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Stimulation of Glycolysis and Amino acid Uptake in NRK-49F Cells by Transforming Growth Factor β and Epidermal Growth Factor

Glycolysis in normal resting rat kidney cells (NRK-49F) was stimulated by a 2-hr exposure to transforming growth factors prior to assay. Transforming growth factor β (TGF-β ) was effective when added alone, and further addition of epidermal growth factor (EGF) had little effect. The stimulation by T...

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Published in:Proceedings of the National Academy of Sciences - PNAS 1985-03, Vol.82 (5), p.1350-1353
Main Authors: Boerner, Paula, Resnick, Ross J., Racker, Efraim
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creator Boerner, Paula
Resnick, Ross J.
Racker, Efraim
description Glycolysis in normal resting rat kidney cells (NRK-49F) was stimulated by a 2-hr exposure to transforming growth factors prior to assay. Transforming growth factor β (TGF-β ) was effective when added alone, and further addition of epidermal growth factor (EGF) had little effect. The stimulation by TGF-β was abolished when cycloheximide was present during the incubation, suggesting that protein synthesis is required for the effect. Incubation of the cells with 25 mM methionine abolished the stimulation of glycolysis by TGF-β . The uptake of methylaminoisobutyrate via system A was stimulated by either TGF-β or EGF. The >3-fold stimulation of uptake by 1 ng of pure TGF-β per ml was usually somewhat enhanced on addition of 0.5 ng of EGF per ml. Moreover, an antiserum against EGF receptor partially depressed the response to TGF-β , suggesting some overlapping interactions of EGF and TGF-β .
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Transforming growth factor β (TGF-β ) was effective when added alone, and further addition of epidermal growth factor (EGF) had little effect. The stimulation by TGF-β was abolished when cycloheximide was present during the incubation, suggesting that protein synthesis is required for the effect. Incubation of the cells with 25 mM methionine abolished the stimulation of glycolysis by TGF-β . The uptake of methylaminoisobutyrate via system A was stimulated by either TGF-β or EGF. The &gt;3-fold stimulation of uptake by 1 ng of pure TGF-β per ml was usually somewhat enhanced on addition of 0.5 ng of EGF per ml. Moreover, an antiserum against EGF receptor partially depressed the response to TGF-β , suggesting some overlapping interactions of EGF and TGF-β .</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>3871948</pmid><doi>10.1073/pnas.82.5.1350</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record>
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identifier ISSN: 0027-8424
ispartof Proceedings of the National Academy of Sciences - PNAS, 1985-03, Vol.82 (5), p.1350-1353
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1091-6490
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_397258
source JSTOR Archival Journals and Primary Sources Collection; PubMed Central
subjects 3T3 cells
Amino acids
Amino Acids - metabolism
Animals
Biological and medical sciences
Biological Transport - drug effects
Blood Platelets - analysis
Cell growth
Cell lines
Cell physiology
Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes
Cells, Cultured
Cycloheximide - pharmacology
epidermal growth factor
Epidermal Growth Factor - pharmacology
Fundamental and applied biological sciences. Psychology
Glycolysis
Glycolysis - drug effects
Growth Substances - pharmacology
Kidney
Kidney cells
Kinetics
Lactates
Methionine - pharmacology
Molecular and cellular biology
Peptides - pharmacology
Rats
Receptors
transforming growth factor beta
Transforming Growth Factors
Tumor cell line
Tumors
title Stimulation of Glycolysis and Amino acid Uptake in NRK-49F Cells by Transforming Growth Factor β and Epidermal Growth Factor
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