Abstract
A 27-kDa protein from adult rat brain synaptosomes was purified by matrix-affinity chromatography. The matrix receptor interacted with the Arg-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, conventional integrin subunits exhibited robust degradation. This unique resistance to proteolysis may allow the new matrix receptor to contribute to the stability of synaptic contacts.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acids / metabolism
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Animals
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Brain Chemistry / physiology*
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Calcium / chemistry*
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Cell Membrane / chemistry
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Cell Membrane / metabolism
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Chromatography, Affinity
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Extracellular Matrix / chemistry
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Extracellular Matrix / metabolism*
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Hydrolysis
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Integrins / metabolism
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Male
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Molecular Weight
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Rats
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Receptors, Cell Surface / chemistry
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Receptors, Cell Surface / metabolism*
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Synaptosomes / chemistry
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Synaptosomes / metabolism*
Substances
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Amino Acids
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Integrins
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Receptors, Cell Surface
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Calcium