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Titolo:
A ryanodine fluorescent derivative reveals the presence of high-affinity ryanodine binding sites in the Golgi complex of rat sympathetic neurons, with possible functional roles in intracellular Ca2+ signaling
Autore:
Cifuentes, F; Gonzalez, CE; Fiordelisio, T; Guerrero, G; Lai, FA; Hernandez-Cruz, A;
Indirizzi:
Univ Nacl Autonoma Mexico, Inst Fisiol Celular, Dept Biofis, Mexico City 04510, DF, Mexico Univ Nacl Autonoma Mexico Mexico City DF Mexico 04510 y 04510, DF, Mexico Univ Wales Coll Med, Dept Cardiol, Cardiff CF14 4XN, S Glam, Wales Univ Wales Coll Med Cardiff S Glam Wales CF14 4XN CF14 4XN, S Glam, Wales
Titolo Testata:
CELLULAR SIGNALLING
fascicolo: 5, volume: 13, anno: 2001,
pagine: 353 - 362
SICI:
0898-6568(200105)13:5<353:ARFDRT>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENDOPLASMIC-RETICULUM; RELEASE CHANNEL; CALCIUM-RELEASE; BREFELDIN-A; APPARATUS; CELLS; RECEPTOR; MUSCLE; PROTEIN; STAIN;
Keywords:
ryanodine; Golgi complex; Ca2+ release channels; caffeine; Ca2+ stores;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Hernandez-Cruz, A Univ Nacl Autonoma Mexico, Inst Fisiol Celular, Dept Biofis, Circuito Exterior,POB 70-253, Mexico City 04510, DF, Mexico Univ Nacl Autonoma Mexico Circuito Exterior,POB 70-253 Mexico City DF Mexico 04510
Citazione:
F. Cifuentes et al., "A ryanodine fluorescent derivative reveals the presence of high-affinity ryanodine binding sites in the Golgi complex of rat sympathetic neurons, with possible functional roles in intracellular Ca2+ signaling", CELL SIGNAL, 13(5), 2001, pp. 353-362

Abstract

The plant alkaloid ryanodine (Ry) is a high-affinity modulator of ryanodine receptor (RyR) Ca2+ release channels. Although these channels are presentin a variety of cell types, their functional role in nerve cells is still puzzling. Here, a monosubstituted fluorescent Ry analogue, B-FL-X Ry, was used to reveal the distribution of RyRs in cultured rat sympathetic neurons. B-FL-X Ry competitively inhibited the binding of [H-3]Ry to rabbit skeletal muscle SR membranes, with an IC50, of 150 nM, compared to 7 nM of unlabeled Ry. Binding of B-FL-X Ry to the cytoplasm of sympathetic neurons is saturable, reversible and of high affinity. The pharmacology of B-FL-X Ry showed marked differences with unlabeled Ry, which are partially explained by its lower affinity: (1) use-dependent reversible inhibition of caffeine-induced intracellular Ca2+ release; (2) diminished voltage-gated Ca2+ influx, due to a positive shift in the activation of voltage gated Ca currents. B-FL-X Ry-stained sympathetic neurons, viewed under confocal microscopy. showed conspicuous labeling of crescent-shaped structures pertaining to the Golgi complex, a conclusion supported by experiments showing co-localization withGolgi-specific fluorescent probes and the breaking up of crescent-shaped staining after treatment with drugs that disassemble Golgi complex. The presence of RyRs to the Golgi could be confirmed with specific anti-RyR(2) antibodies, but evidence of caffeine-induced Ca2+ release from this organelle could not be obtained using fast confocal microscopy. Rather, an apparent decrease of the cytosolic Ca2+ signal was detected close to this organelle. In spite of that, short-term incubation with brefeldin A (BFA) suppressed the fast component of caffeine-induced Ca2+ release, and the Ca2+ release process lasted longer and appeared less organized. These observations, which suggest a possible role of the Golgi complex in Ca homeostasis and signalingin nerve cells, could be relevant to reports involving derangement of the Golgi complex as a probable cause of some forms of progressive neuronal degeneration, such as Alzheimer's disease and amyotrophic lateral sclerosis. (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 06:53:55