Fluorescence demonstration of a cathepsin H-like protease in cardiac, skeletal and vascular smooth muscles.
A cathepsin H-like enzyme was localized by histochemical techniques in cardiac muscle, extensor digitorum longus and soleus skeletal muscles, and vascular smooth muscle. Using the specific exopeptidase activity of this enzyme against the substrate arg-4-methoxy-beta-naphthylamide, valid histochemical assay conditions were developed. More fluorescent granules were observed in cardiac muscle than in the soleus and about equal amounts in vascular smooth muscle and the extensor digitorum longus. The reaction rate was enhanced by chloride ions and inhibited by 1 mM p-chloromercuribenzoate. The maximal activity was observed between pH 5.5 and 6.0 Chemical fixation with periodate-lysine-paraformaldehyde preserved a small amount of enzymatic activity.
D000818:Animals; D056655:Cathepsin H; D002403:Cathepsins / Q000032:analysis* / Q000378:metabolism; D003546:Cysteine Endopeptidases; D006651:Histocytochemistry; D008297:Male; D009131:Muscle, Smooth, Vascular / Q000201:enzymology*; D009132:Muscles / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000032:analysis*; D051381:Rats; D011919:Rats, Inbred Strains; D013194:Staining and Labeling; D013379:Substrate Specificity
D002403:Cathepsins; D010447:Peptide Hydrolases; D003546:Cysteine Endopeptidases; D056655:Cathepsin H; C534128:Ctsh protein, rat