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CD38 — MAPK1
Text-mined interactions from Literome
Zubiaur et al., J Biol Chem 1999
:
The CD3-gamma delta epsilon transducing module mediates
CD38 induced protein-tyrosine kinase and
mitogen activated protein kinase activation in Jurkat T cells ... Despite these differences, in both cell types
CD38 ligation
resulted in protein-tyrosine kinase and
mitogen activated protein kinase activation ... However, in cells expressing chimerical CD25-zeta or CD25-epsilon receptors or in a TCR-beta- Jurkat T cell line,
CD38 ligation did not
result in tyrosine phosphorylation of the chimeric receptors, or CD3 subunits, or protein-tyrosine kinase or
mitogen activated protein kinase activation
Cho et al., World J Gastroenterol 2005
(Colonic Neoplasms) :
Neither
t10c12 nor c9t11
had any effect on HRG-beta induced phosphorylation of
ERK-1/2
Tirumurugaan et al., Am J Physiol Lung Cell Mol Physiol 2007
(MAP Kinase Signaling System) :
Stability of TNF-alpha induced
CD38 transcripts were determined in the
presence of
MAPK inhibitors after arresting the transcription with actinomycin D. Transcript stability decreased in the presence of ERK and p38 MAPK, but not the JNK, inhibitors
Crawford et al., J Virol 2011
(HIV Infections) :
The relationship between
MAPK pathway function, HIV-1 induced
activation (
CD38 and HLA-DR ), and exhaustion ( Tim-3 ) markers in circulating CD8 ( + ) T cells remains unknown
Zubiaur et al., J Immunol 1997
:
CD38 ligation
results in activation of the
Raf-1/mitogen activated protein kinase and the CD3-zeta/zeta associated protein-70 signaling pathways in Jurkat T lymphocytes ... In addition,
CD38 ligation induced Ras dependent events such as Erk-2 mobility shift and
increased Erk-2 kinase activity ... Further evidence that
Erk-2 activation is
regulated by
CD38 ligation was obtained indirectly with the observed induction of Raf-1, Lck, and Sos-1 mobility shifts, processes that are believed to be dependent, at least in part, on MAP kinase activation ... Using a protein tyrosine kinase inhibitor, herbimycin A, or a protein kinase C inhibitor, Ro-31-8220, we found that the
anti-CD38 induced
Erk-2 activation is both protein tyrosine kinase and protein kinase C dependent