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Muscle proteolytic enzyme activities in diabetic rats
The American Journal of Physiology
|November 1, 1981
Summary
Alkaline serine protease activity increased in diabetic rat muscle but did not contribute to muscle protein breakdown. This protease originates from mast cells, not muscle tissue.
Area of Science:
- Biochemistry
- Physiology
Background:
- Diabetes mellitus is associated with altered protein metabolism.
- The role of proteolytic enzymes in diabetic muscle wasting is not fully understood.
Purpose of the Study:
- To investigate the activity and origin of proteolytic enzymes in skeletal muscle of diabetic rats.
Main Methods:
- Streptozotocin-induced diabetes in Sprague-Dawley rats.
- Assay of alkaline serine protease and lysosomal cathepsin activities in muscle homogenates.
- Analysis of myofibril-associated protease activity.
- Investigation of mast cell involvement using compound 48/80.
Main Results:
- Diabetic rat muscle showed significantly increased alkaline serine protease activity compared to controls and insulin-treated rats.
- Lysosomal cathepsin activities remained unchanged in diabetic muscle.
- The alkaline serine protease was associated with myofibrils and originated from mast cells, as evidenced by its abolition after compound 48/80 treatment.
Conclusions:
- Alkaline serine proteases are not involved in muscle protein breakdown in diabetes.
- The observed serine protease activity in diabetic muscle is of mast cell origin.