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Preformed PAF‐acether and lyso PAF‐acether are bound to blood lipoproteins
Author(s) -
Benveniste Jacques,
Nunez Daniele,
Duriez Patrick,
Korth Ruth,
Bidault Jocelyne,
Fruchart Jean-Charles
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81456-x
Subject(s) - phosphatidylcholine , high performance liquid chromatography , chemistry , platelet activating factor , chromatography , ultracentrifuge , human blood , platelet , phospholipid , biochemistry , endocrinology , biology , immunology , membrane , physiology
PAF‐acether (PAF) is a newly formed mediator not normally present in circulating blood. A compound exhibiting all of its biological characteristics but coeluting with phosphatidylcholine (PC) in high‐pressure liquid chromatography (HPLC) was unveiled (‘peak X’) in normal human plasma. A second HPLC run of peak X HPLC fractions revealed the presence of PAF itself with concomitant disappearance of peak X. Beside PAF, immunoreactive apolipoproteins A‐I and E were found in peak X. Also lipoproteins (Ls) purified using either ultracentrifugation or immunoaffinity chromatography yielded peak X and, in a second HPLC run, authentic PAF. L‐free plasma was devoid of peak X. Finally, after preincubation with plasma, labeled PAF was found associated with Ls. Thus in human blood preformed PAF is bound in high amounts to Ls, a result of interest given the role of Ls and platelets in vascular diseases and the present knowledge on PAF biosynthesis.