By Jean-Michel Foidart, Ruth J. Muschel

In recent times, serine proteases and matrix metalloproteinases (MMPs) have received enormous cognizance in tumor biology. for many of those proteases, their expression is a competent indication of ongoing tissue home improvement. This ebook offers a complete review of the mechanisms of motion of proteases and their inhibitors in tumor biology. the 1st half offers the reader with a selective evaluation of the molecular biology of serine proteases, MMPs and their physiological inhibitors. crucial proteases and their physiological in addition to artificial inhibitors are evaluated within the such a lot suitable versions of experimental and human melanoma. The scientific points also are taken under consideration. This quantity bargains an replace in this hard element of melanoma remedy, its curiosity bias, and attainable scientific implication.

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Plasminogen activators, integrins and the coordinated regulation of cell adhesion and migration. Curr Opin Cell Biol 1997; 9: 714–724. Chapman HA, Wei Y, Simon DI, Waltz DA. Role of urokinase receptor and caveolin in regulation of integrin signaling. Thromb Haemost 1999; 82: 291–297. Dano K, Romer J, Nielsen BS, Bjorn S, Pyke C, Rygaard J, Lund LR. Cancer invasion and tissue remodeling-cooperation of protease systems and cell types. APMIS 1999; 107: 120–127. de Groot FMH, van Berkom LWA, Scheeren HW.

Protease inhibitors of the MMPs and of the plasminogen activation system and antiangiogenic agents might therefore be excellent candidates to cancer treatments targeting normal host cells. In contrast, to tumoral cells, they are indeed genetically stable and do not regularly develop mutational resistance to anti-cancerous agents. Naturally occurring and synthetic inhibitors of uPA, antibodies to uPAR and uPA, antisense oligodeoxynucleotides, recombinant and synthetic ATF or soluble uPAR are being evaluated (Schmitt et al, 2000) in various tumor models in animals.

PAI-1 could also be considered as the molecular switch that governs uPAR- and/or integrin-mediated cell adhesion and release. Vitronectin contains a RGD sequence recognized by integrins and located Cterminally and to the vicinity of its somatomedin B domain. Although plasma vitronectin is in a ‘closed conformation’ that does not interact with integrins, PAI-1 converts this latent form to the open integrin binding conformation of vitronectin (Deng et al, 1996). Paradoxically, PAI-1 inhibits the binding of the integrin αvβ3 to vitronectin and in this way blocks smooth muscle cell migration (Stefansson and Lawrence, 1996).

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