Coclustering CD45 with CD4 or CD8 alters the phosphorylation and kinase activity of p56lck

Antibody-mediated CD4 crosslinking results in increased tyrosine phosphorylation and tyrosine kinase activity of the associated p56lck. Treatment with anti-CD4 and anti-Ig also induced the phosphorylation of p56lck in a CD45- mutant cell line, indicating that the increase in phosphotyrosine content...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1990
Materias:
Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188152/
https://www.ncbi.nlm.nih.gov/pubmed/2141630
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description Antibody-mediated CD4 crosslinking results in increased tyrosine phosphorylation and tyrosine kinase activity of the associated p56lck. Treatment with anti-CD4 and anti-Ig also induced the phosphorylation of p56lck in a CD45- mutant cell line, indicating that the increase in phosphotyrosine content of p56lck is not the result of being sequestered from CD45 protein tyrosine phosphatase (PTPase). Antibody- mediated coclustering of CD45 with CD4 inhibited the anti-CD4-induced phosphorylation of p56lck on tyrosine and the concomitant increase in in vitro kinase activity. Similar results were obtained when CD45 was coclustered with CD8 on cytotoxic T cell lines. These observations provide strong evidence that p56lck is a substrate for CD45 in vivo and provide an assay to study the regulation and specificity of CD45 PTPase activity.
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spelling pubmed-21881522008-04-17 Coclustering CD45 with CD4 or CD8 alters the phosphorylation and kinase activity of p56lck J Exp Med Articles Antibody-mediated CD4 crosslinking results in increased tyrosine phosphorylation and tyrosine kinase activity of the associated p56lck. Treatment with anti-CD4 and anti-Ig also induced the phosphorylation of p56lck in a CD45- mutant cell line, indicating that the increase in phosphotyrosine content of p56lck is not the result of being sequestered from CD45 protein tyrosine phosphatase (PTPase). Antibody- mediated coclustering of CD45 with CD4 inhibited the anti-CD4-induced phosphorylation of p56lck on tyrosine and the concomitant increase in in vitro kinase activity. Similar results were obtained when CD45 was coclustered with CD8 on cytotoxic T cell lines. These observations provide strong evidence that p56lck is a substrate for CD45 in vivo and provide an assay to study the regulation and specificity of CD45 PTPase activity. The Rockefeller University Press 1990-07-01 /pmc/articles/PMC2188152/ /pubmed/2141630 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Coclustering CD45 with CD4 or CD8 alters the phosphorylation and kinase activity of p56lck
title Coclustering CD45 with CD4 or CD8 alters the phosphorylation and kinase activity of p56lck
title_full Coclustering CD45 with CD4 or CD8 alters the phosphorylation and kinase activity of p56lck
title_fullStr Coclustering CD45 with CD4 or CD8 alters the phosphorylation and kinase activity of p56lck
title_full_unstemmed Coclustering CD45 with CD4 or CD8 alters the phosphorylation and kinase activity of p56lck
title_short Coclustering CD45 with CD4 or CD8 alters the phosphorylation and kinase activity of p56lck
title_sort coclustering cd45 with cd4 or cd8 alters the phosphorylation and kinase activity of p56lck
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188152/
https://www.ncbi.nlm.nih.gov/pubmed/2141630

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