Regulation by insulin of cyclic nucleotide phosphodiesterase (PDE) from rat luteal cells

The effect of insulin on cyclic nucleotide phosphodiesterase (PDE) in rat luteal cells was studied. Cells were obtained from PMSG/hCG primed rats and further incubated or not with insulin. The hormone produced an increase of enzyme activity after a 10 min incubation of intact cells. Maximal stimulat...

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Autores principales: Téllez-Iñón, M.T., Ladenheim, R.G., Ulloa, R., Charreau, E.H., Tesone, M.
Formato: JOUR
Materias:
insulin
animal cell
dose response
drug mechanism
female genital system
nonhuman
pharmacokinetics
priority journal
rat
Animalia
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00185043_v19_n6_p249_TellezInon
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_00185043_v19_n6_p249_TellezInon
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spelling todo:paper_00185043_v19_n6_p249_TellezInon2023-10-03T14:15:37Z Regulation by insulin of cyclic nucleotide phosphodiesterase (PDE) from rat luteal cells Téllez-Iñón, M.T. Ladenheim, R.G. Ulloa, R. Charreau, E.H. Tesone, M. insulin animal cell dose response drug mechanism female genital system nonhuman pharmacokinetics priority journal rat Animalia The effect of insulin on cyclic nucleotide phosphodiesterase (PDE) in rat luteal cells was studied. Cells were obtained from PMSG/hCG primed rats and further incubated or not with insulin. The hormone produced an increase of enzyme activity after a 10 min incubation of intact cells. Maximal stimulation was achieved at 0.2 nM of insulin. Two peaks of cyclic nucleotide phosphodiesterase activity were resolved after chromatography of cell cytosolic extracts on DEAE-cellulose. These peaks (I and II) were active with cAMP as substrate but only peak I was active with cGMP. The enzyme activity of both peaks was increased in cells treated with insulin. Phosphodiesterase activity in the two peaks show two kinetic components for cAMP hydrolysis, one of high affinity (Km 2-4 μM) and the other of low affinity (47-56 μM). Treatment of the cells with insulin produced a 2 to 8 fold increase of the Vmax of these peaks. In addition after stimulation with insulin, the activation of peak I phosphodiesterase by calmodulin was less effective. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00185043_v19_n6_p249_TellezInon
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic insulin
animal cell
dose response
drug mechanism
female genital system
nonhuman
pharmacokinetics
priority journal
rat
Animalia
spellingShingle insulin
animal cell
dose response
drug mechanism
female genital system
nonhuman
pharmacokinetics
priority journal
rat
Animalia
Téllez-Iñón, M.T.
Ladenheim, R.G.
Ulloa, R.
Charreau, E.H.
Tesone, M.
Regulation by insulin of cyclic nucleotide phosphodiesterase (PDE) from rat luteal cells
topic_facet insulin
animal cell
dose response
drug mechanism
female genital system
nonhuman
pharmacokinetics
priority journal
rat
Animalia
description The effect of insulin on cyclic nucleotide phosphodiesterase (PDE) in rat luteal cells was studied. Cells were obtained from PMSG/hCG primed rats and further incubated or not with insulin. The hormone produced an increase of enzyme activity after a 10 min incubation of intact cells. Maximal stimulation was achieved at 0.2 nM of insulin. Two peaks of cyclic nucleotide phosphodiesterase activity were resolved after chromatography of cell cytosolic extracts on DEAE-cellulose. These peaks (I and II) were active with cAMP as substrate but only peak I was active with cGMP. The enzyme activity of both peaks was increased in cells treated with insulin. Phosphodiesterase activity in the two peaks show two kinetic components for cAMP hydrolysis, one of high affinity (Km 2-4 μM) and the other of low affinity (47-56 μM). Treatment of the cells with insulin produced a 2 to 8 fold increase of the Vmax of these peaks. In addition after stimulation with insulin, the activation of peak I phosphodiesterase by calmodulin was less effective.
format JOUR
author Téllez-Iñón, M.T.
Ladenheim, R.G.
Ulloa, R.
Charreau, E.H.
Tesone, M.
author_facet Téllez-Iñón, M.T.
Ladenheim, R.G.
Ulloa, R.
Charreau, E.H.
Tesone, M.
author_sort Téllez-Iñón, M.T.
title Regulation by insulin of cyclic nucleotide phosphodiesterase (PDE) from rat luteal cells
title_short Regulation by insulin of cyclic nucleotide phosphodiesterase (PDE) from rat luteal cells
title_full Regulation by insulin of cyclic nucleotide phosphodiesterase (PDE) from rat luteal cells
title_fullStr Regulation by insulin of cyclic nucleotide phosphodiesterase (PDE) from rat luteal cells
title_full_unstemmed Regulation by insulin of cyclic nucleotide phosphodiesterase (PDE) from rat luteal cells
title_sort regulation by insulin of cyclic nucleotide phosphodiesterase (pde) from rat luteal cells
url http://hdl.handle.net/20.500.12110/paper_00185043_v19_n6_p249_TellezInon
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