Effects of modifications of the RGD sequence and its context on recognition by the fibronectin receptor.
作者： A Hautanen , J Gailit , D M Mann , E Ruoslahti
DOI: 10.1016/S0021-9258(18)94206-7
关键词:
摘要: Abstract The receptor for fibronectin is a member of the integrin superfamily cell surface adhesion receptors, many which recognize sequence RGD in their ligands. We have developed sensitive enzyme-linked and radioreceptor assays to examine ligand specificity receptor. bound only various Arg-Gly-Asp (RGD)-containing proteins tested. smallest amount detectable assay was about 10 ng. Mn2+ enhanced binding 3-10-fold as compared Ca2+ Mg2+. Scatchard analysis saturation plot from gave dissociation constant (Kd) 3 x 10(-8) M presence Mn2+. Inhibition experiments showed that affinities ligands decreased order approximately 110-kDa fragment greater than GRGDSP peptide 11.5-kDa fragment. Peptides not containing an were several hundred thousand-fold less inhibitory GRGDSP. These included closely related peptides GRADSP GRGESP, well three reverse DGR. A fibrinogen gamma-chain, KQAGDV, had 0.5% activity standard peptide, most active RGD. results document exquisite sequence.
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