Platelet-Collagen Adhesion: Evidence for Participation of Antigenically Distinct Entities

Univalent antibody fragments prepared from a rabbit antiserum raised against whole human platelets completely inhibited adhesion of platelets to immobilized trimeric collagen in a defined, Mg2+-dependent, adhesion assay. An octylglucoside extract of whole platelets completely neutralized this antibo...

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Published inThe Journal of cell biology Vol. 99; no. 6; pp. 2048 - 2055
Main Authors Shadle, Paula J., Barondes, Samuel H.
Format Journal Article
LanguageEnglish
Published New York, NY Rockefeller University Press 01.12.1984
The Rockefeller University Press
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Summary:Univalent antibody fragments prepared from a rabbit antiserum raised against whole human platelets completely inhibited adhesion of platelets to immobilized trimeric collagen in a defined, Mg2+-dependent, adhesion assay. An octylglucoside extract of whole platelets completely neutralized this antibody, and all neutralizing activity bound to immobilized wheat germ agglutinin. Further fractionation on concanavalin A gave rise to subfractions that each neutralized only partially at saturation, when tested against antibody concentrations that inhibit 50% of platelet-collagen adhesion. When tested against higher antibody concentrations that completely inhibited adhesion, each subfraction had no detectable neutralizing effect, although the combined subfractions neutralized completely. This and other evidence suggests that more than one platelet entity participates in platelet-collagen adhesion. Although distinct, they appear to play interdependent roles in a single adhesion process.
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ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.99.6.2048