Download PDF
Int J Sports Med 2012; 33(02): 137-141
DOI: 10.1055/s-0031-1291224
Training &Testing
© Georg Thieme Verlag KG Stuttgart · New York

MMP−2 Expression in Skeletal Muscle after Strength Training

A.P. L. Deus
1   UFSCar, Physiotherapy, Sao Carlos, Brazil
,
D. Bassi
1   UFSCar, Physiotherapy, Sao Carlos, Brazil
,
R. P. Simões
1   UFSCar, Physiotherapy, Sao Carlos, Brazil
,
C. R. Oliveira
2   Federal University of Sao Carlos, Medicine Department, Sao Carlos, Brazil
,
V. Baldissera
3   UFSCar, Physiological Sciences, Sao Carlos, Brazil
,
R. de Cássia Marqueti
4   Universidade Federal de São Carlos, Ciências Fisiológicas, São Carlos, Brazil
,
H.S. S. Araujo
4   Universidade Federal de São Carlos, Ciências Fisiológicas, São Carlos, Brazil
,
R. Arena
5   University of New Mexico, Department of Orthopaedics and Rehabilitation, Albuquerque, United States
,
A. Borghi-Silva
1   UFSCar, Physiotherapy, Sao Carlos, Brazil
› Author Affiliations
Further Information

Publication History



accepted after revision 12 September 2011

Publication Date:
17 November 2011 (online)

Also available at
    Permissions and Reprints

Abstract

The aim of this study was to assess the effects of resistance training on ladders (RTL) on MMP−2 expression and blood lactate concentration [La−]. 30 male (3 months of age), albino rats were divided into 3 groups: sedentary control (SC, n=10), low resistance exercise training (Low-IntRT, n=10) and high-intensive exercise training (High-IntRT, n=10). Animals of High-IntRT were submitted to a progressively increasing overload in relation to body weight until exhaustion, while the Low-IntRT group performed the same exercise regimen with no external load. The program had a frequency of 3 times per week over 8 weeks. MMP−2 expression of tibialis anterior muscle and [La−] were measured. While there was a significant increase of MMP−2 (pro-form) in both groups, only High-IntRT significantly increased MMP−2 in active-form (p<0.05). Both trained groups exhibited an increase in [La−] when compared to controls, however, the increase in [La−] was significantly higher in the High-IntRT compared to Low-IntRT (p<0.05). Strong correlation was found between MMP−2 (active form) and [La−] in High-IntRT (r=0.91). RTL in using low and high-intensity exercise can serve as a model to demonstrate different responses of MMP−2 expression in an animal model. It appears active form expression of MMP−2 is modulated by exercise intensity.

Key words

resistance exercise - blood lactate - matrix metalopeptidases - ladder exercise
 

  • References

  • 1 Carmeli E, Maor M, Kodesh E. Expression of superoxide dismutase and matrix metalloproteinase type 2 in diaphragm muscles of young rats. J Physiol Pharmacol 2009; 60: 31-36
    PubMedGoogle Scholar
  • 2 Carmeli E, Moas M, Lennon S, Powers SK. High intensity exercise increases expression of matrix metalloproteinases in fast skeletal muscle fibres. Exp Physiol 2005; 90: 613-619
    CrossrefPubMedGoogle Scholar
  • 3 Carmeli E, Moas M, Reznick AZ, Coleman R. Matrix metalloproteinases and skeletal muscle: a brief review. Muscle Nerve 2004; 29: 191-197
    CrossrefPubMedGoogle Scholar
  • 4 Collins JM, Ramamoorthy K, Silveira A, Patston P, Mão J. Expression of matrix metalloproteinase genes in the rat intramembranous bone during postnatal growth and upon mechanical stresses. J Biomech 2005; 38: 485-492
    CrossrefPubMedGoogle Scholar
  • 5 Fry AC. The role of the resistance exercise intensity on muscle fiber adaptations. Sports Med 2004; 34: 663-679
    CrossrefPubMedGoogle Scholar
  • 6 Gladden LB. Muscle as a consumer of lactate. Med Sci Sport Exerc 2000; 32: 764-771
    CrossrefPubMedGoogle Scholar
  • 7 Glass DJ. Skeletal muscle hypertrophy and atrophy signaling pathways. Int J Biochem Cell Biol 2005; 37: 1974-1984
    CrossrefPubMedGoogle Scholar
  • 8 Goldspink G. Gene expression in muscle in response to exercise. J Muscle Res Cell Motil 2003; 24: 121-126
    CrossrefPubMedGoogle Scholar
  • 9 Harriss DJ, Atkinson G. Update – Ethical Standards in Sport and Exercise Science Research. Int J Sports Med 2011; 32: 819-821
    Article in Thieme ConnectPubMedGoogle Scholar
  • 10 Hornberger TA, Farrar RP. Physiological hypertrophy of the FHL muscle following 8 weeks of progressive resistance exercise in the rat. Can J Appl Physiol 2004; 29: 16-31
    CrossrefPubMedGoogle Scholar
  • 11 James RS, Navas CA, Herrel A. How important are skeletal muscle mechanics in setting limits on jumping performance?. J Exp Biol 2007; 210: 923-933
    CrossrefPubMedGoogle Scholar
  • 12 Kjaer M, Magnusson P, Krogsgaard M, Boysen Møller J, Olesen J, Heinemeier K, Hansen M, Haraldsson B, Koskinen S, Esmarck B, Langberg H. Extracellular matrix adaptation of tendon and skeletal muscle to exercise. J Anat 2006; 208: 445-450 Review
    CrossrefPubMedGoogle Scholar
  • 13 Koskinen SOA, Heinemeier KM, Olesen JL, Langberg H, Kjaer M. Physical exercise can influence local levels of matrix metalloproteinases and their inhibitors in tendon-related connective tissue. J Appl Physiol 2004; 96: 861-864
    PubMedGoogle Scholar
  • 14 Koskinen SO, Wang W, Ahtikoski AM, Kjaer M, Han XY, Komulainen J, Kovanen V, Takala TE. Acute exercise induced changes in rat skeletal muscle mRNAs and proteins regulating type IV collagen content. Am J Physiol 2001; 280: R1292-R1300
    PubMedGoogle Scholar
  • 15 Marqueti RC, Parizotto NA, Chriguer RS, Perez SE, Selistre-de-Araujo HS. Androgenic-anabolic steroids associated with mechanical loading inhibit matrix metallopeptidase activity and affect the remodeling of the Achilles tendon in rats. Am J Sports Med 2006; 34: 1274-1280
    CrossrefPubMedGoogle Scholar
  • 16 Marqueti RC, Prestes J, Stotzer US, Paschoal M, Leite RD, Perez SE, Selistre de Araujo HS. MMP−2, Jumping exercise and nandrolone in skeletal muscle. Int J Sports Med 2008; 29: 559-563
    Article in Thieme ConnectPubMedGoogle Scholar
  • 17 Maxová H, Novotná J, Vajner L, Tomásová H, Vytásek R, Vízek M, Bacáková L, Valousková V, Eliásová T, Herget J. In vitro hypoxia increases production of matrix metalloproteinases and tryptase in isolated rat lung mast cells. Physiol Res 2008; 57: 903-910
    PubMedGoogle Scholar
  • 18 Muhs BE, Gagne P, Plitas G, Shaw JP, Shamamian P. Experimental hindlimb ischemia leads to neutrophilmediated increases in gastrocnemius MMP−2 and −9 activity: a potential mechanism for ischemia induced MMP activation. J Surg Res 2004; 117: 249-254
    CrossrefPubMedGoogle Scholar
  • 19 Nishimura A, Sugita M, Kato K, Fukuda A, Sudo A, Uchida A. Hypoxia increases muscle hypertrophy induced by resistance training. Int J Sports Physiol Perform 2010; 5: 497-508
    PubMedGoogle Scholar
  • 20 Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol 2007; 8: 221-233
    CrossrefPubMedGoogle Scholar
  • 21 Roach DM, Fitridge RA, Laws PE, Millard SH, Varelias A, Cowled PA. Up-regulation of MMP−2 and MMP−9 leads to degradation of type IV collagen during skeletal muscle reperfusion injury; protection by the MMP inhibitor, doxycycline. Eur J Vasc Endovasc Surg 2002; 23: 260-269
    CrossrefPubMedGoogle Scholar
  • 22 Rullman E, Norrbom J, Stromberg A, Wagsater D, Rundqvist H, Haas T, Gustafsson T. Endurance exercise activates matrix metalloproteinases in human skeletal muscle. J Appl Physiol 2009; 106: 804-812
    CrossrefPubMedGoogle Scholar
  • 23 Suominen H, Kiiskinen A, Heikkinen E. Effects of physical training on metabolism of connective tissues in young mice. Acta Physiol Scand 1980; 108: 17-22
    CrossrefPubMedGoogle Scholar
  • 24 Verzola RM, Mesquita RA, Peviani S, Ramos OH, Moriscot AS, Perez SE, Selistre-de-Araújo HS. Early remodeling of rat cardiac muscle induced by swimming training. Braz J Med Biol Res 2006; 39: 621-627
    CrossrefPubMedGoogle Scholar
  • 25 Vu TH, Werb Z. Matrix metalloproteinases: effectors of development and normal physiology. Gene Dev 2000; 14: 2123-2133
    CrossrefPubMedGoogle Scholar