Matrix metalloproteinases

Current Opinion in Chemical Biology

Volumn 2, Issue 4, 1998, Pages 466-471

  Johnson, Linda L ^a   Dyer, Richard ^a   Hupe, Donald J ^a  

^a PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGENASE; GELATINASE; MATRIX METALLOPROTEINASE; METALLOPROTEINASE; PROTEINASE INHIBITOR; STROMELYSIN;

ANIMAL; CLINICAL TRIAL; DRUG ANTAGONISM; ENZYME ACTIVATION; HUMAN; METABOLISM; MOUSE; REVIEW; TRANSGENIC MOUSE;

ANIMALS; CLINICAL TRIALS; COLLAGENASES; ENZYME ACTIVATION; GELATINASES; HUMANS; MATRIX METALLOPROTEINASE 3; MATRIX METALLOPROTEINASES, MEMBRANE-ASSOCIATED; METALLOENDOPEPTIDASES; MICE; MICE, TRANSGENIC; PROTEASE INHIBITORS;

EID: 0032134538     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(98)80122-1     Document Type: Article

References (51)

1. Stetler-Stevenson W: Dynamics of matrix turnover during pathologic remodeling of the extracellular matrix. Am J Pathol 1996, 148:1345-1350.
2. Cawston T: Metalloproteinase inhibitors and the prevention of connective tissue breakdown. Pharmocol Ther 1996, 70:163-182.
3. Chandler S, Miller K, Clements J, Lury J, Corkill D, Anthony D, Adams S, Gearing A: Matrix metalloproteinases, tumor necrosis factor and multiple sclerosis: an overview. J Neuroimmunol 1997, 72:155-161.
4. Reynolds J, Meikle M: The functional balance of metalloproteinases and inhibitors in tissue degradation: relevance to oral pathologies. J R Coll Surg Edinb 1997, 42:154-160.
5. Dollery C, McEwan J, Henney A: Matrix metalloproteinases and cardiovascular disease. Circ Res 1995, 77:863-868.
6. White A, Bocan T, Boxer P, Peterson J, Schrier D: Emerging therapeutic advances for the development of second generation matrix metalloproteinas inhibitors. Curr Pharm Des 1997, 3:45-58.
7. Nagase H: Matrix metalloproteinases. In Zinc Metalloproteinases in Health and Disease. Edited by Hooper NM. London: Taylor and Francis; 1996:153-204.
8. Nagase H: Activation mechanisms of matrix metallopro teinases. Biol Chem 1997, 378:151-160. This review describes current understanding of the regulation of expression, natural inhibition and activation of this family of enzymes, emphasizing the importance of membrane-type matrix metalloproteinases for their localized activation at the surface of migrating cells.
9. Sato H, Okada Y, Seiki M: Membrane-type matrix metalloproteinases (MT-MMPs) in cell invasion. Thromb Haemost 1997, 78:497-500.
10. Pei D, Weiss S: Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J Biol Chem 1996, 271:9135-9140.
11. Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, Seiki M: A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 1994, 370:61-65.
12. Knauper V, Will H, Lopez-Otin C, Smith B, Atkinson S, Stanton H, Hembry R, Murphy G: Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase A (MMP-2) are able to generate active enzyme. J Biol Chem 1996, 271:17124-17131.
13. Strongin A, Collier I, Bannikov G, Marmer B, Grant G, Goldberg G: Mechanism of cell surface activation of 72-kDa type IV collagenase. J Biol Chem 1995, 270:5331-5338.
14. Zucker S, Drews M, Conner C, Foda H, DeClerck Y, Langley K, Bahou W, Docherty A, Cao J: Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type-1 matrix metalloproteinase 1 (MT1-MMP). J Biol Chem 1998, 273:1216-1222. Defining the interactions involved between membrane-type matrix metalloproteinases (MT-MMP), gelatinase A and tissue inhibitor of metalloproteinase (TIMP) in the formation of an activation complex at the cell membrane will be crucial to understanding the dynamics of cellular migration. At high concentrations, TIMP-2, a natural inhibitor of matrix metalloproteinases, blocks the activation of gelatinase A, but stoichiometric amounts seem to be required for formation of the activation complex. This article investigates the interactions of TIMP-2 and MT1 MMP.
15. Brooks P, Stromblad S, Sanders L, von Schalscha T, Aimes R, Stetler-Stevenson W, Quigley J, Cheresh D: Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin αv β3. Cell 1996, 85:683-693.
16. Nakahara H, Howard L, Thompson EW, Sato H, Seiki M, Yeh Y, Chen WT: Transmembrane/cytoplasmic domain-mediated membrane type 1 -matrix metalloprotease docking to invadopodia is required for cell invasion. Proc Acad Acad Sci USA 1997, 94:7959-7964. It's not enough to localize the gelatinase A activation complex to the cell surface of migrating cells, but active enzyme apparently must be concentrated on the invadopodia. The authors used recombinant chimeric proteins to show that the cytoplasmic domain of membrane type-1 matrix metalloproteinase is crucial for this directional localization.
17. Sato T, del Carmen Ovejero M, Hou P, Heegaard A-M, Kumegawa M, Foged N, Delaisse J-M: Identification of the membrane-type matrix metalloproteinase MT1-MMP in osteoclasts. J Cell Sci 1997, 110:589-596.
18. Ohuchi E, Imai K, Fujii Y, Sato H, Seiki M, Okada Y: Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J Biol Chem 1997, 272:2446-2451.
19. Wilson C, Heppner K, Labosky P, Hogan B, Matrisian L: ntestinal tumorigenesis is suppressed in mice lacking the metalloproteinase matrilysin. Proc Natl Acad Sci USA 1997, 94:1402-1407. Transgenic models will be pivotal for demonstrating that a specific matrix metalloproteinase(s) is involved in a given disease and will support the development of enzyme-selective inhibitors for clinical use. In this matrilysin knockout model, it is apparent that matrix metalloproteinases are involved not only in the later stages of cancer invasion and metastasis, but also in the very early stages of tumor formation.
20. Hautamaki R, Kobayashi D, Senior R, Shapiro S: Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice. Science 1997, 277:2002-2004. This transgenic model showed that the knockout of a single enzyme, macrophage elastase, was sufficient to prevent emphysema in this animal model, indicating that a selective inhibitor could provide effective treatment for this debilitating disease.
21. Mudgett J, Hutchinson N, Chartrain N, Forsyth A, McDonnell J, Singer I, Bayne E, Flanagan J, Kawka D, Shen C et al.: Susceptibility of stromelysin 1 -deficient mice to collageninduced arthritis and cartilage destruction. Arthritis Rheum 1998, 41:110-121.
22. Trapp B, Peterson J, Ransohoff R, Rudick R, Mork S, Bo L: Axonal transection in the lesions of multiple sclerosis. N Engl J Med 1998, 338:278-285. Permanent axonal damage may be an underlying cause of the progressive deterioration seen in more than 50% of patients with multiple sclerosis. Although this article does not specifically describe matrix metalloproteinase (MMP) activity, it identifies axonal transection within areas of demyelination in human brain tissue. Demyelination has been associated with MMP activity, and it is possible that the actual axonal damage may be attributed at least in part to these proteases. MMP inhibition could provide therapeutic intervention in the progression of multiple sclerosis.
23. Clements J, Cossins J, Wells G, Corkill D, Helfrich K, Wood L, Pigott R, Stabler G, Ward G, Gearing A, Miller K: Matrix metalloproteinase expression during experimental autoimmune encephalomyelitis and effects of a combined matrix metalloproteinase and tumour necrosis factor-α inhibitor. J Neuroimmunol 1997, 74:85-94.
24. Gijbels K, Galardy R, Steinman L: Reversal of experimental autoimmune encephalomyelitis with a hydroxamate inhibitor of matrix metalloproteases. J Clin Invest 1994, 94:2177-2182.
25. Hewson A, Smith T, Leonard J, Cuzner M: Suppression of experimental allergic encephalomyelitis in the Lewis rat by the matrix metalloproteinase inhibitor Ro31-9790. Inflamm Res 1995, 44:345-349.
26. Yong V, Krekoski C, Forsyth P, Bell R, Edwards D: Matrix metalloproteinases and diseases of the CNS. Trends Neurosci 1998, 21:75-80.
27. Thompson R, Parks W: Role of matrix metalloproteinases in abdominal aortic aneurysms. Ann NY Acad Sci 1996, 800:157-174.
28. Freestone T, Turner R, Higman D, Lever M, Powell J: Influence of hypercholesterolemia and adventitial inflammation on the development of aortic aneurysm in rabbits. Arterioscler Thromb Vasc Biol 1997, 17:10-17.
29. Halpert I, Sires U, Roby J, Potter-Perigo S, Wight T, Shapiro S, Welgus H, Wickline S, Parks W: Matrilysin is expressed by lipid-laden macrophages at sites of potential rupture in atherosclerotic lesions and localizes to areas of versican deposition, a proteoglycan substrate for the enzyme. Proc Natl Acad Sci USA 1996, 93:9748-9753.
30. Lee E, Vaughan D, Parikh S, Grodzinsky A, Libby P, Lark M, Lee R: Regulation of matrix metalloproteinases and plasminogen activator inhibitor-1 synthesis by plasminogen in cultured human vascular smooth muscle cells. Circ Res 1996, 78:44-49.
31. Schonbeck U, Mach F, Sukhova G, Murphy C, Bonnefoy J, Fabunmi R, Libby P: Regulation of matrix metalloproteinase expression in human vascular smooth muscle cells by T lymphocytes: a role for CD40 signaling in plaque rupture? Circ Res 1997, 81:448-454. This article further elucidates the molecular interactions in the development of plaques and the potential involvement of matrix metalloproteinases in the initiation of plaque rupture.
32. Tyagi S: Proteinases and myocardial extracellular matrix turnover. Mol Cell Biochem 1997, 168:1-12.
33. Gilbert S, Wotton P, Tarlton J, Duance V, Bailey A: Increased expression of promatrix metalloproteinase-9 and neutrophil elastase in canine dilated cardiomyopathy. Cardiovasc Res 1997, 34:377-383.
34. Spinale F, Coker M, Thomas C, Walker J, Mukherjee R, Hebbar L: Time-dependent changes in matrix metalloproteinase activity and expression during the progression of congestive heart failure. Circ Res 1998, 82:482-495.
35. Spinale FG, Krombach RS, Coker ML, Mukherjee R, Houck WV, Clair MJ, Kribbs SB, Hebbar L, Peterson JT: Matrix metalloproteinase inhibition with congestive heart failure improves left ventricular geometry and pump function. Circulation 1997, 96(suppl 8):1520.
36. Peterson J, Rosebury W, Robertson A, Washington R, Li H, O'Brien P, Sliscovic D, Hallak H, Uprichard A: Matrix metalloproteinase inhibition blocks progression of heart failure. Circulation 1997, 96(suppl 8):1520.
37. Sato T, Foged N, Delaisse J-M: The migration of purified osteoclasts through collagen is inhibited by matrix metalloproteinase inhibitors. J Bone Miner Res 1998, 13:59-66.
38. Holliday L, Welgus H, Fliszar C, Veith G, Jeffrey J, Gluck S: Initiation of osteoclast bone resorption by interstitial collagenase. J Biol Chem 1997, 272:22053-22058.
39. Irwin J, Kirk D, Gwatkin R, Navre M, Cannon P, Giudice L: Human endometrial matrix metalloproteinase-2, a putative menstrual proteinase. J Clin Invest 1996, 97:438-447.
40. Pender S, Tickle S, Docherty A, Howie D, Wathen N, MacDonald T: A major role for matrix metalloproteinases in T cell injury in the gut. J Immunol 1997, 158:1582-1590.
41. Levy D, Lapierre F, Liang W, Ye W, Lange C, Li X, Grobelny D, Casabonne M, Tyrrell D, Holme K et al.: Matrix metalloproteinase inhibitors: a structure activity study. J Med Chem 1998, 41:199-223.
42. Gomis-Ruth F, Maskos K, Betz M, Bergner A, Huber R, Suzuki K, Yoshida N, Nagase H, Brew K, Bourenkov G et al.: Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature 1997, 389:77-81. This is the first published structure of a matrix metalloproteinase complexed with its natural inhibitor, tissue inhibitor of metalloproteinase-1. The intermolecular interactions will aid in the understanding of the formation of natural activation and inhibition complexes which serve to regulate the activity of these enzymes in vivo.
43. Dhanaraj V, Ye Q-Z, Johnson L, Hupe D, Ortwine D, Dunbar J Jr, Rubin J, Pavlovsky A, Humblet C, Blundell T: X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily. Structure 1996, 4:375-386.
44. Ye Q-Z, Hupe D, Johnson L: Catalytic domains of matrix metalloproteinases: a molecular biology approach to drug discovery. Curr Med Chem 1996, 3:407-418.
45. Browner M, Smith W, Castelhano A: Crystal structures of matrilysin-inhibitor complexes: common themes among metalloproteinases. Biochemistry 1995, 34:6602-6610.
46. Beckett R, Whittaker M: Matrix metalloproteinase inhibitors 1998. Exp Opin Ther Patents 1998, 8:259-282. This article summarizes the developments of synthetic matrix metallopro-teinase inhibitors from the past year. The overall similarity of these enzymes and the overlap of substrate specificity has resulted in a very crowded patent field that may be approaching maturity.
47. Levy D, Ezrin A: Matrix metalloproteinase inhibitor drugs. Emerg Drugs 1997, 2:205-230. This article provides an analysis of the current clinical development of matrix metalloproteinase inhibitors and their potential as therapeutic agents in a variety of diseases.
48. Shuker S, Hajduk P, Meadows R, Fesik S: Discovering high affinity ligands for proteins: SAR by NMR. Science 1996, 274:1531-1534.
49. Hodgson J: Remodeling MMPIs. Biotechnology 1995, 13:554-557.
50. Rasmussen H, McCann P: Matrix metalloproteinase inhibition as a novel anticancer strategy: a review with special focus on batimastat and marimastat. Pharmacol Ther 1997, 75:69-75.
51. Millar A, Brown P: 360 patient meta-analysis of studies of marimastat. A novel matrix metalloproteinase inhibitor. Ann Oncol 1996, 7(suppl 5):123.