The cytochemical localization of adenyl cyclase activity in rat sublingual gland.
Adenyl cyclase activity in mucous acinar cells and serous demilune cells of the rat sublingual gland was localized cytochemically. After incubation with adenylyl-imidodiphosphate (AMP-PNP) as substrate, deposits of reaction product are found along the cell membranes  bordering the secretory surfaces of serous demilune cells. These are the membranes which participate directly in secretion by fusing with the granule membranes. The granule membranes of the demilune cells do not reveal reaction product, but the membranes of the granules which are fused with and become part of the cell membrane do show deposits. Thus, it appears that the cell membranes which fuse with granule membranes during secretion are associated with a high level of adenyl cyclase activity. In support of this, the luminal membranes of the mucous acinar cells which do not fuse with granule membranes during secretion are not associated with detectable amounts of adenyl cyclase activity.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000266:Adenylyl Imidodiphosphate; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D003594:Cytoplasmic Granules / Q000201:enzymology; D008297:Male; D051381:Rats / Q000378:metabolism*; D013361:Sublingual Gland / Q000201:enzymology* / Q000648:ultrastructure
D000266:Adenylyl Imidodiphosphate; D000262:Adenylyl Cyclases