Relating matrix metalloproteinase structure to function: Why the 'Hemopexin' domain?

Matrix Biology

Volumn 15, Issue 8-9, 1997, Pages 511-518

  Murphy, Gillian ^a,b   Knäuper, Vera ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF EAST ANGLIA   (United Kingdom)

Author keywords

Matrix metalloproteinases; Tissue inhibitor of metalloproteinases

Indexed keywords

HEMOPEXIN; MATRIX METALLOPROTEINASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL ACTIVITY; GENETIC CONSERVATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION;

EID: 0343812072     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(97)90025-1     Document Type: Short Survey

References (56)

1. Adams J.C., Wattt F.M. Regulation of development and differentiation by the extracellular matrix. Development. 117:1993;1183-1198.
2. Allan J.A., Hembry R.M., Angal S., Reynolds J.J., Murphy G. Binding of latent high Mr active forms of stromelysin to collagen is mediated by the C-terminal domain. J. Cell Sci. 99:1991;789-795.
3. Atkinson S.J., Crabhe T., Cowell S., Ward R.V., Butler M.J., Sato H., Seiki M., Reynolds J.J., Murphy G. Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes. J. Biol. Chem. 270:1995;30479-30485.
4. Banyai I., Tordai H., Patthy L. The gelatin-binding site of human 72 kDa type IV collagenase (gelatinase A). Biochem. J. 298:1994;403-407.
5. Basbaum C.B., Werb Z. Focalised proteolysis: spatial and temporal regulation of extracellular matrix degradation at the cell surface. Curr. Opin. Cell Biol. 8:1996;731-738.
6. Becker J.W., Marcy A.I., Rokosz L.L., Axel M.G., Burbaum J.J., Fitzgerald P.M.D., Cameron P.M., Esser C.K., Hagmann W.K., Hermes J.D., Springer J.D. Storemelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Protein. Sci. 4:1995;1966-1976.
7. Beckett R.P., Davidson A.H., Drummond A.H., Huxley P., Whittaker M. Recent advances in matrix metalloproteinase inhibitor research. Drug Discov. Today. 1:1995;16-26.
8. Benbow, U. and Brinckerhoff, C.E.: The AP-1 site and MMP gene regulation. Matrix Biology 15, this issue.
9. Birkedal-Hansen H., Moore W.G.I., Bodden M.K., Windsor L.J., Birkedal-Hansen B., DeCarlo A., Engler J.A. Matrix metalloproteinases: a review. Crit. Rev. Oral Biol. Med. 4:1993;197-250.
10. Bode W. A helping hand for collagenases: The hemopexin-like domain. Structure. 3:1995;527-530.
11. Bode W., Gomist-Ruth F.-X., Stockler W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXIIXXGXXH and Metturn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett. 331:1993;134-140.
12. Bode W., Reinemer P., Huber R., Kleine T., Schnierer S., Tschesche H. The X-ray crystal structure of the catalytic domain of human neutrophil collgenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. EMBO J. 13:1994;1263-1269.
13. Brown P.D., Kleiner D.E., Unsworth E.J., Stetler-Stevenson W.G. Cellular activation of the 72 kDa type IV procollagenase/TIMP-2 complex. Kidney Inst. 43:1993;163-170.
14. Browner M.E., Smith W.W., Castelhano A.L. Matrilysin-inhibitor complexes: Common themes among metalloproteases. Biochemistry. 34:1995;6602-6610.
15. Clark I.M., Cawston T.E. Fragments of human fibroblast collagenase. Biochem. J. 263:1989;201-206.
16. Collier, I.E., Wilhelm, S.M., Eisen, A.Z., Marmer, B.L., Grant, G.A., Seltzer, J.L., Kronberger, A., He, C., Bauer E.A. and Goldberg, G.I., H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen., J. Biol. Chem., 263.,6579-6587.
17. Coller I.E., Krasnov P.A., Strongin A.Y., Birkedal-Hansen H., Goldberg G.I. Alanine scanning mutagenesis and functional analysis of the fibronectin-like collagen-binding domain from human 92 kDa type IV collagenase. J. Biol. Chem. 267:1992;6776-6781.
18. Crabbe T., Ioannou C., Docherty A.J.P. Human progelatinase A can be activated by autolysis at a rate that is concentration-dependent and enhanced by heparin bound to the C-terminal domain. Eur. J. Biochem. 218:1993;431-438.
19. Fridman R., Fuerst R.R., Bird R.E., Hoyhtya M., Oelkuct M., Kraus S., Komarck D., Liotta L.A., Berman M.L, Stetler-Stevenson W.G. Domain structure of human 72-kDa gelatinase/type IV collagenase. Characterisation of proteolytic activity and identification of the tissue inhibitor or metalloproteinases-2 (TIMP-2) binding regions. J. Biol. Chem. 267:1992;15398-15405.
20. Gohlke U., Gomis-Rüth F.X., Crabbe T., Murphy G., Docherty A.J.P., Bode W. The C-terminal (hemopexin-like) domain structure of human gelatinase A (MMP-2): Structural implications for its function. FEBS Lett. 378:1996;126-130.
21. Goldberg G.L., Strongin A., Collier I.E., Genrich L.T., Marmer B.L. Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerisation,complex formation with interstitial collagenase and activation of the proenzyme with stromelysin. J. Biol. Chem. 267:1992;4583-4591.
22. Gomis-Rüth F.-X., Gohlke U., Betz M., Knäuper V., Murphy G., López-Otin C., Bode W. The helping hand of collagenase-3 (MMP-13): 2.7 (crystal structure of its C-terminal hemopexin-like domain. J. Mol. Biol. 264:1996;556-566.
23. Guidry C., Miller E.S., Hook M. A second fibronectin-binding region is present in collage (-chains. J. Biol. Chem. 265:1990;19230-19236.
24. Hirose T., Patterson C., Pourmotabbed T., Mainardi C.L., Hasty K.A. Structure-function relationship of human neutrophil collagenase: identification of regions responsible for substrate specificity and general proteinase activity. Proc. Natl. Acad. Sci. USA. 90:1993;2569-2573.
25. Howard E.W., Banda M.J. Binding of tissue inhibitor of metalloproteinases-2 to two distinct sites on human 72-kDa gelatinase. J. Biol. Chem. 266:1991;17972-17977.
26. Imai K., Ohuchi E., Aoki T., Nomura H., Fuji Y., Sato H., Seiki M., Okada Y. Membrane-type matrix metalloproteinase 1 is a gelatinolytic enzyme and is secreted in a complex with tissue inhibitor of metalloproteinases 2. Cancer Res. 56:1996;2707-2710.
27. Knäuper V., Osthues A., DeClerck Y.A., Langley K.E., Bläser J., Tschesche H. Fragmentation of human polymorphonuclear-leucocyte collagenase. Biochem. J. 291:1993;847-854.
28. Knäuper V., Will H., López-Otin C., Smith B., Atkinson S.J., Stanton H., Hembry R.m., 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. 271:1996;17124-17131.
29. Knäuper V., Cowell S., Smith B., López-Otin C., O'Shea M., Morris H., Zardi L., Murphy G. The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity and tissue of inhibitor of metalloproteinase (TIMP) interaction. J. Biol. Chem. 1997;. in press.
30. Li J., Brick P., O'Hare m.C., Skarzynski T., Lloyd L.F., Curry V.A., Clark I.M., Bigg H.E., Hazleman B.L., Cawston T.E., Blow D.M. Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed properller. Structure. 3:1995;541-549.
31. Libson A.M., Gittis A.G., Collier I.E., Marmer B.L., Gouldberg G.I., Lattman E.E. Crystal structure of the hemopexin-like C-terminal domain of gelatinase A. Nature Struct. Biol. 2:1995;938-942.
32. Lovejoy B., Cleasby A., Hassell A.M., Longley K., Luther M.A., Weigl D., McGeehan G., McElroy A.B., Drewry D., Lambert M.H., Jordan S.R. Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor. Science. 263:1994;375-377.
33. Murphy G., Willenbrock E. Tissue inhibitors of matrix metalloendopeptideases. Methods Enzymol. 248:1995;496-510.
34. Murphy G., Allan J.A., Willenbrock E., Cockett M.L., O'Connell J.P., Docherty A.J.P. The role of the C-terminal domain in collagenase and stromelysin specificity. J. Biol. Chem. 267:1992;9612-9618.
35. Nguyen Q., Willenbrock E., Cockett M.I., O'Shea M., Docherty A.J.P., Murphy G. Different domain interactions are involved in the binding of tissue inhibitors of metalloproteinases to stromelysin-1 and gelatinase A. Biochemistry. 33:1994;2089-2095.
36. O'Connell J.P., Willenbrock F., Docherty A.J.P., Eaton D., Murphy G. Analysis of the role of the COOH-terminal domain in the activation, proteolytic activity, and tissue inhibitor of metalloproteinase interactions of gelatinase B. J. Biol. Chem. 269:1994;14967-14973.
37. Ohuchi E., Imai K., Fuji Y., Sato H., Seiki M., Okada Y. Membrane-type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 212:1997;2446-2451.
38. Overall C.M., Sodek J. Concanavalin A produces a matrix degradative phenotype in human fibroblasts. Induction and endogenous activation of collagenase, 72-kDa gelatinase, and Pump-1 is accompanied by the suppression of the tissue inhibitor of matrix metalloproteinase. J. Biol. Chem. 265:1990;21141-21151.
39. Pei D., Weiss S.J. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature. 375:1995;244-247.
40. Pei D., Weiss S.J. Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J. Biol. Chem. 271:1996;9135-9140.
41. Poole R.A., Alini M., Hollander A.P. Cellular Biology of Cartilage Degradation. Henderson B., Edwards J.C.W., Pettipher E.R. Mechanisms and Models in Rheumatoid Arthritis. 1995;163-204 Academic Press, London.
42. Porter J.R, Beeley N.R.A, Boyce B.A., Mason B., Millican A., Miller K., Leonard J., Morphy J.R., O'Connell J.P. Potent and selective inhibitors of gelatinase-A. 1. Hydroxamic acid derivatives. Bioorg. Med. Chem. Letts. 4:1994;2741-2746.
43. Powell W.C., Matrisian L.M. Complex roles of matrix metalloproteinases in tumour progression. Günther U., Birchmeier W. Current Topics in Microbiology and Immunology. 1996;1-21 Springer Verlag, Berlin.
44. Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Methods Enzymol. 248:1995;183-227.
45. Reinemer P., Grams F., Huber R., Kleine T., Schnierer S., Piper M., Tschesche H., Bode W. Structural implications for the role of the N-terminus in the 'superactivation' of collagenases. FEBS Lett. 338:1994;227-233.
46. Rouille J., Duguay S.J., Lund K., Furuta M., Gong Q., Lipkind G., Oliva A.A., Chan S.J., Steiner D.F. Proteolytic processing mechanisms in the biosynthesis of neuroendocrine peptides:The subtilisin-like proprotein convertases. Frontiers Neuroendocrinol. 16:1995;322-361.
47. Sanchez-Lopez R., Alexander C.M., Behrendson O., Breathnach R., Werb Z. Role of the zinc-binding- and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric enzymes. J. Biol. Chem. 268:1993;7238-7247.
48. Springman E.B., Angleton E.L., Birkedal-Hansen H., Van Wart H.E. Multiple modes of activation of latent fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation. Proc. Natl. Acad. Sci. USA. 87:1990;364-368.
49. Steffensen B., Wallon U.M., Overall C.M. Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa geleatinase/type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen. J. Biol. Chem. 270:1995;11555-11566.
50. Stöcker W., Grams F., Baumann U., Reinemer P., Gomis-Rüth F.-X., McKay D.B., Bode W. The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4:1995;823-840.
51. Strongin A.Y., Collier I., Bannikov G., Marmer B.L., Grant G.A., Goldberg G.I. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 270:1995;5331-5338.
52. Taylor K.B., Windsor L.J., Caterina N.C.M., Bodden M.K., Engler J.A. The mechanism of inhibition of collagenase by TIMP-1. J. Biol. Chem. 271:1996;23938-23945.
53. Ward R.V., Atkinson S.J., Reynolds J.J., Murphy G. Cell surface-mediated activation of protelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts. Biochem. J. 304:1994;263-269.
54. Will H., Atkinson S.J., Butler G., Smith B., Murphy G. The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation - Regulation by TIMP-2 and TIMP-3. J. Biol. Chem. 271:1996;17119-17123.
55. Willenbrock F., Murphy G. Structure-function relationships in the tissue inhibitors of metalloproteinases. Am. J. Respir. Crit. Care Med. 150:1994;S165-S170.
56. Willenbrock F., Crabbe T., Slocombe P.M., Sutton C.W., Docherty A.J.P., Cocket M.L., O'Shea M., Brocklehurst K., Phillips I.R., Murphy G. The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A. Biochemistry. 32:1993;4330-4337.