[HTML][HTML] Endogenous Cleavage of Phospholipase C-β3 by Agonist-induced Activation of Calpain in Human Platelets (∗)
Y Banno, S Nakashima, T Hachiya… - Journal of Biological …, 1995 - ASBMB
Two membrane-associated phosphoinositide-specific phospholipase Cs (mPI-PLC-1 and
mPI-PLC-2) and a cytosolic enzyme (cPI-PLC) that were activated by brain G-protein βγ
subunits have been isolated from human platelets. The truncation of mPI-PLC-1 that was
mediated by μ-calpain induced much higher activation by βγ subunits (Banno, Y., Asano, T.,
and Nozawa, Y.(1994) FEBS Lett. 340, 185-188). On the basis of size and immunological
cross-reactivity, mPI-PLC-1 (155 kDa) was PLC-β3, and mPI-PLC-2 (100 kDa) was its …
mPI-PLC-2) and a cytosolic enzyme (cPI-PLC) that were activated by brain G-protein βγ
subunits have been isolated from human platelets. The truncation of mPI-PLC-1 that was
mediated by μ-calpain induced much higher activation by βγ subunits (Banno, Y., Asano, T.,
and Nozawa, Y.(1994) FEBS Lett. 340, 185-188). On the basis of size and immunological
cross-reactivity, mPI-PLC-1 (155 kDa) was PLC-β3, and mPI-PLC-2 (100 kDa) was its …