1002/jnr.10836

10.1016/S0167-4838(99)00279-4

10.1002/neu.20205

10.1007/s00427-003-0333-9

10.1016/S0012-1606(03)00318-X

10.1172/JCI200113171

10.1078/0171-9335-00072

10.1006/jmbi.1998.2223

10.1242/jcs.00063

10.1016/S0014-5793(98)01031-X

10.1172/JCI6870

10.1074/jbc.M000907200

10.1016/jbiocel.2007.12.006

10.1016/S0014-5793(04)00281-9

10.1091/mbc.8.8.1513

10.1172/JCI4586

10.1016/0888-7543(92)90286-2

10.1038/990031

10.1006/geno.1999.5776

10.1098/rstb.1999.0378

10.1074/jbc.275.42.32664

10.1152/physiolgenomics.00160.2006

10.1074/jbc.M001271200

10.1074/jbc.M001270200

10.1158/0008-5472.CAN-07-0232

10.1002/hep.20618

10.1083/jcb.146.4.881

10.1038/318066a0

J. C. Gasson, N. Bersch, D. W. Golde, Characterization of purified human erythroid-potentiating activity. Prog. Clin. Biol. Res. 184, 95–104 (1985).3931094

10.1016/0014-5793(92)80386-U

10.1111/j.1365-3083.2005.01585.x

Z. Pasieka, H. Stepien, W. Czyz, L. Pomorski, K. Kuzdak, Concentration of metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 in the serum of patients with benign and malignant thyroid tumours treated surgically. Endocr. Regul. 38, 57–63 (2004).15497929

10.1111/1523-1747.ep12483956

10.1074/jbc.270.22.13453

10.1242/jcs.107.9.2373

10.1016/0014-5793(92)80015-9

10.1006/excr.1993.1204

10.1006/excr.1996.0117

10.1182/blood.V86.12.4506.bloodjournal86124506

10.1016/0014-5793(95)00345-A

10.1016/0014-5793(96)01066-6

10.1016/S0006-291X(02)00741-6

10.1073/pnas.89.22.10676

10.1172/JCI2881

10.1182/blood.V97.6.1796

10.1016/S0002-9440(10)64070-9

G. Li, R. Fridman, H. R. Kim, Tissue inhibitor of metalloproteinase-1 inhibits apoptosis of human breast epithelial cells. Cancer Res. 59, 6267–6275 (1999).10626822

10.1074/jbc.M302999200

X. W. Liu, M. E. Taube, K. K. Jung, Z. Dong, Y. J. Lee, S. Roshy, B. F. Sloane, R. Fridman, H. R. Kim, Tissue inhibitor of metalloproteinase-1 protects human breast epithelial cells from extrinsic cell death: A potential oncogenic activity of tissue inhibitor of metalloproteinase-1. Cancer Res. 65, 898–906 (2005).15705888

10.2337/diabetes.50.5.1047

10.1152/ajpheart.00431.2007

10.1002/(SICI)1097-0215(19980119)75:2<246::AID-IJC13>3.0.CO;2-B

10.1111/j.1749-6632.1999.tb07715.x

10.1172/JCI1584

10.1038/sj.onc.1206292

10.1038/sj.bjc.6690217

10.1038/ng1413

10.1093/carcin/17.9.1805

10.1006/cyto.1997.0233

Y. Jiang, M. Wang, M. Y. Celiker, Y. E. Liu, Q. X. Sang, I. D. Goldberg, Y. E. Shi, Stimulation of mammary tumorigenesis by systemic tissue inhibitor of matrix metalloproteinase 4 gene delivery. Cancer Res. 61, 2365–2370 (2001).11289097

10.1006/dbio.1999.9313

10.1038/sj.onc.1209336

10.1126/science.1694043

10.1002/jcp.1041570219

K. H. Kang S. Y. Park S. B. Rho J. H. Lee Tissue inhibitor of metalloproteinases-3 interacts with angiogtensin II type receptor and additively inhibits angiogensis. Cardiovasc. Res. published online in press.

10.1038/nm846

10.1038/sj.onc.1204508

10.1074/jbc.274.30.21362

10.1074/jbc.M008157200

10.1074/jbc.273.38.24360

10.1042/bj20030557

10.1074/jbc.M306176200

10.1016/S0092-8674(03)00551-8

10.1074/jbc.M509932200

10.1158/0008-5472.CAN-04-1981

10.1038/nn1922

10.1038/sj.onc.1209444

10.1074/jbc.M705492200

10.1242/jcs.111.9.1147

10.1038/sj.emboj.7601281

10.1083/jcb.146.2.477

10.1007/s10555-006-7893-x

B. Anand-Apte, M. S. Pepper, E. Voest, R. Montesano, B. Olsen, G. Murphy, S. S. Apte, B. Zetter, Inhibition of angiogenesis by tissue inhibitor of metalloproteinase-3. Invest. Ophthalmol. Vis. Sci. 38, 817–823 (1997).9112976

10.1038/sj.onc.1208599

10.1038/sj.bjc.6603307

10.1038/sj.onc.1210329

10.1002/ijc.11652

E. Vairaktaris, C. Yapijakis, A. Yiannopoulos, S. Vassiliou, Z. Serefoglou, A. Vylliotis, E. Nkenke, S. Derka, E. Critselis, D. Avgoustidis, F. W. Neukam, E. Patsouris, Strong association of the tissue inhibitor of metalloproteinase-2 polymorphism with an increased risk of oral squamous cell carcinoma in Europeans. Oncol. Rep. 17, 963–968 (2007).17342343

10.1016/j.ejso.2007.09.003

10.1007/s10555-007-9105-8

10.1016/j.molmed.2005.01.007

10.1523/JNEUROSCI.5066-04.2005

10.1111/j.1471-4159.2006.03855.x

10.1016/j.ejca.2003.09.019

10.1016/j.ejca.2004.06.011

10.1002/(SICI)1097-0215(19990219)84:1<44::AID-IJC9>3.0.CO;2-P

10.1002/path.1129

10.1074/mcp.M300019-MCP200

Thông tin
Thông tin xuất bản

Science Signaling

Tập 1 Số 27

Thông tin tác giả