Purification of multiple forms of glial growth factor
Glial growth factors (GGFs) were purified from bovine pituitaries using an in vitro rat Schwann cell mitogenesis assay. In addition to an approximately 34-kDa species termed GGF-I, similar in molecular mass to a previously identified molecule (Lemke, G. E., and Brockes, J. P. (1984) J. Neuroscience...
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Veröffentlicht in: | The Journal of biological chemistry 1993-08, Vol.268 (24), p.18095-18102 |
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container_title | The Journal of biological chemistry |
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creator | Goodearl, A.D. Davis, J.B. Mistry, K. Minghetti, L. Otsu, M. Waterfield, M.D. Stroobant, P. |
description | Glial growth factors (GGFs) were purified from bovine pituitaries using an in vitro rat Schwann cell mitogenesis assay. In addition to an approximately 34-kDa species termed GGF-I, similar in molecular mass to a previously identified molecule (Lemke, G. E., and Brockes, J. P. (1984) J. Neuroscience 4, 75-83), two species named GGF-II and GGF-III were characterized with apparent molecular masses of approximately 59 and approximately 45 kDa, respectively. Highly purified preparations of all species share a similar dose-dependent stimulation of Schwann cell DNA synthesis at nanomolar concentrations. Forskolin synergizes with all three GGFs, shifting their dose dependence 3-8-fold into the sub-nanomolar range. The GGFs, which contain N-linked carbohydrate groups not essential for their in vitro mitogenic effects, are three distinct members of a novel family of glial cell mitogens. |
doi_str_mv | 10.1016/S0021-9258(17)46816-5 |
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In addition to an approximately 34-kDa species termed GGF-I, similar in molecular mass to a previously identified molecule (Lemke, G. E., and Brockes, J. P. (1984) J. Neuroscience 4, 75-83), two species named GGF-II and GGF-III were characterized with apparent molecular masses of approximately 59 and approximately 45 kDa, respectively. Highly purified preparations of all species share a similar dose-dependent stimulation of Schwann cell DNA synthesis at nanomolar concentrations. Forskolin synergizes with all three GGFs, shifting their dose dependence 3-8-fold into the sub-nanomolar range. The GGFs, which contain N-linked carbohydrate groups not essential for their in vitro mitogenic effects, are three distinct members of a novel family of glial cell mitogens.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)46816-5</identifier><identifier>PMID: 8394360</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cattle ; Cells, Cultured ; Chromatography, Affinity ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Chromatography, Liquid ; DNA Replication - drug effects ; Durapatite ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Glia Maturation Factor ; Growth Inhibitors - isolation & purification ; Growth Inhibitors - pharmacology ; Hydroxyapatites ; Molecular Weight ; Nerve Tissue Proteins - isolation & purification ; Nerve Tissue Proteins - pharmacology ; Pituitary Gland - chemistry ; Protein hormones. Growth factors. Cytokines ; Proteins ; Rats ; Schwann Cells - cytology ; Schwann Cells - drug effects ; Schwann Cells - metabolism ; Sciatic Nerve - cytology</subject><ispartof>The Journal of biological chemistry, 1993-08, Vol.268 (24), p.18095-18102</ispartof><rights>1993 © 1993 ASBMB. 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In addition to an approximately 34-kDa species termed GGF-I, similar in molecular mass to a previously identified molecule (Lemke, G. E., and Brockes, J. P. (1984) J. Neuroscience 4, 75-83), two species named GGF-II and GGF-III were characterized with apparent molecular masses of approximately 59 and approximately 45 kDa, respectively. Highly purified preparations of all species share a similar dose-dependent stimulation of Schwann cell DNA synthesis at nanomolar concentrations. Forskolin synergizes with all three GGFs, shifting their dose dependence 3-8-fold into the sub-nanomolar range. The GGFs, which contain N-linked carbohydrate groups not essential for their in vitro mitogenic effects, are three distinct members of a novel family of glial cell mitogens.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Cells, Cultured</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Gel</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Chromatography, Liquid</subject><subject>DNA Replication - drug effects</subject><subject>Durapatite</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glia Maturation Factor</subject><subject>Growth Inhibitors - isolation & purification</subject><subject>Growth Inhibitors - pharmacology</subject><subject>Hydroxyapatites</subject><subject>Molecular Weight</subject><subject>Nerve Tissue Proteins - isolation & purification</subject><subject>Nerve Tissue Proteins - pharmacology</subject><subject>Pituitary Gland - chemistry</subject><subject>Protein hormones. Growth factors. Cytokines</subject><subject>Proteins</subject><subject>Rats</subject><subject>Schwann Cells - cytology</subject><subject>Schwann Cells - drug effects</subject><subject>Schwann Cells - metabolism</subject><subject>Sciatic Nerve - cytology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMoun78BKEHET1UM0mapCcR8QsEBRW8hTRNdiPtZk1axX9v6y7r0VwGMs_MOzwIHQI-Awz8_BljAnlJCnkC4pRxCTwvNtAEsKQ5LeBtE03WyA7aTekdD4-VsI22JS0Z5XiCiqc-eueN7nyYZ8Flbd90ftHYzIXYpvFn2njdZNMYvrpZ5rTpQtxHW043yR6s6h56vbl-ubrLHx5v768uH3LDSt7lAjB1QIkkQtSYMBCMVkRIXWkoCRWuYpV1NZNVyaCGunLCMl7IkkoKxhZ0Dx0v9y5i-Oht6lTrk7FNo-c29EkBFwIzTAewWIImhpSidWoRfavjtwKsRl3qV5caXSgQ6leXGgMOVwF91dp6PbXyM_SPVn2djG5c1HPj0xqjggNI-MNmfjr78tGqygczs60iXCrCFEhcjmkXS8wOzj69jSoZb-fG1sOI6VQd_D_3_gAbspCw</recordid><startdate>19930825</startdate><enddate>19930825</enddate><creator>Goodearl, A.D.</creator><creator>Davis, J.B.</creator><creator>Mistry, K.</creator><creator>Minghetti, L.</creator><creator>Otsu, M.</creator><creator>Waterfield, M.D.</creator><creator>Stroobant, P.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>7TK</scope></search><sort><creationdate>19930825</creationdate><title>Purification of multiple forms of glial growth factor</title><author>Goodearl, A.D. ; Davis, J.B. ; Mistry, K. ; Minghetti, L. ; Otsu, M. ; Waterfield, M.D. ; Stroobant, P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c496t-7103f1328277d0241743b278aba19237fb4befd48b941d1dbf7e465893831ce53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Cells, Cultured</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, Gel</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Chromatography, Liquid</topic><topic>DNA Replication - drug effects</topic><topic>Durapatite</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glia Maturation Factor</topic><topic>Growth Inhibitors - isolation & purification</topic><topic>Growth Inhibitors - pharmacology</topic><topic>Hydroxyapatites</topic><topic>Molecular Weight</topic><topic>Nerve Tissue Proteins - isolation & purification</topic><topic>Nerve Tissue Proteins - pharmacology</topic><topic>Pituitary Gland - chemistry</topic><topic>Protein hormones. Growth factors. Cytokines</topic><topic>Proteins</topic><topic>Rats</topic><topic>Schwann Cells - cytology</topic><topic>Schwann Cells - drug effects</topic><topic>Schwann Cells - metabolism</topic><topic>Sciatic Nerve - cytology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goodearl, A.D.</creatorcontrib><creatorcontrib>Davis, J.B.</creatorcontrib><creatorcontrib>Mistry, K.</creatorcontrib><creatorcontrib>Minghetti, L.</creatorcontrib><creatorcontrib>Otsu, M.</creatorcontrib><creatorcontrib>Waterfield, M.D.</creatorcontrib><creatorcontrib>Stroobant, P.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Neurosciences Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goodearl, A.D.</au><au>Davis, J.B.</au><au>Mistry, K.</au><au>Minghetti, L.</au><au>Otsu, M.</au><au>Waterfield, M.D.</au><au>Stroobant, P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification of multiple forms of glial growth factor</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-08-25</date><risdate>1993</risdate><volume>268</volume><issue>24</issue><spage>18095</spage><epage>18102</epage><pages>18095-18102</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Glial growth factors (GGFs) were purified from bovine pituitaries using an in vitro rat Schwann cell mitogenesis assay. In addition to an approximately 34-kDa species termed GGF-I, similar in molecular mass to a previously identified molecule (Lemke, G. E., and Brockes, J. P. (1984) J. Neuroscience 4, 75-83), two species named GGF-II and GGF-III were characterized with apparent molecular masses of approximately 59 and approximately 45 kDa, respectively. Highly purified preparations of all species share a similar dose-dependent stimulation of Schwann cell DNA synthesis at nanomolar concentrations. Forskolin synergizes with all three GGFs, shifting their dose dependence 3-8-fold into the sub-nanomolar range. The GGFs, which contain N-linked carbohydrate groups not essential for their in vitro mitogenic effects, are three distinct members of a novel family of glial cell mitogens.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>8394360</pmid><doi>10.1016/S0021-9258(17)46816-5</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle Cells, Cultured Chromatography, Affinity Chromatography, Gel Chromatography, High Pressure Liquid Chromatography, Liquid DNA Replication - drug effects Durapatite Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Glia Maturation Factor Growth Inhibitors - isolation & purification Growth Inhibitors - pharmacology Hydroxyapatites Molecular Weight Nerve Tissue Proteins - isolation & purification Nerve Tissue Proteins - pharmacology Pituitary Gland - chemistry Protein hormones. Growth factors. Cytokines Proteins Rats Schwann Cells - cytology Schwann Cells - drug effects Schwann Cells - metabolism Sciatic Nerve - cytology |
title | Purification of multiple forms of glial growth factor |
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