Cytochemical demonstration of latency of lysosomal hydrolases in digestive cells of the common mussel, mytilus edulis, and changes induced by thermal stress.
Latent beta-glucuronidase and glucosaminidase activities have been demonstrated in small cytoplasmic particles, which may possibly be primary lysosomes, as well as some larger granules of the digestive cells of the common mussel. Latency was indicated by increased staining of these structures following incubation in buffer at pH 4.5 at 37 degrees C. The exposure of mussels to temperatures of 25-28 degrees C over a period of four days induced a significant decrease in the latency of lysosomal glucosaminidase. Thermal death produced labilization of lysosomes although selective release of hydrolase activity was indicated by the differential latency of glucosaminidase and glucuronidase. The injection of hydrocortisone induced a significant increase in latency in stressed animals, indicating that the stress response involved changes in structure and function of membranes.
D000818:Animals; D001329:Autolysis; D049872:Bivalvia; D004064:Digestive System / Q000201:enzymology* / Q000648:ultrastructure; D005966:Glucuronidase / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006596:Hexosaminidases / Q000378:metabolism; D006651:Histocytochemistry; D006358:Hot Temperature; D006854:Hydrocortisone / Q000494:pharmacology; D008247:Lysosomes / Q000187:drug effects / Q000201:enzymology*
D006026:Glycoside Hydrolases; D006596:Hexosaminidases; D005966:Glucuronidase; D006854:Hydrocortisone