Metal-ion stimulation and inhibition of lysophospholipase D which generates bioactive lysophosphatidic acid in rat plasma - PubMed (original) (raw)

Metal-ion stimulation and inhibition of lysophospholipase D which generates bioactive lysophosphatidic acid in rat plasma

A Tokumura et al. Lipids. 1998 Oct.

Abstract

We found that lysophospholipase D (LPLD) in rat plasma prefers unsaturated to saturated lysophosphatidylcholines as substrates, generating a biologically active lipid, lysophosphatidic acid, but it does not hydrolyze diacyl-phospholipids. In this study, this LPLD required a metal ion for activity, Co2+ being the most effective, followed in order by Zn2+, Mn2+, and Ni2+. This metal-ion-stimulated LPLD with unique substrate specificity, which has not been described previously, was susceptible to thiol-blocking reagents and serine esterase inhibitors, but not to a histidine-modifying reagent. Consistent with results using thiol-modifying agents, short-chain fatty aldehydes, secondary products of lipid peroxidation, were found to inhibit LPLD. Addition of dibutylhydroxytoluene or butylhydroxyanisole to the plasma increased the activity of this enzyme, probably in a manner independent of its antioxidant activity, since another antioxidant, propyl gallate, was rather inhibitory. These results suggest that rat plasma contains an active LPLD that differs in some properties from other members of the known phospholipase D family detected in animal tissues and body fluids.

PubMed Disclaimer

References

1. Cell. 1992 Aug 7;70(3):389-99 - PubMed
1. Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14367-72 - PubMed
1. Biochem Biophys Res Commun. 1993 Jun 15;193(2):497-503 - PubMed
1. Atherosclerosis. 1993 Dec;104(1-2):213-9 - PubMed
1. Cell. 1995 Mar 24;80(6):919-27 - PubMed

Metal-ion stimulation and inhibition of lysophospholipase D which generates bioactive lysophosphatidic acid in rat plasma - PubMed (original) (raw)