An inositol phosphoglycan from Trypanosoma cruzi inhibits ACTH action in calf adrenocortical cells

We describe the effect of an inositol phosphoglycan (IPG) purified from Trypanosoma cruzi on the stimulation of aldosterone and cAMP production by ACTH in calf adrenocortical cells. T. cruzi IPG has two galactofuranose residues (Galf) which are not frequent in other IPGs. The effect of IPG with gala...

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Autores principales:	Vila, María del Carmen, Cozza, Eduardo Néstor, Ramírez, María Isabel, Muchnik de Lederkremer, Rosa María
Publicado:	1995
Materias:	ACTH aldosterone biosynthesis Glycosyl-phosphatidylinositol aldosterone corticotropin cyclic amp glucosamine glycan derivative phosphatidylinositol phospholipase c adrenal cortex cell aldosterone release animal cell article controlled study hydrolysis nonhuman phospholipid metabolism priority journal trypanosoma cruzi Adrenal Cortex Aldosterone Alkaline Phosphatase Animal Bucladesine Carbohydrate Sequence Cattle Cells, Cultured Corticotropin Cyclic AMP Dose-Response Relationship, Drug Enzyme Activation Glycosphingolipids Hormone Antagonists Inositol Phosphates Molecular Sequence Data Phospholipase C Phosphoric Diester Hydrolases Polysaccharides Support, Non-U.S. Gov't Trypanosoma cruzi
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v7_n4_p331_Vila http://hdl.handle.net/20.500.12110/paper_08986568_v7_n4_p331_Vila
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_08986568_v7_n4_p331_Vila
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spelling	paper:paper_08986568_v7_n4_p331_Vila2023-06-08T15:49:27Z An inositol phosphoglycan from Trypanosoma cruzi inhibits ACTH action in calf adrenocortical cells Vila, María del Carmen Cozza, Eduardo Néstor Ramírez, María Isabel Muchnik de Lederkremer, Rosa María ACTH aldosterone biosynthesis Glycosyl-phosphatidylinositol aldosterone corticotropin cyclic amp glucosamine glycan derivative phosphatidylinositol phospholipase c adrenal cortex cell aldosterone release animal cell article controlled study hydrolysis nonhuman phospholipid metabolism priority journal trypanosoma cruzi Adrenal Cortex Aldosterone Alkaline Phosphatase Animal Bucladesine Carbohydrate Sequence Cattle Cells, Cultured Corticotropin Cyclic AMP Dose-Response Relationship, Drug Enzyme Activation Glycosphingolipids Hormone Antagonists Inositol Phosphates Molecular Sequence Data Phospholipase C Phosphoric Diester Hydrolases Polysaccharides Support, Non-U.S. Gov't Trypanosoma cruzi We describe the effect of an inositol phosphoglycan (IPG) purified from Trypanosoma cruzi on the stimulation of aldosterone and cAMP production by ACTH in calf adrenocortical cells. T. cruzi IPG has two galactofuranose residues (Galf) which are not frequent in other IPGs. The effect of IPG with galactofuranose residues (IPG Galf) and IPG without these residues (IPG) was investigated. It was found that IPG Galf slightly decreased the stimulation of aldosterone and cAMP production by ACTH, whereas IPG significantly inhibited ACTH-mediated accumulation of both aldosterone and cAMP. The inhibition of aldosterone content in ACTH-treated cells by IPG was dose dependent. It was also found that the pretreatment of calf adrenocortical cells with IPG inhibited the accumulation of aldosterone provoked by ACTH and dibutyryladenosine-3′,5′-cyclic monophosphate (db-cAMP). On the other hand, the activation of a GPI (glycosyl phosphatidylinositol)-phospholipase C by ACTH was evaluated. First it was found that the release of ceramide from a GPI-like molecule: a glycoinositol-phosphoceramide (LPPG) purified from T. cruzi is increased in ACTH-treated cells. Second, the release of alkaline phosphatase, a GPI-anchored enzyme, to the extracellular medium was increased in these cells by ACTH. These data suggest that ACTH activates a phospholipase C in calf adrenocortical cells, releasing IPG, which in turn may inhibit, or modulate ACTH action. © 1995. Fil:Vila, M.D.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Cozza, E.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ramirez, M.I. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:De Lederkremer, R.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1995 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v7_n4_p331_Vila http://hdl.handle.net/20.500.12110/paper_08986568_v7_n4_p331_Vila
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 biosynthesis Glycosyl-phosphatidylinositol aldosterone corticotropin cyclic amp glucosamine glycan derivative phosphatidylinositol phospholipase c adrenal cortex cell aldosterone release animal cell article controlled study hydrolysis nonhuman phospholipid metabolism priority journal trypanosoma cruzi Adrenal Cortex Aldosterone Alkaline Phosphatase Animal Bucladesine Carbohydrate Sequence Cattle Cells, Cultured Corticotropin Cyclic AMP Dose-Response Relationship, Drug Enzyme Activation Glycosphingolipids Hormone Antagonists Inositol Phosphates Molecular Sequence Data Phospholipase C Phosphoric Diester Hydrolases Polysaccharides Support, Non-U.S. Gov't Trypanosoma cruzi
spellingShingle	ACTH aldosterone biosynthesis Glycosyl-phosphatidylinositol aldosterone corticotropin cyclic amp glucosamine glycan derivative phosphatidylinositol phospholipase c adrenal cortex cell aldosterone release animal cell article controlled study hydrolysis nonhuman phospholipid metabolism priority journal trypanosoma cruzi Adrenal Cortex Aldosterone Alkaline Phosphatase Animal Bucladesine Carbohydrate Sequence Cattle Cells, Cultured Corticotropin Cyclic AMP Dose-Response Relationship, Drug Enzyme Activation Glycosphingolipids Hormone Antagonists Inositol Phosphates Molecular Sequence Data Phospholipase C Phosphoric Diester Hydrolases Polysaccharides Support, Non-U.S. Gov't Trypanosoma cruzi Vila, María del Carmen Cozza, Eduardo Néstor Ramírez, María Isabel Muchnik de Lederkremer, Rosa María An inositol phosphoglycan from Trypanosoma cruzi inhibits ACTH action in calf adrenocortical cells
topic_facet	ACTH aldosterone biosynthesis Glycosyl-phosphatidylinositol aldosterone corticotropin cyclic amp glucosamine glycan derivative phosphatidylinositol phospholipase c adrenal cortex cell aldosterone release animal cell article controlled study hydrolysis nonhuman phospholipid metabolism priority journal trypanosoma cruzi Adrenal Cortex Aldosterone Alkaline Phosphatase Animal Bucladesine Carbohydrate Sequence Cattle Cells, Cultured Corticotropin Cyclic AMP Dose-Response Relationship, Drug Enzyme Activation Glycosphingolipids Hormone Antagonists Inositol Phosphates Molecular Sequence Data Phospholipase C Phosphoric Diester Hydrolases Polysaccharides Support, Non-U.S. Gov't Trypanosoma cruzi
description	We describe the effect of an inositol phosphoglycan (IPG) purified from Trypanosoma cruzi on the stimulation of aldosterone and cAMP production by ACTH in calf adrenocortical cells. T. cruzi IPG has two galactofuranose residues (Galf) which are not frequent in other IPGs. The effect of IPG with galactofuranose residues (IPG Galf) and IPG without these residues (IPG) was investigated. It was found that IPG Galf slightly decreased the stimulation of aldosterone and cAMP production by ACTH, whereas IPG significantly inhibited ACTH-mediated accumulation of both aldosterone and cAMP. The inhibition of aldosterone content in ACTH-treated cells by IPG was dose dependent. It was also found that the pretreatment of calf adrenocortical cells with IPG inhibited the accumulation of aldosterone provoked by ACTH and dibutyryladenosine-3′,5′-cyclic monophosphate (db-cAMP). On the other hand, the activation of a GPI (glycosyl phosphatidylinositol)-phospholipase C by ACTH was evaluated. First it was found that the release of ceramide from a GPI-like molecule: a glycoinositol-phosphoceramide (LPPG) purified from T. cruzi is increased in ACTH-treated cells. Second, the release of alkaline phosphatase, a GPI-anchored enzyme, to the extracellular medium was increased in these cells by ACTH. These data suggest that ACTH activates a phospholipase C in calf adrenocortical cells, releasing IPG, which in turn may inhibit, or modulate ACTH action. © 1995.
author	Vila, María del Carmen Cozza, Eduardo Néstor Ramírez, María Isabel Muchnik de Lederkremer, Rosa María
author_facet	Vila, María del Carmen Cozza, Eduardo Néstor Ramírez, María Isabel Muchnik de Lederkremer, Rosa María
author_sort	Vila, María del Carmen
title	An inositol phosphoglycan from Trypanosoma cruzi inhibits ACTH action in calf adrenocortical cells
title_short	An inositol phosphoglycan from Trypanosoma cruzi inhibits ACTH action in calf adrenocortical cells
title_full	An inositol phosphoglycan from Trypanosoma cruzi inhibits ACTH action in calf adrenocortical cells
title_fullStr	An inositol phosphoglycan from Trypanosoma cruzi inhibits ACTH action in calf adrenocortical cells
title_full_unstemmed	An inositol phosphoglycan from Trypanosoma cruzi inhibits ACTH action in calf adrenocortical cells
title_sort	inositol phosphoglycan from trypanosoma cruzi inhibits acth action in calf adrenocortical cells
publishDate	1995
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v7_n4_p331_Vila http://hdl.handle.net/20.500.12110/paper_08986568_v7_n4_p331_Vila
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An inositol phosphoglycan from Trypanosoma cruzi inhibits ACTH action in calf adrenocortical cells

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