Journal of Applied Physiology http://www.adinstruments.com/labchart/faseb
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Appl Physiol 73: 631-641, 1992;
8750-7587/92 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 Chalmers, G. R.
Right arrow Articles by Edgerton, V. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chalmers, G. R.
Right arrow Articles by Edgerton, V. R.

Journal of Applied Physiology, Vol 73, Issue 2 631-641, Copyright © 1992 by American Physiological Society


ARTICLES

Variation and limitations in fiber enzymatic and size responses in hypertrophied muscle

G. R. Chalmers, R. R. Roy and V. R. Edgerton
Brain Research Institute, University of California, Los Angeles 90024-1527.

The present study was designed to determine whether the degree and kind of adaptation of a muscle fiber to a functional overload (FO) are determined by properties that are intrinsic to that fiber. The study also addresses the question of the capability of fibers to maintain a normal level of coordination of proteins per fiber as fiber volume changes dramatically. The plantaris muscle of six adult female cats was overloaded for 12 wk by bilateral synergist removal. Plantaris muscle fiber mean size doubled after FO, although some very small fibers that stained dark for adenosinetriphosphatase (ATPase) were observed in some of the FO muscles. There appeared to be no change in total succinate dehydrogenase activity per fiber. A reduction in succinate dehydrogenase activity per unit volume was observed in a substantial number of fibers, reflecting a disproportionate increase in fiber volume relative to mitochondrial volume. In contrast, total alpha-glycerophosphate dehydrogenase activity and actomyosin ATPase activity increased as fiber size increased, whereas there was no change in alpha-glycerophosphate dehydrogenase and ATPase activities per unit volume. Control and FO muscle fibers generally expressed either a fast or slow myosin heavy chain type, but in some cases FO muscle fibers expressed both fast and slow myosin heavy chains. The persistence of variability in fiber sizes and enzyme activities in fibers of overloaded muscles suggests a wide range in the adaptive potential of individual fibers to FO. These data indicate that a severalfold increase in cell size may occur without significant qualitative changes in the coordination of protein regulation associated with metabolic pathways and ATP utilization.


This article has been cited by other articles:


Home page
J. Appl. Physiol.Home page
V. A. DePalo, A. L. Parker, F. Al-Bilbeisi, and F. D. McCool
Respiratory muscle strength training with nonrespiratory maneuvers
J Appl Physiol, February 1, 2004; 96(2): 731 - 734.
[Abstract] [Full Text] [PDF]


Home page
J. Appl. Physiol.Home page
R. R. Roy, S. R. Monke, D. L. Allen, and V. R. Edgerton
Modulation of myonuclear number in functionally overloaded and exercised rat plantaris fibers
J Appl Physiol, August 1, 1999; 87(2): 634 - 642.
[Abstract] [Full Text] [PDF]


Home page
J. Appl. Physiol.Home page
R. R. Roy, R. J. Talmadge, K. Fox, M. Lee, A. Ishihara, and V. R. Edgerton
Modulation of MHC isoforms in functionally overloaded and exercised rat plantaris fibers
J Appl Physiol, July 1, 1997; 83(1): 280 - 290.
[Abstract] [Full Text] [PDF]




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