FASEB J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
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 Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by FRANZINI-ARMSTRONG, C.
Right arrow Search for Related Content
PubMed
Right arrow Articles by FRANZINI-ARMSTRONG, C.
(The FASEB Journal. 1999;13:S266-S270.)
© 1999 FASEB

The sarcoplasmic reticulum and the control of muscle contraction

CLARA FRANZINI-ARMSTRONG1

Department of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA

1Correspondence: B1 Anatomy-Chemistry Bldg, Department of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, PA 19104-6058, USA. E-mail: armstroc{at}mail.med.upenn.edu

Activation of muscle contraction is a rapid event that is initiated by electrical activity in the surface membrane and transverse (T) tubules. This is followed by release of calcium from the inner membrane system, the sarcoplasmic reticulum (SR). Using electron microscopy (EM), K. R. Porter and his laboratory defined the SR, the unique junctions between SR and T tubules, and the continuity between T tubules and surface membrane. Current research in this area centers on the interaction between T tubules and SR. This is mediated by 2 well-identified calcium channels: the dihydropyridine receptors (DHPRs) that act as voltage sensors in the T tubules, and the ryanodine receptors (RyRs) or calcium release channels of the SR. The relative positions of these 2 molecules differ significantly in skeletal and cardiac muscle, and this correlates well with known functional differences in the control of contraction. Molecular biology experiments combined with EM indicate that DHPRs are linked to RyRs in skeletal but probably not in cardiac muscle.—Franzini-Armstrong, C. The sarcoplasmic reticulum and the control of muscle contraction.


Key Words:




This article has been cited by other articles:


Home page
Biophys. JHome page
G. S. B. Williams, M. A. Huertas, E. A. Sobie, M. S. Jafri, and G. D. Smith
Moment Closure for Local Control Models of Calcium-Induced Calcium Release in Cardiac Myocytes
Biophys. J., August 15, 2008; 95(4): 1689 - 1703.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. A. Borzok, D. H. Catino, J. D. Nicholson, A. Kontrogianni-Konstantopoulos, and R. J. Bloch
Mapping the Binding Site on Small Ankyrin 1 for Obscurin
J. Biol. Chem., November 2, 2007; 282(44): 32384 - 32396.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
H. Kong, R. Wang, W. Chen, L. Zhang, K. Chen, Y. Shimoni, H. J. Duff, and S. R. W. Chen
Skeletal and Cardiac Ryanodine Receptors Exhibit Different Responses to Ca2+ Overload and Luminal Ca2+
Biophys. J., April 15, 2007; 92(8): 2757 - 2770.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
G. S. B. Williams, M. A. Huertas, E. A. Sobie, M. S. Jafri, and G. D. Smith
A Probability Density Approach to Modeling Local Control of Calcium-Induced Calcium Release in Cardiac Myocytes
Biophys. J., April 1, 2007; 92(7): 2311 - 2328.
[Abstract] [Full Text] [PDF]


Home page
Cardiovasc ResHome page
J. Gorelik, L. Q. Yang, Y. Zhang, M. Lab, Y. Korchev, and S. E. Harding
A novel Z-groove index characterizing myocardial surface structure
Cardiovasc Res, December 1, 2006; 72(3): 422 - 429.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
X.-F. Hu, X. Liang, K.-Y. Chen, H. Xie, Y. Xu, P.-H. Zhu, and J. Hu
Modulation of the Oligomerization of Isolated Ryanodine Receptors by their Functional States
Biophys. J., September 1, 2005; 89(3): 1692 - 1699.
[Abstract] [Full Text] [PDF]


Home page
J. Physiol.Home page
B. S. Launikonis, J. Zhou, L. Royer, T. R. Shannon, G. Brum, and E. Rios
Confocal imaging of [Ca2+] in cellular organelles by SEER, shifted excitation and emission ratioing of fluorescence
J. Physiol., September 1, 2005; 567(2): 523 - 543.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Heart Circ. Physiol.Home page
R. M. Guzzo, M. Salih, E. D. Moore, and B. S. Tuana
Molecular properties of cardiac tail-anchored membrane protein SLMAP are consistent with structural role in arrangement of excitation-contraction coupling apparatus
Am J Physiol Heart Circ Physiol, April 1, 2005; 288(4): H1810 - H1819.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
W. J. H. Koopman, M. Renders, A. Oosterhof, T. H. van Kuppevelt, B. G. M. van Engelen, and P. H. G. M. Willems
Upregulation of Ca2+ removal in human skeletal muscle: a possible role for Ca2+-dependent priming of mitochondrial ATP synthesis
Am J Physiol Cell Physiol, November 1, 2003; 285(5): C1263 - C1269.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Kontrogianni-Konstantopoulos and R. J. Bloch
The Hydrophilic Domain of Small Ankyrin-1 Interacts with the Two N-terminal Immunoglobulin Domains of Titin
J. Biol. Chem., January 31, 2003; 278(6): 3985 - 3991.
[Abstract] [Full Text] [PDF]


Home page
Cardiovasc ResHome page
J. Hescheler and B. K. Fleischmann
Integrins and cell structure: powerful determinants of heart development and heart function
Cardiovasc Res, September 1, 2000; 47(4): 645 - 647.
[Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1999 by The Federation of American Societies for Experimental Biology.