Elsevier

Methods in Enzymology

Volume 144, 1987, Pages 475-489
Methods in Enzymology

D. Glycoprotein
[27] Arginine-glycine-aspartic acid adhesion receptors

https://doi.org/10.1016/0076-6879(87)44196-7Get rights and content

Publisher Summary

This chapter discusses the isolation and properties of cell surface receptors for fibronectin and vitronectin. These receptors recognize the same arginine-glycine-aspartic acid (Arg-Gly-Asp) cell attachment determinant in their ligands. The cell attachment site of fibronectin can be isolated as an 11.5kDa peptic fragment of fibronectin which retains this cell attachment-promoting function. It is possible synthetically to reconstruct the cell attachment determinant that is contained within this natural fragment. By testing smaller and smaller synthetic fragments of fibronectin for their ability to support cell attachment, it can be shown that the minimum structural component of this cell attachment activity is composed of the tripeptide Arg-Gly-Asp. It appears then that a number of extracellular proteins are recognized by the cell surface via an Arg-Gly-Asp-dependent mechanism. Such recognition is mediated by receptors specific for the Arg-Gly-Asp sequence in fibronectin, vitronectin, and some other proteins. The discovery of the Arg-Gly-Asp cell adhesion system has considerably enhanced the opportunities for increasing our understanding of cell surface recognition phenomena. The availability of methods for the purification of the Arg-Gly-Asp receptors will now allow studies of their structure, distribution, and binding specificities.

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