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• W2074507788 abstract "Integrins were cross-linked to their extracellular matrix ligands using non-penetrating chemical cross-linkers. This procedure did not disturb the distribution of integrin in the adhesion structure and adhesion plaque integrin staining remained even when the cultures were extracted with ionic detergents. 80-90% of the pi integrin in the cross-linked culture was extracted with RIPA buffer and the remaining 10-20% was recovered following reversal of the cross-linking. This separated two distinct integrin pools, one which can be cross-linked to substrate bound extracellular matrix and one which is not. The specificity of this procedure for cross-linking of integrins involved in substrate adhesion was demonstrated using NIH 3T3 cells which express both α5β1 and α5β1 integrins. α6 was cross-linked only in cells plated on laminin whereas α5 was cross-linked when fibronectin was present. Using antisera directed to the cytoplasmic domains of either α5 or β1 integrin, it was demonstrated that these domains can be blocked in the intact cell but the blocking can be removed using ionic detergent extraction after chemical cross-linking. The extracellular matrix associated with the substrate surface but not that associated with the media exposed surface is both cross-linked and retained on the plastic dish following cross-linking." @default.
• W2074507788 created "2016-06-24" @default.
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• W2074507788 date "1993-01-01" @default.
• W2074507788 modified "2023-10-17" @default.
• W2074507788 title "Evaluation of Integrin Molecules Involved in Substrate Adhesion" @default.
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• W2074507788 doi "https://doi.org/10.3109/15419069309097253" @default.
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