| 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. | |
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MedLine Citation:
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PMID: 1965679 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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M Ando; Y Nakashima; Y Nagata |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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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:
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Created Date: 1991-07-15 Completed Date: 1991-07-15 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8910358 Medline TA: Mol Chem Neuropathol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 33-46 Citation Subset: IM |
Affiliation:
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Department of Physiology, Fujita Health University School of Medicine, Aichi, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids
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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:
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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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