Am J Physiol Cell Physiol Watch the video to see how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 291: C147-C154, 2006. First published February 15, 2006; doi:10.1152/ajpcell.00578.2005
0363-6143/06 $8.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
291/1/C147    most recent
00578.2005v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 ISI Web of Science (6)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zhang, S.-J.
Right arrow Articles by Katz, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhang, S.-J.
Right arrow Articles by Katz, A.

CELLULAR METABOLISM

Cross bridges account for only 20% of total ATP consumption during submaximal isometric contraction in mouse fast-twitch skeletal muscle

Shi-Jin Zhang, Daniel C. Andersson, Marie E. Sandström, Håkan Westerblad, and Abram Katz

Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden

Submitted 18 November 2005 ; accepted in final form 2 February 2006

It is generally believed that cross bridges account for >50% of the total ATP consumed by skeletal muscle during contraction. We investigated the effect of N-benzyl-p-toluene sulfonamide (BTS), an inhibitor of myosin ATPase, on muscle force production and energy metabolism under near-physiological conditions (50-Hz stimulation frequency at 30°C results in 35% of maximal force). Extensor digitorum longus muscles from mice were isolated and stimulated to perform continuous isometric tetanic contractions. Metabolites of energy metabolism were analyzed with fluorometric techniques. ATP turnover was estimated from the changes in phosphocreatine (PCr), ATP, and lactate (–2{Delta}ATP – {Delta}PCr + [1.5{Delta}lactate]). During contractions (2–10 s), BTS decreased force production to ~5% of control. Under these conditions, BTS inhibited ATP turnover by only 18–25%. ATP turnover decreased markedly and similarly with and without BTS as the duration of contraction progressed. In conclusion, cross bridges (i.e., actomyosin ATPase) account for only a small fraction (~20%) of the ATP consumption during contraction in mouse fast-twitch skeletal muscle under near-physiological conditions, suggesting that ion pumping is the major energy-consuming process.

ATPase; high-energy phosphates; lactate


Address for reprint requests and other correspondence: A. Katz, Dept. of Physiology and Pharmacology, Karolinska Institutet, Von Eulers väg 8, 171 77 Stockholm, Sweden (e-mail: abram.katz{at}fyfa.ki.se)




This article has been cited by other articles:


Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
D. R. Blair, K. Funai, G. G. Schweitzer, and G. D. Cartee
A myosin II ATPase inhibitor reduces force production, glucose transport, and phosphorylation of AMPK and TBC1D1 in electrically stimulated rat skeletal muscle
Am J Physiol Endocrinol Metab, May 1, 2009; 296(5): E993 - E1002.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
A. J. Rose, T. J. Alsted, T. E. Jensen, J. B. Kobbero, S. J. Maarbjerg, J. Jensen, and E. A. Richter
A Ca2+-calmodulin-eEF2K-eEF2 signalling cascade, but not AMPK, contributes to the suppression of skeletal muscle protein synthesis during contractions
J. Physiol., April 1, 2009; 587(7): 1547 - 1563.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
N. Lefort, E. St.-Amand, S. Morasse, C. H. Cote, and A. Marette
The {alpha}-subunit of AMPK is essential for submaximal contraction-mediated glucose transport in skeletal muscle in vitro
Am J Physiol Endocrinol Metab, December 1, 2008; 295(6): E1447 - E1454.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
T. E. Jensen, A. J. Rose, Y. Hellsten, J. F. P. Wojtaszewski, and E. A. Richter
Caffeine-induced Ca2+ release increases AMPK-dependent glucose uptake in rodent soleus muscle
Am J Physiol Endocrinol Metab, July 1, 2007; 293(1): E286 - E292.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
K. T. Murphy and T. Clausen
The importance of limitations in aerobic metabolism, glycolysis, and membrane excitability for the development of high-frequency fatigue in isolated rat soleus muscle
Am J Physiol Regulatory Integrative Comp Physiol, May 1, 2007; 292(5): R2001 - R2011.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
M. E. Sandstrom, S.-J. Zhang, H. Westerblad, and A. Katz
Mechanical load plays little role in contraction-mediated glucose transport in mouse skeletal muscle
J. Physiol., March 1, 2007; 579(2): 527 - 534.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
C. J. Barclay and D. S. Loiselle
Can activation account for 80% of skeletal muscle energy use during isometric contraction?
Am J Physiol Cell Physiol, January 1, 2007; 292(1): C612 - C612.
[Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
S.-J. Zhang, D. C. Andersson, M. E. Sandstrom, H. Westerblad, and A. Katz
Reply to Barclay and Loiselle
Am J Physiol Cell Physiol, January 1, 2007; 292(1): C613 - C614.
[Full Text] [PDF]

Home page
 J. Physiol.Home page
A. J. Rose, B. Kiens, and E. A. Richter
Ca2+-calmodulin-dependent protein kinase expression and signalling in skeletal muscle during exercise
J. Physiol., August 1, 2006; 574(3): 889 - 903.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online
Copyright © 2006 by the American Physiological Society.