© 2005 The Japanese Biochemical Society
Regular Paper |
Roles of C-Terminal Processing, and Involvement in Transacylation Reaction of Human Group IVC Phospholipase A2 (cPLA2
)
Faculty of Pharmaceutical Sciences, Teikyo University, Sagamiko, Kanagawa 199-0195
* To whom correspondence should be addressed. Fax: +81-426-85-1345, E-mail: ayamashi{at}pharm.teikyo-u.ac.jp
The phospholipase A2s (PLA2s) are a diverse group of enzymes that hydrolyze the sn-2 fatty acid from phospholipids and play a role in a wide range of physiological functions. A 61-kDa calcium-independent PLA2, termed cPLA2
, was identified as an ortholog of cPLA2
with approximately 30% overall sequence identity. cPLA2 contains a potential prenylation motif at its C terminus, and is known to have PLA2 and lysophospholipase activities, but its physiological roles have not been clarified. In the present study, we expressed various forms of recombinant cPLA2, including non-prenylated and non-cleaved forms, in order to investigate the effects of C-terminal processing. We examined the expression of the wild type and non-prenylated (SCLA) forms of cPLA2, and found that the SCLA form was expressed normally and retained almost full activity. Expression of the prenylated and non-cleaved form of cPLA2 using yeast mutants lacking prenyl protein proteases AFC1 (a-factor–converting enzyme) and RCE1 (Ras-converting enzyme) revealed decreased expression in the mutant strain compared to that in the wild type yeast, suggesting that complete C-terminal processing is important for the functional expression of cPLA2. In addition, cPLA2 was found to have coenzyme A (CoA)–independent transacylation and lysophospholipid (LPL) dismutase (LPLase/transacylase) activities, suggesting that it may be involved in fatty acid remodeling of phospholipids and the clearance of toxic lysophospholipids in cells.
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