Document Detail


Effects of GM1-ganglioside and alpha-sialyl cholesterol on amino acid uptake, protein synthesis, and Na+,K(+)-ATPase activity in superior cervical and nodose ganglia excised from adult rats.
MedLine Citation:
PMID:  1965679     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We examined the effect of GM1-ganglioside in combination with cholera toxin B, and synthetic alpha-sialyl cholesterol (alpha-SC) on neutral amino acid (tritiated alpha-aminoisobutyric acid, [3H]AIB) uptake, protein synthesis [( 3H]leucine incorporation), and Na+,K(+)-ATPase activity in isolated superior cervical ganglia (SCG) and nodose ganglia (NG) from adult rats after aerobic incubation, usually for 2 h at 37 degrees C in vitro. Cholera toxin B, that specifically masks the oligosaccharide chain of GM1-ganglioside, antagonized the GM1-induced changes in [3H]AIB uptake, [3H]leucine incorporation, and Na+,K(+)-ATPase activity almost completely in SCG, but partially in NG. Although cholesterol itself had little effect on either [3H]AIB uptake and Na+,K(+)-ATPase activity both in SCG and NG, alpha-SC caused considerable reduction of both amino acid uptake and the transport enzyme activity in each ganglia. However, cholesterol was more effective than alpha-SC in decreasing [3H]leucine incorporation in either ganglia. Whereas addition of EGTA markedly reduced either GM1-induced or alpha-SC-induced change in [3H]leucine incorporation into acid-insoluble fraction in both SCG and NG, application of Ca2+ ionophore produced considerable recovery of the protein synthesis from the inhibited level by Ca2(+)-deprivation. ATP and creatine phosphate contents in SCG were elevated by the presence of GM1 or alpha-SC, whereas [3H]AIB uptake and Na+,K(+)-ATPase activity were inhibited, suggesting that utilization for membrane transport was diminished as a result of GM1- or alpha-SC-induced decrease of ATPase activity.
Authors:
M Ando; Y Nakashima; Y Nagata
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular and chemical neuropathology / sponsored by the International Society for Neurochemistry and the World Federation of Neurology and research groups on neurochemistry and cerebrospinal fluid     Volume:  13     ISSN:  1044-7393     ISO Abbreviation:  Mol. Chem. Neuropathol.     Publication Date:    1990 Aug-Oct
Date Detail:
Created Date:  1991-07-15     Completed Date:  1991-07-15     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  8910358     Medline TA:  Mol Chem Neuropathol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  33-46     Citation Subset:  IM    
Affiliation:
Department of Physiology, Fujita Health University School of Medicine, Aichi, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / metabolism*
Aminoisobutyric Acids / pharmacokinetics*
Animals
Cholera Toxin / pharmacology
Cholesterol Esters / pharmacology*
Female
G(M1) Ganglioside / pharmacology*
Ganglia, Sympathetic / metabolism*
Male
Nerve Tissue Proteins / biosynthesis*
Nodose Ganglion / metabolism*
Rats
Sialic Acids / pharmacology*
Sodium-Potassium-Exchanging ATPase / metabolism*
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Aminoisobutyric Acids; 0/Cholesterol Esters; 0/Nerve Tissue Proteins; 0/Sialic Acids; 113108-90-0/N-acetylneuraminyl cholesterol; 37758-47-7/G(M1) Ganglioside; 62-57-7/2-aminoisobutyric acid; 9012-63-9/Cholera Toxin; EC 3.6.3.9/Sodium-Potassium-Exchanging ATPase

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


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