Characterization and partial purification of the insulin-like growth factor (IGF)-dependent IGF binding protein-4-specific protease from human fibroblast conditioned media
Insulin-like growth factors (IGFs) are one of the most potent stimulators of cell growth. IGFs are modulated by six high affinity binding proteins (IGFBPs) which are, in turn, regulated through post-translational modifications such as proteolysis. In the conditioned media of human fibroblasts, IGFBP...
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| Veröffentlicht in: | Growth hormone & IGF research 1999-02, Vol.9 (1), p.25-34 |
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| creator | Lawrence, James B Bale, Laurie K Haddad, Tufia C Clarkson, Jay T Conover, Cheryl A |
| description | Insulin-like growth factors (IGFs) are one of the most potent stimulators of cell growth. IGFs are modulated by six high affinity binding proteins (IGFBPs) which are, in turn, regulated through post-translational modifications such as proteolysis. In the conditioned media of human fibroblasts, IGFBP-4 is cleaved by an apparently novel IGFBP-4-specific protease that requires IGF for functional activity. We have used several biochemical manipulations, including size exclusion chromatography, native gel electrophoresis, chaotropic salt precipitation, hydrophobic interaction chromatography, ion exchange chromatography, isoelectric focusing, lectin affinity chromatography, and metal chelating affinity chromatography to both characterize and partially purify the IGF-dependent IGFBP-4 protease. Our results indicate that this protease is a highly glycosylated, Zn+2binding metalloprotease with a native molecular weight greater than 200 kDa. |
| doi_str_mv | 10.1054/ghir.1998.0083 |
| format | Article |
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IGFs are modulated by six high affinity binding proteins (IGFBPs) which are, in turn, regulated through post-translational modifications such as proteolysis. In the conditioned media of human fibroblasts, IGFBP-4 is cleaved by an apparently novel IGFBP-4-specific protease that requires IGF for functional activity. We have used several biochemical manipulations, including size exclusion chromatography, native gel electrophoresis, chaotropic salt precipitation, hydrophobic interaction chromatography, ion exchange chromatography, isoelectric focusing, lectin affinity chromatography, and metal chelating affinity chromatography to both characterize and partially purify the IGF-dependent IGFBP-4 protease. 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Our results indicate that this protease is a highly glycosylated, Zn+2binding metalloprotease with a native molecular weight greater than 200 kDa.</description><subject>Cell Line</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Gel</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Chromatography, Ion Exchange</subject><subject>Culture Media, Conditioned</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Stability</subject><subject>Fibroblasts - cytology</subject><subject>Fibroblasts - enzymology</subject><subject>Humans</subject><subject>IGFBP-4, IGF-II, human fibroblasts, metalloprotease</subject><subject>Insulin-Like Growth Factor Binding Protein 4 - metabolism</subject><subject>Kinetics</subject><subject>Metalloendopeptidases - chemistry</subject><subject>Metalloendopeptidases - isolation & purification</subject><subject>Metalloendopeptidases - metabolism</subject><subject>Molecular Weight</subject><subject>Pregnancy-Associated Plasma Protein-A</subject><subject>Substrate Specificity</subject><subject>Zinc - metabolism</subject><issn>1096-6374</issn><issn>1532-2238</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kT1v1TAYhS1ERUthZUSeUBlycWIntkd0RT-kSizdLcd5fWNI7GA7VPQv8SfrKB1YmPz1nPP66CD0oSaHmrTsy2l08VBLKQ6ECPoKXdQtbaqmoeJ12RPZVR3l7By9TekHIURSwd6g85o0hLekvUB_j6OO2mSI7klnFzzWfsCLjtnpCS9rdNaZ_SFYnEfAzqd1cr6a3E_Apxge84htcQgRX93dXH-uBljAD-AzLkfcOz84f8JLDBmKjFVpAbO57lc6AbYxzHhcZ-2xdX0M_aRTxiYU5TYZBjzD4PQ7dGb1lOD9y3qJHq6_PRxvq_vvN3fHr_eVoYzkCqjsbEdER2VjuJCs5ppaaEhPqLWitpywvuMaGsGZFHUrNJAN4FbzTtJL9Gm3Lf_7tULKanbJwDRpD2FNqpOdlIxv4GEHTQwpRbBqiW7W8Y-qidraUVs7amtHbe0UwccX57Uvif7B9zoKIHYASrzfDqJKxoE3JX0Ek9UQ3P-8nwEvW6Gg</recordid><startdate>19990201</startdate><enddate>19990201</enddate><creator>Lawrence, James B</creator><creator>Bale, Laurie K</creator><creator>Haddad, Tufia C</creator><creator>Clarkson, Jay T</creator><creator>Conover, Cheryl A</creator><general>Elsevier Ltd</general><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>7X8</scope></search><sort><creationdate>19990201</creationdate><title>Characterization and partial purification of the insulin-like growth factor (IGF)-dependent IGF binding protein-4-specific protease from human fibroblast conditioned media</title><author>Lawrence, James B ; Bale, Laurie K ; Haddad, Tufia C ; Clarkson, Jay T ; Conover, Cheryl A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-e396f6086392c789417a3fe20b03ff81f704b67ae287498158ae03fe27fa7693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Cell Line</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, Gel</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Chromatography, Ion Exchange</topic><topic>Culture Media, Conditioned</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Stability</topic><topic>Fibroblasts - cytology</topic><topic>Fibroblasts - enzymology</topic><topic>Humans</topic><topic>IGFBP-4, IGF-II, human fibroblasts, metalloprotease</topic><topic>Insulin-Like Growth Factor Binding Protein 4 - metabolism</topic><topic>Kinetics</topic><topic>Metalloendopeptidases - chemistry</topic><topic>Metalloendopeptidases - isolation & purification</topic><topic>Metalloendopeptidases - metabolism</topic><topic>Molecular Weight</topic><topic>Pregnancy-Associated Plasma Protein-A</topic><topic>Substrate Specificity</topic><topic>Zinc - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lawrence, James B</creatorcontrib><creatorcontrib>Bale, Laurie K</creatorcontrib><creatorcontrib>Haddad, Tufia C</creatorcontrib><creatorcontrib>Clarkson, Jay T</creatorcontrib><creatorcontrib>Conover, Cheryl A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Growth hormone & IGF research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lawrence, James B</au><au>Bale, Laurie K</au><au>Haddad, Tufia C</au><au>Clarkson, Jay T</au><au>Conover, Cheryl A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization and partial purification of the insulin-like growth factor (IGF)-dependent IGF binding protein-4-specific protease from human fibroblast conditioned media</atitle><jtitle>Growth hormone & IGF research</jtitle><addtitle>Growth Horm IGF Res</addtitle><date>1999-02-01</date><risdate>1999</risdate><volume>9</volume><issue>1</issue><spage>25</spage><epage>34</epage><pages>25-34</pages><issn>1096-6374</issn><eissn>1532-2238</eissn><abstract>Insulin-like growth factors (IGFs) are one of the most potent stimulators of cell growth. IGFs are modulated by six high affinity binding proteins (IGFBPs) which are, in turn, regulated through post-translational modifications such as proteolysis. In the conditioned media of human fibroblasts, IGFBP-4 is cleaved by an apparently novel IGFBP-4-specific protease that requires IGF for functional activity. We have used several biochemical manipulations, including size exclusion chromatography, native gel electrophoresis, chaotropic salt precipitation, hydrophobic interaction chromatography, ion exchange chromatography, isoelectric focusing, lectin affinity chromatography, and metal chelating affinity chromatography to both characterize and partially purify the IGF-dependent IGFBP-4 protease. Our results indicate that this protease is a highly glycosylated, Zn+2binding metalloprotease with a native molecular weight greater than 200 kDa.</abstract><cop>Scotland</cop><pub>Elsevier Ltd</pub><pmid>10207505</pmid><doi>10.1054/ghir.1998.0083</doi><tpages>10</tpages></addata></record> |
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| identifier | ISSN: 1096-6374 |
| ispartof | Growth hormone & IGF research, 1999-02, Vol.9 (1), p.25-34 |
| issn | 1096-6374 1532-2238 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Cell Line Chromatography, Affinity Chromatography, Gel Chromatography, High Pressure Liquid Chromatography, Ion Exchange Culture Media, Conditioned Electrophoresis, Polyacrylamide Gel Enzyme Stability Fibroblasts - cytology Fibroblasts - enzymology Humans IGFBP-4, IGF-II, human fibroblasts, metalloprotease Insulin-Like Growth Factor Binding Protein 4 - metabolism Kinetics Metalloendopeptidases - chemistry Metalloendopeptidases - isolation & purification Metalloendopeptidases - metabolism Molecular Weight Pregnancy-Associated Plasma Protein-A Substrate Specificity Zinc - metabolism |
| title | Characterization and partial purification of the insulin-like growth factor (IGF)-dependent IGF binding protein-4-specific protease from human fibroblast conditioned media |
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