Expression of calpastatin isoforms in muscle and functionality of multiple calpastatin promoters
Calpastatin is the specific endogenous inhibitor of calpain proteinase that is encoded by a single gene. Transient transfection assays in both a non-fusing skeletal muscle and non-muscle cell-line demonstrated that the putative porcine calpastatin promoter regions 5 ′ to exons 1xa, 1xb, and 1u were...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 2004-07, Vol.427 (1), p.8-15 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Parr, Tim Jewell, Kirsty K Sensky, Paul L Brameld, John M Bardsley, Ronald G Buttery, Peter J |
| description | Calpastatin is the specific endogenous inhibitor of calpain proteinase that is encoded by a single gene. Transient transfection assays in both a non-fusing skeletal muscle and non-muscle cell-line demonstrated that the putative porcine calpastatin promoter regions 5
′ to exons 1xa, 1xb, and 1u were functional. Both real-time quantitative and semi-quantitative RT-PCR on porcine skeletal muscle total RNA indicated that steady-state expression of Type I and III mRNAs containing exons 1xa and 1u, respectively, was at equivalent levels whilst the expression of Type II mRNA containing exon 1xb was significantly less (
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| doi_str_mv | 10.1016/j.abb.2004.04.001 |
| format | Article |
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′ to exons 1xa, 1xb, and 1u were functional. Both real-time quantitative and semi-quantitative RT-PCR on porcine skeletal muscle total RNA indicated that steady-state expression of Type I and III mRNAs containing exons 1xa and 1u, respectively, was at equivalent levels whilst the expression of Type II mRNA containing exon 1xb was significantly less (
p<0.001). Immunoprobing of Western blotted muscle extracts with an antibody raised against a peptide sequence encoded by exon 1xa indicated that Type I protein was expressed and that there was significantly more Type I protein in cardiac than skeletal muscle (
p<0.001). The results suggest that the expression of the single calpastatin gene was differentially controlled at several levels.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/j.abb.2004.04.001</identifier><identifier>PMID: 15178483</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Western ; Calcium-Binding Proteins - genetics ; Calcium-Binding Proteins - metabolism ; Calpain ; Calpastatin ; Cardiac muscle ; DNA Primers ; Muscle, Skeletal - enzymology ; Promoter analysis ; Promoter Regions, Genetic ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Messenger - genetics ; Skeletal muscle ; Swine ; Transfection</subject><ispartof>Archives of biochemistry and biophysics, 2004-07, Vol.427 (1), p.8-15</ispartof><rights>2004 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-404404b2da8c9a5458a7ff4e1596f3b9d02d8ccaf607f4a8a6823715efa962793</citedby><cites>FETCH-LOGICAL-c415t-404404b2da8c9a5458a7ff4e1596f3b9d02d8ccaf607f4a8a6823715efa962793</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.abb.2004.04.001$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15178483$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Parr, Tim</creatorcontrib><creatorcontrib>Jewell, Kirsty K</creatorcontrib><creatorcontrib>Sensky, Paul L</creatorcontrib><creatorcontrib>Brameld, John M</creatorcontrib><creatorcontrib>Bardsley, Ronald G</creatorcontrib><creatorcontrib>Buttery, Peter J</creatorcontrib><title>Expression of calpastatin isoforms in muscle and functionality of multiple calpastatin promoters</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Calpastatin is the specific endogenous inhibitor of calpain proteinase that is encoded by a single gene. Transient transfection assays in both a non-fusing skeletal muscle and non-muscle cell-line demonstrated that the putative porcine calpastatin promoter regions 5
′ to exons 1xa, 1xb, and 1u were functional. Both real-time quantitative and semi-quantitative RT-PCR on porcine skeletal muscle total RNA indicated that steady-state expression of Type I and III mRNAs containing exons 1xa and 1u, respectively, was at equivalent levels whilst the expression of Type II mRNA containing exon 1xb was significantly less (
p<0.001). Immunoprobing of Western blotted muscle extracts with an antibody raised against a peptide sequence encoded by exon 1xa indicated that Type I protein was expressed and that there was significantly more Type I protein in cardiac than skeletal muscle (
p<0.001). The results suggest that the expression of the single calpastatin gene was differentially controlled at several levels.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Blotting, Western</subject><subject>Calcium-Binding Proteins - genetics</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Calpain</subject><subject>Calpastatin</subject><subject>Cardiac muscle</subject><subject>DNA Primers</subject><subject>Muscle, Skeletal - enzymology</subject><subject>Promoter analysis</subject><subject>Promoter Regions, Genetic</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - genetics</subject><subject>Skeletal muscle</subject><subject>Swine</subject><subject>Transfection</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1KxDAUhYMozjj6AG6kK3etuW3aJriSYfyBATe6jmmaQIa2qUkqztubMgO6Eg7cC_nOueQgdA04AwzV3S4TTZPlGJNsFoYTtATMqhQXlJyiJca4SBmtYIEuvN9FAEiVn6MFlFBTQosl-th8j055b-yQWJ1I0Y3CBxHMkBhvtXW9T-LeT152KhFDm-hpkCHiojNhP3v6qQtmjK9_zaOzvQ3K-Ut0pkXn1dVxrtD74-Zt_ZxuX59e1g_bVBIoQ0owiWryVlDJRElKKmqtiYKSVbpoWIvzlkopdIVrTQQVFc2LGkqlBavymhUrdHvIjZc_J-UD742XquvEoOzkeQ2M1RhoBOEASme9d0rz0ZleuD0HzOda-Y7HWvlcK5-FIXpujuFT06v213HsMQL3B0DFL34Z5biXRg1StcYpGXhrzT_xP-7Cidk</recordid><startdate>20040701</startdate><enddate>20040701</enddate><creator>Parr, Tim</creator><creator>Jewell, Kirsty K</creator><creator>Sensky, Paul L</creator><creator>Brameld, John M</creator><creator>Bardsley, Ronald G</creator><creator>Buttery, Peter J</creator><general>Elsevier Inc</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>20040701</creationdate><title>Expression of calpastatin isoforms in muscle and functionality of multiple calpastatin promoters</title><author>Parr, Tim ; Jewell, Kirsty K ; Sensky, Paul L ; Brameld, John M ; Bardsley, Ronald G ; Buttery, Peter J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-404404b2da8c9a5458a7ff4e1596f3b9d02d8ccaf607f4a8a6823715efa962793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Blotting, Western</topic><topic>Calcium-Binding Proteins - genetics</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Calpain</topic><topic>Calpastatin</topic><topic>Cardiac muscle</topic><topic>DNA Primers</topic><topic>Muscle, Skeletal - enzymology</topic><topic>Promoter analysis</topic><topic>Promoter Regions, Genetic</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - genetics</topic><topic>Skeletal muscle</topic><topic>Swine</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Parr, Tim</creatorcontrib><creatorcontrib>Jewell, Kirsty K</creatorcontrib><creatorcontrib>Sensky, Paul L</creatorcontrib><creatorcontrib>Brameld, John M</creatorcontrib><creatorcontrib>Bardsley, Ronald G</creatorcontrib><creatorcontrib>Buttery, Peter J</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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Parr, Tim</au><au>Jewell, Kirsty K</au><au>Sensky, Paul L</au><au>Brameld, John M</au><au>Bardsley, Ronald G</au><au>Buttery, Peter J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression of calpastatin isoforms in muscle and functionality of multiple calpastatin promoters</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2004-07-01</date><risdate>2004</risdate><volume>427</volume><issue>1</issue><spage>8</spage><epage>15</epage><pages>8-15</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Calpastatin is the specific endogenous inhibitor of calpain proteinase that is encoded by a single gene. Transient transfection assays in both a non-fusing skeletal muscle and non-muscle cell-line demonstrated that the putative porcine calpastatin promoter regions 5
′ to exons 1xa, 1xb, and 1u were functional. Both real-time quantitative and semi-quantitative RT-PCR on porcine skeletal muscle total RNA indicated that steady-state expression of Type I and III mRNAs containing exons 1xa and 1u, respectively, was at equivalent levels whilst the expression of Type II mRNA containing exon 1xb was significantly less (
p<0.001). Immunoprobing of Western blotted muscle extracts with an antibody raised against a peptide sequence encoded by exon 1xa indicated that Type I protein was expressed and that there was significantly more Type I protein in cardiac than skeletal muscle (
p<0.001). The results suggest that the expression of the single calpastatin gene was differentially controlled at several levels.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15178483</pmid><doi>10.1016/j.abb.2004.04.001</doi><tpages>8</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 2004-07, Vol.427 (1), p.8-15 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Animals Base Sequence Blotting, Western Calcium-Binding Proteins - genetics Calcium-Binding Proteins - metabolism Calpain Calpastatin Cardiac muscle DNA Primers Muscle, Skeletal - enzymology Promoter analysis Promoter Regions, Genetic Protein Isoforms - genetics Protein Isoforms - metabolism Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - genetics Skeletal muscle Swine Transfection |
| title | Expression of calpastatin isoforms in muscle and functionality of multiple calpastatin promoters |
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