Biological and Pathobiological Functions of Gelatinase Dimers and Complexes

REFERENCES

• Nagase H., Visse R., Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc. Res. 2006; 69: 562–573
   PubMed Web of Science ®Google Scholar
• Cawston T. E., Wilson A. J. Understanding the role of tissue degrading enzymes and their inhibitors in development and disease. Best Pract. Res. Clin. Rheumatol. 2006; 20: 983–1002
   PubMed Web of Science ®Google Scholar
• Van Den Steen P. E., Opdenakker G., Wormald M. R., Dwek R. A., Rudd P. M. Matrix remodelling enzymes, the protease cascade and glycosylation. Biochim. Biophys. Acta. 2001; 1528: 61–73
   PubMed Web of Science ®Google Scholar
• Bjorklund M., Koivunen E. Gelatinase-mediated migration and invasion of cancer cells. Biochim. Biophys. Acta. 2005; 1755: 37–69
   PubMed Web of Science ®Google Scholar
• Hibbs M. S., Hasty K. A., Seyer J. M., Kang A. H., Mainardi C. L. Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase. J. Biol. Chem. 1985; 260: 2493–2500
   PubMed Web of Science ®Google Scholar
• Goldberg G. I., 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 dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin. J. Biol. Chem. 1992; 267: 4583–4591
   PubMed Web of Science ®Google Scholar
• Triebel S., Blaser J., Reinke H., Tschesche H. A 25 kDa alpha 2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase. FEBS. Lett. 1992; 314: 386–388
   PubMed Web of Science ®Google Scholar
• Kjeldsen L., Johnsen A. H., Sengelov H., Borregaard N. Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase. J. Biol. Chem. 1993; 268: 10425–10432
   PubMed Web of Science ®Google Scholar
• Olson M. W., Bernardo M. M., Pietila M., Gervasi D. C., Toth M., Kotra L. P., Massova I., Mobashery S., Fridman R. Characterization of the monomeric and dimeric forms of latent and active matrix metalloproteinase-9. Differential rates for activation by stromelysin 1. J. Biol. Chem. 2000; 275: 2661–2668
   PubMed Web of Science ®Google Scholar
• Winberg J. O., Kolset S. O., Berg E., Uhlin-Hansen L. Macrophages secrete matrix metalloproteinase 9 covalently linked to the core protein of chondroitin sulphate proteoglycans. J. Mol. Biol. 2000; 304: 669–680
   PubMed Web of Science ®Google Scholar
• Crabbe T., Ioannou C., Docherty A. J. 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. 1993; 218: 431–438
   PubMedGoogle Scholar
• Ilda J., Wilhelmson K. L., Ng J., Lee P., Morrison C., Tam E., Overall C. M., McCarthy J. B. Cell surface chondroitin sulfate glycosaminoglycan in melanoma: role in the activation of pro-MMP-2 (pro-gelatinase A). Biochem. J. 2007; 403: 553–563
   PubMed Web of Science ®Google Scholar
• Cha H., Kopetzki E., Huber R., Lanzendorfer M., Brandstetter H. Structural basis of the adaptive molecular recognition by MMP9. J. Mol. Biol. 2002; 320: 1065–1079
   PubMed Web of Science ®Google Scholar
• Van Den Steen P. E., Van Aelst I., Hvidberg V., Piccard H., Fiten P., Jacobsen C., Moestrup S. K., Fry S., Royle L., Wormald M. R., Wallis R., Rudd P. M., Dwek R. A., Opdenakker G. The hemopexin and O-glycosylated domains tune gelatinase B/MMP-9 bioavailability via inhibition and binding to cargo receptors. J. Biol. Chem. 2006; 281: 18626–18637
   PubMed Web of Science ®Google Scholar
• Tschesche H., Zolzer V., Triebel S., Bartsch S. The human neutrophil lipocalin supports the allosteric activation of matrix metalloproteinases. Eur. J. Biochem. 2001; 268: 1918–1928
   PubMedGoogle Scholar
• Bannikov G. A., Mattoon J. S., Abrahamsen E. J., Premanandan C., Green-Church K. B., Marsh A. E., Lakritz J. Biochemical and enzymatic characterization of purified covalent complexes of matrix metalloproteinase-9 and haptoglobin released by bovine granulocytes in vitro. Am. J. Vet. Res. 2007; 68: 995–1004
   PubMed Web of Science ®Google Scholar
• Ray S., Lukyanov P., Ochieng J. Members of the cystatin superfamily interact with MMP-9 and protect it from autolytic degradation without affecting its gelatinolytic activities. Biochim. Biophys. Acta. 2003; 1652: 91–102
   PubMed Web of Science ®Google Scholar
• Winberg J. O., Berg E., Kolset S. O., Uhlin-Hansen L. Calcium-induced activation and truncation of promatrix metalloproteinase-9 linked to the core protein of chondroitin sulfate proteoglycans. Eur. J. Biochem. 2003; 270: 3996–4007
   PubMedGoogle Scholar
• Malemud C. J. Matrix metalloproteinases (MMPs) in health and disease: an overview. Front. Biosci. 2006; 11: 1696–1701
   PubMed Web of Science ®Google Scholar
• Munesue S., Yoshitomi Y., Kusano Y., Koyama Y., Nishiyama A., Nakanishi H., Miyazaki K., Ishimaru T., Miyaura S., Okayama M., Oguri K. A novel function of syndecan-2, suppression of matrix metalloproteinase-2 activation, which causes suppression of metastasis. J. Biol. Chem. 2007; 282: 28164–28174
   PubMed Web of Science ®Google Scholar
• Yu Q., Stamenkovic I. Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev. 1999; 13: 35–48
   PubMed Web of Science ®Google Scholar
• Hemdahl A. L., Gabrielsen A., Zhu C., Eriksson P., Hedin U., Kastrup J., Thoren P., Hansson G. K. Expression of neutrophil gelatinase-associated lipocalin in atherosclerosis and myocardial infarction. Arterioscler. Thromb. Vasc. Biol. 2006; 26: 136–142
   PubMed Web of Science ®Google Scholar
• Zhang H., Xu L., Xiao D., Xie J., Zeng H., Wang Z., Zhang X., Niu Y., Shen Z., Shen J., Wu X., Li E. Upregulation of neutrophil gelatinase-associated lipocalin in oesophageal squamous cell carcinoma: significant correlation with cell differentiation and tumour invasion. J. Clin. Pathol. 2007; 60: 555–561
   PubMed Web of Science ®Google Scholar
• Gupta K., Shukla M., Cowland J. B., Malemud C. J., Haqqi T. M. Neutrophil gelatinase-associated lipocalin is expressed in osteoarthritis and forms a complex with matrix metalloproteinase 9. Arthritis. Rheum. 2007; 56: 3326–3335
   PubMed Web of Science ®Google Scholar
• Øynebråten I., Hansen B., Smedsrød B., Uhlin-Hansen L. Serglycin secreted by leucocytes is efficiently eliminated from the circulation by sinusoidal scavanger endothelial cells in the liver. J Leukoc. Biol. 2000; 67: 183–188
   PubMed Web of Science ®Google Scholar
• Bourguignon L. Y., Gunja-Smith Z., Iida N., Zhu H. B., Young L. J., Muller W. J., Cardiff R. D. CD44v(3,8–10) is involved in cytoskeleton-mediated tumor cell migration and matrix metalloproteinase (MMP-9) association in metastatic breast cancer cells. J. Cell. Physiol. 1998; 176: 206–215
   PubMed Web of Science ®Google Scholar
• Toyama-Sorimachi N., Kitamura F., Habuchi H., Tobita Y., Kimata K., Miyasaka M. Widespread expression of chondroitin sulfate-type serglycins with CD44 binding ability in hematopoietic cells. J. Biol. Chem. 1997; 272: 26714–26719
   PubMed Web of Science ®Google Scholar
• Theocharis A. D., Seidel C., Borset M., Dobra K., Baykov V., Labropoulou V., Kanakis I., Dalas E., Karamanos N. K., Sundan A., Hjerpe A. Serglycin constitutively secreted by myeloma plasma cells is a potent inhibitor of bone mineralization in vitro. J. Biol. Chem. 2006; 281: 35116–35128
   PubMed Web of Science ®Google Scholar
• Zhou J., Zhu P., Jiang J. L., Zhang Q., Wu Z. B., Yao X. Y., Tang H., Lu N., Yang Y., Chen Z. N. Involvement of CD147 in overexpression of MMP-2 and MMP-9 and enhancement of invasive potential of PMA-differentiated THP-1. BMC Cell Biol. 2005; 6: 25
   PubMed Web of Science ®Google Scholar