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Plasma lipoprotein‐associated arylesterase is induced by bacterial lipopolysaccharide
Author(s) -
Bøg-Hansen T.C.,
krog H.H.,
Back U.
Publication year - 1978
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(78)80811-4
Subject(s) - escherichia coli , citation , library science , collaboratory , chemistry , world wide web , computer science , biochemistry , gene
The biological function of plasma arylesterase (AI-E, EC 3.1 .1.2) is not known, but it is associated to high density lipoprotein (HDL, a-lipoprotein) [l] and is implicated in normal lipid metabolism through fatty acid exchange of cholesterol esters [2] . In addition, the enzyme may participate in host defence against toxins (including endotoxins, lipopolysaccharides, LPS) [3,4, and Erd6s as cited in 21, but there is little evidence for an actual degradation of LPS, as reviewed by Olitzki [5] . On the other hand, the amphiphilic nature of LPS is well established, including its affinity for cell membrane phospholipids [6,7] . Therefore we found it interesting to study the interaction of LPS with other amphiphilic structures, and we were able to show that LPS binds to the HDLassociated arylesterase in plasma in vitro, which led us to support the views of Skarnes [3] by suggesting