Calcium Entry, Calcium Redistribution, and Exocytosis
: At a given cytosolic domain of a chromaffin cell, the rate and amplitude of the Ca2+ concentration, [Ca2+]c, depend on at least three efficient regulatory mechanisms: (1) the plasmalemmal Ca2+ channels; (2) the endoplasmic reticulum (ER); and (3) the mitochondria. High‐voltage activated Ca2+ chann...
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| Published in | Annals of the New York Academy of Sciences Vol. 971; no. 1; pp. 108 - 116 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford, UK
Blackwell Publishing Ltd
01.10.2002
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0077-8923 1749-6632 |
| DOI | 10.1111/j.1749-6632.2002.tb04444.x |
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| Abstract | : At a given cytosolic domain of a chromaffin cell, the rate and amplitude of the Ca2+ concentration, [Ca2+]c, depend on at least three efficient regulatory mechanisms: (1) the plasmalemmal Ca2+ channels; (2) the endoplasmic reticulum (ER); and (3) the mitochondria. High‐voltage activated Ca2+ 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 [Ca2+]c. Targeted aequorin and confocal microscopy show that Ca2+ entry through Ca2+ channels can refill the ER to near millimolar concentrations and causes the release of ER Ca2+ (CICR). We have also seen that, depending on its degree of filling, the ER may act as a sink or source of Ca2+ that modulates the release of catecholamine. Targeted aequorins with different Ca2+ affinities show that mitochondria undergo surprisingly rapid millimolar Ca2+ transients ([Ca2+]M) upon stimulation of chromaffin cells with ACh, high K+, or caffeine. Physiological stimuli generate [Ca2+]c microdomains at these functional complexes in which the local subplasmalemmal [Ca2+]c rises abruptly from 0.1 μM to about 50 μM. This triggers CICR, mitochondrial Ca2+ uptake, and exocytosis in nearby secretory active sites. That this is true is shown by the observation that protonophores abolish mitochondrial Ca2+ 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 Ca2+ redistribution to the cytoskeleton, through CICR and/or mitochondrial Ca2+ release. |
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| AbstractList | 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.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. : At a given cytosolic domain of a chromaffin cell, the rate and amplitude of the Ca2+ concentration, [Ca2+]c, depend on at least three efficient regulatory mechanisms: (1) the plasmalemmal Ca2+ channels; (2) the endoplasmic reticulum (ER); and (3) the mitochondria. High‐voltage activated Ca2+ 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 [Ca2+]c. Targeted aequorin and confocal microscopy show that Ca2+ entry through Ca2+ channels can refill the ER to near millimolar concentrations and causes the release of ER Ca2+ (CICR). We have also seen that, depending on its degree of filling, the ER may act as a sink or source of Ca2+ that modulates the release of catecholamine. Targeted aequorins with different Ca2+ affinities show that mitochondria undergo surprisingly rapid millimolar Ca2+ transients ([Ca2+]M) upon stimulation of chromaffin cells with ACh, high K+, or caffeine. Physiological stimuli generate [Ca2+]c microdomains at these functional complexes in which the local subplasmalemmal [Ca2+]c rises abruptly from 0.1 μM to about 50 μM. This triggers CICR, mitochondrial Ca2+ uptake, and exocytosis in nearby secretory active sites. That this is true is shown by the observation that protonophores abolish mitochondrial Ca2+ 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 Ca2+ redistribution to the cytoskeleton, through CICR and/or mitochondrial Ca2+ release. A bstract : 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 μM to about 50 μM. 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. 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. |
| Author | CUCHILLO-IBÁÑEZ, INMACULADA ARROYO, GLORIA ALBILLOS, ALMUDENA FUENTEALBA, JORGE GARCÍA, ANTONIO G. ALDEA, MARCOS |
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| Snippet | : At a given cytosolic domain of a chromaffin cell, the rate and amplitude of the Ca2+ concentration, [Ca2+]c, depend on at least three efficient regulatory... A bstract : 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... 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... |
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| SubjectTerms | Animals Binding Sites Caffeine - pharmacology Calcium - metabolism calcium signal Catecholamines - metabolism Cattle chromaffin cell Chromaffin Cells - metabolism Cytoskeleton Endoplasmic Reticulum - metabolism Exocytosis Humans Kinetics Models, Biological Potassium - metabolism Potassium - pharmacology Protein Structure, Tertiary |
| Title | Calcium Entry, Calcium Redistribution, and Exocytosis |
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