Am J Physiol Cell Physiol Ad Instruments
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Cell Physiol 254: C651-C656, 1988;
0363-6143/88 $5.00
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
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 Google Scholar
Google Scholar
Right arrow Articles by Babij, P.
Right arrow Articles by Booth, F. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Babij, P.
Right arrow Articles by Booth, F. W.

AJP - Cell Physiology, Vol 254, Issue 5 C651-C656, Copyright © 1988 by American Physiological Society


ARTICLES

Alpha-actin and cytochrome c mRNAs in atrophied adult rat skeletal muscle

P. Babij and F. W. Booth
Department of Physiology and Cell Biology, Medical School, University of Texas Health Science Center, Houston 77225.

Specific complementary DNA (cDNA) hybridization probes were used to estimate the levels of alpha-actin and cytochrome c mRNAs and also 18S rRNA in three models of skeletal muscle atrophy. After 7 days of hindlimb suspension, or immobilization, or denervation, protein content decreased 26-32% in all muscles studied except suspended fast-twitch muscle, which lost only half as much protein. alpha-Actin mRNA content decreased 51-66% and cytochrome c mRNA content decreased 42-61% in slow- and fast-twitch muscles in all three models of atrophy. However, total RNA content did not show similar directional changes; RNA content decreased 27-44% in suspended and immobilized muscle but was unchanged in denervated fast-twitch muscle. The results were interpreted to suggest that loss of weight-bearing function of skeletal muscle is a major factor affecting the levels of alpha-actin and cytochrome c mRNAs during muscle atrophy.


This article has been cited by other articles:


Home page
J. Appl. Physiol.Home page
J. M. Giger, P. W. Bodell, M. Zeng, K. M. Baldwin, and F. Haddad
Rapid muscle atrophy response to unloading: pretranslational processes involving MHC and actin
J Appl Physiol, October 1, 2009; 107(4): 1204 - 1212.
[Abstract] [Full Text] [PDF]


Home page
J. Exp. Biol.Home page
N. J. Hudson and C. E. Franklin
Maintaining muscle mass during extended disuse: aestivating frogs as a model species
J. Exp. Biol., August 1, 2002; 205(15): 2297 - 2303.
[Abstract] [Full Text] [PDF]


Home page
J. Appl. Physiol.Home page
E. Smol, E. Zernicka, D. Czarnowski, and J. Langfort
Lipoprotein lipase activity in skeletal muscles of the rat: effects of denervation and tenotomy
J Appl Physiol, March 1, 2001; 90(3): 954 - 960.
[Abstract] [Full Text] [PDF]


Home page
J. Appl. Physiol.Home page
S. E. Gordon, M. Fluck, and F. W. Booth
Plasticity in Skeletal, Cardiac, and Smooth Muscle: Selected Contribution: Skeletal muscle focal adhesion kinase, paxillin, and serum response factor are loading dependent
J Appl Physiol, March 1, 2001; 90(3): 1174 - 1183.
[Abstract] [Full Text] [PDF]


Home page
J. Appl. Physiol.Home page
R. H. Fitts, D. R. Riley, and J. J. Widrick
Physiology of a Microgravity Environment Invited Review: Microgravity and skeletal muscle
J Appl Physiol, August 1, 2000; 89(2): 823 - 839.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
C. J. Carlson, F. W. Booth, and S. E. Gordon
Skeletal muscle myostatin mRNA expression is fiber-type specific and increases during hindlimb unloading
Am J Physiol Regulatory Integrative Comp Physiol, August 1, 1999; 277(2): R601 - R606.
[Abstract] [Full Text] [PDF]


Home page
J. Appl. Physiol.Home page
X.-Y. Han, W. Wang, R. Myllyla, P. Virtanen, J. Karpakka, and T. E. S. Takala
mRNA levels for alpha -subunit of prolyl 4-hydroxylase and fibrillar collagens in immobilized rat skeletal muscle
J Appl Physiol, July 1, 1999; 87(1): 90 - 96.
[Abstract] [Full Text] [PDF]


Home page
J. Appl. Physiol.Home page
R. Kell, H. Pierce, and S. J. Swoap
PGAM-M expression is regulated pretranslationally in hindlimb muscles and under altered loading conditions
J Appl Physiol, January 1, 1999; 86(1): 236 - 242.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Endocrinol. Metab.Home page
D. S. Criswell, F. W. Booth, F. DeMayo, R. J. Schwartz, S. E. Gordon, and M. L. Fiorotto
Overexpression of IGF-I in skeletal muscle of transgenic mice does not prevent unloading-induced atrophy
Am J Physiol Endocrinol Metab, September 1, 1998; 275(3): E373 - E379.
[Abstract] [Full Text] [PDF]


Home page
J. Appl. Physiol.Home page
D. S. Criswell, V. R. M. Hodgson, E. C. Hardeman, and F. W. Booth
Nerve-responsive troponin I slow promoter does not respond to unloading
J Appl Physiol, March 1, 1998; 84(3): 1083 - 1087.
[Abstract] [Full Text] [PDF]


Home page
J. Appl. Physiol.Home page
H. Jankala, V.-P. Harjola, N. E. Petersen, and M. Harkonen
Myosin heavy chain mRNA transform to faster isoforms in immobilized skeletal muscle: a quantitative PCR study
J Appl Physiol, March 1, 1997; 82(3): 977 - 982.
[Abstract] [Full Text] [PDF]


Home page
Circ. Res.Home page
A. Simonini, C. S. Long, G. A. Dudley, P. Yue, J. McElhinny, and B. M. Massie
Heart Failure in Rats Causes Changes in Skeletal Muscle Morphology and Gene Expression That Are Not Explained by Reduced Activity
Circ. Res., July 1, 1996; 79(1): 128 - 136.
[Abstract] [Full Text]




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