Am J Physiol Cell Physiol Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 257: C504-C511, 1989;
0363-6143/89 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zorzato, F.
Right arrow Articles by Margreth, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zorzato, F.
Right arrow Articles by Margreth, A.

AJP - Cell Physiology, Vol 257, Issue 3 C504-C511, Copyright © 1989 by American Physiological Society

ARTICLES

Terminal cisternae of denervated rabbit skeletal muscle: alterations of functional properties of Ca2+ release channels

F. Zorzato, P. Volpe, E. Damiani, D. Quaglino Jr and A. Margreth
Centro di Studio per la Biologia e la Fisiopatologia Muscolare del Consiglio Nazionale delle Ricerche, Istituto di Patologia Generale dell'Universita di Padova, Padua, Italy.

Terminal cisternae (TC) of skeletal muscle represent the specialized compartment from which Ca2+ is released into the myoplasm after a propagated action potential. In this study we have investigated the morphology, protein composition, and Ca2+ release properties of TC isolated from rabbit gastrocnemius muscle 2 wk after nerve sectioning. Thin-section electron microscopy showed that TC vesicles from denervated muscle were enriched in calsequestrin (CS) and contained a larger fraction of the junctional sarcoplasmic reticulum (SR), as judged by membrane profiles with morphologically intact feet structures. Accordingly, the yield of junctional SR from denervated muscle was twice that of control muscle, and the protein pattern of TC vesicles exhibited an increase in junctional protein components, e.g., CS and the 350-kDa protein. The larger content of the 350-kDa protein, or ryanodine receptor (F.A. Lai, H. Erickson, E. Rousseau, Q.-Y. Liu, and G. Meissner, Nature Lond. 331: 315-319, 1988; T. Imagawa, J. S. Smith, R. Coronado, and K. P. Campbell. J. Biol. Chem. 262: 10636-10643, 1987; L. Hymel, M. Inui, S. Fleischer, and H. Schindler, Proc. Natl. Acad. Sci. USA 85:441-445, 1988) was paralleled by an increased binding site density (Bmax) for ryanodine binding in denervated muscle TC. The effects of ruthenium red, a Ca2+ release blocker, on Ca2+ loading rate and Ca2+-ATPase activity suggested that TC from denervated muscle were less permeable to Ca2+. After active Ca2+ loading, both doxorubicin and caffeine induced Ca2+ release from isolated TC, yet Ca2+ release rates were reduced in denervated muscle TC.(ABSTRACT TRUNCATED AT 250 WORDS)


This article has been cited by other articles:


Home page
 J. Physiol.Home page
C. Paolini, M. Quarta, A. Nori, S. Boncompagni, M. Canato, P. Volpe, P. D. Allen, C. Reggiani, and F. Protasi
Reorganized stores and impaired calcium handling in skeletal muscle of mice lacking calsequestrin-1
J. Physiol., September 1, 2007; 583(2): 767 - 784.
[Abstract] [Full Text] [PDF]

Home page
 Pharmacol. Rev.Home page
R. Zucchi and S. Ronca-Testoni
The Sarcoplasmic Reticulum Ca2+ Channel/Ryanodine Receptor: Modulation by Endogenous Effectors, Drugs and Disease States
Pharmacol. Rev., March 1, 1997; 49(1): 1 - 52.
[Abstract] [Full Text] [PDF]

Home page
 J. Appl. Physiol.Home page
E. Germinario, A. Esposito, A. Megighian, M. Midrio, D. Biral, R. Betto, and D. Danieli-Betto
Early changes of type 2B fibers after denervation of rat EDL skeletal muscle
J Appl Physiol, May 1, 2002; 92(5): 2045 - 2052.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online