| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Généthon, CNRS URA 1922-1923, 91002 Evry; 2 Laboratoire de Physiologie, Atelier de Régénération Neuromusculaire, Faculté de Médecine Saint-Antoine, 75012 Paris, France; and 3 Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel
Lack of functional calpain 3 in humans is a cause
of limb girdle muscular dystrophy, but the function(s) of calpain 3 remain(s) unknown. Special muscle conditions in which calpain 3 is
downregulated could yield valuable clues to the understanding of its
function(s). We monitored calpain 3 mRNA amounts by quantitative RT-PCR
and compared them with those of 
-skeletal actin mRNA in mouse leg muscles for different types of denervation and muscle injury. Intact
muscle denervation reduced calpain 3 mRNA expression by a factor of 5 to 10, while -skeletal actin mRNA was reduced in a slower and less
extensive manner. Muscle injury (denervation-devascularization), which
leads to muscle degeneration and regeneration, induced a 20-fold
decrease in the mRNA level of both calpain 3 and -skeletal actin.
Furthermore, whereas in normal muscle and intact denervated muscle, the
full-length transcript is the major calpain 3 mRNA, in injured muscle,
isoforms lacking exon 6 are predominant during the early regeneration
process. These data suggest that muscle condition determines the
specific calpain 3 isoform pattern of expression and that calpain 3 expression is downregulated by denervation.
calpain; -skeletal actin; regeneration; reverse
transcriptase-polymerase chain reaction
This article has been cited by other articles:
|
|
 |
|
  I. J. Smith, S. H. Lecker, and P.-O. Hasselgren Calpain activity and muscle wasting in sepsis Am J Physiol Endocrinol Metab, October 1, 2008; 295(4): E762 - E771. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y.-W. Chen, C. M. Gregory, M. T. Scarborough, R. Shi, G. A. Walter, and K. Vandenborne Transcriptional pathways associated with skeletal muscle disuse atrophy in humans Physiol Genomics, November 14, 2007; 31(3): 510 - 520. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Bartoli, N. Bourg, D. Stockholm, F. Raynaud, A. Delevacque, Y. Han, P. Borel, K. Seddik, N. Armande, and I. Richard A Mouse Model for Monitoring Calpain Activity under Physiological and Pathological Conditions J. Biol. Chem., December 22, 2006; 281(51): 39672 - 39680. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Morita, K. Iizuka, K. Okita, T. Oikawa, K. Yonezawa, T. Nagai, Y. Tokumitsu, T. Murakami, A. Kitabatake, and H. Kawaguchi Exposure to pressure stimulus enhances succinate dehydrogenase activity in L6 myoblasts Am J Physiol Endocrinol Metab, December 1, 2004; 287(6): E1064 - E1069. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 X. Yu and D. L. Mykles Cloning of a muscle-specific calpain from the American lobster Homarus americanus: expression associated with muscle atrophy and restoration during moulting J. Exp. Biol., February 1, 2003; 206(3): 561 - 575. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. T. JAGOE, S. H. LECKER, M. GOMES, and A. L. GOLDBERG Patterns of gene expression in atrophying skeletal muscles: response to food deprivation FASEB J, November 1, 2002; 16(13): 1697 - 1712. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L Feasson, D Stockholm, D Freyssenet, I Richard, S Duguez, J S Beckmann, and C Denis Molecular adaptations of neuromuscular disease-associated proteins in response to eccentric exercise in human skeletal muscle J. Physiol., August 15, 2002; 543(1): 297 - 306. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Visit Other APS Journals Online |
