A 27-KDA MATRIX RECEPTOR FROM RAT-BRAIN SYNAPTOSOMES - SELECTIVE RECOGNITION OF THE ARG-GLY-ASP-SER DOMAIN AND UNIQUE RESISTANCE TO CALCIUM-DEPENDENT PROTEOLYSIS
D. Capaldi et al., A 27-KDA MATRIX RECEPTOR FROM RAT-BRAIN SYNAPTOSOMES - SELECTIVE RECOGNITION OF THE ARG-GLY-ASP-SER DOMAIN AND UNIQUE RESISTANCE TO CALCIUM-DEPENDENT PROTEOLYSIS, Neuroscience research, 28(3), 1997, pp. 275-279
A 27-kDa protein from adult rat brain synaptosomes was purified by mat
rix-affinity chromatography. The matrix receptor interacted with the A
rg-Gly-Asp-Ser sequence recognized by integrin-type adhesion molecules
, and was labeled by integrin antibodies. Levels of the 27-kDa species
in brain membranes were unaffected by proteolysis, however, conventio
nal integrin subunits exhibited robust degradation. This unique resist
ance to proteolysis may allow the new matrix receptor to contribute to
the stability of synaptic contacts. (C) 1997 Elsevier Science Ireland
Ltd.