This proposal is for support of an international research conference on metalloproteinases and their role in extracellular matrix degradation in health and disease. The conference is unique and timely because of recent advances which have shown that matrix metalloproteinases constitute a family of genetically and functionally distinct but structurally homologous enzymes which play an important role in the biologic degradation of extracellular matrices. So far, five enzymes encoded for by a family of highly conserved genes have been identified: fibroblast-type IV collagenase, PMN-type collagenase, stromelysin, Mr 72,000 gelatinase/type IV collagenase, and Mr 95,000 gelatinase. The conference will summarize new and existing data on (1) structure and catalytic properties; (2) regulation of catalytic activity at the levels of gene expression, enzyme activation, and inactivation by natural and synthetic inhibitors; and (3) role in biologic degradation of extracellular matrices. The conference will provide for discussion of information and ideas to an extent not achievable by conventional means of communication, such as publication and more formal scientific meetings. We propose to bring together leading scientists from the U.S. and abroad for a 4 1/2 day conference to evaluate current knowledge and to discuss future avenues of research. A total of 55-60 invited speakers and moderators, each an expert in their field, will be asked to present a timely overview and new data on an assigned topic in their area of expertise. Speakers will also be requested to submit a written manuscript, and these will form the basis for publication of the proceedings of the conference. Poster sessions are planned to be open to those who wish to present new data.
| (1992) Proceedings of the Matrix Metalloproteinase Conference. Sandestin Beach, Florida, September 11-15, 1989. Matrix Suppl 1:1-504 |
