Matrix metalloproteinase-2: Not (just) a 'hero' of the past

Autor: Hervé Emonard, Patrick Henriet
Přispěvatelé: École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL), Laboratory of Biochemistry and Molecular Biology (LBMB), Faculty of Medicine-UPRESA 6021, UCL - SSS/DDUV/CELL - Biologie cellulaire
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Zdroj: Biochimie
Biochimie, Elsevier, 2019, 166, pp.223-232. ⟨10.1016/j.biochi.2019.07.019⟩
Biochimie, Vol. 166, p. 223-232 (2019)
ISSN: 0300-9084
Popis: The 72-kDa type IV collagenase or gelatinase A is the second member of the matrix metalloproteinase family, MMP-2. Since the discovery of its first two substrates within components of the extracellular matrix, denatured interstitial type I collagen and native type IV collagen, the roles and various levels of regulation of MMP-2 have been intensively studied, mainly in vitro. Its (over)expression in most if not all tumors was considered a hallmark of cancer aggressiveness and boosted investigations aiming at its inhibition. Unfortunately, the enthusiasm subsided like a souffle after clinical trial failures, mostly because of insufficient knowledge of in vivo MMP-2 activities and detrimental side effects of broad-spectrum MMP inhibition. Nowadays, MMP-2 remains a major topic of interest in research, the second in the MMP family after MMP-9. This review presents a broad overview of the major features of this protease. This knowledge is crucial to identify diagnostic or therapeutic strategies focusing on MMP-2. In this sense, recent publications and clinical trials underline the potential value of measuring circulating or tissular MMP-2 levels as diagnostic or prognostic tools, or as a useful secondary outcome for therapies against other primary targets. Direct MMP-2 inhibition has benefited from substantial progress in the design of more specific inhibitors but their in vivo application remains challenging but certainly worth the efforts it receives.
Databáze: OpenAIRE
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