Editorials |
From the Unit of Cardiac Physiology, University of Manchester, Manchester, UK.
Correspondence to D.A. Eisner, Unit of Cardiac Physiology, 1.524 Stopford Bldg, University of Manchester, Oxford Road, Manchester M13 9PT. E-mail eisner@man.ac.uk
Key Words: calcium sarcoplasmic reticulum fluorescence
An extract of the first 250 words of the full text is provided, because this article has no abstract. |
The bulk of the Ca2+ that activates contraction in the heart comes from the sarcoplasmic reticulum (SR). Calcium is released by the process of Ca2+-induced Ca2+ release (CICR) in which the entry of a small amount of Ca2+ across the cell membrane triggers the release of much more from the SR. This mechanism depends on the fact that Ca2+ entry from the extracellular fluid (via the L-type Ca2+ current) increases the probability that the SR Ca2+ release channel (ryanodine receptor, RyR) is open. The greater the open probability of the RyR, the greater the release of Ca2+ from the SR and therefore the larger the contraction of the heart. A major factor determining the contractility of the heart is the Ca2+ content of the SR. As one might expect, the more Ca2+ that there is in the SR, the more is released on each contraction. However the degree of filling of the SR has other important implications for cardiac physiology and pathology. Excessive filling of the SR (Ca2+ overload) results in Ca2+ release even in the absence of a trigger. When this Ca2+ release occurs in diastole, it can activate inward membrane currents and produce afterdepolarizations. In the field of heart failure, the decrease of the systolic Ca2+ transient is generally associated with a decrease of SR Ca2+ content, although the precise mechanisms responsible for this remain controversial.1,2
Given the importance of SR Ca2+ content, it is essential to be able to measure it. Many previous studies have used
This article has been cited by other articles:
![]() |
T. Guo, X. Ai, T. R. Shannon, S. M. Pogwizd, and D. M. Bers Intra Sarcoplasmic Reticulum Free [Ca2+] and Buffering in Arrhythmogenic Failing Rabbit Heart Circ. Res., October 12, 2007; 101(8): 802 - 810. [Abstract] [Full Text] [PDF] |
||||
![]() |
Y. Chen-Izu, C. W. Ward, W. Stark Jr., T. Banyasz, M. P. Sumandea, C. W. Balke, L. T. Izu, and X. H. T. Wehrens Phosphorylation of RyR2 and shortening of RyR2 cluster spacing in spontaneously hypertensive rat with heart failure Am J Physiol Heart Circ Physiol, October 1, 2007; 293(4): H2409 - H2417. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. R. Wilding, F. Joubert, C. de Araujo, D. Fortin, M. Novotova, V. Veksler, and R. Ventura-Clapier Altered energy transfer from mitochondria to sarcoplasmic reticulum after cytoarchitectural perturbations in mice hearts J. Physiol., August 15, 2006; 575(1): 191 - 200. [Abstract] [Full Text] [PDF] |
||||
![]() |
X. Wu and D. M. Bers Sarcoplasmic Reticulum and Nuclear Envelope Are One Highly Interconnected Ca2+ Store Throughout Cardiac Myocyte Circ. Res., August 4, 2006; 99(3): 283 - 291. [Abstract] [Full Text] [PDF] |
||||
|
Circulation Research Home | Subscriptions | Archives | Feedback | Authors | Help | AHA Journals Home | Search Copyright © 2003 American Heart Association, Inc. All rights reserved. Unauthorized use prohibited. |