Short-term effects of forced eccentric contractions on collagen synthesis and degradation in rat skeletal muscle.
Acute downhill running has been shown to activate matrix metalloproteinase- (MMP-) 2 and to change type IV collagen concentration in some muscle types. In order to study the influence of more intense exercise on total collagen and type IV collagen concentrations, molecules regulating their synthesis and degradation were investigated after forced lengthening contractions in rat skeletal muscle. Tibialis anterior (TA) muscle of 24 male Wistar rats was subjected to 240 forced lengthening contractions. TA muscle was excised at consecutive time points (0 and 6 h, 2, 4, and 7 days) after stimulation. With immunohistochemistry, types I, III and IV collagen were located in the swollen, necrotic and regenerated fibres in a similar manner as in intact undamaged skeletal muscle fibre. An increase in the activity of prolyl 4-hydroxylase was indicative of an overall elevated collagen biosynthesis. No change was demonstrated in total collagen concentration, whereas type IV collagen concentration increased after exercise. MMP-2 and MMP-9, which are the proteins that degrade type IV collagen, elevated after exercise. In conclusion, the increase in type IV collagen concentration seems to be the result of an increase in both the synthesis and activation of degrading enzymes and their inhibitors during recovery after forced lengthening contractions.
Koskinen
Satu O A
SO
Neuromuscular Research Center, Department of Biology of Physical Activity, University of Jyväskylä, PO Box 35, 40351, Finland. koskinen@maila.jyu.fi
Ahtikoski
Anne M
AM
Komulainen
Jyrki
J
Hesselink
Matthijs K C
MK
Drost
Maarten R
MR
Takala
Timo E S
TE
D000818:Animals; D001345:Autoradiography; D015152:Blotting, Northern; D003094:Collagen / Q000096:biosynthesis* / Q000737:chemistry; D003488:Cyanogen Bromide / Q000737:chemistry; D004558:Electric Stimulation; D005109:Extracellular Matrix / Q000378:metabolism; D005780:Gelatin / Q000737:chemistry; D006909:Hydroxyproline / Q000378:metabolism; D015151:Immunoblotting; D007150:Immunohistochemistry; D008297:Male; D020780:Matrix Metalloproteinase 9 / Q000378:metabolism; D009119:Muscle Contraction / Q000502:physiology; D018485:Muscle Fibers, Skeletal / Q000378:metabolism; D018482:Muscle, Skeletal / Q000378:metabolism* / Q000473:pathology / Q000502:physiology*; D009336:Necrosis; D010455:Peptides / Q000737:chemistry; D011393:Procollagen-Proline Dioxygenase / Q000378:metabolism; D012333:RNA, Messenger / Q000096:biosynthesis; D051381:Rats; D017208:Rats, Wistar; D019716:Tissue Inhibitor of Metalloproteinase-2 / Q000378:metabolism
D010455:Peptides; D012333:RNA, Messenger; D019716:Tissue Inhibitor of Metalloproteinase-2; D005780:Gelatin; D003094:Collagen; D011393:Procollagen-Proline Dioxygenase; D020780:Matrix Metalloproteinase 9; D003488:Cyanogen Bromide; D006909:Hydroxyproline