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Activation of ryanodine receptor/Ca 2+ release channels downregulates CD38 in the Namalwa B lymphoma
Author(s) -
McCarthy Tommie V.,
Datar Sue,
Mackrill John J.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01122-0
Subject(s) - ryanodine receptor , cd38 , cyclic adp ribose , second messenger system , cyclase , signal transduction , chemistry , calpain , microbiology and biotechnology , receptor , biophysics , biochemistry , biology , enzyme , stem cell , cd34
CD38 is a multifunctional ectoenzyme that catalyses formation of cyclic ADP ribose (cADPr), a second messenger that opens ryanodine receptor (RyR) Ca 2+ channels. Despite its importance in signal transduction processes, little is known about the mechanisms regulating CD38 expression levels. In the current study, ryanodine stimulation of Ca 2+ release in Namalwa cells decreased both CD38 protein abundance and cyclase activity. Reductions in cyclase activity were prevented by RyR antagonists, by lysosomal blockers, though not by calpain or proteasomal inhibitors. These findings indicate a novel negative feedback mechanism between RyR channel activity and CD38 abundance acts in cADPr signal transduction.
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