◀ Back to CASP3

CASP3 — GRAP2

Text-mined interactions from Literome

Galán et al., J Biol Chem 2000 (Necrosis) : In a similar manner, p38 ( MAPK ) phosphorylation was not affected by the caspase inhibitors Z-VAD and DEVD-CHO, which nevertheless prevented apoptosis
Lynch et al., Eur J Neurosci 2002 (MAP Kinase Signaling System) : Analysis of colocalization of activated caspase-3 with activated p38 ( p-p38 ) suggested that p-p38 was necessary for activation of caspase-3 ; while in vitro analysis indicated that the IL-1beta induced increase in caspase-3 activity was abrogated by the p38 inhibitor, SB203580
Kim et al., Toxicol Appl Pharmacol 2004 (Necrosis) : P38 mediated caspase activation regulates mercury induced apoptosis and p38 mediated TNFalpha regulates necrosis in these cells
Kaushal et al., American journal of physiology. Renal physiology 2004 : Inhibition of ERK1/2 phosphorylation but not P38 and JNK kinase increased caspase-3 and -9 activation ; however, this activation was far less than induced by inhibition of Akt phosphorylation
De Chiara et al., J Biol Chem 2006 (MAP Kinase Signaling System) : Both cytochrome c release and caspase activation triggered by p38 MAPK activation and Bcl-2 phosphorylation are absent in embryonic fibroblasts from p38alpha knock-out mice ( p38alpha ( -/- ) MEF ), whereas they occur within 12 h of serum withdrawal in p38alpha ( +/+ ) MEF ; moreover, they can be prevented by p38 MAPK inhibitors and are not associated with the synthesis of the proapoptotic proteins Bax and Fas
Wang et al., Apoptosis 2007 (MAP Kinase Signaling System) : Inhibition of ERK1/2 with PD98059 caused further enhancement in apoptosis and caspase-3 and 9 activity, while a selective p38 MAPK inhibitor, SB203580 and JNK inhibitor, SP600125 significantly inhibited E. coli induced apoptosis and caspase-3 and 9 activity in U937 cells
Wang et al., Biomed Pharmacother 2009 : P38MAPK regulates caspase-3 by binding to caspase-3 in nucleus of human hepatoma Bel-7402 cells during anti-Fas antibody- and actinomycin D-induced apoptosis
Mao et al., Cell Res 2008 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive) : Treatment of K562 cells with shikonin ( e.g., 0.5 muM ) resulted in profound induction of apoptosis accompanied by rapid generation of reactive oxygen species ( ROS ), striking activation of c-Jun-N-terminal kinase (JNK) and p38 , marked release of the mitochondrial proteins cytochrome c and Smac/DIABLO, activation of caspase-9 and -3 , and cleavage of PARP
Berg et al., FEBS J 2009 (Multiple Myeloma) : Although TRAIL induced stimulation of c-Jun N-terminal kinase and p38 was caspase dependent in a cell type-specific fashion, activation of nuclear factor kappaB and p42/44 was caspase independent in all cases
Lu et al., Sci China Life Sci 2010 : Full inhibition of caspase-3 activity reduced Mst1 activation and partially inhibited H2B phosphorylation ( Ser14 ), but ERK1/2, JNK1/2 and p38 activities were not affected
He et al., J Zhejiang Univ Sci B 2010 (Colorectal Neoplasms) : Caspase-3/7 and -9 activity significantly increased and the protein expression levels of JNK, p38 , and Bax, Bid, Bim, and Puma from Bcl-2 pro-apoptosis molecules also increased after the treatment with cordycepin
Wasik et al., Cell death & disease 2011 (Lymphoma, Mantle-Cell) : Agonists to CB1 and CB2 promote ceramide de novo synthesis, p38-mitogen activated protein kinase dependent activation of caspase-3 and apoptotic cell death in most MCLs
Slawinska-Brych et al., Leuk Res 2013 (Multiple Myeloma) : The combination of simvastatin and thalidomide augmented caspase 8 and 3 activation , and the additional application of p38 MAPK inhibitor resulted in enhanced apoptosis of MM cells concomitant with increased caspase 9 and 3 activation, as well as JNK phosphorylation
Shiragami et al., Int J Oncol 2013 (Colonic Neoplasms) : Cerulenin treatment was associated with reduced levels of phosphorylated Akt, activation of p38 and induced caspase-3 cleavage and finally caused apoptosis
Gao et al., PloS one 2013 : We further observed that rotenone induced caspase-1 activation and mature IL-1ß release, both of which are strictly dependent on p38 mitogen activated protein kinase ( MAPK )