INVESTIGADORES
GENTILI Claudia Rosana
artículos
Título:
1alpha,25(OH)2D3 and PTH signaling in rat intestinal cells: activation of cytosolic PLA2
Autor/es:
GENTILI CLAUDIA; MORELLI SUSANA; RUSSO DE BOLAND ANA
Revista:
JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY
Editorial:
Elsevier
Referencias:
Lugar: USA; Año: 2004 vol. 89 p. 297 - 301
ISSN:
0960-0760
Resumen:
Abstract
In the current study, we have probed the role of cytosolic phospholipase A2 (cPLA2) activity in the cellular response to the calciotropic
hormones, 1,25,dihydroxy-vitamin D3 [1,25(OH)2D3] and PTH. Stimulation of rat enterocytes with either hormone, increased release
of arachidonic acid (AA) [3H-AA] onetwo fold in a concentration and time-dependent manner. The effect of either hormone on enterocytes
was totally reduced by preincubation with the intracellular Ca2+ chelator BAPTA-AM (5M), suggesting that the release of AA following
cell exposure to the calciotropic hormones occurs mainly through a Ca2+-dependent mechanism involving activation of Ca2+-dependent
cPLA2. Calciotropic homone stimulation of rat intestinal cells increases cPLA2 phosphorylation (three to four fold). This effect was
decreased by PD 98059 (20M), a MAP kinase inhibitor, indicating that this action is, in part, mediated through activation of the
MAP kinases ERK 1 and ERK2. Enterocytes exposure to 1,25(OH)2D3 (1 nM) or PTH (10 nM) also resulted in P-cPLA2 translocation
from cytosol to nuclei and membrane fractions, where phospholipase subtrates reside. Collectively, these data suggest that PTH and
1,25(OH)2D3 activate in duodenal cells, a Ca2+-dependent cytosolic PLA2 and attendant arachidonic acid release and that this activation
requieres prior stimulation of intracellular ERK1/2. 1,25(OH)2D3 and PTH modulation of cPLA2 activity may change membrane fluidity
and permeability and thereby affecting intestinal cell membrane function.
© 2004 Elsevier Ltd. All rights reserved.,25,dihydroxy-vitamin D3 [1,25(OH)2D3] and PTH. Stimulation of rat enterocytes with either hormone, increased release
of arachidonic acid (AA) [3H-AA] onetwo fold in a concentration and time-dependent manner. The effect of either hormone on enterocytes
was totally reduced by preincubation with the intracellular Ca2+ chelator BAPTA-AM (5M), suggesting that the release of AA following
cell exposure to the calciotropic hormones occurs mainly through a Ca2+-dependent mechanism involving activation of Ca2+-dependent
cPLA2. Calciotropic homone stimulation of rat intestinal cells increases cPLA2 phosphorylation (three to four fold). This effect was
decreased by PD 98059 (20M), a MAP kinase inhibitor, indicating that this action is, in part, mediated through activation of the
MAP kinases ERK 1 and ERK2. Enterocytes exposure to 1,25(OH)2D3 (1 nM) or PTH (10 nM) also resulted in P-cPLA2 translocation
from cytosol to nuclei and membrane fractions, where phospholipase subtrates reside. Collectively, these data suggest that PTH and
1,25(OH)2D3 activate in duodenal cells, a Ca2+-dependent cytosolic PLA2 and attendant arachidonic acid release and that this activation
requieres prior stimulation of intracellular ERK1/2. 1,25(OH)2D3 and PTH modulation of cPLA2 activity may change membrane fluidity
and permeability and thereby affecting intestinal cell membrane function.
© 2004 Elsevier Ltd. All rights reserved.3H-AA] onetwo fold in a concentration and time-dependent manner. The effect of either hormone on enterocytes
was totally reduced by preincubation with the intracellular Ca2+ chelator BAPTA-AM (5M), suggesting that the release of AA following
cell exposure to the calciotropic hormones occurs mainly through a Ca2+-dependent mechanism involving activation of Ca2+-dependent
cPLA2. Calciotropic homone stimulation of rat intestinal cells increases cPLA2 phosphorylation (three to four fold). This effect was
decreased by PD 98059 (20M), a MAP kinase inhibitor, indicating that this action is, in part, mediated through activation of the
MAP kinases ERK 1 and ERK2. Enterocytes exposure to 1,25(OH)2D3 (1 nM) or PTH (10 nM) also resulted in P-cPLA2 translocation
from cytosol to nuclei and membrane fractions, where phospholipase subtrates reside. Collectively, these data suggest that PTH and
1,25(OH)2D3 activate in duodenal cells, a Ca2+-dependent cytosolic PLA2 and attendant arachidonic acid release and that this activation
requieres prior stimulation of intracellular ERK1/2. 1,25(OH)2D3 and PTH modulation of cPLA2 activity may change membrane fluidity
and permeability and thereby affecting intestinal cell membrane function.
© 2004 Elsevier Ltd. All rights reserved.2+ chelator BAPTA-AM (5M), suggesting that the release of AA following
cell exposure to the calciotropic hormones occurs mainly through a Ca2+-dependent mechanism involving activation of Ca2+-dependent
cPLA2. Calciotropic homone stimulation of rat intestinal cells increases cPLA2 phosphorylation (three to four fold). This effect was
decreased by PD 98059 (20M), a MAP kinase inhibitor, indicating that this action is, in part, mediated through activation of the
MAP kinases ERK 1 and ERK2. Enterocytes exposure to 1,25(OH)2D3 (1 nM) or PTH (10 nM) also resulted in P-cPLA2 translocation
from cytosol to nuclei and membrane fractions, where phospholipase subtrates reside. Collectively, these data suggest that PTH and
1,25(OH)2D3 activate in duodenal cells, a Ca2+-dependent cytosolic PLA2 and attendant arachidonic acid release and that this activation
requieres prior stimulation of intracellular ERK1/2. 1,25(OH)2D3 and PTH modulation of cPLA2 activity may change membrane fluidity
and permeability and thereby affecting intestinal cell membrane function.
© 2004 Elsevier Ltd. All rights reserved.2+-dependent mechanism involving activation of Ca2+-dependent
cPLA2. Calciotropic homone stimulation of rat intestinal cells increases cPLA2 phosphorylation (three to four fold). This effect was
decreased by PD 98059 (20M), a MAP kinase inhibitor, indicating that this action is, in part, mediated through activation of the
MAP kinases ERK 1 and ERK2. Enterocytes exposure to 1,25(OH)2D3 (1 nM) or PTH (10 nM) also resulted in P-cPLA2 translocation
from cytosol to nuclei and membrane fractions, where phospholipase subtrates reside. Collectively, these data suggest that PTH and
1,25(OH)2D3 activate in duodenal cells, a Ca2+-dependent cytosolic PLA2 and attendant arachidonic acid release and that this activation
requieres prior stimulation of intracellular ERK1/2. 1,25(OH)2D3 and PTH modulation of cPLA2 activity may change membrane fluidity
and permeability and thereby affecting intestinal cell membrane function.
© 2004 Elsevier Ltd. All rights reserved.,25(OH)2D3 (1 nM) or PTH (10 nM) also resulted in P-cPLA2 translocation
from cytosol to nuclei and membrane fractions, where phospholipase subtrates reside. Collectively, these data suggest that PTH and
1,25(OH)2D3 activate in duodenal cells, a Ca2+-dependent cytosolic PLA2 and attendant arachidonic acid release and that this activation
requieres prior stimulation of intracellular ERK1/2. 1,25(OH)2D3 and PTH modulation of cPLA2 activity may change membrane fluidity
and permeability and thereby affecting intestinal cell membrane function.
© 2004 Elsevier Ltd. All rights reserved.,25(OH)2D3 activate in duodenal cells, a Ca2+-dependent cytosolic PLA2 and attendant arachidonic acid release and that this activation
requieres prior stimulation of intracellular ERK1/2. 1,25(OH)2D3 and PTH modulation of cPLA2 activity may change membrane fluidity
and permeability and thereby affecting intestinal cell membrane function.
© 2004 Elsevier Ltd. All rights reserved.,25(OH)2D3 and PTH modulation of cPLA2 activity may change membrane fluidity
and permeability and thereby affecting intestinal cell membrane function.
© 2004 Elsevier Ltd. All rights reserved.
Keywords: 1,25,Dihydroxy-vitamin D3; PTH; Rat enterocytes; cPLA2; Arachidonic acid; Signal transduction1,25,Dihydroxy-vitamin D3; PTH; Rat enterocytes; cPLA2; Arachidonic acid; Signal transduction