Abstract：
:At a given cytosolic domain of a chromaffin cell, the rate and amplitude of the Ca(2+) concentration, [Ca(2+)](c), depend on at least three efficient regulatory mechanisms: (1) the plasmalemmal Ca(2+) channels; (2) the endoplasmic reticulum (ER); and (3) the mitochondria. High-voltage activated Ca(2+) channels of the L, N, P/Q, and R subtypes are expressed with different densities in various mammalian species; they are regulated by G proteins coupled to purinergic and opiate receptors, as well as by voltage and the local changes of [Ca(2+)](c). Targeted aequorin and confocal microscopy show that Ca(2+) entry through Ca(2+) channels can refill the ER to near millimolar concentrations and causes the release of ER Ca(2+) (CICR). We have also seen that, depending on its degree of filling, the ER may act as a sink or source of Ca(2+) that modulates the release of catecholamine. Targeted aequorins with different Ca(2+) affinities show that mitochondria undergo surprisingly rapid millimolar Ca(2+) transients ([Ca(2+)](M)) upon stimulation of chromaffin cells with ACh, high K(+), or caffeine. Physiological stimuli generate [Ca(2+)](c) microdomains at these functional complexes in which the local subplasmalemmal [Ca(2+)](c) rises abruptly from 0.1 micro M to about 50 micro M. This triggers CICR, mitochondrial Ca(2+) uptake, and exocytosis in nearby secretory active sites. That this is true is shown by the observation that protonophores abolish mitochondrial Ca(2+) uptake and drastically increase catecholamine release by 3- to 5-fold. This increase is likely due to acceleration of vesicle transport from a reserve pool to a ready-release vesicle pool; such transport might be controlled by Ca(2+) redistribution to the cytoskeleton, through CICR and/or mitochondrial Ca(2+) release.
journal_name
Ann N Y Acad Scijournal_title
Annals of the New York Academy of Sciencesauthors
Cuchillo-Ibanez I,Albillos A,Aldea M,Arroyo G,Fuentealba J,Garcia AGdoi
10.1111/j.1749-6632.2002.tb04444.xsubject
Has Abstractpub_date
2002-10-01 00:00:00pages
108-16eissn
0077-8923issn
1749-6632journal_volume
971pub_type
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