Publication Date:
1994-01-07
Description:
Selective activation of cyclic adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase type I (cAKI), but not type II, is sufficient to mediate inhibition of T cell replication induced through the antigen-specific T cell receptor-CD3 (TCR-CD3) complex. Immunocytochemistry and immunoprecipitation studies of the molecular mechanism by which cAKI inhibits TCR-CD3-dependent T cell replication demonstrated that regulatory subunit I alpha, along with its associated kinase activity, translocated to and interacted with the TCR-CD3 complex during T cell activation and capping. Regulatory subunit II alpha did not. When stimulated by cAMP, the cAKI localized to the TCR-CD3 complex may release kinase activity that, through phosphorylation, might uncouple the TCR-CD3 complex from intracellular signaling systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Skalhegg, B S -- Tasken, K -- Hansson, V -- Huitfeldt, H S -- Jahnsen, T -- Lea, T -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):84-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Medical Biochemistry, University of Oslo, Blindern, Norway.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8272870" target="_blank"〉PubMed〈/a〉
Keywords:
Carrier Proteins/analysis/*metabolism
;
Cyclic AMP/metabolism
;
Cyclic AMP-Dependent Protein Kinase Type II
;
Cyclic AMP-Dependent Protein Kinases/analysis/*metabolism
;
Enzyme Activation
;
Fluorescent Antibody Technique
;
Humans
;
Immunologic Capping
;
*Intracellular Signaling Peptides and Proteins
;
Lymphocyte Activation
;
Phosphorylation
;
Precipitin Tests
;
Receptor-CD3 Complex, Antigen, T-Cell/analysis/*metabolism
;
Signal Transduction
;
T-Lymphocytes/*enzymology/immunology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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