Basic and acidic fibroblast growth factors modulate the epidermal growth factor receptor by a protein kinase C-independent pathway
Human acidic and basic fibroblast growth factors (aFGF and bFGF) inhibit epidermal growth factor (EGF) receptor binding in mouse Swiss 3T3 cells. Scatchard analysis indicates that aFGF and bFGF cause a decrease in the high affinity EGF receptor population, similar to that observed for activators of...
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Veröffentlicht in: | Biochemical and biophysical research communications 1989-10, Vol.164 (2), p.796-803 |
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description | Human acidic and basic fibroblast growth factors (aFGF and bFGF) inhibit epidermal growth factor (EGF) receptor binding in mouse Swiss 3T3 cells. Scatchard analysis indicates that aFGF and bFGF cause a decrease in the high affinity EGF receptor population, similar to that observed for activators of protein kinase C such as phorbol esters, platelet-derived growth factor (PDGF) and bombesin. However, unlike phorbol esters, aFGF and bFGF inhibit EGF binding in protein kinase C-deficient cells. The time course and dose response of inhibition of EGF binding by both aFGF and bFGF are very similar, with an ID
50 of approximately 0.10 ng/ml. In contrast to bombesin but like PDGF, neither aFGF nor bFGF act on the EGF receptor through a pertussis toxinsensitive G protein. These results indicate that both acidic and basic FGF depress high affinity EGF binding in Swiss 3T3 cells with similar potency through a protein kinase
C
G
i
-independent
pathway. |
doi_str_mv | 10.1016/0006-291X(89)91529-5 |
format | Article |
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50 of approximately 0.10 ng/ml. In contrast to bombesin but like PDGF, neither aFGF nor bFGF act on the EGF receptor through a pertussis toxinsensitive G protein. These results indicate that both acidic and basic FGF depress high affinity EGF binding in Swiss 3T3 cells with similar potency through a protein kinase
C
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i
-independent
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50 of approximately 0.10 ng/ml. In contrast to bombesin but like PDGF, neither aFGF nor bFGF act on the EGF receptor through a pertussis toxinsensitive G protein. These results indicate that both acidic and basic FGF depress high affinity EGF binding in Swiss 3T3 cells with similar potency through a protein kinase
C
G
i
-independent
pathway.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Bombesin - pharmacology</subject><subject>Cattle</subject><subject>Cells, Cultured</subject><subject>Epidermal Growth Factor - metabolism</subject><subject>ErbB Receptors - drug effects</subject><subject>ErbB Receptors - metabolism</subject><subject>Fibroblast Growth Factors - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Mice</subject><subject>Pertussis Toxin</subject><subject>Phorbol 12,13-Dibutyrate - pharmacology</subject><subject>Platelet-Derived Growth Factor - pharmacology</subject><subject>Protein hormones. Growth factors. Cytokines</subject><subject>Protein Kinase C - metabolism</subject><subject>Proteins</subject><subject>Virulence Factors, Bordetella - pharmacology</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE2LFDEQhoMo6-zqP1DIQWQ9tCbpdNK5LOjgFyx4UfAWqpNqJ9pfJhmXufrLTTvDgBcvVQX1VPHyEPKEs5eccfWKMaYqYfjX69a8MLwRpmrukQ1nhlWCM3mfbM7IQ3KZ0nfGOJfKXJAL0fK2adsN-f0GUnAUJk_BBV_GPnRx7gZImX6L813e0R5cnmOi4-z3A2SkeYcUl-AxjjD8S9GIDpd16A4U6BLnjGGiP8IECem2CpPHBUuZMl0g7-7g8Ig86GFI-PjUr8iXd28_bz9Ut5_ef9y-vq2c5DpXKGonQEnwNbaetQDKNUr3vvO8r4U2TnvRgJBc6qavmVYcoC5Ajyi8ZPUVeX78W0L93GPKdgzJ4TDAhPM-Wd5IrYxpCiiPoItzShF7u8QwQjxYzuyq3q5e7erVtsb-VW_Xs6en__tuRH8-Orku-2enPSQHQx9hciGdMaVrLVtVsJsjhsXFr4DRJhdwcuhDcZutn8P_c_wBi5yimw</recordid><startdate>19891031</startdate><enddate>19891031</enddate><creator>Hicks, Karen</creator><creator>Friedman, BethAnn</creator><creator>Rosner, Marsha Rich</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TO</scope><scope>H94</scope></search><sort><creationdate>19891031</creationdate><title>Basic and acidic fibroblast growth factors modulate the epidermal growth factor receptor by a protein kinase C-independent pathway</title><author>Hicks, Karen ; Friedman, BethAnn ; Rosner, Marsha Rich</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-e23c2a64ad3e8d08aa6c567fdbd1f3279c7d25a241475f30761aa367ffee2d403</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Bombesin - pharmacology</topic><topic>Cattle</topic><topic>Cells, Cultured</topic><topic>Epidermal Growth Factor - metabolism</topic><topic>ErbB Receptors - drug effects</topic><topic>ErbB Receptors - metabolism</topic><topic>Fibroblast Growth Factors - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Mice</topic><topic>Pertussis Toxin</topic><topic>Phorbol 12,13-Dibutyrate - pharmacology</topic><topic>Platelet-Derived Growth Factor - pharmacology</topic><topic>Protein hormones. Growth factors. Cytokines</topic><topic>Protein Kinase C - metabolism</topic><topic>Proteins</topic><topic>Virulence Factors, Bordetella - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hicks, Karen</creatorcontrib><creatorcontrib>Friedman, BethAnn</creatorcontrib><creatorcontrib>Rosner, Marsha Rich</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hicks, Karen</au><au>Friedman, BethAnn</au><au>Rosner, Marsha Rich</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Basic and acidic fibroblast growth factors modulate the epidermal growth factor receptor by a protein kinase C-independent pathway</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1989-10-31</date><risdate>1989</risdate><volume>164</volume><issue>2</issue><spage>796</spage><epage>803</epage><pages>796-803</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Human acidic and basic fibroblast growth factors (aFGF and bFGF) inhibit epidermal growth factor (EGF) receptor binding in mouse Swiss 3T3 cells. Scatchard analysis indicates that aFGF and bFGF cause a decrease in the high affinity EGF receptor population, similar to that observed for activators of protein kinase C such as phorbol esters, platelet-derived growth factor (PDGF) and bombesin. However, unlike phorbol esters, aFGF and bFGF inhibit EGF binding in protein kinase C-deficient cells. The time course and dose response of inhibition of EGF binding by both aFGF and bFGF are very similar, with an ID
50 of approximately 0.10 ng/ml. In contrast to bombesin but like PDGF, neither aFGF nor bFGF act on the EGF receptor through a pertussis toxinsensitive G protein. These results indicate that both acidic and basic FGF depress high affinity EGF binding in Swiss 3T3 cells with similar potency through a protein kinase
C
G
i
-independent
pathway.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2818588</pmid><doi>10.1016/0006-291X(89)91529-5</doi><tpages>8</tpages></addata></record> |
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subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Bombesin - pharmacology Cattle Cells, Cultured Epidermal Growth Factor - metabolism ErbB Receptors - drug effects ErbB Receptors - metabolism Fibroblast Growth Factors - pharmacology Fundamental and applied biological sciences. Psychology Humans Kinetics Mice Pertussis Toxin Phorbol 12,13-Dibutyrate - pharmacology Platelet-Derived Growth Factor - pharmacology Protein hormones. Growth factors. Cytokines Protein Kinase C - metabolism Proteins Virulence Factors, Bordetella - pharmacology |
title | Basic and acidic fibroblast growth factors modulate the epidermal growth factor receptor by a protein kinase C-independent pathway |
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