Regulation of Integrin-Mediated T Cell Adhesion by the Transmembrane Protein Tyrosine Phosphatase CD45
作者： Matthew L. Thomas , Alexander Zheleznyak , Eric J. Brown , John Seavitt , Hemanth Shenoi
DOI:
关键词: Integrin 、 Transmembrane domain 、 L1 、 Cell biology 、 Neural cell adhesion molecule 、 Biology 、 Molecular biology 、 Cell adhesion 、 Cell adhesion molecule 、 Adhesion 、 Protein tyrosine phosphatase
摘要: The transmembrane protein tyrosine phosphatase CD45 is required for Ag receptor signal transduction in lymphocytes. Recently, a role the regulation of macrophage adhesion has been demonstrated as well. To investigate further adhesion, we examined integrin-mediated to fibronectin two T cell lines and their CD45-deficient variants. absence correlated with enhanced via integrin alpha5beta1 (VLA-5), but not alpha4beta1 (VLA-4) both lines. Adhesion returned normal levels upon transfection wild-type into Transfection chimeric or mutant molecules expressing some, all, domains activities that domain activity were integrin-dependent highly glycosylated extracellular was dispensable. In contrast, only catalytically active cytoplasmic TCR signaling. Transfectants restored coimmunoprecipitated known CD45-associated protein. These studies demonstrate novel suggest possible function its association
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