Cellular and Molecular Life Sciences CMLS

, Volume 54, Issue 6, pp 527–540

What have snakes taught us about integrins?

  • T.-F. Huang

DOI: 10.1007/s000180050181

Cite this article as:
Huang, TF. CMLS, Cell. Mol. Life Sci. (1998) 54: 527. doi:10.1007/s000180050181

Abstract.

Snake venoms contain unique components that affect cell-matrix interactions. Disintegrins represent a class of low molecular weight, Arg-Gly-Asp (RGD)-containing, cysteine-rich peptides purified from the venom of various snakes among the Viperidae and Crotalidae. They bind with various degrees of specificity to integrins αIIbβ3 , α5β1 and αVβ3 expressed on cells. Snake venom metalloproteases (high molecular mass haemorrhagins) also contain disintegrin-like domains, in addition to zinc-chelating sequences. Membrane-anchored ADAMs (A Disintegrin And Metalloprotease domain), multidomain molecules consisting of metalloprotease, disintegrin-like, cysteine-rich, and epidermal growth factor domains, a transmembrane domain and a cytoplasmic tail, are a new family of proteins. In the light of the large number and wide distribution of ADAMs, they may participate in cell-cell fusion events, including sperm-egg binding and fusion, myoblast fusion and other cell-cell and cell-matrix interactions. The structure-function relationship of these molecules is discussed.

Key words. Snake venom disintegrin; metalloprotease; ADAMs; integrin αIIb β3 , α2 β1 , αV β 3 ; platelet aggregation; haemorrhage; cell-matrix interaction; cell fusion. 

Copyright information

© Birkhäuser Verlag Basel, 1998

Authors and Affiliations

  • T.-F. Huang
    • 1
  1. 1.Pharmacological Institute, College of Medicine, National Taiwan University, 1, Jen-Ai Rd., 1st Sec, Taipei (Taiwan), Fax +886 02 341 7930, e-mail: turfu@ccms.ntu.edu.twTW