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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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 |
work_keys_str_mv |
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