Document Detail


A study on the regulation of N-glycoloylneuraminic acid biosynthesis and utilization in rat and mouse liver.
MedLine Citation:
PMID:  2249689     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The relative contribution of N-glycoloyl-beta-D-neuraminic acid (Neu5Gc) to total sialic acids expressed in mouse and rat liver glycoconjugates was found to be 95% and 11%, respectively. This considerable difference in sialic acid composition made these two tissues suitable models for a comparative investigation into the regulation of Neu5Gc biosynthesis and utilization. An examination of the CMP-glycoside specificity of Golgi-associated sialyltransferases using CMP-N-acetyl-beta-D-neuraminic acid (CMP-Neu5Ac) and CMP-Neu5Gc revealed no significant tissue-dependent differences. The Golgi membrane CMP-sialic acid transport system from rat liver did, however, exhibit a slightly higher internalisation rate for CMP-Neu5Ac, though no preferential affinity for this sugar nucleotide over CMP-Neu5Gc was observed. In experiments, where Golgi membrane preparations were incubated with an equimolar mixture of labelled CMP-Neu5Ac and CMP-Neu5Gc, no significant tissue-dependent differences in [14C]sialic acid composition were observed, either in the luminal soluble sialic acid fraction or in the precipitable sialic acid fraction, results which are consistent with the above observations. From this experiment, evidence was also obtained for the presence of a Golgi-lumen-associated CMP--sialic acid hydrolase which exhibited no apparent specificity for either CMP-Neu5Ac or CMP-Neu5Gc. The specific activity of the CMP-Neu5Ac hydroxylase, the enzyme responsible for the biosynthesis of Neu5Gc, was found to be 28-fold greater in high-speed supernatants of mouse liver than of rat liver. No hydroxylase activity was detected in the Golgi membrane preparations. It is therefore proposed that the cytoplasmic ratio of CMP-Neu5Ac and CMP-Neu5Gc produced by the hydroxylase, remains largely unmodified after CMP-glycoside uptake into the Golgi apparatus and transfer on to growing glycoconjugate glycan chains. The close relationship between the total sialic acid composition and the sialic acid pattern in the CMP-glycoside pools of the tissues lends considerable weight to this hypothesis.
Authors:
A Lepers; L Shaw; P Schneckenburger; R Cacan; A Verbert; R Schauer
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  193     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1990 Nov 
Date Detail:
Created Date:  1991-01-11     Completed Date:  1991-01-11     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  715-23     Citation Subset:  IM    
Affiliation:
Laboratoire de Chimie Biologique, Centre National de Recherche Scientifique no. 111, Université de Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq, France.
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MeSH Terms
Descriptor/Qualifier:
Animals
Chromatography, Thin Layer
Cytidine Monophosphate N-Acetylneuraminic Acid / metabolism
Female
Golgi Apparatus / metabolism
Liver / metabolism*
Male
Mice
Mice, Inbred BALB C
Neuraminic Acids / isolation & purification,  metabolism*
Rats
Rats, Inbred Strains
Sialic Acids / isolation & purification
Species Specificity
Chemical
Reg. No./Substance:
0/Neuraminic Acids; 0/Sialic Acids; 1113-83-3/N-glycolylneuraminic acid; 3063-71-6/Cytidine Monophosphate N-Acetylneuraminic Acid

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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