Activators of Protein Kinase C Down-Regulate and Phosphorylate the T3/T-Cell Antigen Receptor Complex of Human T Lymphocytes

As judged by indirect immunofluorescence, phorbol 12, 13-dibutyrate and 1-oleoyl-2-acetylglycerol induced a rapid, concentration-dependent decrease of about 50% in the surface expression of the T3 antigen on human T lymphoblasts, and of T3 and the T-cell antigen receptor on HPB-ALL cells. Direct bin...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1985-12, Vol.82 (23), p.8158-8162
Hauptverfasser: Cantrell, Doreen A., Davies, Adelina A., Crumpton, Michael J.
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container_end_page 8162
container_issue 23
container_start_page 8158
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 82
creator Cantrell, Doreen A.
Davies, Adelina A.
Crumpton, Michael J.
description As judged by indirect immunofluorescence, phorbol 12, 13-dibutyrate and 1-oleoyl-2-acetylglycerol induced a rapid, concentration-dependent decrease of about 50% in the surface expression of the T3 antigen on human T lymphoblasts, and of T3 and the T-cell antigen receptor on HPB-ALL cells. Direct binding experiments using125I-labeled antibody indicated that the reduction in T3 expression corresponded to a decrease in the number of antigen molecules rather than a change in their affinity. Biochemical analyses revealed that phorbol dibutyrate induced a rapid, prominent phosphorylation of the T3 Mr26,000 γ chain and to a lesser extent of the Mr21,000 δ chain. No phosphorylation of the T3 ε chain or of the α and β subunits of the T-cell antigen receptor was detected. The data suggest that protein kinase C induces a phosphorylation of the T3 γ and δ chains that may lead to the down-regulation of the T3/T-cell antigen receptor complex.
doi_str_mv 10.1073/pnas.82.23.8158
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Direct binding experiments using125I-labeled antibody indicated that the reduction in T3 expression corresponded to a decrease in the number of antigen molecules rather than a change in their affinity. Biochemical analyses revealed that phorbol dibutyrate induced a rapid, prominent phosphorylation of the T3 Mr26,000 γ chain and to a lesser extent of the Mr21,000 δ chain. No phosphorylation of the T3 ε chain or of the α and β subunits of the T-cell antigen receptor was detected. 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The data suggest that protein kinase C induces a phosphorylation of the T3 γ and δ chains that may lead to the down-regulation of the T3/T-cell antigen receptor complex.</description><subject>Antibodies</subject><subject>Antibodies, Monoclonal</subject><subject>Antigens</subject><subject>Antigens, Differentiation, T-Lymphocyte</subject><subject>Antigens, Surface</subject><subject>Cell Compartmentation - drug effects</subject><subject>Cell lines</subject><subject>Cell Membrane - metabolism</subject><subject>Diglycerides - pharmacology</subject><subject>Down regulation</subject><subject>Enzyme Activation - drug effects</subject><subject>Fluorescence</subject><subject>Humans</subject><subject>Macromolecular Substances</subject><subject>Molecules</subject><subject>Monoclonal antibodies</subject><subject>Phorbol 12,13-Dibutyrate</subject><subject>Phorbol Esters - pharmacology</subject><subject>Phorbols</subject><subject>Phosphorylation</subject><subject>Protein Kinase C - physiology</subject><subject>Receptors, Antigen, T-Cell - metabolism</subject><subject>T lymphocytes</subject><subject>T-Lymphocytes - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUtrGzEURkVpSZ2060KhRbusxtZrJM2iCzN9JNTQENy1kGXJnjAjDSM5jaE_vpracZtNVoL7nfMJ7gXgHUZTjASd9V7HqSRTQqcSl_IFmGBU4YKzCr0EE4SIKCQj7DU4j_EOIVSVEp2BM1pRxrmcgN9zk5p7ncIQYXDwZgjJNh5-b3KvhTX8HH754tZudq1OFmq_hjfbEPttGPZ_J2lr4ZLOlkVt2xbOfWo21sNba2yfO2Edur61D2P11a7THi7hYt9l3eyTjW_AK6fbaN8e3wvw8-uXZX1VLH58u67ni8JQwWWBRcWclhK70lm6qjhhnLlSytIYrLGjpUCCO06FoMaQipVutRac4DUiVApOL8CnQ2-_W3V2baxPg25VPzSdHvYq6EY9TXyzVZtwr2iFGSfZnx18M4QYB-tOKkZqPIMaz6AkUYSq8QzZ-PD_jyf-uPecXx7zUXxM_xUot2vbZB9SJj8-S2bg_QG4i3njJ4LwkiH6B_LdpdA</recordid><startdate>19851201</startdate><enddate>19851201</enddate><creator>Cantrell, Doreen A.</creator><creator>Davies, Adelina A.</creator><creator>Crumpton, Michael J.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>5PM</scope></search><sort><creationdate>19851201</creationdate><title>Activators of Protein Kinase C Down-Regulate and Phosphorylate the T3/T-Cell Antigen Receptor Complex of Human T Lymphocytes</title><author>Cantrell, Doreen A. ; 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subjects Antibodies
Antibodies, Monoclonal
Antigens
Antigens, Differentiation, T-Lymphocyte
Antigens, Surface
Cell Compartmentation - drug effects
Cell lines
Cell Membrane - metabolism
Diglycerides - pharmacology
Down regulation
Enzyme Activation - drug effects
Fluorescence
Humans
Macromolecular Substances
Molecules
Monoclonal antibodies
Phorbol 12,13-Dibutyrate
Phorbol Esters - pharmacology
Phorbols
Phosphorylation
Protein Kinase C - physiology
Receptors, Antigen, T-Cell - metabolism
T lymphocytes
T-Lymphocytes - metabolism
title Activators of Protein Kinase C Down-Regulate and Phosphorylate the T3/T-Cell Antigen Receptor Complex of Human T Lymphocytes
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