Insulin-like growth factor-I regulates transcription of the elastin gene
Neonatal rat aortic smooth muscle cell cultures were used to investigate the mechanisms by which insulin-like growth factor-I (IGF-I) up-regulates aortic elastogenesis. The addition of IGF-I (50 ng/ml) to quiescent smooth muscle cell cultures resulted in a 5-fold increase in the steady-state levels...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-06, Vol.268 (17), p.12418-12426 |
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| container_issue | 17 |
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| container_title | The Journal of biological chemistry |
| container_volume | 268 |
| creator | WOLFE, B. L RICH, C. B GOUD, H. D TERPSTRA, A. J BASHIR, M ROSENBLOOMS, J SONENSHEIN, G. E FOSTER, J. A |
| description | Neonatal rat aortic smooth muscle cell cultures were used to investigate the mechanisms by which insulin-like growth factor-I
(IGF-I) up-regulates aortic elastogenesis. The addition of IGF-I (50 ng/ml) to quiescent smooth muscle cell cultures resulted
in a 5-fold increase in the steady-state levels of tropoelastin mRNA beginning between 2 and 4 h and reaching maximal levels
at 8 h. Addition of cycloheximide blocked the effect of IGF-I. Nuclear run-on transcription analyses of nuclei isolated from
IGF-I-treated cells showed increased synthesis of new tropoelastin transcripts indicating that transcriptional activation
is a major component of IGF-I up-regulation. Transient transfections with deletion constructs containing different portions
of the elastin 5'-upstream region localized the IGF-I-responsive area to sequences between -195 and -136 base pairs and further
showed that this region contains a negative element. Gel retardation assays using nuclear proteins extracted from control
and IGF-I-treated cells demonstrated that IGF-I treatment results in the loss of binding complexes. Footprint analyses of
specific binding complexes affected by IGF-I show the deprotection of two closely positioned sequences spanning positions
-165 to -137 base pairs. These results suggest that IGF-I up-regulation of elastogenesis involves the abrogation of a negative
element functionality. |
| doi_str_mv | 10.1016/s0021-9258(18)31406-6 |
| format | Article |
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(IGF-I) up-regulates aortic elastogenesis. The addition of IGF-I (50 ng/ml) to quiescent smooth muscle cell cultures resulted
in a 5-fold increase in the steady-state levels of tropoelastin mRNA beginning between 2 and 4 h and reaching maximal levels
at 8 h. Addition of cycloheximide blocked the effect of IGF-I. Nuclear run-on transcription analyses of nuclei isolated from
IGF-I-treated cells showed increased synthesis of new tropoelastin transcripts indicating that transcriptional activation
is a major component of IGF-I up-regulation. Transient transfections with deletion constructs containing different portions
of the elastin 5'-upstream region localized the IGF-I-responsive area to sequences between -195 and -136 base pairs and further
showed that this region contains a negative element. Gel retardation assays using nuclear proteins extracted from control
and IGF-I-treated cells demonstrated that IGF-I treatment results in the loss of binding complexes. Footprint analyses of
specific binding complexes affected by IGF-I show the deprotection of two closely positioned sequences spanning positions
-165 to -137 base pairs. These results suggest that IGF-I up-regulation of elastogenesis involves the abrogation of a negative
element functionality.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(18)31406-6</identifier><identifier>PMID: 8509381</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Animals, Newborn ; Aorta - metabolism ; Base Sequence ; Biological and medical sciences ; Cells, Cultured ; Chloramphenicol O-Acetyltransferase - biosynthesis ; DNA - biosynthesis ; Elastin - biosynthesis ; Elastin - genetics ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation ; Insulin-Like Growth Factor I - pharmacology ; Kinetics ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Muscle, Smooth, Vascular - metabolism ; Oligodeoxyribonucleotides ; Rats ; Rats, Sprague-Dawley ; Recombinant Fusion Proteins - biosynthesis ; RNA, Messenger - metabolism ; Thymidine - metabolism ; Transcription, Genetic - drug effects ; Transcription. Transcription factor. Splicing. Rna processing ; Tritium ; Tropoelastin - biosynthesis ; Tropoelastin - genetics</subject><ispartof>The Journal of biological chemistry, 1993-06, Vol.268 (17), p.12418-12426</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c506t-1d6e5ae4e7d04da4edfe6f41e60b74f0bb1e17574c6d28f40e4e9521fc07efbe3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4820555$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8509381$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>WOLFE, B. L</creatorcontrib><creatorcontrib>RICH, C. B</creatorcontrib><creatorcontrib>GOUD, H. D</creatorcontrib><creatorcontrib>TERPSTRA, A. J</creatorcontrib><creatorcontrib>BASHIR, M</creatorcontrib><creatorcontrib>ROSENBLOOMS, J</creatorcontrib><creatorcontrib>SONENSHEIN, G. E</creatorcontrib><creatorcontrib>FOSTER, J. A</creatorcontrib><title>Insulin-like growth factor-I regulates transcription of the elastin gene</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Neonatal rat aortic smooth muscle cell cultures were used to investigate the mechanisms by which insulin-like growth factor-I
(IGF-I) up-regulates aortic elastogenesis. The addition of IGF-I (50 ng/ml) to quiescent smooth muscle cell cultures resulted
in a 5-fold increase in the steady-state levels of tropoelastin mRNA beginning between 2 and 4 h and reaching maximal levels
at 8 h. Addition of cycloheximide blocked the effect of IGF-I. Nuclear run-on transcription analyses of nuclei isolated from
IGF-I-treated cells showed increased synthesis of new tropoelastin transcripts indicating that transcriptional activation
is a major component of IGF-I up-regulation. Transient transfections with deletion constructs containing different portions
of the elastin 5'-upstream region localized the IGF-I-responsive area to sequences between -195 and -136 base pairs and further
showed that this region contains a negative element. Gel retardation assays using nuclear proteins extracted from control
and IGF-I-treated cells demonstrated that IGF-I treatment results in the loss of binding complexes. Footprint analyses of
specific binding complexes affected by IGF-I show the deprotection of two closely positioned sequences spanning positions
-165 to -137 base pairs. These results suggest that IGF-I up-regulation of elastogenesis involves the abrogation of a negative
element functionality.</description><subject>Animals</subject><subject>Animals, Newborn</subject><subject>Aorta - metabolism</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cells, Cultured</subject><subject>Chloramphenicol O-Acetyltransferase - biosynthesis</subject><subject>DNA - biosynthesis</subject><subject>Elastin - biosynthesis</subject><subject>Elastin - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation</subject><subject>Insulin-Like Growth Factor I - pharmacology</subject><subject>Kinetics</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Muscle, Smooth, Vascular - metabolism</subject><subject>Oligodeoxyribonucleotides</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Recombinant Fusion Proteins - biosynthesis</subject><subject>RNA, Messenger - metabolism</subject><subject>Thymidine - metabolism</subject><subject>Transcription, Genetic - drug effects</subject><subject>Transcription. Transcription factor. Splicing. Rna processing</subject><subject>Tritium</subject><subject>Tropoelastin - biosynthesis</subject><subject>Tropoelastin - genetics</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>eNpFkE1LxDAQhoMouq7-BKEHET1UM22SpkdZ_FhY8KCCt5Cmk220265Jivjv7eqyzmUO7_POwEPIGdBroCBuAqUZpGXG5SXIqxwYFanYIxOgMk9zDm_7ZLJDjshxCO90HFbCITmUnJa5hAl5nHdhaF2Xtu4Dk6Xvv2KTWG1i79N54nE5tDpiSKLXXTDeraPru6S3SWwwwVaH6LpkiR2ekAOr24Cn2z0lr_d3L7PHdPH0MJ_dLlLDqYgp1AK5RoZFTVmtGdYWhWWAglYFs7SqAKHgBTOizqRldERLnoE1tEBbYT4lF393177_HDBEtXLBYNvqDvshKBCiHOvlCPI_0Pg-BI9Wrb1baf-tgKqNQfW80aM2ehRI9WtQibF3tn0wVCusd62tsjE_3-Y6GN3aUYxxYYcxmVHO-T_WuGXz5TyqyvWmwZXKxPivUJAxkPkPv2uFtw</recordid><startdate>19930615</startdate><enddate>19930615</enddate><creator>WOLFE, B. L</creator><creator>RICH, C. B</creator><creator>GOUD, H. D</creator><creator>TERPSTRA, A. J</creator><creator>BASHIR, M</creator><creator>ROSENBLOOMS, J</creator><creator>SONENSHEIN, G. E</creator><creator>FOSTER, J. A</creator><general>American Society for Biochemistry and Molecular Biology</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>7TM</scope></search><sort><creationdate>19930615</creationdate><title>Insulin-like growth factor-I regulates transcription of the elastin gene</title><author>WOLFE, B. L ; RICH, C. B ; GOUD, H. D ; TERPSTRA, A. J ; BASHIR, M ; ROSENBLOOMS, J ; SONENSHEIN, G. E ; FOSTER, J. A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-1d6e5ae4e7d04da4edfe6f41e60b74f0bb1e17574c6d28f40e4e9521fc07efbe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Animals, Newborn</topic><topic>Aorta - metabolism</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cells, Cultured</topic><topic>Chloramphenicol O-Acetyltransferase - biosynthesis</topic><topic>DNA - biosynthesis</topic><topic>Elastin - biosynthesis</topic><topic>Elastin - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation</topic><topic>Insulin-Like Growth Factor I - pharmacology</topic><topic>Kinetics</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Muscle, Smooth, Vascular - metabolism</topic><topic>Oligodeoxyribonucleotides</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Recombinant Fusion Proteins - biosynthesis</topic><topic>RNA, Messenger - metabolism</topic><topic>Thymidine - metabolism</topic><topic>Transcription, Genetic - drug effects</topic><topic>Transcription. Transcription factor. Splicing. Rna processing</topic><topic>Tritium</topic><topic>Tropoelastin - biosynthesis</topic><topic>Tropoelastin - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>WOLFE, B. L</creatorcontrib><creatorcontrib>RICH, C. B</creatorcontrib><creatorcontrib>GOUD, H. D</creatorcontrib><creatorcontrib>TERPSTRA, A. J</creatorcontrib><creatorcontrib>BASHIR, M</creatorcontrib><creatorcontrib>ROSENBLOOMS, J</creatorcontrib><creatorcontrib>SONENSHEIN, G. E</creatorcontrib><creatorcontrib>FOSTER, J. A</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>Nucleic Acids Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>WOLFE, B. L</au><au>RICH, C. B</au><au>GOUD, H. D</au><au>TERPSTRA, A. J</au><au>BASHIR, M</au><au>ROSENBLOOMS, J</au><au>SONENSHEIN, G. E</au><au>FOSTER, J. A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Insulin-like growth factor-I regulates transcription of the elastin gene</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-06-15</date><risdate>1993</risdate><volume>268</volume><issue>17</issue><spage>12418</spage><epage>12426</epage><pages>12418-12426</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Neonatal rat aortic smooth muscle cell cultures were used to investigate the mechanisms by which insulin-like growth factor-I
(IGF-I) up-regulates aortic elastogenesis. The addition of IGF-I (50 ng/ml) to quiescent smooth muscle cell cultures resulted
in a 5-fold increase in the steady-state levels of tropoelastin mRNA beginning between 2 and 4 h and reaching maximal levels
at 8 h. Addition of cycloheximide blocked the effect of IGF-I. Nuclear run-on transcription analyses of nuclei isolated from
IGF-I-treated cells showed increased synthesis of new tropoelastin transcripts indicating that transcriptional activation
is a major component of IGF-I up-regulation. Transient transfections with deletion constructs containing different portions
of the elastin 5'-upstream region localized the IGF-I-responsive area to sequences between -195 and -136 base pairs and further
showed that this region contains a negative element. Gel retardation assays using nuclear proteins extracted from control
and IGF-I-treated cells demonstrated that IGF-I treatment results in the loss of binding complexes. Footprint analyses of
specific binding complexes affected by IGF-I show the deprotection of two closely positioned sequences spanning positions
-165 to -137 base pairs. These results suggest that IGF-I up-regulation of elastogenesis involves the abrogation of a negative
element functionality.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8509381</pmid><doi>10.1016/s0021-9258(18)31406-6</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1993-06, Vol.268 (17), p.12418-12426 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16695749 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Animals, Newborn Aorta - metabolism Base Sequence Biological and medical sciences Cells, Cultured Chloramphenicol O-Acetyltransferase - biosynthesis DNA - biosynthesis Elastin - biosynthesis Elastin - genetics Fundamental and applied biological sciences. Psychology Gene Expression Regulation Insulin-Like Growth Factor I - pharmacology Kinetics Molecular and cellular biology Molecular genetics Molecular Sequence Data Muscle, Smooth, Vascular - metabolism Oligodeoxyribonucleotides Rats Rats, Sprague-Dawley Recombinant Fusion Proteins - biosynthesis RNA, Messenger - metabolism Thymidine - metabolism Transcription, Genetic - drug effects Transcription. Transcription factor. Splicing. Rna processing Tritium Tropoelastin - biosynthesis Tropoelastin - genetics |
| title | Insulin-like growth factor-I regulates transcription of the elastin gene |
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