Apolipoprotein B exhibits phospholipase A1 and phospholipase A2 activities

Nurit Reisfeld, Dov Lichtenberg, Arie Dagan, Saul Yedgar*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


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.

Original languageEnglish
Pages (from-to)267-270
Number of pages4
JournalFEBS Letters
Issue number3
StatePublished - 11 Jan 1993


  • Apolipoprotein B
  • Low density lipoprotein: Phospholipase A
  • Phospholipase A


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