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J. Biol. Chem., Vol. 267, Issue 4, 2164-2172, Feb, 1992
E Clementi, H Scheer, D Zacchetti, C Fasolato, T Pozzan and J Meldolesi
Receptor-activated Ca2+ influx was investigated in PC12 cells clones loaded
with fura-2. Cells were stimulated in a Ca(2+)-free medium and studied
after reintroduction of the cation or addition of Mn2+ into the medium. A
first influx component, independent of receptor activation and sustained by
depletion of the intracellular inositol 1,4,5- trisphosphate sensitive Ca2+
store (store-dependent Ca2+ influx, SDCI), was identified by experiments
with carbachol followed by atropine and with agents that induce store
discharge without polyphosphoinositide hydrolysis: thapsigargin, an
inhibitor of Ca(2+)-ATPase activity; ryanodine and caffeine, activators of
the ryanodine receptor. A second component of Ca2+ influx, induced by
carbachol and rapidly blocked by atropine, relies on receptor-effector
coupling via G protein(s) different from that (those) involved in
phospholipase C activation. SDCI and receptor-coupled influx are similar in
their voltage dependence and insensitivity to forskolin and phorbol esters
but they differ with respect to their Mn2+ permeability and their
sensitivity to the SC 38249 imidazole blocker. The two components might
play different roles. SDCI might act as a safety device to prevent Ca2+
store depletion whereas receptor-dependent influx might control
physiological functions such as secretion and growth.
Receptor-activated Ca2+ influx. Two independently regulated mechanisms of influx stimulation coexist in neurosecretory PC12 cells
Department of Pharmacology, University of Milano, Italy.
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