ACTH-mediated glucocorticoid and mineralocorticoid production is inhibited by an inositolphosphoglycan and a glycosylphosphatidylinositol- phospholipase C is activated by the hormone in mammalian adrenocortical cells
In the present paper, we report that an inositolphosphoglycan (IPG), derived from a Trypanosoma cruzi glycoinositolphosphoceramide (LPPG), is able to inhibit ACTH-mediated accumulation of a glucocorticoid, cortisol, in calf adrenocortical cells. This IPG is also able to inhibit the stimulation by AC...
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1998
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0039128X_v63_n2_p70_DeAvalos http://hdl.handle.net/20.500.12110/paper_0039128X_v63_n2_p70_DeAvalos |
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paper:paper_0039128X_v63_n2_p70_DeAvalos2023-06-08T15:03:17Z ACTH-mediated glucocorticoid and mineralocorticoid production is inhibited by an inositolphosphoglycan and a glycosylphosphatidylinositol- phospholipase C is activated by the hormone in mammalian adrenocortical cells ACTH Aldosterone Corticostero ne Cortisol Glycosylphosphatidylinositol Inositolphosphoglycan corticotropin glucocorticoid glycosylphosphatidylinositol mineralocorticoid phospholipase c adrenal cortex aldosterone release animal cell article cattle enzyme activation hydrocortisone release nonhuman trypanosoma cruzi Adrenal Cortex Adrenocorticotropic Hormone Aldosterone Animals Cattle Corticosterone Enzyme Activation Glucocorticoids Glycolipids Hydrocortisone Inositol Phosphates Male Mineralocorticoids Oligosaccharides Phosphatidylinositol Diacylglycerol-Lyase Phospholipase C Polysaccharides Rats Rats, Sprague-Dawley Trypanosoma cruzi In the present paper, we report that an inositolphosphoglycan (IPG), derived from a Trypanosoma cruzi glycoinositolphosphoceramide (LPPG), is able to inhibit ACTH-mediated accumulation of a glucocorticoid, cortisol, in calf adrenocortical cells. This IPG is also able to inhibit the stimulation by ACTH of the production of the main glucocorticoid, corticosterone and the main mineralocorticoid, aldosterone, in rat adrenocortical cells. Nitrous acid deamination confirmed that IPG is responsible for this inhibition. In order to study the involvement of glycosylphosphatidylinositol (GPI) in ACTH response in rat adrenal cortex, the activation of a phospholipase that hydrolyzes GPI (GPI-PLC) was evaluated. It was found that the release of alkaline phosphatase, a GPI-anchored enzyme, to the extracellular medium is increased in rat adrenocortical cells by ACTH treatment. In addition, ACTH stimulates the release of ceramide from the glycoinositolphosphoceramide purified from T. cruzi. These data suggest that ACTH activates a GPI-PLC in rat adrenal cortex, which is in agreement with our previous data in calf adrenocortical cells; thus, the hydrolysis of GPI provoked by ACTH takes place in different mammals and the IPG released could inhibit ACTH-mediated synthesis of aldosterone, corticosterone and cortisol. 1998 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0039128X_v63_n2_p70_DeAvalos http://hdl.handle.net/20.500.12110/paper_0039128X_v63_n2_p70_DeAvalos |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
ACTH Aldosterone Corticostero ne Cortisol Glycosylphosphatidylinositol Inositolphosphoglycan corticotropin glucocorticoid glycosylphosphatidylinositol mineralocorticoid phospholipase c adrenal cortex aldosterone release animal cell article cattle enzyme activation hydrocortisone release nonhuman trypanosoma cruzi Adrenal Cortex Adrenocorticotropic Hormone Aldosterone Animals Cattle Corticosterone Enzyme Activation Glucocorticoids Glycolipids Hydrocortisone Inositol Phosphates Male Mineralocorticoids Oligosaccharides Phosphatidylinositol Diacylglycerol-Lyase Phospholipase C Polysaccharides Rats Rats, Sprague-Dawley Trypanosoma cruzi |
| spellingShingle |
ACTH Aldosterone Corticostero ne Cortisol Glycosylphosphatidylinositol Inositolphosphoglycan corticotropin glucocorticoid glycosylphosphatidylinositol mineralocorticoid phospholipase c adrenal cortex aldosterone release animal cell article cattle enzyme activation hydrocortisone release nonhuman trypanosoma cruzi Adrenal Cortex Adrenocorticotropic Hormone Aldosterone Animals Cattle Corticosterone Enzyme Activation Glucocorticoids Glycolipids Hydrocortisone Inositol Phosphates Male Mineralocorticoids Oligosaccharides Phosphatidylinositol Diacylglycerol-Lyase Phospholipase C Polysaccharides Rats Rats, Sprague-Dawley Trypanosoma cruzi ACTH-mediated glucocorticoid and mineralocorticoid production is inhibited by an inositolphosphoglycan and a glycosylphosphatidylinositol- phospholipase C is activated by the hormone in mammalian adrenocortical cells |
| topic_facet |
ACTH Aldosterone Corticostero ne Cortisol Glycosylphosphatidylinositol Inositolphosphoglycan corticotropin glucocorticoid glycosylphosphatidylinositol mineralocorticoid phospholipase c adrenal cortex aldosterone release animal cell article cattle enzyme activation hydrocortisone release nonhuman trypanosoma cruzi Adrenal Cortex Adrenocorticotropic Hormone Aldosterone Animals Cattle Corticosterone Enzyme Activation Glucocorticoids Glycolipids Hydrocortisone Inositol Phosphates Male Mineralocorticoids Oligosaccharides Phosphatidylinositol Diacylglycerol-Lyase Phospholipase C Polysaccharides Rats Rats, Sprague-Dawley Trypanosoma cruzi |
| description |
In the present paper, we report that an inositolphosphoglycan (IPG), derived from a Trypanosoma cruzi glycoinositolphosphoceramide (LPPG), is able to inhibit ACTH-mediated accumulation of a glucocorticoid, cortisol, in calf adrenocortical cells. This IPG is also able to inhibit the stimulation by ACTH of the production of the main glucocorticoid, corticosterone and the main mineralocorticoid, aldosterone, in rat adrenocortical cells. Nitrous acid deamination confirmed that IPG is responsible for this inhibition. In order to study the involvement of glycosylphosphatidylinositol (GPI) in ACTH response in rat adrenal cortex, the activation of a phospholipase that hydrolyzes GPI (GPI-PLC) was evaluated. It was found that the release of alkaline phosphatase, a GPI-anchored enzyme, to the extracellular medium is increased in rat adrenocortical cells by ACTH treatment. In addition, ACTH stimulates the release of ceramide from the glycoinositolphosphoceramide purified from T. cruzi. These data suggest that ACTH activates a GPI-PLC in rat adrenal cortex, which is in agreement with our previous data in calf adrenocortical cells; thus, the hydrolysis of GPI provoked by ACTH takes place in different mammals and the IPG released could inhibit ACTH-mediated synthesis of aldosterone, corticosterone and cortisol. |
| title |
ACTH-mediated glucocorticoid and mineralocorticoid production is inhibited by an inositolphosphoglycan and a glycosylphosphatidylinositol- phospholipase C is activated by the hormone in mammalian adrenocortical cells |
| title_short |
ACTH-mediated glucocorticoid and mineralocorticoid production is inhibited by an inositolphosphoglycan and a glycosylphosphatidylinositol- phospholipase C is activated by the hormone in mammalian adrenocortical cells |
| title_full |
ACTH-mediated glucocorticoid and mineralocorticoid production is inhibited by an inositolphosphoglycan and a glycosylphosphatidylinositol- phospholipase C is activated by the hormone in mammalian adrenocortical cells |
| title_fullStr |
ACTH-mediated glucocorticoid and mineralocorticoid production is inhibited by an inositolphosphoglycan and a glycosylphosphatidylinositol- phospholipase C is activated by the hormone in mammalian adrenocortical cells |
| title_full_unstemmed |
ACTH-mediated glucocorticoid and mineralocorticoid production is inhibited by an inositolphosphoglycan and a glycosylphosphatidylinositol- phospholipase C is activated by the hormone in mammalian adrenocortical cells |
| title_sort |
acth-mediated glucocorticoid and mineralocorticoid production is inhibited by an inositolphosphoglycan and a glycosylphosphatidylinositol- phospholipase c is activated by the hormone in mammalian adrenocortical cells |
| publishDate |
1998 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0039128X_v63_n2_p70_DeAvalos http://hdl.handle.net/20.500.12110/paper_0039128X_v63_n2_p70_DeAvalos |
| _version_ |
1768542026518757376 |