Fluorescent histochemistry of acid proteases in adult Schistosoma mansoni and Schistosoma japonicum.
The acid proteases, cathepsin B, dipeptidyl aminopeptidase I and II were demonstrated by fluorescent histochemistry in adult Schistosoma mansoni and Schistosoma japonicum. Alanyl- and leucine-aminopeptidase activities were not observed. The substrates consisted of 4-methoxy-beta-naphthylamide derivatives coupled to the fluorescent molecule, 5-nitrosalicylaldehyde. Reaction product was observed as discrete granules in the gastrodermis; activity was also observed in the testes and vitelline cells of males and females, respectively. No activity was noted in the foregut or esophageal glands of either worm. In light of previous biochemical studies on "hemoglobinase" activity in the schistosomes, it appears likely that a group of acid proteases may be involved in the ultimate digestion of hemoglobin. The absence of activity in the esophageal glands lends further support to the hypothesis that the gastrodermis is the site of the proteases responsible for hemoglobin digestion.
D000818:Animals; D002402:Cathepsin D; D002403:Cathepsins / Q000032:analysis*; D004064:Digestive System / Q000201:enzymology; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000032:analysis*; D010450:Endopeptidases / Q000032:analysis*; D004947:Esophagus; D005088:Exocrine Glands / Q000201:enzymology; D005260:Female; D006651:Histocytochemistry; D008297:Male; D012549:Schistosoma japonicum / Q000201:enzymology*; D012550:Schistosoma mansoni / Q000201:enzymology*
D002403:Cathepsins; D010450:Endopeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D002402:Cathepsin D