By Andrew F. G. Quest, Daniel M. Raben, Robert M. Bell (auth.), Robert M. Bell, John H. Exton, Stephen M. Prescott (eds.)
Lipids typically were considered as serving services: to shape mobile membranes and to function strength shops. over the past twenty years, a brand new position for lipids has taken heart degree: lipids can act as signalling molecules. This booklet bargains with a number of lipids which were proven to be messengers. best scientists discover all recognized lipid periods other than steroid hormones. Researchers and educators in biochemistry in addition to in molecular and mobile biology will take pleasure in this volume.
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TPAstimulated PC synthesis is attributed to a two- to threefold increase in the rate of CT-catalyzed reaction and correlates with a redistribution ofCT from the cytosol to ER (Pelech and Vance, 1989). , 1991). In rat hepatocytes, cAMP analogues and glucagon reduce DAG levels by 30%. , 1992). DAG levels are thought to directly regulate CT activity by stimulating membrane translocation. CT contains a motif reminiscent of a cysteine-rich region in PKC. , 1990). , 1992). These observations implicate DAG as a major regulatory component of phospholipid biosynthesis.
1990). The human counterpart of this DGK has been purified from normal white blood cells. , 1990). , 1991). , 1991). , 1986b). In Swiss 3T3 cells roughly 60-70% ofDGKis in the cytosol while the remainder is associated with the particulate fraction. Treatment of the cells with phorbol esters enhances association with the particulate fraction, but probably does so by increasing DAG levels. Redistribution ofDGK is also seen when cells are treated with cell-permeable diC 8 (Maroney and Macara, 1989).
DAG Phosphorylation by DGKs Mammalian DGKs are a diverse family of enzymes. , 1988). , 1989). Membrane-bound DGK activities have been described in several tissues, but may be identical to better characterized cytosolic isoforms. , 1986). However, two distinct proteins of110 and 150 kDa were recently purified to homogeneity starting from either rat brain cytosol or membranes, respectively. The 150-kDa protein is a peripheral membrane protein (Kato and Takenawa, 1990). , 1988). , 1990). , 1994). Since mammalian phosphoinositides are selectively enriched in arachidonate at the sn-1,2 position, arachidonoyl-specific DGK has been implicated in the rapid and selective clearance of the arachidonate-rich DAG pool arising from stimulus-induced phosphoinositide turnover.