The neonatal sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCA1b): a neglected pump in scope

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• 作者：Ern? Zádor ; Magdolna Kósa
• 关键词：SERCA1b ; SERCA1a ; Skeletal muscle development ; SOCE
• 刊名：Pfl篓鹿gers Archiv - European Journal of Physiology
• 出版年：2015
• 出版时间：July 2015
• 年：2015
• 卷：467
• 期：7
• 页码：1395-1401
• 全文大小：340 KB
• 参考文献：1.Babu GJ, Bhupathy P, Carnes CA, Billman GE, Periasamy M (2007) Differential expression of sarcolipin protein during muscle development and cardiac pathophysiology. J Mol Cell Cardiol 43:215-2PubMed Central PubMed View Article
  2.Brandl CJ, deLeon S, Martin DR, MacLennan DH (1987) Adult forms of the Ca2+ ATPase of sarcoplasmic reticulum. Expression in developing skeletal muscle. J Biol Chem 262:3768-774PubMed
  3.Brandl CJ, Green NM, Korczak B, MacLennan DH (1986) Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences. Cell 44:597-07PubMed View Article
  4.Chami M, Gozuacik D, Lagorce D, Brini M, Falson P, Peaucellier G, Pinton P, Lecoeur H, Gougeon ML, le Maire M, Rizzuto R, Bréchot C, Paterlini-Bréchot P (2001) SERCA1 truncated proteins unable to pump calcium reduce the endoplasmic reticulum calcium concentration and induce apoptosis. J Cell Biol 153:1301-4PubMed Central PubMed View Article
  5.Collet C, Ma J (2004) Calcium-dependent facilitation and graded deactivation of store-operated calcium entry in fetal skeletal muscle. Biophys J 87:268-75PubMed Central PubMed View Article
  6.Fajardo VA, Bombardier E, Vigna C, Devji T, Bloemberg D, Gamu D, Gramolini AO, Quadrilatero J, Tupling AR (2013) Co-expression of SERCA isoforms, phospholamban and sarcolipin in human muscles. PLoS ONE 8:e84304. doi:10.-371/?journal.?pone.-084304 PubMed Central PubMed View Article
  7.Goonasekera SA, Lam CK, Millay DP, Sargent MA, Hajjar RJ, Kranias EG, Molkentin JD (2011) Mitigation of muscular dystrophy in mice by SERCA overexpression in skeletal muscle. J Clin Invest 121:1044-2. doi:10.-172/?JCI43844 PubMed Central PubMed View Article
  8.Guglielmi V, Vattemi G, Gualandi F, Voermans NC, Marini M, Scotton C, Pegoraro E, Oosterhof A, Kósa M, Zádor E, Valente EM, De Grandis D, Neri M, Codemo V, Novelli A, van Kuppevelt TH, Dallapiccola B, van Engelen BG, Ferlini A, Tomelleri G (2013) SERCA1 protein expression in muscle of patients with Brody disease and Brody syndrome and in cultured human muscle fibers. Mol Genet Metab 110:162-. doi:10.-016/?j.?ymgme.-013.-7.-15 PubMed View Article
  9.Guglielmi V, Voermans NC, Gualandi F, Van Engelen BG, Ferlini A, Tomelleri G, Vattemi G (2013) Fourty-four years of Brody disease: it is time to review. J Genet Syndr Gene Ther 4:2. doi:10.-172/-157-7412.-000181
  10.Kimura T, Nakamori M, Lueck JD, Pouliquin P, Aoike F, Fujimura H, Dirksen RT, Takahashi MP, Dulhunty AF, Sakoda S (2005) Altered mRNA splicing of the skeletal muscle ryanodine receptor and sarcoplasmic/endoplasmic reticulum Ca2--ATPase in myotonic dystrophy type 1. Hum Mol Genet 14:2189-200PubMed View Article
  11.Kósa M, Zádor E (2013) Transfection efficiency along the regenerating soleus muscle of the rat. Mol Biotechnol 54:220-27. doi:10.-007/?s12033-012-9555-2 PubMed View Article
  12.Launikonis BS, Murphy RM, Edwards JN (2010) Toward the roles of store-operated Ca2+ entry in skeletal muscle. Pflugers Arch 460:813-3. doi:10.-007/?s00424-010-0856-7 PubMed View Article
  13.Lee KJ, Hyun C, Woo JS, Park CS, do Kim H, Lee EH (2014) Stromal interaction molecule 1 (STIM1) regulates sarcoplasmic/endoplasmic reticulum Ca2+-ATPase 1a (SERCA1a) in skeletal muscle. Pflugers Arch 466:987-001PubMed View Article
  14.Manjarrés IM, Rodríguez-García A, Alonso MT, García-Sancho J (2010) The sarco/endoplasmic reticulum Ca(2+) ATPase (SERCA) is the third element in capacitative calcium entry. Cell Calcium 47:412-. doi:10.-016/?j.?ceca.-010.-3.-01 PubMed View Article
  15.Maruyama K, MacLennan DH (1988) Mutation of aspartic acid-351, lysine-352, and lysine-515 alters the Ca2+ transport activity of the Ca2--ATPase expressed in COS-1 cells. Proc Natl Acad Sci U S A 85:3314-318PubMed Central PubMed View Article
  16.Mendler L, Szakonyi G, Zádor E, G?rbe A, Dux L, Wuytack F (1998) Expression of sarcoplasmic/endoplasmic reticulum Ca2+ ATPases in the rat extensor digitorum longus (EDL) muscle regenerating from notexin-induced necrosis. J Muscle Res Cell Motil 19:777-85PubMed View Article
  17.Michalak M, Opas M (2009) Endoplasmic and sarcoplasmic reticulum in the heart. Trends Cell Biol 19:253-59. doi:10.-016/?j.?tcb.-009.-3.-06 PubMed View Article
  18.Odermatt A, Taschner PE, Khanna VK, Busch HF, Karpati G, Jablecki CK, Breuning MH, MacLennan DH (1996) Mutations in the gene-encoding SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+ ATPase, are associated with Brody disease. Nat Genet 14:191-PubMed View Article
  19.Pan Y, Zvaritch E, Tupling AR, Rice WJ, de Leon S, Rudnicki M, McKerlie C, Banwell BL, MacLennan DH (2003) Targeted disruption of the ATP2A1 gene encoding the sarco(endo)plasmic reticulum Ca2+ ATPase isoform 1 (SERCA1) impairs diaphragm function and is lethal in neonatal mice. J Biol Chem 278:13367-3375PubMed View Article
  20.Periasamy M, Kalyanasundaram A (2007) SERCA pump isoforms: their role in calc
• 作者单位：Ern? Zádor (1)
  Magdolna Kósa (1)
  
  1. Institute of Biochemistry, Faculty of Medicine, University of Szeged, Dóm tér 9, Szeged, 6720, Hungary
  
• 刊物主题：Human Physiology;
• 出版者：Springer Berlin Heidelberg
• ISSN：1432-2013

文摘

The neonatal isoform of the sarcoplasmic/endoplasmic reticulum Ca2+ ATPase (SERCA1b) is formed by developmental splicing and expressed fully only in developing muscle. As a major Ca2+ 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.