Ultracytochemical localization of acid phosphatase and trimetaphosphatase activities in the transitional epithelium of the rat urinary bladder.
Acid phosphatase and trimetaphosphatase activities have been demonstrated cytochemically in the transitional epithelium of the rat urinary bladder. Acid phosphatase activity was examined by the method of Robinson and Karnovsky (1983), and trimetaphosphatase activity was examined by the method of Kobayashi et al. (1988). Intense positive reaction for acid phosphatase activity was observed with both beta-glycerophosphate and p-nitrophenyl phosphate as substrates, in lysosomes, Golgi complex, GERL, multi-vesicular bodies and wrapping lysosomes. The reaction product of the trimetaphosphatase activity was visualized as fine particulated deposits along the limiting membrane of some lysosomes, and of tubular structures located in the basal cytoplasm. There seems to be a fine distinction and reciprocal complementary functional relationship between two kinds of lysosomes containing either acid phosphatase or trimetaphosphatase activity.
Zhang
S X
SX
Department of Anatomy and Cell Biology, Kochi Medical School, Japan.
Kobayashi
T
T
Okada
T
T
Garcia del Saz
E
E
Seguchi
H
H
D017766:Acid Anhydride Hydrolases; D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D004847:Epithelial Cells; D004848:Epithelium / Q000201:enzymology / Q000648:ultrastructure; D006056:Golgi Apparatus / Q000201:enzymology / Q000648:ultrastructure; D006651:Histocytochemistry; D008247:Lysosomes / Q000201:enzymology / Q000648:ultrastructure; D008854:Microscopy, Electron; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D001743:Urinary Bladder / Q000166:cytology / Q000201:enzymology* / Q000648:ultrastructure
D000135:Acid Phosphatase; D010744:Phosphoric Monoester Hydrolases; D017766:Acid Anhydride Hydrolases; C022768:trimetaphosphatase