Author: J. Komulainen

0000000001311409

AUTHOR

J. Komulainen

The disruption of myofibre structures in skeletal muscle after forced lengthening contractions

Specific antibodies against structural proteins (actin, desmin, dystrophin, fibronectin) of muscle fibres were used to study the effect of forced lengthening contractions on muscle microarchitecture. Tibialis anterior (TA) muscle of male Wistar rats were subjected to 240 forced lengthening contractions. At consecutive time points (0, and 6 h, 2, 4, and 7 days) after stimulation, the TA muscle was excised for biochemical and histological assays. β-Glucuronidase activity, a quantitative indicator of muscle damage, showed increased values 2–7 days after the lengthening, peaking on day 4 (11.7-fold increase). A typical course of histopathological changes (myofibre swelling, necrosis and regener…

research product

CCDC 192292: Experimental Crystal Structure Determination

Related Article: M.S.Hannu-Kuure, J.Komulainen, R.Oilunkaniemi, R.S.Laitinen, R.Suontamo, M.Ahlgren|2003|J.Organomet.Chem.|666|111|doi:10.1016/S0022-328X(02)02108-3

research product

CCDC 192291: Experimental Crystal Structure Determination

Related Article: M.S.Hannu-Kuure, J.Komulainen, R.Oilunkaniemi, R.S.Laitinen, R.Suontamo, M.Ahlgren|2003|J.Organomet.Chem.|666|111|doi:10.1016/S0022-328X(02)02108-3

research product

CCDC 192290: Experimental Crystal Structure Determination

Related Article: M.S.Hannu-Kuure, J.Komulainen, R.Oilunkaniemi, R.S.Laitinen, R.Suontamo, M.Ahlgren|2003|J.Organomet.Chem.|666|111|doi:10.1016/S0022-328X(02)02108-3

research product

PEPhysical Sciences and Engineering
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LSLife Sciences
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