| Characterization of calsequestrin of avian skeletal muscle. | |
| | |
MedLine Citation:
|
PMID: 2351747 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
A calsequentrin (CS)-like glycoprotein is present in the sarcoplasmic reticulum (SR) of chicken pectoralis muscle, which displays unusual properties: it binds relatively low amounts of Ca2+, compared to CS in mammalian skeletal muscle (Yap & MacLennan, 1976), it does not exhibit a marked pH-dependent shift in mobility in sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), and its metachromatic staining properties with Stains All are likewise peculiar (Damiani et al., 1986). We have now definitively localized the same protein to the junctional terminal cisternae (TC) fraction of the SR of chicken pectoralis muscle and have further characterized it, following purification by crystallization with Ca2+ and by Ca2(+)-dependent elution from phenyl-Sepharose columns. The purified protein (apparent Mr: 51 kDa), isoelectrofocuses at pH 4.5, and is readily identified on blots by a 45Ca overlay technique, similar to CS of rabbit skeletal muscle, but it binds half as much Ca2+ (about 20 moles of Ca2+ per mole of protein), as estimated by equilibrium dialysis. However, the chicken protein shares extensive similarities with mammalian CSs, concerning Ca2(+)-induced changes in maximum intrinsic fluorescence and the Ca2(+)-modulated interaction with phenyl-Sepharose, as well as in being protected by Ca2+ from proteolysis by either trypsin or chymotrypsin. We discuss how the presence of a Ca2(+)-regulated hydrophobic site in the CS molecule appears to be the most invariant property of the CS-family of Ca2(+)-binding proteins. |
| | |
Authors:
|
E Damiani; S Salvatori; A Margreth |
Related Documents
:
|
11855657 - Phospholamban: a promising therapeutic target in heart failure? 1309287 - Properties of immunoaffinity purified 106-kda ca2+ release channels from the skeletal s... 17601757 - Role of the calcium store in uterine contractility. 10066677 - Cellular mechanisms of altered contractility in the hypertrophied heart: big hearts, bi... 15862567 - Involvement of phospholipase c and intracellular calcium signaling in the gonadotropin-... 1899567 - Ca2(+)-dependent amylase secretion from pancreatic acinar cells occurs without activati... |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: Journal of muscle research and cell motility Volume: 11 ISSN: 0142-4319 ISO Abbreviation: J. Muscle Res. Cell. Motil. Publication Date: 1990 Feb |
Date Detail:
|
Created Date: 1990-07-18 Completed Date: 1990-07-18 Revised Date: 2006-11-15 |
Medline Journal Info:
|
Nlm Unique ID: 8006298 Medline TA: J Muscle Res Cell Motil Country: ENGLAND |
Other Details:
|
Languages: eng Pagination: 48-55 Citation Subset: IM |
Affiliation:
|
Consiglio Nazionale delle Ricerche, Centro di Studio per la Biologia e la Fisiopatologia Muscolare, Padova, Italy. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Animals Blotting, Western Calcium / metabolism, physiology Calsequestrin / analysis*, metabolism, ultrastructure Chickens / metabolism* Electrophoresis, Polyacrylamide Gel Muscle Proteins / analysis* Muscles / analysis*, metabolism, ultrastructure Sarcoplasmic Reticulum / ultrastructure Species Specificity |
| Chemical | |
Reg. No./Substance:
|
0/Calsequestrin; 0/Muscle Proteins; 7440-70-2/Calcium |
| Comments/Corrections | |
Erratum In:
|
J Muscle Res Cell Motil 1990 Oct;11(5):463 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Deterioration induced by physiological concentration of calcium ions in skinned muscle fibres.
Next Document: Different metabolic responses to exercise training programmes in single rat muscle fibres.