Endophilin I is a presynaptic protein of unknown function that binds to dynamin, a GTPase that is implicated in endocytosis and recycling of synaptic vesicles. Here we show that endophilin I is essential for the formation of synaptic-like microvesicles (SLMVs) from the plasma membrane. Endophilin I exhibits lysophosphatidic acid acyl transferase (LPAAT) activity, and endophilin-I-mediated SLMV formation requires the transfer of the unsaturated fatty acid arachidonate to lysophosphatidic acid, converting it to phosphatidic acid.
View Article and Find Full Text PDFStimulation of secretion in guinea pig parotid gland lobules by either isoproterenol or carbachol is associated with a removal of acyl groups from the acyl-CoA pool and their incorporation into diacylglycerols and triglycerides (Söling, H. D., Machado-De Domenech, E.
View Article and Find Full Text PDFIn isolated guinea pig parotid gland lobules the activities of the following enzymes were measured 30 sec after stimulation with either 2 X 10(-5) M isoproterenol or 10(-5) M carbachol: glycerol kinase (EC 2.7.1.
View Article and Find Full Text PDFThe early effects (0-120 s) of the beta-adrenergic secretagogue isoproterenol (2.10(-5) M) and the muscarinic secretagogue carbamoylcholine (2.10(-6) M) on various parameters of lipid and phospholipid metabolism were studied in isolated guinea pig parotid acinar cells.
View Article and Find Full Text PDF1-O-Alkyl-2-acetyl-sn-glycero-3-phosphocholines (platelet-activating factor (PAF] stimulate exocytosis in isolated lobules from guinea pig parotid glands or pancreas by an acetylcholine-like mechanism (Söling, H. D., Eibl, H.
View Article and Find Full Text PDF