|
|
|
|
|
||
|
|||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
doi: 10.1242/10.1242/jcs.00303
Research Article |
1 Institute of Medical Technology and Medical School, University of Tampere,
Tampere, Finland
2 Department of Surgery, Tampere University Hospital, Tampere, Finland
3 Department of Morphology, National Institute of Traumatology, Budapest,
Hungary
4 The Accident and Trauma Research Center, the UKK-Institute and the Tampere
Research Center of Sports Medicine, Tampere; Finland
5 Department of Pathology, University Hospital of Turku and Paavo Nurmi Center,
Turku, Finland
* Author for correspondence (e-mail: blteja{at}uta.fi)
Accepted 4 December 2002
Tenascin-C is a hexabrachion-shaped matricellular protein with a very restricted expression in normal musculoskeletal tissues, but it is expressed abundantly during regenerative processes of these tissues and embryogenesis. To examine the importance of mechanical stress for the regulation of tenascin-C expression in the muscle-tendon unit, the effects of various states of mechanical loading (inactivity by cast-immobilization and three-varying intensities of subsequent re-activity by treadmill running) on the expression of tenascin-C were studied using immunohistochemistry and mRNA in situ hybridization at the different locations of the muscle-tendon unit of the rat gastrocnemius muscle, the Achilles tendon complex. This muscle-tendon unit was selected as the study site, because the contracting activity of the gastrocnemius-soleus muscle complex, and thus the mechanical loading-induced stimulation, is easy to block by cast immobilization.
Tenascin-C was expressed abundantly in the normal myotendinous and myofascial junctions, as well as around the cells and the collagen fibers of the Achilles tendon. Tenascin-C expression was not found in the normal skeletal muscle, although it was found in blood vessels within the muscle tissue. Following the removal of the mechanical loading-induced stimulation on the muscle-tendon unit by cast immobilization for 3 weeks, the immonoreactivity of tenascin-C substantially decreased or was completely absent in the regions expressing tenascin-C normally. Restitution of the mechanical loading by removing the cast and allowing free cage activity for 8 weeks resulted in an increase in tenascin-C expression, but it could not restore the expression of tenascin-C to the normal level (in healthy contralateral leg). In response to the application of a more strenuous mechanical loading stimulus after the removal of the cast (after 8 weeks of low- and high-intensity treadmill running), the expression of tenascin-C was markedly increased and reached the level seen in the healthy contralateral limb. Tenascin-C was abundantly expressed in myotendinous and myofascial junctions and in the Achilles tendon, but even the most strenuous mechanical loading (high-intensity treadmill running) could not induce the expression of tenascin-C in the skeletal muscle. This was in spite of the marked immobilization-induced atrophy of the previously immobilized skeletal muscle, which had been subjected to intensive stress during remobilization. mRNA in situ hybridization analysis confirmed the immunohistochemical results for the expression of tenascin-C in the study groups.
In summary, this study shows that mechanical loading regulates the expression of tenascin-C in an apparently dose-dependent fashion at sites of the muscle-tendon unit normally expressing tenascin-C but can not induce de novo synthesis of tenascin-C in the skeletal muscle without accompanying injury to the tissue. Our results suggest that tenascin-C provides elasticity in mesenchymal tissues subjected to heavy tensile loading.
Key words: Tenascin-C, Mechanical strain, Fibronectin, Skeletal muscle, Tendon, Cartilage, Bone, Tensile, Elastic, Extracellular matrix, Adhesion, Integrin
This article has been cited by other articles:
|
|
 |
|
  E. Zinovieva, N. Lebrun, F. Letourneur, F.-X. Laurent, R. Said-Nahal, G. Chiocchia, and M. Breban Lack of association between Tenascin-C gene and spondyloarthritis Rheumatology, November 1, 2008; 47(11): 1655 - 1658. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Fluck, S. I. Mund, J. C. Schittny, S. Klossner, A.-C. Durieux, and M.-N. Giraud Mechano-regulated Tenascin-C orchestrates muscle repair PNAS, September 9, 2008; 105(36): 13662 - 13667. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. M. Crameri, P. Aagaard, K. Qvortrup, H. Langberg, J. Olesen, and M. Kjaer Myofibre damage in human skeletal muscle: effects of electrical stimulation versus voluntary contraction J. Physiol., August 15, 2007; 583(1): 365 - 380. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. V September, M. P Schwellnus, M. Collins, and W. Gibson Tendon and ligament injuries: the genetic component * COMMENTARY Br. J. Sports Med., April 1, 2007; 41(4): 241 - 246. [Full Text] [PDF]
|
|
|
|
 |
|
 G. G. Mokone, M. Gajjar, A. V. September, M. P. Schwellnus, J. Greenberg, T. D. Noakes, and M. Collins The Guanine-Thymine Dinucleotide Repeat Polymorphism Within the Tenascin-C Gene Is Associated With Achilles Tendon Injuries Am. J. Sports Med., July 1, 2005; 33(7): 1016 - 1021. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. A. H. Jarvinen, T. L. N. Jarvinen, M. Kaariainen, H. Kalimo, and M. Jarvinen Muscle Injuries: Biology and Treatment Am. J. Sports Med., May 1, 2005; 33(5): 745 - 764. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. Szoke, S.-H. Lee, A. H. R. W. Simpson, and J. Prescott Response of the tendon during limb lengthening J Bone Joint Surg Br, April 1, 2005; 87-B(4): 583 - 587. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y.-W. Chen, M. J. Hubal, E. P. Hoffman, P. D. Thompson, and P. M. Clarkson Molecular responses of human muscle to eccentric exercise J Appl Physiol, December 1, 2003; 95(6): 2485 - 2494. [Abstract] [Full Text]
|
|
|
|
 |
|
 M. Chiquet and M. Fluck Ectopic expression of tenascin-C J. Cell Sci., October 1, 2003; 116(19): 3851 - 3851. [Full Text] [PDF]
|
|
|
|
|
|
M. Chiquet and M. Fluck Rebuttal J. Cell Sci., October 1, 2003; 116(19): 3853 - 3853. [Full Text]
|
|
|
|
|
|
T. A. H. Jarvinen, T. L. N. Jarvinen, P. Kannus, and H. Kalimo Reply J. Cell Sci., October 1, 2003; 116(19): 3851 - 3853. [Full Text]
|
|
