FEBS Letters | |
Apolipoprotein B exhibits phospholipase A1 and phospholipase A2 activities | |
Yedgar, Saul2  Lichtenberg, Dov1  Dagan, Arie2  Reisfeld, Nurit2  | |
[1] Department of Physiology and Pharmacology, The Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel;Department of Biochemistry, Hebrew University - Hadassah Medical School, Jerusalem, 91010, Israel | |
关键词: Apolipoprotein B; Low density lipoprotein: Phospholipase A1; Phospholipase A2; LDL; low density lipoproteins; ApoB; apolipoprotein B; C6-NBD-PC; 1-acyl-2-(N-4-nitrobenzo-2-oxa-1; 3-diazole)-amino-caproylphosphatidylcholine; C6-NBD-FA; NBD-caproic acid; C6-NBD-DAG; C6NBD-diacylglycerol; C6-NBD-LPC; C6-NBD-LysoPC; GPC; glycerophosphorylcholine; PLA1; phospholipase A1; PLA2; phospholipase A2; PLC; phospholipase C; LPase; lysophospholipase.; | |
DOI : 10.1016/0014-5793(93)81176-Z | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Low density lipoproteins (LDL) as well as isolated apolipoprotein B (ApoB) have been shown to exhibit phospholipase A2 (PLA2) 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), C6-NBD-PC, containing NBD-caproic acid (C6-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 PLA2-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 C6-NBD-FA from both carbon 1 and carbon 2 of these phospholipids, thus exhibiting independent and simultaneous activities of phospholipase A1 and phospholipase A2.
【 授权许可】
Unknown
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