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spelling todo:paper_08986568_v7_n4_p331_Vila2023-10-03T15:44:03Z An inositol phosphoglycan from Trypanosoma cruzi inhibits ACTH action in calf adrenocortical cells Vila, M.D.C. Cozza, E.N. Lima, C. Ramirez, M.I. De Lederkremer, R.M. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, M.D.C.
Cozza, E.N.
Lima, C.
Ramirez, M.I.
De Lederkremer, R.M.
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.
format JOUR
author Vila, M.D.C.
Cozza, E.N.
Lima, C.
Ramirez, M.I.
De Lederkremer, R.M.
author_facet Vila, M.D.C.
Cozza, E.N.
Lima, C.
Ramirez, M.I.
De Lederkremer, R.M.
author_sort Vila, M.D.C.
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
url http://hdl.handle.net/20.500.12110/paper_08986568_v7_n4_p331_Vila
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