What have snakes taught us about integrins?
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 alpha IIb beta 3, alpha 5 beta 1 and alpha V beta 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.
Pharmacological Institute, College of Medicine, National Taiwan University, Taipei. turfu@ccms.ntu.edu.tw
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D000595:Amino Acid Sequence; D001792:Blood Platelets / Q000502:physiology; D019483:Disintegrins / Q000737:chemistry*; D016023:Integrins / Q000502:physiology*; D008667:Metalloproteins / Q000737:chemistry; D008969:Molecular Sequence Data; D018919:Neovascularization, Physiologic; D010980:Platelet Membrane Glycoproteins / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D012910:Snake Venoms / Q000737:chemistry*; D013927:Thrombosis / Q000503:physiopathology
D019483:Disintegrins; D016023:Integrins; D008667:Metalloproteins; D010980:Platelet Membrane Glycoproteins; D012910:Snake Venoms