Premium
Acylation of Secretory Phospholipases A2 Alter the Catalytic Activity on Erythrocyte Membrane
Author(s) -
Gonzalez Carol,
Echevarría Ileabett,
Vázquez Edwin,
Restituyo Elizabeth,
Morales Krystal,
Erazo Alfredo,
Quesada Orestes,
Morales Reginald
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1019
Subject(s) - chemistry , phospholipase a2 , biochemistry , enzyme , phospholipase , hydrolysis , covalent bond , pyrophosphate , phospholipid , snake venom , membrane , phospholipase a , acylation , catalysis , organic chemistry
Secretory Phospholipases A2 (sPLA2’s) catalyze the calcium dependent hydrolysis of sn‐2 linkages in phosphoglicerades Simultaneous assay of binding and hydrolysis of radiolabeled sPLA2 with a suspension of intact human erythrocytes was carried out. One of the enzymes used in these studies has been a Group IA PLA isolated from the snake venom of Naja nigricollis (NnPLA) and the Agkistrodon halys blomhofffii (AhPLA) which has been shown to display a preference for arachidonoyl containing species. In an effort to direct these sPLA2’s toward specific regions of the human erythrocyte membrane surface, this enzyme was covalently coupled to methyl arachidonyl fluorophosphonate (MAFP) and farnesyl pyrophosphate (FPP). Approximately, 60 percent of inhibition was observed when NnPLA was covalently couple to MAFP or FPP, but a significant increase in specificity toward the 20:4 fatty acids species was observed with the former. Interestingly, FFP induced a slightly increase on the activity of AhPLA but MAFP had an almost 2.4 fold increasing effect on the activity of AhPLA with a decrease specificity against 20:4 fatty acids species. The covalent modification of these sPLA2’s was confirmed by ESI‐MS. The increase in sPLA2 molecular mass correspond to one equivalent of the modifying compound used in each case. Work support by UPR‐RP RISE Program (2R25GM061151)