Cellular and Molecular Life Sciences CMLS

, Volume 54, Issue 6, pp 527-540

First online:

What have snakes taught us about integrins?

  • T.-F. HuangAffiliated withPharmacological 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.tw

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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 α IIbβ 3 , α 5β 1 and α Vβ 3 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.