| Importance of the malate-aspartate shuttle for the reoxidation of glycolytically produced NADH and for cell aggregation in porcine blood platelets. | |
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MedLine Citation:
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PMID: 3687299 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Malate dehydrogenase (EC 1.1.1.37) and aspartate aminotransferase (EC 2.6.1.1) are present in porcine blood platelets in both mitochondria and the cytosol. The latter enzyme is inhibited in a typical way by aminooxycompounds and cycloserine. Blocking of aminotransferase or inhibition of the mitochondrial dicarboxylate carrier by butylmalonate stimulates lactate production by intact platelets and inhibits their aggregation induced by ADP or collagen. These results indicate that the reoxidation of cytosolic NADH via the malate-aspartate shuttle is important for covering the energy demand of platelets necessary for their stimulation. |
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Authors:
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M Tomasiak |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Acta biochimica Polonica Volume: 34 ISSN: 0001-527X ISO Abbreviation: Acta Biochim. Pol. Publication Date: 1987 |
Date Detail:
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Created Date: 1988-01-21 Completed Date: 1988-01-21 Revised Date: 2003-11-14 |
Medline Journal Info:
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Nlm Unique ID: 14520300R Medline TA: Acta Biochim Pol Country: POLAND |
Other Details:
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Languages: eng Pagination: 269-84 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, Medical Academy, Bialystok, Poland. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Aspartate Aminotransferases / antagonists & inhibitors, blood Aspartic Acid / blood* Blood Platelets / metabolism* Cytosol / enzymology Glycolysis* Malate Dehydrogenase / blood Malates / blood* Mitochondria / enzymology NAD / blood* Oxidation-Reduction Oxygen Consumption / drug effects Platelet Aggregation* Swine Uncoupling Agents / pharmacology |
| Chemical | |
Reg. No./Substance:
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0/Malates; 0/Uncoupling Agents; 53-84-9/NAD; 56-84-8/Aspartic Acid; 6915-15-7/malic acid; EC 1.1.1.37/Malate Dehydrogenase; EC 2.6.1.1/Aspartate Aminotransferases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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