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The alkyl and alk-1-enyl (plasmalogen) types of ether-linked phospholipids are present in mammalian cells almost exclusively as structural analogues of phosphatidylcholine and phosphatidylethanolamine, which are major membrane phospholipid compositions1). The alkyl type is found predominantly as choline phosphoglycerolipids, whereas plasmalogen occurs mainly as ethanolamine phosphoglycerolipids1). Recently, many specific physiological functions of alkyl and alkenyl-type phospholipids have been reported2). Not only have significant discoveries and advancements in the studies of alkyl type phospholipid like platelet activating factor (PAF: 1-alkyl-2acetyl-sn-glycero-3-phosphorylcholine)3) and antitumor ether lipids (AELs)4,5) been reported, but also the alkenyl type of phospholipids have been shown to play a role in the regulation of certain protein kinase C isozymes6,7), a possible role in membrane-membrane fusion events8,9) and the ability to serve as endogenous antioxidants10,11). It has also been suggested that alkenyl glycerophospholipids serve as a reservoir for polyunsaturated fatty acids,12,13) which, when released by a calcium-independent, plasmalogenspecific, phospholipase A2, can form bioactive molecules such as prostaglandins and leukotrienes14). In the submandibular and sublingual salivary glands, the analyses of ether-linked phospholipids and the characterizations of their synthesizing enzymes have been reported15). However, there is very little information about ether-linked phospholipids in the parotid glands. Recently, analyses of membrane phospholipid compositions and their physical properties were reported, and it was shown that there are three types of phosphatidylcholines, 1-acyl-2-acyl, 1-alkenyl-2-acyl and 1-alkyl-2-acyl, in the rat parotid gland16-18). In the present study, a phospholipid-remodelling enzyme, acyltransferase, was characterized and the possible mechanism of enriching polyunsaturated fatty acid in choline plasmalogen was suggested.

Characterization of 1-Alkenyl-sn-glycero-3-phosphorylcholine Acyltransferase Activity in the Microsomes from Rat Parotid Gland.