Endogenous glycosphingolipid acceptor specificity of sialosyltransferase systems in intact golgi membranes, synaptosomes, and synaptic plasma membranes from rat brain
Abstract
Preparations highly enriched in Golgi complex membranes, synaptosomes, and synaptic plasma membranes (SPM) by marker enzyme analysis and electron microscopic morphology were made from the brains of 28-day-old rats. These were incubated with cytidine 5'-monophosphate-N-acetyl(/sup 14/C)neuraminic acid (CMP-NeuAc) in a physiologic buffer, without detergents. Glycolipid sialosyltransferase activities (SATs) were measured by analyzing incorporation of radiolabeled NeuAc into endogenous membrane gangliosides. Golgi SAT was diversified in producing all the various molecular species of labeled gangliosides. Synaptosomal SAT exhibited a lower activity, but it was highly specific in its labeling pattern, with a marked preference for labeling NeuAc..cap alpha..2 ..-->.. 8NeuAc..cap alpha..2 ..-->.. 3Gal..beta..1 ..-->.. 4Glc..beta..1 ..-->.. 1Cer (GD3 ganglioside). SPM prepared from the synaptosomes retained the GD3-related SAT (or SAT-2), and the total specific activity increased, which suggests that the location of the synaptosomal activity is in the SPM. These results indicate that SAT activity in Golgi membranes differs from that in synaptosomes with regard to endogenous acceptor substrate specificity and SAT activity of synaptosomes should be located in the synaptosomal plasma membrane. This SAT could function as an ectoenzyme in concert with ecto-sialidase to modulate the GD3 and other ganglioside population in situ at the SPM of the central nervousmore »
- Authors:
- Publication Date:
- Research Org.:
- Nathan S. Kline Institute for Psychiatric Research, Orangeburg, NY (USA)
- OSTI Identifier:
- 7191242
- Resource Type:
- Journal Article
- Journal Name:
- Biochemistry; (United States)
- Additional Journal Information:
- Journal Volume: 27:10
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 62 RADIOLOGY AND NUCLEAR MEDICINE; CELL MEMBRANES; MOLECULAR STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY; GANGLIOSIDES; AUTORADIOGRAPHY; BRAIN; CARBON 14 COMPOUNDS; ORGANOIDS; RATS; ANIMALS; BODY; CARBOHYDRATES; CELL CONSTITUENTS; CENTRAL NERVOUS SYSTEM; ELECTRON MICROSCOPY; GLYCOLIPIDS; LABELLED COMPOUNDS; LIPIDS; MAMMALS; MEMBRANES; MICROSCOPY; NERVOUS SYSTEM; ORGANIC COMPOUNDS; ORGANS; RODENTS; SACCHARIDES; VERTEBRATES; 550601* - Medicine- Unsealed Radionuclides in Diagnostics
Citation Formats
Durrie, R, Saito, M, and Rosenberg, A. Endogenous glycosphingolipid acceptor specificity of sialosyltransferase systems in intact golgi membranes, synaptosomes, and synaptic plasma membranes from rat brain. United States: N. p., 1988.
Web. doi:10.1021/bi00410a036.
Durrie, R, Saito, M, & Rosenberg, A. Endogenous glycosphingolipid acceptor specificity of sialosyltransferase systems in intact golgi membranes, synaptosomes, and synaptic plasma membranes from rat brain. United States. https://doi.org/10.1021/bi00410a036
Durrie, R, Saito, M, and Rosenberg, A. 1988.
"Endogenous glycosphingolipid acceptor specificity of sialosyltransferase systems in intact golgi membranes, synaptosomes, and synaptic plasma membranes from rat brain". United States. https://doi.org/10.1021/bi00410a036.
@article{osti_7191242,
title = {Endogenous glycosphingolipid acceptor specificity of sialosyltransferase systems in intact golgi membranes, synaptosomes, and synaptic plasma membranes from rat brain},
author = {Durrie, R and Saito, M and Rosenberg, A},
abstractNote = {Preparations highly enriched in Golgi complex membranes, synaptosomes, and synaptic plasma membranes (SPM) by marker enzyme analysis and electron microscopic morphology were made from the brains of 28-day-old rats. These were incubated with cytidine 5'-monophosphate-N-acetyl(/sup 14/C)neuraminic acid (CMP-NeuAc) in a physiologic buffer, without detergents. Glycolipid sialosyltransferase activities (SATs) were measured by analyzing incorporation of radiolabeled NeuAc into endogenous membrane gangliosides. Golgi SAT was diversified in producing all the various molecular species of labeled gangliosides. Synaptosomal SAT exhibited a lower activity, but it was highly specific in its labeling pattern, with a marked preference for labeling NeuAc..cap alpha..2 ..-->.. 8NeuAc..cap alpha..2 ..-->.. 3Gal..beta..1 ..-->.. 4Glc..beta..1 ..-->.. 1Cer (GD3 ganglioside). SPM prepared from the synaptosomes retained the GD3-related SAT (or SAT-2), and the total specific activity increased, which suggests that the location of the synaptosomal activity is in the SPM. These results indicate that SAT activity in Golgi membranes differs from that in synaptosomes with regard to endogenous acceptor substrate specificity and SAT activity of synaptosomes should be located in the synaptosomal plasma membrane. This SAT could function as an ectoenzyme in concert with ecto-sialidase to modulate the GD3 and other ganglioside population in situ at the SPM of the central nervous system.},
doi = {10.1021/bi00410a036},
url = {https://www.osti.gov/biblio/7191242},
journal = {Biochemistry; (United States)},
number = ,
volume = 27:10,
place = {United States},
year = {Tue May 17 00:00:00 EDT 1988},
month = {Tue May 17 00:00:00 EDT 1988}
}