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Apolipoprotein B exhibits phospholipase A 1 and phospholipase A 2 activities
Author(s) -
Reisfeld Nurit,
Lichtenberg Dov,
Dagan Arie,
Yedgar Saul
Publication year - 1993
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(93)81176-z
Subject(s) - phospholipase a2 , apolipoprotein b , chemistry , phospholipase , fatty acid , biochemistry , hydrolysis , enzyme , phospholipase a , lysophospholipase , phospholipase c , caproic acid , phosphoinositide phospholipase c , stereochemistry , organic chemistry , cholesterol
Low density lipoproteins (LDL) as well as isolated apolipoprotein B (ApoB) have been shown to exhibit phospholipase A 2 (PLA 2 ) activity toward phospholipids containing an oxidized or short fatty acyl chain at position 2. Some of these studies employed the fluorescent analogue of phosphatidyl choline (PC), C 6 ‐NBD‐PC, containing NBD‐caproic acid (C 6 ‐NBD‐FA) at position 2 as a substrate, representative of short fatty acyl chains. The release of NBD‐caproic acid from position 2 is attributed to PLA 2 ‐catalysed hydrolysis. However, this fatty acid can be released also by other enzymatic pathways. In the present study we examined, and ruled out, other enzymatic pathways which may be responsible for the hydrolysis of fatty acids from position 2 of phospholipids. On the other hand, we found that LDL as well as isolated ApoB hydrolyse C 6 ‐NBD‐FA from both carbon 1 and carbon 2 of these phospholipids, thus exhibiting independent and simultaneous activities of phospholipase A 1 and phospholipase A 2 .