P/Q Ca2+ channels are functionally coupled to exocytosis of the immediately releasable pool in mouse chromaffin cells

Cell Calcium ◽  
2008 ◽  
Vol 43 (2) ◽  
pp. 155-164 ◽  
Author(s):  
Yanina D. Álvarez ◽  
Lorena I. Ibañez ◽  
Osvaldo D. Uchitel ◽  
Fernando D. Marengo
Keyword(s):  
Chromaffin Cells ◽  
Releasable Pool ◽  
Ca2 Channels

scholarly journals Rapid vesicle replenishment after the immediately releasable pool exocytosis is tightly linked to fast endocytosis, and depends on basal calcium and cortical actin in chromaffin cells

2021 ◽  
Author(s):  
Mauricio Montenegro ◽  
Lucas Bayonés ◽  
José Moya‐Díaz ◽  
Cecilia Borassi ◽  
Andrés Martín Toscani ◽  
...  
Keyword(s):  
Chromaffin Cells ◽  
Cortical Actin ◽  
Releasable Pool

Prostaglandin E2Activates Ca2+Channels in Bovine Adrenal Chromaffin Cells

1991 ◽  
Vol 56 (2) ◽  
pp. 541-547 ◽  
Author(s):  
Noriko Mochizuki-Oda ◽  
Kensaku Mori ◽  
Manabu Negishi ◽  
Seiji Ito
Keyword(s):  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Adrenal Chromaffin ◽  
Ca2 Channels

Different contributions of L- and Q-type Ca2+ channels to Ca2+ signals and secretion in chromaffin cell subtypes

1997 ◽  
Vol 272 (2) ◽  
pp. C476-C484 ◽  
Author(s):  
R. B. Lomax ◽  
P. Michelena ◽  
L. Nunez ◽  
J. Garcia-Sancho ◽  
A. G. Garcia ◽  
...  
Keyword(s):  
Chromaffin Cells ◽  
Chromaffin Cell ◽  
Channel Blocker ◽  
Cell Types ◽  
Bay K 8644 ◽  
High K ◽  
Voltage Dependent ◽  
Bovine Chromaffin Cells ◽  
P Type ◽  
Ca2 Channels

In this study, we investigated the contribution of different subtypes of voltage-dependent Ca2+ channels to changes in cytosolic free Ca2+ ([Ca2+]i) and secretion in noradrenergic and adrenergic bovine chromaffin cells. In single immunocytochemically identified chromaffin cells, [Ca2+]i increased transiently during high K+ depolarization. Furnidipine and BAY K 8644, L-type Ca2+ channel blocker and activator, respectively, affected the [Ca2+]i rise more in noradrenergic than in adrenergic cells. In contrast, the Q-type Ca2+ channel blocker omega-conotoxin MVIIC inhibited the [Ca2+]i rise more in adrenergic cells. omega-Agatoxin IVA (30 nM), which blocks P-type Ca2+ channels, had little effect on the [Ca2+]i signal. The N-type Ca2+ channel blocker omega-conotoxin GVIA similarly inhibited the [Ca2+]i rise in both cell types. The effects of furnidipine, BAY K 8644, and omega-conotoxin MVIIC on K+-evoked norepinephrine and epinephrine release paralleled those effects on [Ca2+]i signals. However, omega-conotoxin GVIA and 30 nM omega-agatoxin IVA did not affect the secretion of either amine. The data suggest that, in the bovine adrenal medulla, the release of epinephrine and norepinephrine are preferentially controlled by Q- and L-type Ca2+ channels, respectively. P- and N-type Ca2+ channels do not seem to control the secretion of either catecholamine.

scholarly journals Calcium-Dependent Inhibition of L, N, and P/Q Ca2+Channels in Chromaffin Cells: Role of Mitochondria

2001 ◽  
Vol 21 (8) ◽  
pp. 2553-2560 ◽  
Author(s):  
Jesús M. Hernández-Guijo ◽  
Victoria E. Maneu-Flores ◽  
Ana Ruiz-Nuño ◽  
Mercedes Villarroya ◽  
Antonio G. García ◽  
...  
Keyword(s):  
Chromaffin Cells ◽  
Calcium Dependent ◽  
Dependent Inhibition ◽  
Ca2 Channels

scholarly journals The Bruchpilot cytomatrix determines the size of the readily releasable pool of synaptic vesicles

2013 ◽  
Vol 202 (4) ◽  
pp. 667-683 ◽  
Author(s):  
Tanja Matkovic ◽  
Matthias Siebert ◽  
Elena Knoche ◽  
Harald Depner ◽  
Sara Mertel ◽  
...  
Keyword(s):  
Synaptic Vesicles ◽  
Circular Array ◽  
Membrane Domain ◽  
Releasable Pool ◽  
Readily Releasable Pool ◽  
Family Protein ◽  
Biochemical Identification ◽  
Macromolecular Architecture ◽  
Bar Formation ◽  
Ca2 Channels

Synaptic vesicles (SVs) fuse at a specialized membrane domain called the active zone (AZ), covered by a conserved cytomatrix. How exactly cytomatrix components intersect with SV release remains insufficiently understood. We showed previously that loss of the Drosophila melanogaster ELKS family protein Bruchpilot (BRP) eliminates the cytomatrix (T bar) and declusters Ca2+ channels. In this paper, we explored additional functions of the cytomatrix, starting with the biochemical identification of two BRP isoforms. Both isoforms alternated in a circular array and were important for proper T-bar formation. Basal transmission was decreased in isoform-specific mutants, which we attributed to a reduction in the size of the readily releasable pool (RRP) of SVs. We also found a corresponding reduction in the number of SVs docked close to the remaining cytomatrix. We propose that the macromolecular architecture created by the alternating pattern of the BRP isoforms determines the number of Ca2+ channel-coupled SV release slots available per AZ and thereby sets the size of the RRP.

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