Experimental Physiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Experimental Physiology 77.3 pp 433-442
© The Physiological Society 1992
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 Pattullo, M.
Right arrow Articles by Barry, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pattullo, M.
Right arrow Articles by Barry, J.
Experimental Physiology, Vol 77, Issue 3, 433-442
Copyright © 1992 by The Physiological Society


Article

Effects of lengthened immobilization on functional and histochemical properties of rabbit tibialis anterior muscle

MC Pattullo, MA Cotter, NE Cameron, and JA Barry

The imposition of long-term lengthened immobilization on rabbit tibialis anterior (TA) muscles resulted in rapid increases in slow oxidative (SO) fibre number. After 2 weeks, SO number had increased 2-fold and was 5 times greater after 6 weeks immobilization. There were also fibre-type-specific effects on SO, fast oxidative glycolytic (FOG) and fast glycolytic (FG) fibre areas. Twitch strength was unchanged throughout immobilization whilst production of tetanic tension was impaired during the initial period but had returned to control levels by 6 weeks. Twitch contraction times and isometrically determined rates of rise and relaxation were largely unaffected by immobilization despite the marked increase in expression of slow myosin. The change in phenotypic expression of the lengthened TA was not attributable to chronically increased levels of activation since integrated EMG activity was unchanged from control values throughout the immobilization period. Thus it is suggested that a chronic increase in tension consequent on the lengthening procedure is a potent stimulus for fast-to-slow myosin transformation.


This article has been cited by other articles:


Home page
Am. J. Respir. Crit. Care Med.Home page
J. GEA, Q. HAMID, G. CZAIKA, E. ZHU, V. MOHAN-RAM, G. GOLDSPINK, and A. GRASSINO
Expression of Myosin Heavy-Chain Isoforms in the Respiratory Muscles Following Inspiratory Resistive Breathing
Am. J. Respir. Crit. Care Med., April 1, 2000; 161(4): 1274 - 1278.
[Abstract] [Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1992 by the The Physiological Society.