Citation

Kamiguti AS, Zuzel M, Theakston RDG. Braz. J. Med. Biol. Res. 1998; 31(7): 853-862.

Affiliation

Department of Haematology, Royal Liverpool University Hospital, University of Liverpool, UK. aurakami@liverpool.ac.uk

Copyright

(Copyright © 1998, Associacao Brasileira De Divulgacao Cientifica)

DOI

unavailable

PMID

9698750

Abstract

Metalloproteinases and disintegrins are important components of most viperid and crotalid venoms. Large metalloproteinases referred to as MDC enzymes are composed of an N-terminal Metalloproteinase domain, a Disintegrin-like domain and a Cys-rich C-terminus. In contrast, disintegrins are small non-enzymatic RGD-containing cysteine-rich polypeptides. However, the disintegrin region of MDC enzymes bears a high degree of structural homology to that of the disintegrins, although it lacks the RGD motif. Despite these differences, both components share the property of being able to recognize integrin cell surface receptors and thereby to inhibit integrin-dependent cell reactions. Recently, several membrane-bound MDC enzymes, closely related to soluble venom MDC enzymes, have been described in mammalian cells. This group of membrane-anchored mammalian enzymes is also called the ADAM family of proteins due to the structure revealing A Disintegrin And Metalloproteinase domains. ADAMs are involved in the shedding of molecules from the cell surface, a property which is also shared by some venom MDC enzymes.

Language: en