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J Biol Chem, Vol. 273, Issue 51, 33954-33960, December 18, 1998
,25-Dihydroxy-vitamin-D3-induced
Store-operated Ca2+ Influx in Skeletal Muscle Cells
From the Departamento de Biología, Bioquímica y
Farmacia, Universidad Nacional del Sur,
(8000) Bahía Blanca, Argentina
In skeletal muscle cells the steroid hormone
1
,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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