EFFECTS OF INTEGRIN ALPHAⅡb<sup>R995A</sup> MUTATION ON RECEPTOR AFFINITY AND pp125 （FAK） PHOSPHORYLATION

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EFFECTS OF INTEGRIN ALPHAⅡb^R995A MUTATION ON RECEPTOR AFFINITY AND pp125 （FAK） PHOSPHORYLATION

中国医学科学杂志（英文版） 2004年0卷第4期页码：276-281

Updated：2024-04-10

- EFFECTS OF INTEGRIN ALPHAⅡb^R995A MUTATION ON RECEPTOR AFFINITY AND pp125 （FAK） PHOSPHORYLATION
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  中图分类号： R363
- 纸质出版日期：2004
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EFFECTS OF INTEGRIN ALPHAⅡb^R995A MUTATION ON RECEPTOR AFFINITY AND pp125 （FAK） PHOSPHORYLATION[J]. 中国医学科学杂志（英文版）, 2004,0(4):276-281.

EFFECTS OF INTEGRIN ALPHAⅡb^R995A MUTATION ON RECEPTOR AFFINITY AND pp125 （FAK） PHOSPHORYLATION[J]. Chinese medical sciences journal, 2004, 0(4): 276-281.
EFFECTS OF INTEGRIN ALPHAⅡb^R995A MUTATION ON RECEPTOR AFFINITY AND pp125 （FAK） PHOSPHORYLATION[J]. 中国医学科学杂志（英文版）, 2004,0(4):276-281. DOI：

EFFECTS OF INTEGRIN ALPHAⅡb^R995A MUTATION ON RECEPTOR AFFINITY AND pp125 （FAK） PHOSPHORYLATION[J]. Chinese medical sciences journal, 2004, 0(4): 276-281. DOI：

摘要

Abstract

Objective To investigate the role of cytoplasmic domain of integrin alphaⅡb in platelet signal transduction. Methods Binding capacity of integrin alphaⅡb R995A to antibody platelet activation complex-1 （PAC-1） and pp125 focal adhesion kinase （FAK） phosphorylation of cells were detected by flow cytometry

immune precipitation

and Western blotting. Results Without activation

wild-type alphaⅡbbeta3 Chinese hamster ovary （CHO） cells failed to bind to PAC-1

but mutant chimera alphaⅡb R995A beta3 CHO cells were able to bind with PAC-1. Furthermore

phosphorylation of pp125 （FAK） in wild-type alphaⅡbbeta3 CHO cells occured only when cells were adhered to fibrinogen

but could not be detected in bovine serum albumin suspension. However in the mutant chimera group

it could be detected in both conditions. Conclusion The mutation in integrin alphaⅡb R995A alters its affinity state as a receptor

thus also mediating cytoplasmic signal transduction leading to the phosphorylation of pp125 （FAK） without ligand binding.

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EFFECTS OF INTEGRIN ALPHAⅡbR995A MUTATION ON RECEPTOR AFFINITY AND pp125 （FAK） PHOSPHORYLATION

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EFFECTS OF INTEGRIN ALPHAⅡb^R995A MUTATION ON RECEPTOR AFFINITY AND pp125 （FAK） PHOSPHORYLATION