the enzyme in venom effectively inhibits A-type K+ currents in mice and cause alterations of channel gating characters, such as the shifts of steadystate activation and inactivation curves to hyperpolarization direction and changes of V1/2 and slope factor, the effects are independent of the enzymatic activity as phospholipase, overview
the enzyme in venom effectively inhibits A-type K+ currents in mice and cause alterations of channel gating characters, such as the shifts of steadystate activation and inactivation curves to hyperpolarization direction and changes of V1/2 and slope factor, the effects are independent of the enzymatic activity as phospholipase, overview
induces apoptotic death of human leukemia K562 cells in a concentration- and time-dependent manner. Degradation of procaspases, production of tBid, loss of mitochondrial membrane potential, Bcl-2 degradation, mitochondrial translocation of Bax, and cytochrome c release in PLA2-treated cells. PLA2 treatment increases Fas and FasL protein expression and activates p38 MAPK (mitogen-activated protein kinase) and JNK (c-Jun NH2-terminal kinase) in K562 cells. SB202190 pretreatment promotes the cytotoxic effect of PLA2 toward K562 cells in a time-dependent manner. SP600125 (JNK inhibitor) abolishes the cytotoxic effect of PLA2 and PLA2-induced autocrine Fas death pathway
PLA2 induces caspase-dependent death in human SK-N-SH cells. PLA2 treatment induces Fas and FasL protein expression, leads to activation of p38 MAPK, inactivation of ERK, reactive oxygen species generation and elevation in intracellular Ca2+ concentration. PLA2-induced cell death is, in part, elicited by upregulation of Fas and FasL, which is regulated by Ca2+- and reactive oxygen species-evoked p38 MAPK activation, and suggests that non-catalytic PLA2 plays a role for the signaling pathway
site-directed mutagenesis, the mutants with an extra Met before Asn1 or substituting Asn1 with Met still retain approximately 40.9% and 82.9% membrane-damaging activity of the native enzyme, respectively. Mutations on the N-terminal region do not greatly affect the Ca2+-binding ability but cause a precipitous drop in PLA2 activity. The gross conformation of the mutant is altered compared to the native enzyme, overview. The enzymatic activity of the mutant is approximately 5.3% of that of native PLA2
removal of N-terminal heptapeptide causes a complete loss of membrane-damaging activity, whilst the mutants with an extra Met before Asn1 or substituting Asn1 with Met still retain approximately 40.9% and 82.9% membrane-damaging activity of the native enzyme, respectively. Mutations on the N-terminal region do not greatly affect the Ca2+-binding ability but cause a precipitous drop in PLA2 activity. The gross conformation of the mutants is altered compared to the native enzyme, overview. The enzymatic activity of mutants M-PLA2, PLA2(N1M) and PLA2(DELTAN7) are approximately 3.6%, 5.3% and 0.6% of that of native PLA2
removal of N-terminal heptapeptide causes a complete loss of membrane-damaging activity, whilst the mutants with an extra Met before Asn1 or substituting Asn1 with Met still retain approximately 40.9% and 82.9% membrane-damaging activity of the native enzyme, respectively. Mutations on the N-terminal region do not greatly affect the Ca2+-binding ability but cause a precipitous drop in PLA2 activity. The gross conformation of the mutants is altered compared to the native enzyme, overview. The enzymatic activity of mutants M-PLA2, PLA2(N1M) and PLA2(DELTAN7) are approximately 3.6%, 5.3% and 0.6% of that of native PLA2
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
native PLA2 is labeled with NTSB and then refolded according to the same procedure for refolding of mutated PLA2. The refolded PLA2 exhibited enzymatic activity and electrophoretic mobility indistinguishable from those of native PLA2
Chiou, Y.; Cheng, Y.; Kao, P.; Wang, J.; Chang, L.
Mutations on the N-terminal region abolish differentially the enzymatic activity, membrane-damaging activity and cytotoxicity of Taiwan cobra phospholipase A2
Upregulation of Fas and FasL in Taiwan cobra phospholipase A2-treated human neuroblastoma SK-N-SH cells through ROS- and Ca2+-mediated p38 MAPK activation
Taiwan cobra phospholipase A2-elicited JNK activation is responsible for autocrine fas-mediated cell death and modulating Bcl-2 and Bax protein expression in human leukemia K562 cells