Tissue distribution, inhibition and activation of gelatinolytic activities in Atlantic cod (Gadus morhua)

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 137, Issue 3, 2004, Pages 363-371

  Lødemel, Jørgen B ^a   Mæhre, Hanne K ^a   Winberg, Jan Olof ^a   Olsen, Ragnar L ^a  

^a UNIVERSITY OF TROMSØ   (Norway)

Author keywords

APMA activated; Fish; Galardin; Matrix metalloproteinases; Tissues; Trypsin activated

Indexed keywords

GELATIN; GELATINASE A; GELATINASE B; LECTIN; MATRIX METALLOPROTEINASE; PROTEINASE INHIBITOR;

AFFINITY CHROMATOGRAPHY; ANIMAL TISSUE; ARTICLE; ATLANTIC COD; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME BINDING; ENZYME INHIBITION; ENZYME LOCALIZATION; ENZYME MECHANISM; FISH; GILL; GONAD; HEART; LIVER; NONHUMAN; PHYSICAL CHEMISTRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN LOCALIZATION; SPECIES DIFFERENTIATION; TISSUE DISTRIBUTION;

GADUS; GADUS MORHUA; LENS CULINARIS;

EID: 1842526686     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2003.12.007     Document Type: Article

References (42)

1. Ando M., Toyohara H., Shimizu Y., Sakaguchi M. Postmortem tenderization of rainbow trout (Oncorhynchus mykiss) muscle caused by gradual disintegration of the extracellular matrix structure. J. Sci. Food Agric. 55:1991;589-597.
2. Birkedal-Hansen H., Moore W.G.I., Bodden M.K., Windsor L.J., Birkedal-Hansen B., Decarlo A., et al. Matrix metalloproteinases - a review. Crit. Rev. Oral Biol. Med. 4:1993;197-250.
3. Bracho G.E., Haard N.F. Identification of two matrix metalloproteinases in the skeletal muscle of Pacific rockfish (Sebastes sp). J. Food Biochem. 19:1995;299-319.
4. Bremner H.A., Hallett I.C. Muscle fiber - connective tissue junctions in the fish blue grenadier (Macruronus novaezelandiae). A scanning electron microscope study. J. Food Sci. 50:1985;975-980.
5. Collier I.E., Wilhelm S.M., Eisen A.Z., Marmer B.L., Grant G.A., Seltzer J.L., et al. H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. J. Biol. Chem. 263:1988;6579-6587.
6. Grobelny D., Poncz L., Galardy R.E. Inhibition of human skin fibroblast collagenase, thermolysin, and Pseudomonas aeruginosa elastase by peptide hydroxamic acids. Biochemistry. 31:1992;7152-7154.
7. Hahn-Dantona E.A., Aimes R.T., Quigley J.P. The isolation, characterization, and molecular cloning of a 75-kDa gelatinase B-like enzyme, a member of the matrix metalloproteinase (MMP) family. An avian enzyme that is mmp-9-like in its cell expression pattern but diverges from mammalian gelatinase b in sequence and biochemical properties. J. Biol. Chem. 275:2000;40 827-40 838.
8. Hallett I.C., Bremner H.A. Fine structure of the myokommata-muscle fiber junction in hoki (Macruronus novaezelandiae). J. Sci. Food Agric. 44:1988;245-261.
9. Holleran W.M., Galardy R.E., Gao W.N., Levy D., Tang P.C., Elias P.E. Matrix metalloproteinase inhibitor reduce phorbol ester-induced cutaneous inflammation and hyperplasia. Arch. Dermatol. Res. 289:1997;138-144.
10. Howard E.W., Bullen E.C., Banda M.J. Regulation of the autoactivation of human 72-kDa progelatinase by tissue inhibitor of metalloproteinases-2. J. Biol. Chem. 266:1991;13 064-13 069.
11. Kinoshita M., Yabe T., Kubota M., Takeuchi K., Kubota S., Toyohara H., et al. cDNA cloning and characterization of two gelatinases from Japanese flounder. Fish. Sci. 68:2002;618-626.
12. Kubota S., Kinoshita M., Toyohara H., Sakaguchi M. Gelatinolytic activities in ayu muscle in the spawning stage. Fish. Sci. 64:1998a;1001-1002.
13. Kubota S., Toyohara H., Sakaguchi M. Occurrence of gelatinolytic activities in yellowtail tissues. Fish. Sci. 64:1998b;439-442.
14. Kubota S., Kinoshita M., Yokoyama Y., Toyohara H., Sakaguchi M. Induction of gelatinolytic activities in ayu muscle at the spawning stage. Fish. Sci. 66:2000;574-578.
15. Levy D.E., Lapierre F., Liang W.S., Ye W.Q., Lange C.W., Li X.Y., et al. Matrix metalloproteinase inhibitors: a structure-activity study. J. Med. Chem. 41:1998;199-223.
16. Lødemel J.B., Olsen R.L. Gelatinolytic activities in muscle of Atlantic cod (Gadus morhua), spotted wolffish (Anarhichas minor) and Atlantic salmon (Salmo salar). J. Sci. Food Agric. 83:2003;1031-1036.
17. Massova I., Kotra L.P., Fridman R., Mobashery S. Matrix metalloproteinases: structures, evolution, and diversification. FASEB J. 12:1998;1075-1095.
18. Matrisian L.M. The matrix-degrading metalloproteinases. Bioessays. 14:1992;455-463.
19. Matsui H., Ogiwara K., Ohkura R., Yamashita M., Takahashi T. Expression of gelatinases A and B in the ovary of the medaka fish Oryzias latipes. Eur. J. Biochem. 267:2000;4658-4668.
20. Mattu T.S., Royle L., Langridge J., Wormald M.R., Van den Steen P.E., Van Damme J., et al. O-glycan analysis of natural human neutrophil gelatinase B using a normal phase-HPLC and online tandem mass spectrometry: implications for the domain organization of the enzyme. Biochemistry. 39:2000;15 695-15 704.
21. Morodomi T., Ogata Y., Sasaguri Y., Morimatsu M., Nagase H. Purification and characterization of matrix metalloproteinase-9 from U937 monocytic leukemia and HT1080 fibrosarcoma cells. Biochem. J. 285:1992;603-611.
22. Murphy G., Crabbe T. Gelatinases A and B. Method Enzymol. 248:1995;470-484.
23. Murphy G., Ward R., Hembry R.M., Reynolds J.J., Kühn K., Tryggvason K. Characterization of gelatinase from pig polymorphoneuclear leucocytes. A metalloproteinase resembling tumor type IV collagenase. Biochem. J. 258:1989;463-472.
24. Nagase H., Ogata Y., Suzuki K., Enghild J.J., Salvesen G. Substrate specificities and activation mechanisms of matrix metalloproteinases. Biochem. Soc. Trans. 19:1991;715-718.
25. Nagase H. Activation mechanisms of matrix metalloproteinases. Biol. Chem. 378:1997;151-160.
26. Okada Y., Morodomi T., Enghild J.J., Suzuki K., Yasui A., Nakanishi I., et al. Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties. Eur. J. Biochem. 194:1990;721-730.
27. Okada Y., Gonoji Y., Naka K., Tomita K., Nakanishi I., Iwata K., et al. Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. J. Biol. Chem. 267:1992;21 712-21 719.
28. Rudd P.M., Mattu T.S., Masure S., Bratt T., Van den Steen P.E., Wormald M.R., et al. Glycosylation of natural human neutrophil gelatinase B and neutrophil gelatinase B-associated lipocalin. Biochemistry. 38:1999;13 937-13 950.
29. Saito M., Kunisaki N., Urano N., Kimura S. Characterization of cDNA clone encoding the matrix metalloproteinase 2 from rainbow trout fibroblast. Fish. Sci. 66:2000a;334-342.
30. Saito M., Sato K., Kunisaki N., Kimura S. Characterization of a rainbow trout matrix metalloproteinase capable of degrading type I collagen. Eur. J. Biochem. 267:2000b;6943-6950.
31. Sato K., Ando M., Kubota S., Origasa K., Kawase H., Toyohara H., et al. Involvement of type V collagen in softening of fish muscle during short-term chilled storage. J. Agric. Food Chem. 45:1997;343-348.
32. Stetler-Stevenson W.G., Krutzsch H.C., Wacher M.P., Margulies I.M.K., Liotta L.A. The activation of human type-IV collagenase proenzyme-sequence identification of the major conversion product following organomercurial activation. J. Biol. Chem. 264:1989;1353-1356.
33. Svendsrud D.H., Loennechen T., Winberg J.O. Effect of adenosine analogues on the expression of matrix metalloproteinases and their inhibitors from human dermal fibroblasts. Biochem. Pharmacol. 53:1997;1511-1520.
34. Takeuchi K., Kubota S., Kinoshita M., Toyohara H., Sakaguchi M. Cloning and characterization of cDNA for carp matrix metalloproteinase 9. Fish. Sci. 68:2002;610-617.
35. Van Wart H.E., Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. USA. 87:1990;5578-5582.
36. Vartio T., Baumann M. Human gelatinase/type IV procollagenase is a regular plasma component. FEBS Lett. 255:1989;285-289.
37. Wilhelm S.M., Collier I.E., Marmer B.L., Eisen A.Z., Grant G.A., Goldberg G.I. SV40-transformed human lung fibroblasts secrete a 92-kDa Type IV collagenase which is identical to that secreted by normal human macrophages. J. Biol. Chem. 264:1989;17 213-17 221.
38. Winberg J.O., Gedde-Dahl T. Epidermolysis bullosa simplex: expression of gelatinase activity in cultured human skin fibroblasts. Biochem. Genet. 30:1992;401-420.
39. Winberg J.O., Kolset S.O., Berg E., Uhlin-Hansen L. Macrophages secrete matrix metalloproteinase 9 covalently linked to the core protein of chondroitin sulfate proteoglycans. J. Mol. Biol. 304:2000;669-680.
40. Woessner J.F. Matrix metalloproteinases and their inhibitors in connective-tissue remodeling. FASEB J. 5:1991;2145-2154.
41. Woessner J.F., Nagase H. Matrix Metalloproteases and TIMPs. 2000;Oxford University Press, New York.
42. Zhang, J., Bai, S., Zhang, X., Nagase, H., Sarras, M.P., Jr., 2003. The expression of gelatinase A (MMP-2) is required for normal development of zebrafish embryos Dev. Genes Evol (in press).