Acyltransferase and acid hydrolase activities of the abalone photoreceptor cell.
In order to study the synthesis and degradation processes of the photoreceptor membranes in the abalone, Nordotis discus, the localization of acyltransferase and acid hydrolase activities, respectively, were determined at the electron-microscopic level. Acyltransferase activity was localized on the cytoplasmic sides of thick (greater than 10 nm) membranes of the following organelles: a few cisternae at the trans (or concave) side of Golgi apparatus, Golgi and probably related vesicles, short tubules, curved pentalaminar disks and limiting membranes of the phagosomal multivesicular bodies; all organelles were scattered in the peri- to supranuclear cytoplasm. The phospholipids, which are major components of the photoreceptor membrane, are considered to be synthesized by these membranes. Acid phosphatase activity was localized in the lumina of Golgi cisternae and vesicles, lysosomes, and smaller multivesicular and related bodies, but not in multilamellar bodies. The matrices of the larger multivesicular bodies and of the pigment granule complexes showed arylsulfatase activity. Vesiculated and autophagocytosed photoreceptor microvilli seemed to be degraded by acid hydrolases, forming multivesicular and related bodies. Supporting cells also showed acyltransferase and acid hydrolase activities.
D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D005399:Fishes; D006056:Golgi Apparatus / Q000648:ultrastructure; D006651:Histocytochemistry; D006867:Hydrolases / Q000378:metabolism*; D008854:Microscopy, Electron; D010786:Photoreceptor Cells / Q000201:enzymology* / Q000648:ultrastructure
D000217:Acyltransferases; D006867:Hydrolases