Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer

Article Abstract:

The intact molecule of platelet-activating factor acetylhydrolase (Ib) (PAF-AH(Ib)) that removes the sn-2 acetyl group to inactivate the platelet-activating factor is an unusual G-protein-like trimer. The PAF-AH(Ib) active site is made up of a trypsin-like triad of SER 47, His 195 and Asp 192. In crystal structure, Ser 47 is close to His 195 and the imidazole ring of His 195 is hydrogen bonded through its N-Delta-1 atom to the side-chain carboxyl of Asp 192. The tertiary fold of the protein is similar to that found in p21 and other GTPases.

Enzymes

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Anti-inflammatory properties of a platelet-activating factor acetylhydrolase

Article Abstract:

The use of additional, exogenous platelet-activating factor (PAF) acetylhydrolase may be an effective therapy for acute inflammation. The sequence of human plasma PAF acetylhydrolase possesses a Gly-Xaa-Ser-Xaa-Gly motif, as confirmed from molecular cloning. The substrate specific PAF acetylhydrolase causes lipoprotein association of the native enzyme. The vascular leakage in pleurisy and paw oedema is decreased by the PAF acetylhydrolase.

Care and treatment, Usage, Physiological aspects, Inflammation, Cloning

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Protein kinase C regulates the nuclear localization of diacylglycerol kinase

Article Abstract:

Research shows that biochemical protein kinase C controls nuclear protein diacylglycerol metabolism by affecting the intracellular location of enzymes diacylglycerol kinases (DGKs). Experiments using immunoblotting, immunocytochemistry and transfection techniques establish the presence of DGKs in the nucleus of COS-7 cells. Cell growth is established by DGK gene expression.

Growth factors, Protein kinases

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