Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi
Labeled sialoglycolipids were purified from tissue culture-derived trypomastigotes incubated with [3H]fetuin. Thin layer chromatography of [3H]sialoglycolipids showed three components with the same migration as gangliosides extracted from parasites incubated with [3H]palmitic acid. Neuraminidase tre...
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todo:paper_01666851_v26_n1-2_p135_Zingales2023-10-03T15:04:18Z Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi Zingales, B. Carniol, C. de Lederkremer, R.M. Colli, W. Sialic acid Sialic acid transglycosylase Sialidase Sialoglycolipid Sialyl transferase Trypanosoma cruzi alpha fetoprotein beta D galactoside alpha 2 6 sialyltransferase beta-D-galactoside alpha 2-6-sialyltransferase glycoconjugate glycolipid sialic acid derivative sialoglycolipids sialyltransferase animal article enzymology metabolism paper chromatography thin layer chromatography Trypanosoma cruzi alpha-Fetoproteins Animal Chromatography, Paper Chromatography, Thin Layer Glycoconjugates Glycolipids Sialic Acids Sialyltransferases Support, Non-U.S. Gov't Trypanosoma cruzi Labeled sialoglycolipids were purified from tissue culture-derived trypomastigotes incubated with [3H]fetuin. Thin layer chromatography of [3H]sialoglycolipids showed three components with the same migration as gangliosides extracted from parasites incubated with [3H]palmitic acid. Neuraminidase treatment or mild acid hydrolysis confirmed the presence of [3H]sialyl residues in sialoglycolipids synthesized after [3H]fetuin incubation. Labeling was not observed when parasites were incubated with free [3H]sialic acid (C7 derivative), suggesting that sialyl residues are directly transferred in vivo to gangliosides, by an enzymatic reaction possibly catalysed by a sialyl transferase (transglycosylase). Sonicated extracts of trypomastigotes incubated with [3H]fetuin catalysed the labeling of endogenous glycoconjugates as well as of bovine brain gangliosides. The transglycosylase activity was found associated with the particulate fraction and could be solubilized with Triton X-100. The specific activity of the sialic acid transglycosylase in epimastigotes is 17% of that found in trypomastigotes. Addition of an excess free sialic acid did not inhibit the reaction, suggesting that transfer does not occur via a pool of free sialic acid. © 1987. 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_01666851_v26_n1-2_p135_Zingales |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Sialic acid Sialic acid transglycosylase Sialidase Sialoglycolipid Sialyl transferase Trypanosoma cruzi alpha fetoprotein beta D galactoside alpha 2 6 sialyltransferase beta-D-galactoside alpha 2-6-sialyltransferase glycoconjugate glycolipid sialic acid derivative sialoglycolipids sialyltransferase animal article enzymology metabolism paper chromatography thin layer chromatography Trypanosoma cruzi alpha-Fetoproteins Animal Chromatography, Paper Chromatography, Thin Layer Glycoconjugates Glycolipids Sialic Acids Sialyltransferases Support, Non-U.S. Gov't Trypanosoma cruzi |
| spellingShingle |
Sialic acid Sialic acid transglycosylase Sialidase Sialoglycolipid Sialyl transferase Trypanosoma cruzi alpha fetoprotein beta D galactoside alpha 2 6 sialyltransferase beta-D-galactoside alpha 2-6-sialyltransferase glycoconjugate glycolipid sialic acid derivative sialoglycolipids sialyltransferase animal article enzymology metabolism paper chromatography thin layer chromatography Trypanosoma cruzi alpha-Fetoproteins Animal Chromatography, Paper Chromatography, Thin Layer Glycoconjugates Glycolipids Sialic Acids Sialyltransferases Support, Non-U.S. Gov't Trypanosoma cruzi Zingales, B. Carniol, C. de Lederkremer, R.M. Colli, W. Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| topic_facet |
Sialic acid Sialic acid transglycosylase Sialidase Sialoglycolipid Sialyl transferase Trypanosoma cruzi alpha fetoprotein beta D galactoside alpha 2 6 sialyltransferase beta-D-galactoside alpha 2-6-sialyltransferase glycoconjugate glycolipid sialic acid derivative sialoglycolipids sialyltransferase animal article enzymology metabolism paper chromatography thin layer chromatography Trypanosoma cruzi alpha-Fetoproteins Animal Chromatography, Paper Chromatography, Thin Layer Glycoconjugates Glycolipids Sialic Acids Sialyltransferases Support, Non-U.S. Gov't Trypanosoma cruzi |
| description |
Labeled sialoglycolipids were purified from tissue culture-derived trypomastigotes incubated with [3H]fetuin. Thin layer chromatography of [3H]sialoglycolipids showed three components with the same migration as gangliosides extracted from parasites incubated with [3H]palmitic acid. Neuraminidase treatment or mild acid hydrolysis confirmed the presence of [3H]sialyl residues in sialoglycolipids synthesized after [3H]fetuin incubation. Labeling was not observed when parasites were incubated with free [3H]sialic acid (C7 derivative), suggesting that sialyl residues are directly transferred in vivo to gangliosides, by an enzymatic reaction possibly catalysed by a sialyl transferase (transglycosylase). Sonicated extracts of trypomastigotes incubated with [3H]fetuin catalysed the labeling of endogenous glycoconjugates as well as of bovine brain gangliosides. The transglycosylase activity was found associated with the particulate fraction and could be solubilized with Triton X-100. The specific activity of the sialic acid transglycosylase in epimastigotes is 17% of that found in trypomastigotes. Addition of an excess free sialic acid did not inhibit the reaction, suggesting that transfer does not occur via a pool of free sialic acid. © 1987. |
| format |
JOUR |
| author |
Zingales, B. Carniol, C. de Lederkremer, R.M. Colli, W. |
| author_facet |
Zingales, B. Carniol, C. de Lederkremer, R.M. Colli, W. |
| author_sort |
Zingales, B. |
| title |
Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| title_short |
Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| title_full |
Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| title_fullStr |
Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| title_full_unstemmed |
Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| title_sort |
direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of trypanosoma cruzi |
| url |
http://hdl.handle.net/20.500.12110/paper_01666851_v26_n1-2_p135_Zingales |
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