|Stimulation of glycolysis by placental polypeptides and inhibition by duramycin.|
|PMID: 6142764 Owner: NLM Status: MEDLINE|
|Placental polypeptides present in crude preparations of transforming growth factors stimulate glycolysis when added to quiescent 3T3 cells, normal rat kidney, and chick embryo fibroblasts. The stimulation was apparent over a time period of at least 90 min and was seen at glucose concentrations ranging from 1 to 30 mM. Duramycin, an antibiotic isolated from Streptomyces cinnamomeus, inhibits the polypeptide-stimulated and nonstimulated glycolysis of intact cells, since it permeabilizes cells to Pi and nucleotides. However, duramycin also inhibits the Na+-K+-ATPase as well as the ouabain-insensitive Mg2+-ATPase of plasma membranes. Duramycin has no effect on glycolysis catalyzed by cell-free extracts of Ehrlich ascites tumor cells in the presence of mitochondrial ATPase but partially inhibits glycolysis when ADP and Pi are generated by ATPases of plasma membrane preparations.|
|E Racker; C Riegler; M Abdel-Ghany|
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|Type: Journal Article; Research Support, Non-U.S. Gov't|
|Title: Cancer research Volume: 44 ISSN: 0008-5472 ISO Abbreviation: Cancer Res. Publication Date: 1984 Apr|
|Created Date: 1984-05-04 Completed Date: 1984-05-04 Revised Date: 2007-11-15|
Medline Journal Info:
|Nlm Unique ID: 2984705R Medline TA: Cancer Res Country: UNITED STATES|
|Languages: eng Pagination: 1364-7 Citation Subset: IM|
|APA/MLA Format Download EndNote Download BibTex|
antagonists & inhibitors
Carcinoma, Ehrlich Tumor / metabolism*
Cell Membrane / metabolism
Glycolysis / drug effects
Growth Substances / pharmacology*
Kidney Medulla / enzymology
Lactates / metabolism
Microsomes / metabolism
Peptides / pharmacology
Pregnancy Proteins / pharmacology*
Sodium-Potassium-Exchanging ATPase / antagonists & inhibitors
|0/Anti-Bacterial Agents; 0/Bacteriocins; 0/Growth Substances; 0/Lactates; 0/Peptides; 0/Pregnancy Proteins; 1391-36-2/duramycin; 50-21-5/Lactic Acid; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/Ca(2+) Mg(2+)-ATPase; EC 188.8.131.52/Sodium-Potassium-Exchanging ATPase|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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