Literature DB >> 1544490

Coexistence of two calsequestrin isoforms in rabbit slow-twitch skeletal muscle fibers.

D Biral1, P Volpe, E Damiani, A Margreth.   

Abstract

The cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capacity Ca2+ binding protein localized in the lumen of sarcoplasmic reticulum, are the products of two different genes (Fliegel, L., Leberer, E., Green, N.M. and MacLennan, D.H. (1982) FEBS Lett. 242, 297-300), and can be both purified from slow-twitch skeletal muscle of the rabbit (Damiani, E., Volpe, P. and Margreth, A. (1990) J. Muscle Res. Cell Motil. 11, 522-530). Here we show that both CS isoforms coexist in slow-twitch muscle fibers as indicated by indirect immunofluorescent staining of cryosections with affinity-purified antibodies specific for each CS isoform.

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Year:  1992        PMID： 1544490     DOI： 10.1016/0014-5793(92)80241-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  18 in total

Review 1.  Ca(2+) signaling in striated muscle: the elusive roles of triadin, junctin, and calsequestrin.

Authors:  Nicole A Beard; Lan Wei; Angela Fay Dulhunty
Journal:  Eur Biophys J       Date:  2009-05-12       Impact factor: 1.733

2.  Characterization of fast-twitch and slow-twitch skeletal muscles of calsequestrin 2 (CASQ2)-knock out mice: unexpected adaptive changes of fast-twitch muscles only.

Authors:  Giorgia Valle; Barbara Vergani; Roberta Sacchetto; Carlo Reggiani; Edith De Rosa; Lisa Maccatrozzo; Alessandra Nori; Antonello Villa; Pompeo Volpe
Journal:  J Muscle Res Cell Motil       Date:  2017-01-27       Impact factor: 2.698

3.  Identification of calcium binding sites on calsequestrin 1 and their implications for polymerization.

Authors:  Amit Kumar; Harapriya Chakravarty; Naresh C Bal; Tuniki Balaraju; Nivedita Jena; Gauri Misra; Chandralata Bal; Enrico Pieroni; Muthu Periasamy; Ashoke Sharon
Journal:  Mol Biosyst       Date:  2013-04-29

4.  Specific effects of endurance and sprint training on protein expression of calsequestrin and SERCA in mouse skeletal muscle.

Authors:  Sanni Kinnunen; Satu Mänttäri
Journal:  J Muscle Res Cell Motil       Date:  2012-03-31       Impact factor: 2.698

5.  Constitutive assembly of Ca2+ entry units in soleus muscle from calsequestrin knockout mice.

Authors:  Antonio Michelucci; Laura Pietrangelo; Giorgia Rastelli; Feliciano Protasi; Robert T Dirksen; Simona Boncompagni
Journal:  J Gen Physiol       Date:  2022-10-12       Impact factor: 4.000

6.  The C-terminal calcium-sensitive disordered motifs regulate isoform-specific polymerization characteristics of calsequestrin.

Authors:  Naresh C Bal; Nivedita Jena; Harapriya Chakravarty; Amit Kumar; Mei Chi; Tuniki Balaraju; Sharad V Rawale; Jayashree S Rawale; Ashoke Sharon; Muthu Periasamy
Journal:  Biopolymers       Date:  2015-01       Impact factor: 2.505

7.  Interaction of triadin with histidine-rich Ca(2+)-binding protein at the triadic junction in skeletal muscle fibers.

Authors:  R Sacchetto; F Turcato; E Damiani; A Margreth
Journal:  J Muscle Res Cell Motil       Date:  1999-05       Impact factor: 2.698

8.  Postnatal development of rabbit fast-twitch skeletal muscle: accumulation, isoform transition and fibre distribution of calsequestrin.

Authors:  R Sacchetto; P Volpe; E Damiani; A Margreth
Journal:  J Muscle Res Cell Motil       Date:  1993-12       Impact factor: 2.698

9.  Characterization study of the ryanodine receptor and of calsequestrin isoforms of mammalian skeletal muscles in relation to fibre types.

Authors:  E Damiani; A Margreth
Journal:  J Muscle Res Cell Motil       Date:  1994-04       Impact factor: 2.698

10.  Calsequestrin is a component of smooth muscles: the skeletal- and cardiac-muscle isoforms are both present, although in highly variable amounts and ratios.

Authors:  P Volpe; A Martini; S Furlan; J Meldolesi
Journal:  Biochem J       Date:  1994-07-15       Impact factor: 3.857
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