Snake venom disintegrins

Swenson, S., Costa, F., Minea, R., Sherwin, R. P, Ernst, W., Fujii, G., Yang, D., and Markland, F. S., Jr. (2004), Intravenous liposomal delivery of the snake venom disintegrin contortrostatin limits breast cancer progression, Mol. Cancer Then, 3,499-511. 

Weskamp, G. and Blobel, C.P. (1994). A family of cellular proteins related to snake venom disintegrins. 

In Chapter 6, Blobel discusses the roles of metalloprotease-disintegrins in cell-cell interactions and in the cleavage of TNFa and Notch. A brief summary of the known properties of snake venom disintegrins and metalloproteases is followed by a discussion of the role of membrane-anchored metalloprotease-disintegrins in cell-cell interactions and proteolysis of extracytoplasmic or extracellular protein domains. This timely and exciting area of research bears on aspects of mammalian fertilization and on cell fate decisions during development. 

ADAM. A Disintesrin And MetalloProteinase family of proteins. Disintegrins, as the name implies, are proteins which interfere with interactions of cells with proteins in the extracellular matrix. An example are the inhibitors of the interaction of blood platelets with fibrinogen. Disintegrins are found in snake venom. Metalloproteinases are a family of proteases which need a bivalent cation for catalysis. MMP s are matrix metallo-proteases. They are associated with the extracellular matrix. 

Snake venoms cause a rapid disintegration of the stroma (disintegrin) due to short peptides each containing an ROD integrin-binding sequence. The ROD sequence displaces... 

Kini, R.M. and Evans, H.J. (1992). Structural domains in venom proteins Evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor. Toxicon. 50 1-29. 

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