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1alpha,25-dihydroxy-vitamin-D3-induced store-operated Ca2+ influx in skeletal muscle cells. Modulation by phospholipase c, protein kinase c, and tyrosine kinases.
Vazquez, G; de Boland, A R; Boland, R L.
Afiliación
  • Vazquez G; Departamento de Biología, Bioquímica y Farmacia, Universidad Nacional del Sur, (8000) Bahía Blanca, Argentina.
J Biol Chem ; 273(51): 33954-60, 1998 Dec 18.
Article en En | MEDLINE | ID: mdl-9852048
In skeletal muscle cells the steroid hormone 1alpha, 25-dihydroxy-vitamin-D3 (1,25(OH)2D3) nongenomically promotes Ca2+ release from intracellular stores and cation influx through both L-type and store-operated Ca2+ (SOC) channels. In the present work we evaluated the regulation and kinetics of the 1, 25(OH)2D3-stimulated SOC influx in chick muscle cells. Stimulation with 10(-9) M 1,25(OH)2D3 in Ca2+-free medium resulted in a rapid (40-60 s) but transient [Ca2+]i rise, which correlated with sterol-dependent inositol 1,4,5-trisphosphate production. The SOC influx stimulated by the hormone was insensitive to both L-type channel antagonists and polyphosphoinositide-specific phospholipase C (PPI-PLC) inhibitors but was fully inhibitable by La3+ and Ni2+. PPI-PLC blockade prior to 1,25(OH)2D3 stimulation suppressed both the [Ca2+]i transient and the SOC influx. 1,25(OH)2D3-induced SOC entry was markedly increased after 3 min of treatment (30% above basal) and then rapidly reached a steady-state level. The sterol-stimulated SOC influx was prevented by protein kinase C and tyrosine kinase inhibitors but unaffected by blockade of the protein kinase A pathway. None of these inhibitors altered the thapsigargin-induced SOC entry, suggesting the operation of a signaling mechanism different from that for sterol-dependent SOC influx. The present results indicate that 1,25(OH)2D3-induced activation of PPI-PLC is upstream to Ca2+ influx through SOC channels and point for a role of both protein kinase C and tyrosine kinases but not protein kinase A in the regulation of the sterol-dependent SOCE pathway.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfolipasas de Tipo C / Proteína Quinasa C / Proteínas Tirosina Quinasas / Calcitriol / Canales de Calcio / Calcio / Músculo Esquelético Límite: Animals Idioma: En Revista: J Biol Chem Año: 1998 Tipo del documento: Article País de afiliación: Argentina Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfolipasas de Tipo C / Proteína Quinasa C / Proteínas Tirosina Quinasas / Calcitriol / Canales de Calcio / Calcio / Músculo Esquelético Límite: Animals Idioma: En Revista: J Biol Chem Año: 1998 Tipo del documento: Article País de afiliación: Argentina Pais de publicación: Estados Unidos