✦ LIBER ✦

Activity of platelet-activating factor acetylhydrolase exists in red cell membrane

✍ Scribed by Hidemi Yoshida; Kei Satoh; Dr. Tada-Atsu Imaizumi

Publisher: John Wiley and Sons
Year: 1992
Tongue: English
Weight: 218 KB
Volume: 40
Category: Article
ISSN: 0361-8609
DOI: 10.1002/ajh.2830400113

No coin nor oath required. For personal study only.

✦ Synopsis

We have described the intracellular type of platelet-activating factor acetylhydrolase (PAF-AH) in the membrane extract of human red blood cells (RBCs). The enzymatic activity was inhibited by diisopropylfluorophosphate, trypsin or pronase E, but not affected by EDTA or the addition of 1 -0-hexadecyl-2-hexadecanoyl-rac-glycero-3-phosphocholine or 1 -O-hexadecyl-2-[(cis)-9-octadecenoyl]-rac-glycero-3-phosphocholine. The activity in 10 healthy volunteers was 3.89 * 3.26 pmol/109 RBCs/min (or 148 * 73 nmol/g protein/min) (mean 2 SD). Since PAF-AH is also known to hydrolyze oxidized derivatives of phosphatidylcholine and since RBCs are not effector cells of PAF, the observed activity in RBC membranes may play a potential role in degrading oxidation products of membrane phospholipids.

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