Literature DB >> 2227093

Identification and developmental expression of a chicken calsequestrin homolog.

E S Choi1, D O Clegg.   

Abstract

Calsequestrin (CAL) is a calcium-binding protein whose primary function is thought to involve sequestration of calcium in the muscle sarcoplasmic reticulum (SR). Little is known about the mechanisms regulating CAL expression, or about the role of this protein in muscle development. In addition, CAL may regulate calcium localization in some nonmuscle cells. We have identified an avian calsequestrin homolog. The predicted amino acid sequence of the avian CAL, first described as a laminin binding protein, and named aspartactin, is 70-80% identical to mammalian CAL sequences. We have used affinity-purified antibodies and cDNA probes to investigate expression in developing and adult chicken tissues. In adult chickens, the avian CAL homolog was expressed in slow and fast twitch skeletal muscle as well as in cardiac muscle. Surprisingly high levels of CAL protein were also detected in cerebellum. During development, CAL mRNA and protein were detected in Embryonic Day 5 (E-5) limb primordia, well before the initiation of myoblast fusion. In leg skeletal muscle, CAL protein and mRNA increase approximately 10-fold from E-8 to E-18 with a time course that just precedes myoblast fusion. This early expression pattern was also observed in cultured chicken pectoral myoblasts, and appears to be regulated at the level of mRNA abundance. The developmental profile of CAL expression is compared to that of other muscle proteins and possible additional functions of CAL are discussed.

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Year:  1990        PMID: 2227093     DOI: 10.1016/0012-1606(90)90160-k

Source DB:  PubMed          Journal:  Dev Biol        ISSN: 0012-1606            Impact factor:   3.582


  12 in total

1.  Development of the excitation-contraction coupling apparatus in skeletal muscle: peripheral and internal calcium release units are formed sequentially.

Authors:  H Takekura; X Sun; C Franzini-Armstrong
Journal:  J Muscle Res Cell Motil       Date:  1994-04       Impact factor: 2.698

2.  Calsequestrinlike calcium-binding protein is expressed in calcium-accumulating cells of Pistia stratiotes.

Authors:  V R Franceschi; X Li; D Zhang; T W Okita
Journal:  Proc Natl Acad Sci U S A       Date:  1993-08-01       Impact factor: 11.205

Review 3.  Sarcoplasmic reticulum calsequestrins: structural and functional properties.

Authors:  K Yano; A Zarain-Herzberg
Journal:  Mol Cell Biochem       Date:  1994-06-15       Impact factor: 3.396

4.  Expression of the calsequestrin gene in chicken cerebellum Purkinje neurons.

Authors:  P Volpe; L Gorza; M Brini; R Sacchetto; S Ausoni; D O Clegg
Journal:  Biochem J       Date:  1993-09-01       Impact factor: 3.857

5.  Characterization of a calsequestrin-like protein from sea-urchin eggs.

Authors:  D Lebeche; B Kaminer
Journal:  Biochem J       Date:  1992-11-01       Impact factor: 3.857

6.  Luminal Ca2+ regulation of single cardiac ryanodine receptors: insights provided by calsequestrin and its mutants.

Authors:  Jia Qin; Giorgia Valle; Alma Nani; Alessandra Nori; Nicoletta Rizzi; Silvia G Priori; Pompeo Volpe; Michael Fill
Journal:  J Gen Physiol       Date:  2008-03-17       Impact factor: 4.086

7.  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

8.  s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin.

Authors:  S Arber; K H Krause; P Caroni
Journal:  J Cell Biol       Date:  1992-01       Impact factor: 10.539

9.  Differential localization and functional role of calsequestrin in growing and differentiated myoblasts.

Authors:  M Raichman; M C Panzeri; E Clementi; P Papazafiri; M Eckley; D O Clegg; A Villa; J Meldolesi
Journal:  J Cell Biol       Date:  1995-02       Impact factor: 10.539

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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