Effect of constitutive expression of porcine IGFBP-3 on proliferation and differentiation of L6 myogenic cells
We have previously shown that exogenous recombinant porcine IGFBP-3 (rpIGFBP-3) suppresses proliferation and differentiation of L6 myogenic cells in an IGF-I-dependent manner and suppresses proliferation of L6 myogenic cells via an IGF-I-independent mechanism. In order to assess the effects of endog...
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| creator | Xi, G. Kamanga-Sollo, E. Hathaway, M.R. Dayton, W.R. White, M.E. |
| description | We have previously shown that exogenous recombinant porcine IGFBP-3 (rpIGFBP-3) suppresses proliferation and differentiation of L6 myogenic cells in an IGF-I-dependent manner and suppresses proliferation of L6 myogenic cells via an IGF-I-independent mechanism. In order to assess the effects of endogenously produced IGFBP-3, we have transfected L6 myogenic cells with a pEF6/V5 vector containing pIGFBP-3 cDNA under the control of the human elongation factor 1α (hEF-1α) promoter and with the empty vector. We have isolated a cell population that constitutively produces porcine IGFBP-3 (tL6 cells) and a stable mock transfected cell population containing the empty vector (mtL6 cells). Constitutive expression of IGFBP-3 slightly reduced the expression of IGFBP-5 but had no effect on IGFBP-4 production by L6 myogenic cells. Immunoneutralization of IGFBP-3 increased both IGF-I- and Long-R3-IGF-I-stimulated proliferation of tL6 cells (58 and 33%, respectively) (
P
<
0.01). These data indicate endogenous pIGFBP-3, like exogenous rpIGFBP-3, suppresses the proliferation of L6 myogenic cells via both IGF-I-dependent and -independent pathways. Immunoneutralization of IGFBP-3 also increased IGF-I-stimulated differentiation (21%,
P
<
0.05) but had no effect on Long-R3-IGF-I stimulated differentiation of tL6 myogenic cells. Results indicate that exogenous and endogenous IGFBP-3 affect proliferation and differentiation of L6 myogenic cells in a similar way. Immunohistochemical localization data reveal that pre-incubation with anti-pIGFBP-3 dramatically reduces the level of intracellular IGFBP-3 in tL6 myogenic cells indicating that endogenously produced IGFBP-3 must first be secreted before it is internalized and that anti-pIGFBP-3 prevents internalization of IGFBP-3. TL6 and mtL6 cells provide a good system to further investigate the mechanisms by which IGFBP-3 affects proliferation and differentiation of myogenic cells. |
| doi_str_mv | 10.1016/j.domaniend.2005.09.008 |
| format | Article |
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P
<
0.01). These data indicate endogenous pIGFBP-3, like exogenous rpIGFBP-3, suppresses the proliferation of L6 myogenic cells via both IGF-I-dependent and -independent pathways. Immunoneutralization of IGFBP-3 also increased IGF-I-stimulated differentiation (21%,
P
<
0.05) but had no effect on Long-R3-IGF-I stimulated differentiation of tL6 myogenic cells. Results indicate that exogenous and endogenous IGFBP-3 affect proliferation and differentiation of L6 myogenic cells in a similar way. Immunohistochemical localization data reveal that pre-incubation with anti-pIGFBP-3 dramatically reduces the level of intracellular IGFBP-3 in tL6 myogenic cells indicating that endogenously produced IGFBP-3 must first be secreted before it is internalized and that anti-pIGFBP-3 prevents internalization of IGFBP-3. TL6 and mtL6 cells provide a good system to further investigate the mechanisms by which IGFBP-3 affects proliferation and differentiation of myogenic cells.</description><identifier>ISSN: 0739-7240</identifier><identifier>EISSN: 1879-0054</identifier><identifier>DOI: 10.1016/j.domaniend.2005.09.008</identifier><identifier>PMID: 16233971</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Blotting, Western ; cell differentiation ; Cell Differentiation - physiology ; Cell Growth Processes - drug effects ; Cell Growth Processes - physiology ; Cell Line ; cell lines ; cell proliferation ; Creatine Kinase - metabolism ; Culture Media, Conditioned ; Differentiation ; endogenous sources ; gene expression ; IGFBP-3 ; immunohistochemistry ; Immunohistochemistry - veterinary ; immunolocalization ; Insulin-Like Growth Factor Binding Protein 3 - biosynthesis ; Insulin-Like Growth Factor Binding Protein 3 - genetics ; Insulin-Like Growth Factor Binding Protein 3 - metabolism ; Insulin-Like Growth Factor Binding Protein 4 - metabolism ; Insulin-Like Growth Factor Binding Protein 5 - metabolism ; insulin-like growth factor binding protein-3 ; insulin-like growth factor binding proteins ; insulin-like growth factor I ; Insulin-Like Growth Factor I - metabolism ; L6 myogenic cells ; Myoblasts - cytology ; Myoblasts - drug effects ; Myoblasts - enzymology ; Myoblasts - metabolism ; myocytes ; physiological regulation ; Proliferation ; protein secretion ; Proteins - pharmacology ; Rats ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Messenger - biosynthesis ; RNA, Messenger - genetics ; Stable transfection ; swine ; Transfection</subject><ispartof>Domestic animal endocrinology, 2006-07, Vol.31 (1), p.35-51</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-72950f6bd668efe21a0adaca643d6505006516ac41e62a7b9c9d57f9b37e583e3</citedby><cites>FETCH-LOGICAL-c393t-72950f6bd668efe21a0adaca643d6505006516ac41e62a7b9c9d57f9b37e583e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0739724005001864$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16233971$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xi, G.</creatorcontrib><creatorcontrib>Kamanga-Sollo, E.</creatorcontrib><creatorcontrib>Hathaway, M.R.</creatorcontrib><creatorcontrib>Dayton, W.R.</creatorcontrib><creatorcontrib>White, M.E.</creatorcontrib><title>Effect of constitutive expression of porcine IGFBP-3 on proliferation and differentiation of L6 myogenic cells</title><title>Domestic animal endocrinology</title><addtitle>Domest Anim Endocrinol</addtitle><description>We have previously shown that exogenous recombinant porcine IGFBP-3 (rpIGFBP-3) suppresses proliferation and differentiation of L6 myogenic cells in an IGF-I-dependent manner and suppresses proliferation of L6 myogenic cells via an IGF-I-independent mechanism. In order to assess the effects of endogenously produced IGFBP-3, we have transfected L6 myogenic cells with a pEF6/V5 vector containing pIGFBP-3 cDNA under the control of the human elongation factor 1α (hEF-1α) promoter and with the empty vector. We have isolated a cell population that constitutively produces porcine IGFBP-3 (tL6 cells) and a stable mock transfected cell population containing the empty vector (mtL6 cells). Constitutive expression of IGFBP-3 slightly reduced the expression of IGFBP-5 but had no effect on IGFBP-4 production by L6 myogenic cells. Immunoneutralization of IGFBP-3 increased both IGF-I- and Long-R3-IGF-I-stimulated proliferation of tL6 cells (58 and 33%, respectively) (
P
<
0.01). These data indicate endogenous pIGFBP-3, like exogenous rpIGFBP-3, suppresses the proliferation of L6 myogenic cells via both IGF-I-dependent and -independent pathways. Immunoneutralization of IGFBP-3 also increased IGF-I-stimulated differentiation (21%,
P
<
0.05) but had no effect on Long-R3-IGF-I stimulated differentiation of tL6 myogenic cells. Results indicate that exogenous and endogenous IGFBP-3 affect proliferation and differentiation of L6 myogenic cells in a similar way. Immunohistochemical localization data reveal that pre-incubation with anti-pIGFBP-3 dramatically reduces the level of intracellular IGFBP-3 in tL6 myogenic cells indicating that endogenously produced IGFBP-3 must first be secreted before it is internalized and that anti-pIGFBP-3 prevents internalization of IGFBP-3. TL6 and mtL6 cells provide a good system to further investigate the mechanisms by which IGFBP-3 affects proliferation and differentiation of myogenic cells.</description><subject>Animals</subject><subject>Blotting, Western</subject><subject>cell differentiation</subject><subject>Cell Differentiation - physiology</subject><subject>Cell Growth Processes - drug effects</subject><subject>Cell Growth Processes - physiology</subject><subject>Cell Line</subject><subject>cell lines</subject><subject>cell proliferation</subject><subject>Creatine Kinase - metabolism</subject><subject>Culture Media, Conditioned</subject><subject>Differentiation</subject><subject>endogenous sources</subject><subject>gene expression</subject><subject>IGFBP-3</subject><subject>immunohistochemistry</subject><subject>Immunohistochemistry - veterinary</subject><subject>immunolocalization</subject><subject>Insulin-Like Growth Factor Binding Protein 3 - biosynthesis</subject><subject>Insulin-Like Growth Factor Binding Protein 3 - genetics</subject><subject>Insulin-Like Growth Factor Binding Protein 3 - metabolism</subject><subject>Insulin-Like Growth Factor Binding Protein 4 - metabolism</subject><subject>Insulin-Like Growth Factor Binding Protein 5 - metabolism</subject><subject>insulin-like growth factor binding protein-3</subject><subject>insulin-like growth factor binding proteins</subject><subject>insulin-like growth factor I</subject><subject>Insulin-Like Growth Factor I - metabolism</subject><subject>L6 myogenic cells</subject><subject>Myoblasts - cytology</subject><subject>Myoblasts - drug effects</subject><subject>Myoblasts - enzymology</subject><subject>Myoblasts - metabolism</subject><subject>myocytes</subject><subject>physiological regulation</subject><subject>Proliferation</subject><subject>protein secretion</subject><subject>Proteins - pharmacology</subject><subject>Rats</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - biosynthesis</subject><subject>RNA, Messenger - genetics</subject><subject>Stable transfection</subject><subject>swine</subject><subject>Transfection</subject><issn>0739-7240</issn><issn>1879-0054</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFP3DAQha2qqGxp_0LJqbek4zix4yMgoEgrFQk4W157jLza2Fs7i-Df4yircuzJ0vh7857eEHJOoaFA-a9tY-Oog8dgmxagb0A2AMMnsqKDkHWZdJ_JCgSTtWg7OCVfc94CgCjqL-SU8pYxKeiKhGvn0ExVdJWJIU9-Okz-BSt83SfM2ccwf-1jMj5gdXd7c3lfs6pM9ynuvMOkp5nRwVbWl1UJw-SXWdGteTW-xWcM3lQGd7v8jZw4vcv4_fiekaeb68er3_X6z-3d1cW6NkyyqWSWPTi-sZwP6LClGrTVRvOOWd5DD8B7yrXpKPJWi4000vbCyQ0T2A8M2Rn5uewtMf8eME9q9HlOoAPGQ1Z8gHZgrCugWECTYs4JndonP-r0piiouWq1Vf-qVnPVCqQqVRflj6PFYTOi_dAduy3A-QI4HZV-Tj6rp4cWKANa5JTP5hcLgaWKF49JZVN8DFqfylGKsf9vjHdf3p4P</recordid><startdate>20060701</startdate><enddate>20060701</enddate><creator>Xi, G.</creator><creator>Kamanga-Sollo, E.</creator><creator>Hathaway, M.R.</creator><creator>Dayton, W.R.</creator><creator>White, M.E.</creator><general>Elsevier Inc</general><scope>FBQ</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>7X8</scope></search><sort><creationdate>20060701</creationdate><title>Effect of constitutive expression of porcine IGFBP-3 on proliferation and differentiation of L6 myogenic cells</title><author>Xi, G. ; Kamanga-Sollo, E. ; Hathaway, M.R. ; Dayton, W.R. ; White, M.E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-72950f6bd668efe21a0adaca643d6505006516ac41e62a7b9c9d57f9b37e583e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Blotting, Western</topic><topic>cell differentiation</topic><topic>Cell Differentiation - physiology</topic><topic>Cell Growth Processes - drug effects</topic><topic>Cell Growth Processes - physiology</topic><topic>Cell Line</topic><topic>cell lines</topic><topic>cell proliferation</topic><topic>Creatine Kinase - metabolism</topic><topic>Culture Media, Conditioned</topic><topic>Differentiation</topic><topic>endogenous sources</topic><topic>gene expression</topic><topic>IGFBP-3</topic><topic>immunohistochemistry</topic><topic>Immunohistochemistry - veterinary</topic><topic>immunolocalization</topic><topic>Insulin-Like Growth Factor Binding Protein 3 - biosynthesis</topic><topic>Insulin-Like Growth Factor Binding Protein 3 - genetics</topic><topic>Insulin-Like Growth Factor Binding Protein 3 - metabolism</topic><topic>Insulin-Like Growth Factor Binding Protein 4 - metabolism</topic><topic>Insulin-Like Growth Factor Binding Protein 5 - metabolism</topic><topic>insulin-like growth factor binding protein-3</topic><topic>insulin-like growth factor binding proteins</topic><topic>insulin-like growth factor I</topic><topic>Insulin-Like Growth Factor I - metabolism</topic><topic>L6 myogenic cells</topic><topic>Myoblasts - cytology</topic><topic>Myoblasts - drug effects</topic><topic>Myoblasts - enzymology</topic><topic>Myoblasts - metabolism</topic><topic>myocytes</topic><topic>physiological regulation</topic><topic>Proliferation</topic><topic>protein secretion</topic><topic>Proteins - pharmacology</topic><topic>Rats</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - biosynthesis</topic><topic>RNA, Messenger - genetics</topic><topic>Stable transfection</topic><topic>swine</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xi, G.</creatorcontrib><creatorcontrib>Kamanga-Sollo, E.</creatorcontrib><creatorcontrib>Hathaway, M.R.</creatorcontrib><creatorcontrib>Dayton, W.R.</creatorcontrib><creatorcontrib>White, M.E.</creatorcontrib><collection>AGRIS</collection><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>Domestic animal endocrinology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xi, G.</au><au>Kamanga-Sollo, E.</au><au>Hathaway, M.R.</au><au>Dayton, W.R.</au><au>White, M.E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of constitutive expression of porcine IGFBP-3 on proliferation and differentiation of L6 myogenic cells</atitle><jtitle>Domestic animal endocrinology</jtitle><addtitle>Domest Anim Endocrinol</addtitle><date>2006-07-01</date><risdate>2006</risdate><volume>31</volume><issue>1</issue><spage>35</spage><epage>51</epage><pages>35-51</pages><issn>0739-7240</issn><eissn>1879-0054</eissn><abstract>We have previously shown that exogenous recombinant porcine IGFBP-3 (rpIGFBP-3) suppresses proliferation and differentiation of L6 myogenic cells in an IGF-I-dependent manner and suppresses proliferation of L6 myogenic cells via an IGF-I-independent mechanism. In order to assess the effects of endogenously produced IGFBP-3, we have transfected L6 myogenic cells with a pEF6/V5 vector containing pIGFBP-3 cDNA under the control of the human elongation factor 1α (hEF-1α) promoter and with the empty vector. We have isolated a cell population that constitutively produces porcine IGFBP-3 (tL6 cells) and a stable mock transfected cell population containing the empty vector (mtL6 cells). Constitutive expression of IGFBP-3 slightly reduced the expression of IGFBP-5 but had no effect on IGFBP-4 production by L6 myogenic cells. Immunoneutralization of IGFBP-3 increased both IGF-I- and Long-R3-IGF-I-stimulated proliferation of tL6 cells (58 and 33%, respectively) (
P
<
0.01). These data indicate endogenous pIGFBP-3, like exogenous rpIGFBP-3, suppresses the proliferation of L6 myogenic cells via both IGF-I-dependent and -independent pathways. Immunoneutralization of IGFBP-3 also increased IGF-I-stimulated differentiation (21%,
P
<
0.05) but had no effect on Long-R3-IGF-I stimulated differentiation of tL6 myogenic cells. Results indicate that exogenous and endogenous IGFBP-3 affect proliferation and differentiation of L6 myogenic cells in a similar way. Immunohistochemical localization data reveal that pre-incubation with anti-pIGFBP-3 dramatically reduces the level of intracellular IGFBP-3 in tL6 myogenic cells indicating that endogenously produced IGFBP-3 must first be secreted before it is internalized and that anti-pIGFBP-3 prevents internalization of IGFBP-3. TL6 and mtL6 cells provide a good system to further investigate the mechanisms by which IGFBP-3 affects proliferation and differentiation of myogenic cells.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16233971</pmid><doi>10.1016/j.domaniend.2005.09.008</doi><tpages>17</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Domestic animal endocrinology, 2006-07, Vol.31 (1), p.35-51 |
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| subjects | Animals Blotting, Western cell differentiation Cell Differentiation - physiology Cell Growth Processes - drug effects Cell Growth Processes - physiology Cell Line cell lines cell proliferation Creatine Kinase - metabolism Culture Media, Conditioned Differentiation endogenous sources gene expression IGFBP-3 immunohistochemistry Immunohistochemistry - veterinary immunolocalization Insulin-Like Growth Factor Binding Protein 3 - biosynthesis Insulin-Like Growth Factor Binding Protein 3 - genetics Insulin-Like Growth Factor Binding Protein 3 - metabolism Insulin-Like Growth Factor Binding Protein 4 - metabolism Insulin-Like Growth Factor Binding Protein 5 - metabolism insulin-like growth factor binding protein-3 insulin-like growth factor binding proteins insulin-like growth factor I Insulin-Like Growth Factor I - metabolism L6 myogenic cells Myoblasts - cytology Myoblasts - drug effects Myoblasts - enzymology Myoblasts - metabolism myocytes physiological regulation Proliferation protein secretion Proteins - pharmacology Rats Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - biosynthesis RNA, Messenger - genetics Stable transfection swine Transfection |
| title | Effect of constitutive expression of porcine IGFBP-3 on proliferation and differentiation of L6 myogenic cells |
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