The neonatal sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCA1b): a neglected pump in scope
The neonatal isoform of the sarcoplasmic/endoplasmic reticulum Ca 2+ ATPase (SERCA1b) is formed by developmental splicing and expressed fully only in developing muscle. As a major Ca 2+ pump in myotubes, SERCA1b must be detected in excitation contraction coupling or in store-operated calcium entry....
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description | The neonatal isoform of the sarcoplasmic/endoplasmic reticulum Ca
2+
ATPase (SERCA1b) is formed by developmental splicing and expressed fully only in developing muscle. As a major Ca
2+
pump in myotubes, SERCA1b must be detected in excitation contraction coupling or in store-operated calcium entry. The available pan SERCA1 antibodies also recognise SERCA1b but these are more frequently used to detect SERCA1a, the adult muscle-specific isoform characteristically expressed in fast fibres of skeletal muscle. In such applications, the pan SERCA1 antibodies are frequently claimed to be SERCA1a antibodies without proving it. Realistically, such an antibody cannot be made since it should recognise a single glycine at the C-terminal, the only part of SERCA1a that is different from SERCA1b. The false interpretation of the antibody specificity created inconsistence in the literature and led to false conclusions attributing features only to SERCA1a although those at least are also shared by SERCA1b. In contrast, a SERCA1b antibody has been made against the eight amino acid peptide tail that replaces the glycine of SERCA1a at the C-terminal. Therefore, the expression of SERCA1b can be specifically demonstrated, unlike that of SERCA1a, in various stages and conditions of skeletal muscle. This review argues against misbeliefs related to the distinction, expressions and functions of the two muscle-specific SERCA1 isoforms. |
doi_str_mv | 10.1007/s00424-014-1671-3 |
format | Article |
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2+
ATPase (SERCA1b) is formed by developmental splicing and expressed fully only in developing muscle. As a major Ca
2+
pump in myotubes, SERCA1b must be detected in excitation contraction coupling or in store-operated calcium entry. The available pan SERCA1 antibodies also recognise SERCA1b but these are more frequently used to detect SERCA1a, the adult muscle-specific isoform characteristically expressed in fast fibres of skeletal muscle. In such applications, the pan SERCA1 antibodies are frequently claimed to be SERCA1a antibodies without proving it. Realistically, such an antibody cannot be made since it should recognise a single glycine at the C-terminal, the only part of SERCA1a that is different from SERCA1b. The false interpretation of the antibody specificity created inconsistence in the literature and led to false conclusions attributing features only to SERCA1a although those at least are also shared by SERCA1b. In contrast, a SERCA1b antibody has been made against the eight amino acid peptide tail that replaces the glycine of SERCA1a at the C-terminal. Therefore, the expression of SERCA1b can be specifically demonstrated, unlike that of SERCA1a, in various stages and conditions of skeletal muscle. This review argues against misbeliefs related to the distinction, expressions and functions of the two muscle-specific SERCA1 isoforms.</description><identifier>ISSN: 0031-6768</identifier><identifier>EISSN: 1432-2013</identifier><identifier>DOI: 10.1007/s00424-014-1671-3</identifier><identifier>PMID: 25515082</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Animals ; Biomedical and Life Sciences ; Biomedicine ; Calcium Signaling ; Cell Biology ; Gene Expression Regulation, Developmental ; Human Physiology ; Humans ; Invited Review ; Molecular Medicine ; Muscle, Skeletal - enzymology ; Muscle, Skeletal - growth & development ; Muscle, Skeletal - metabolism ; Neurosciences ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Receptors ; Sarcoplasmic Reticulum Calcium-Transporting ATPases - genetics ; Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism</subject><ispartof>Pflügers Archiv, 2015-07, Vol.467 (7), p.1395-1401</ispartof><rights>Springer-Verlag Berlin Heidelberg 2014</rights><rights>Springer-Verlag Berlin Heidelberg 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-d5206e79c059f790f3d7ea7646178fc9b398ab01ed0d91844d99407b77d381173</citedby><cites>FETCH-LOGICAL-c405t-d5206e79c059f790f3d7ea7646178fc9b398ab01ed0d91844d99407b77d381173</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00424-014-1671-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00424-014-1671-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27902,27903,41466,42535,51296</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25515082$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zador, Ern</creatorcontrib><creatorcontrib>Kosa, Magdolna</creatorcontrib><title>The neonatal sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCA1b): a neglected pump in scope</title><title>Pflügers Archiv</title><addtitle>Pflugers Arch - Eur J Physiol</addtitle><addtitle>Pflugers Arch</addtitle><description>The neonatal isoform of the sarcoplasmic/endoplasmic reticulum Ca
2+
ATPase (SERCA1b) is formed by developmental splicing and expressed fully only in developing muscle. As a major Ca
2+
pump in myotubes, SERCA1b must be detected in excitation contraction coupling or in store-operated calcium entry. The available pan SERCA1 antibodies also recognise SERCA1b but these are more frequently used to detect SERCA1a, the adult muscle-specific isoform characteristically expressed in fast fibres of skeletal muscle. In such applications, the pan SERCA1 antibodies are frequently claimed to be SERCA1a antibodies without proving it. Realistically, such an antibody cannot be made since it should recognise a single glycine at the C-terminal, the only part of SERCA1a that is different from SERCA1b. The false interpretation of the antibody specificity created inconsistence in the literature and led to false conclusions attributing features only to SERCA1a although those at least are also shared by SERCA1b. In contrast, a SERCA1b antibody has been made against the eight amino acid peptide tail that replaces the glycine of SERCA1a at the C-terminal. Therefore, the expression of SERCA1b can be specifically demonstrated, unlike that of SERCA1a, in various stages and conditions of skeletal muscle. This review argues against misbeliefs related to the distinction, expressions and functions of the two muscle-specific SERCA1 isoforms.</description><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Calcium Signaling</subject><subject>Cell Biology</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Human Physiology</subject><subject>Humans</subject><subject>Invited Review</subject><subject>Molecular Medicine</subject><subject>Muscle, Skeletal - enzymology</subject><subject>Muscle, Skeletal - growth & development</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Neurosciences</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Receptors</subject><subject>Sarcoplasmic Reticulum Calcium-Transporting ATPases - genetics</subject><subject>Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism</subject><issn>0031-6768</issn><issn>1432-2013</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkU1LHTEUhoNU9Fb7A9yUQDd2MfWcJDNJurtc7AcIit6uQybJ2JH5MplZ-O-by1UpQunqBPKcJ-fkJeQM4QsCyIsEIJgoAEWBlcSCH5AVCs4KBsjfkRUAx6KSlTom71N6AAAmFDsix6wssQTFVsRtfwc6hHGws-1ostGNU2dT37qLMPiXM41hbt3SLT11tnNtruvtjU2Bnt9d3m7WWH_-Sm323HfBzcHTaekn2g40ZV04JYeN7VL48FxPyK9vl9vNj-Lq-vvPzfqqcALKufAlgypI7aDUjdTQcC-DlZWoUKrG6ZprZWvA4MFrVEJ4rQXIWkrPFaLkJ-R8753i-LiENJu-TS50nc0LLsmgzD-lFIjq_2iVOZDAMKOf3qAP4xKHvMiOkkJLqVmmcE-5OKYUQ2Om2PY2PhkEswvL7MMyeQSzC8vw3PPx2bzUffCvHS_pZIDtgZSvhvsQ_3r6n9Y_GAScEw</recordid><startdate>20150701</startdate><enddate>20150701</enddate><creator>Zador, Ern</creator><creator>Kosa, Magdolna</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</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>3V.</scope><scope>7QP</scope><scope>7TK</scope><scope>7TS</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope></search><sort><creationdate>20150701</creationdate><title>The neonatal sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCA1b): a neglected pump in scope</title><author>Zador, Ern ; Kosa, Magdolna</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c405t-d5206e79c059f790f3d7ea7646178fc9b398ab01ed0d91844d99407b77d381173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Animals</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Calcium Signaling</topic><topic>Cell Biology</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Human Physiology</topic><topic>Humans</topic><topic>Invited Review</topic><topic>Molecular Medicine</topic><topic>Muscle, Skeletal - enzymology</topic><topic>Muscle, Skeletal - growth & development</topic><topic>Muscle, Skeletal - metabolism</topic><topic>Neurosciences</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Receptors</topic><topic>Sarcoplasmic Reticulum Calcium-Transporting ATPases - genetics</topic><topic>Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zador, Ern</creatorcontrib><creatorcontrib>Kosa, Magdolna</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Physical Education Index</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><jtitle>Pflügers Archiv</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zador, Ern</au><au>Kosa, Magdolna</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The neonatal sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCA1b): a neglected pump in scope</atitle><jtitle>Pflügers Archiv</jtitle><stitle>Pflugers Arch - Eur J Physiol</stitle><addtitle>Pflugers Arch</addtitle><date>2015-07-01</date><risdate>2015</risdate><volume>467</volume><issue>7</issue><spage>1395</spage><epage>1401</epage><pages>1395-1401</pages><issn>0031-6768</issn><eissn>1432-2013</eissn><abstract>The neonatal isoform of the sarcoplasmic/endoplasmic reticulum Ca
2+
ATPase (SERCA1b) is formed by developmental splicing and expressed fully only in developing muscle. As a major Ca
2+
pump in myotubes, SERCA1b must be detected in excitation contraction coupling or in store-operated calcium entry. The available pan SERCA1 antibodies also recognise SERCA1b but these are more frequently used to detect SERCA1a, the adult muscle-specific isoform characteristically expressed in fast fibres of skeletal muscle. In such applications, the pan SERCA1 antibodies are frequently claimed to be SERCA1a antibodies without proving it. Realistically, such an antibody cannot be made since it should recognise a single glycine at the C-terminal, the only part of SERCA1a that is different from SERCA1b. The false interpretation of the antibody specificity created inconsistence in the literature and led to false conclusions attributing features only to SERCA1a although those at least are also shared by SERCA1b. In contrast, a SERCA1b antibody has been made against the eight amino acid peptide tail that replaces the glycine of SERCA1a at the C-terminal. Therefore, the expression of SERCA1b can be specifically demonstrated, unlike that of SERCA1a, in various stages and conditions of skeletal muscle. This review argues against misbeliefs related to the distinction, expressions and functions of the two muscle-specific SERCA1 isoforms.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>25515082</pmid><doi>10.1007/s00424-014-1671-3</doi><tpages>7</tpages></addata></record> |
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subjects | Animals Biomedical and Life Sciences Biomedicine Calcium Signaling Cell Biology Gene Expression Regulation, Developmental Human Physiology Humans Invited Review Molecular Medicine Muscle, Skeletal - enzymology Muscle, Skeletal - growth & development Muscle, Skeletal - metabolism Neurosciences Protein Isoforms - genetics Protein Isoforms - metabolism Receptors Sarcoplasmic Reticulum Calcium-Transporting ATPases - genetics Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism |
title | The neonatal sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCA1b): a neglected pump in scope |
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