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Lung injury-dependent oxidative status and chymotrypsin-like activity of skeletal muscles in hamsters with experimental emphysema.

BMC musculoskeletal disorders (2013-01-25)
Jair Tonon, Alessandra Lourenço Cecchini, Cláudia Roberta Brunnquell, Sara Santos Bernardes, Rubens Cecchini, Flávia Alessandra Guarnier
ABSTRACT

Peripheral skeletal muscle is altered in patients suffering from emphysema and chronic obstructive pulmonary disease (COPD). Oxidative stress have been demonstrated to participate on skeletal muscle loss of several states, including disuse atrophy, mechanical ventilation, and chronic diseases. No evidences have demonstrated the occurance in a severity manner. We evaluated body weight, muscle loss, oxidative stress, and chymotrypsin-like proteolytic activity in the gastrocnemius muscle of emphysemic hamsters. The experimental animals had 2 different severities of lung damage from experimental emphysema induced by 20 mg/mL (E20) and 40 mg/mL (E40) papain. The severity of emphysema increased significantly in E20 (60.52 ± 2.8, p < 0.05) and E40 (52.27 ± 4.7; crossed the alveolar intercepts) groups. As compared to the control group, there was a reduction on body (171.6 ± 15.9 g) and muscle weight (251.87 ± 24.87 mg) in the E20 group (157.5 ± 10.3 mg and 230.12 ± 23.52 mg, for body and muscle weight, respectively), which was accentuated in the E40 group (137.4 ± 7.2 g and 197.87 ± 10.49 mg, for body and muscle weight, respectively). Additionally, the thiobarbituric acid reactive substances (TBARS), tert-butyl hydroperoxide-initiated chemiluminescence (CL), carbonylated proteins, and chymotrypsin-like proteolytic activity were elevated in the E40 group as compared to the E20 group (p < 0.05 for all comparisons). The severity of emphysema significantly correlated with the progressive increase in CL (r = -0.95), TBARS (r = -0.98), carbonyl proteins (r = -0.99), and chymotrypsin-like proteolytic activity (r = -0.90). Furthermore, augmentation of proteolytic activity correlated significantly with CL (r = 0.97), TBARS (r = 0.96), and carbonyl proteins (r = 0.91). Taken together, the results of the present study suggest that muscle atrophy observed in this model of emphysema is mediated by increased muscle chymotrypsin-like activity, with possible involvement of oxidative stress in a severity-dependent manner.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Luperox® TBH70X, tert-Butyl hydroperoxide solution, 70 wt. % in H2O
Sigma-Aldrich
α-Chymotrypsin from human pancreas, lyophilized powder
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α-Chymotrypsin−Agarose from bovine pancreas, lyophilized powder, 2,000-3,500 units/g agarose (One ml gel will yield 65-120 units)
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α-Chymotrypsin from bovine pancreas, ≥40 units/mg protein, vial of 5 mg
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α-Chymotrypsin from bovine pancreas, suitable for protein sequencing, salt-free, lyophilized powder
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α-Chymotrypsin from bovine pancreas, Type I-S, essentially salt-free, lyophilized powder
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α-Chymotrypsin from bovine pancreas, Type II, lyophilized powder, ≥40 units/mg protein
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α-Chymotrypsin from bovine pancreas, (TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein
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Papain from papaya latex, crude powder, 1.5-10 units/mg solid
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Papain from papaya latex, lyophilized powder, aseptically filled
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tert-Butyl hydroperoxide solution, 5.0-6.0 M in nonane
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tert-Butyl hydroperoxide solution, 5.0-6.0 M in decane
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Papain from Carica papaya, powder, ≥3 U/mg
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Papain from Carica papaya, solution, light brown, ≥10 U/mg protein (~25 mg/ml)