Inositol triphosphate participates in an oestradiol nongenomic signalling pathway involved in accelerated oviductal transport in cycling rats

Pedro A. Orihuela, Alexis Parada-Bustamante, Lidia M. Zuñiga, Horacio B. Croxatto

Resultado de la investigación: Article

22 Citas (Scopus)

Resumen

Oestradiol (E2) accelerates oviductal transport of oocytes in cycling rats through a nongenomic pathway that involves the cAMP-PKA signalling cascade. Here we examined the role of the inositol triphosphate (IP3) and mitogen-activated protein kinase (MAPK) signalling cascades in this nongenomic pathway. Oestrous rats were injected with E2 s.c. and intrabursally (i.b) with the selective inhibitors of phospholipase C (PLC) ET-18-OCH3 or MAPK PD98059. The number of eggs in the oviduct assessed 24h later showed that ET-18-OCH3 blocked E2-induced egg transport acceleration, whereas PD98059 had no effect. Other oestrous rats were treated with E2 s.c. and 1, 3 or 6 h later oviducts were excised and the levels of IP3 and phosphorylated MAPK p44/42 (activated) were determined by radioreceptor assay and western blot, respectively. Oestradiol administration increased IP3 level at 1 and 6 h after treatment, whereas activated MAPK p44/42 level was unchanged. Finally, we explored whether cAMP-PKA and PLC-IP3 signalling cascades are coupled. Inhibition of adenylyl cyclase by i.b. injection of SQ 22536 blocked the increase of IP3 levels induced by E2, while inhibition of PLC by ET-18-OCH3 had no effect on E2-induced PKA activity. Furthermore, activation of adenylyl cylase by Forskolin increased oviductal IP3 levels. Thus, activation of PLC-IP3 by E2 requires previous stimulation of cAMP-PKA. We conclude that the nongenomic pathway utilised by E2 to accelerate oviductal transport of oocytes in cycling rats involves successive activation of the cAMP-PKA and PLC-IP3 signalling cascades and does not require activation of MAPK. These findings clearly illustrate a non-genomic pathway triggered by E2 that regulates a complex physiologic process accomplished by an entire organ.

Idioma originalEnglish
Páginas (desde-hasta)579-588
Número de páginas10
PublicaciónJournal of Endocrinology
Volumen188
N.º3
DOI
EstadoPublished - mar 2006

Huella dactilar

Type C Phospholipases
Inositol
Mitogen-Activated Protein Kinases
Estradiol
Oviducts
Oocytes
Radioligand Assay
Colforsin
Adenylyl Cyclases
Eggs
Ovum
Western Blotting
triphosphoric acid
Injections
edelfosine
2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Citar esto

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title = "Inositol triphosphate participates in an oestradiol nongenomic signalling pathway involved in accelerated oviductal transport in cycling rats",
abstract = "Oestradiol (E2) accelerates oviductal transport of oocytes in cycling rats through a nongenomic pathway that involves the cAMP-PKA signalling cascade. Here we examined the role of the inositol triphosphate (IP3) and mitogen-activated protein kinase (MAPK) signalling cascades in this nongenomic pathway. Oestrous rats were injected with E2 s.c. and intrabursally (i.b) with the selective inhibitors of phospholipase C (PLC) ET-18-OCH3 or MAPK PD98059. The number of eggs in the oviduct assessed 24h later showed that ET-18-OCH3 blocked E2-induced egg transport acceleration, whereas PD98059 had no effect. Other oestrous rats were treated with E2 s.c. and 1, 3 or 6 h later oviducts were excised and the levels of IP3 and phosphorylated MAPK p44/42 (activated) were determined by radioreceptor assay and western blot, respectively. Oestradiol administration increased IP3 level at 1 and 6 h after treatment, whereas activated MAPK p44/42 level was unchanged. Finally, we explored whether cAMP-PKA and PLC-IP3 signalling cascades are coupled. Inhibition of adenylyl cyclase by i.b. injection of SQ 22536 blocked the increase of IP3 levels induced by E2, while inhibition of PLC by ET-18-OCH3 had no effect on E2-induced PKA activity. Furthermore, activation of adenylyl cylase by Forskolin increased oviductal IP3 levels. Thus, activation of PLC-IP3 by E2 requires previous stimulation of cAMP-PKA. We conclude that the nongenomic pathway utilised by E2 to accelerate oviductal transport of oocytes in cycling rats involves successive activation of the cAMP-PKA and PLC-IP3 signalling cascades and does not require activation of MAPK. These findings clearly illustrate a non-genomic pathway triggered by E2 that regulates a complex physiologic process accomplished by an entire organ.",
author = "Orihuela, {Pedro A.} and Alexis Parada-Bustamante and Zu{\~n}iga, {Lidia M.} and Croxatto, {Horacio B.}",
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Inositol triphosphate participates in an oestradiol nongenomic signalling pathway involved in accelerated oviductal transport in cycling rats. / Orihuela, Pedro A.; Parada-Bustamante, Alexis; Zuñiga, Lidia M.; Croxatto, Horacio B.

En: Journal of Endocrinology, Vol. 188, N.º 3, 03.2006, p. 579-588.

Resultado de la investigación: Article

TY - JOUR

T1 - Inositol triphosphate participates in an oestradiol nongenomic signalling pathway involved in accelerated oviductal transport in cycling rats

AU - Orihuela, Pedro A.

AU - Parada-Bustamante, Alexis

AU - Zuñiga, Lidia M.

AU - Croxatto, Horacio B.

PY - 2006/3

Y1 - 2006/3

N2 - Oestradiol (E2) accelerates oviductal transport of oocytes in cycling rats through a nongenomic pathway that involves the cAMP-PKA signalling cascade. Here we examined the role of the inositol triphosphate (IP3) and mitogen-activated protein kinase (MAPK) signalling cascades in this nongenomic pathway. Oestrous rats were injected with E2 s.c. and intrabursally (i.b) with the selective inhibitors of phospholipase C (PLC) ET-18-OCH3 or MAPK PD98059. The number of eggs in the oviduct assessed 24h later showed that ET-18-OCH3 blocked E2-induced egg transport acceleration, whereas PD98059 had no effect. Other oestrous rats were treated with E2 s.c. and 1, 3 or 6 h later oviducts were excised and the levels of IP3 and phosphorylated MAPK p44/42 (activated) were determined by radioreceptor assay and western blot, respectively. Oestradiol administration increased IP3 level at 1 and 6 h after treatment, whereas activated MAPK p44/42 level was unchanged. Finally, we explored whether cAMP-PKA and PLC-IP3 signalling cascades are coupled. Inhibition of adenylyl cyclase by i.b. injection of SQ 22536 blocked the increase of IP3 levels induced by E2, while inhibition of PLC by ET-18-OCH3 had no effect on E2-induced PKA activity. Furthermore, activation of adenylyl cylase by Forskolin increased oviductal IP3 levels. Thus, activation of PLC-IP3 by E2 requires previous stimulation of cAMP-PKA. We conclude that the nongenomic pathway utilised by E2 to accelerate oviductal transport of oocytes in cycling rats involves successive activation of the cAMP-PKA and PLC-IP3 signalling cascades and does not require activation of MAPK. These findings clearly illustrate a non-genomic pathway triggered by E2 that regulates a complex physiologic process accomplished by an entire organ.

AB - Oestradiol (E2) accelerates oviductal transport of oocytes in cycling rats through a nongenomic pathway that involves the cAMP-PKA signalling cascade. Here we examined the role of the inositol triphosphate (IP3) and mitogen-activated protein kinase (MAPK) signalling cascades in this nongenomic pathway. Oestrous rats were injected with E2 s.c. and intrabursally (i.b) with the selective inhibitors of phospholipase C (PLC) ET-18-OCH3 or MAPK PD98059. The number of eggs in the oviduct assessed 24h later showed that ET-18-OCH3 blocked E2-induced egg transport acceleration, whereas PD98059 had no effect. Other oestrous rats were treated with E2 s.c. and 1, 3 or 6 h later oviducts were excised and the levels of IP3 and phosphorylated MAPK p44/42 (activated) were determined by radioreceptor assay and western blot, respectively. Oestradiol administration increased IP3 level at 1 and 6 h after treatment, whereas activated MAPK p44/42 level was unchanged. Finally, we explored whether cAMP-PKA and PLC-IP3 signalling cascades are coupled. Inhibition of adenylyl cyclase by i.b. injection of SQ 22536 blocked the increase of IP3 levels induced by E2, while inhibition of PLC by ET-18-OCH3 had no effect on E2-induced PKA activity. Furthermore, activation of adenylyl cylase by Forskolin increased oviductal IP3 levels. Thus, activation of PLC-IP3 by E2 requires previous stimulation of cAMP-PKA. We conclude that the nongenomic pathway utilised by E2 to accelerate oviductal transport of oocytes in cycling rats involves successive activation of the cAMP-PKA and PLC-IP3 signalling cascades and does not require activation of MAPK. These findings clearly illustrate a non-genomic pathway triggered by E2 that regulates a complex physiologic process accomplished by an entire organ.

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