Lipoprotein-associated phospholipase A2: role in atherosclerosis and utility as a cardiovascular biomarker

2010 ◽  
Vol 8 (3) ◽  
pp. 425-438 ◽  
Author(s):  
Peter P Toth ◽  
Peter A McCullough ◽  
Michael S Wegner ◽  
Kenneth J Colley
Keyword(s):  
Phospholipase A2 ◽  
Cardiovascular Biomarker

Lipoprotein-associated phospholipase A2 (Lp-PLA2): a review of its role and significance as a cardiovascular biomarker

Biomarkers ◽  
2012 ◽  
Vol 17 (4) ◽  
pp. 289-302 ◽  
Author(s):  
Oana Vittos ◽  
Bogdan Toana ◽  
Alexandros Vittos ◽  
Elena Moldoveanu
Keyword(s):  
Phospholipase A2 ◽  
Cardiovascular Biomarker

Deficiency of Group VIA phospholipase A2 Primes the Cytokine Releases by Kupffer cells and Lymphocytes

2015 ◽  
Vol 53 (12) ◽  
Author(s):  
J Inhoffen ◽  
S Tuma-Kellner ◽  
W Stremmel ◽  
W Chamulitrat
Keyword(s):  
Phospholipase A2 ◽  
Kupffer Cells

Mechanism of Inhibitory Action on Platelet Activation of a Phospholipase A2 Isolated from Lachesis muta (Bushmaster) Snake Venom

1997 ◽  
Vol 78 (05) ◽  
pp. 1372-1380 ◽  
Author(s):  
André L Fuly ◽  
Olga L T Machado ◽  
Elias W Alves ◽  
Célia R Carlinis
Keyword(s):  
Platelet Aggregation ◽  
Enzymatic Activity ◽  
Phospholipase A2 ◽  
Inhibitory Activity ◽  
Thermal Inactivation ◽  
Anticoagulant Activity ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Crude Venom ◽  
Lachesis Muta

SummaryCrude venom from Lachesis muta exhibited procoagulant, proteolytic and phospholipase A2 activities. A phospholipase A2, denoted LM-PLA2 was purified from L. muta venom to homogeneity, through a combination of chromatographic steps involving gel-filtration on Sephacryl S-200 HR and reverse phase chromatography on a C2/C18 column. LM-PLA2 presented a single polypeptide chain with an isoelectric point at pH 4.7 and apparent molecular weight of 17 kDa. Partial aminoacid sequence indicated a high degree of homology for LM-PLA2 with other PLA2 from different sources.LM-PLA2 displayed a potent enzymatic activity as measured by indirect hemolysis of red blood cells but it was neither lethal when injected i.p. into mice nor did it present anticoagulant activity. Furthermore, LM-PLA2 displayed a moderate inhibitory activity on the aggregation of rabbit platelets induced by low levels of ADP, thrombin and arachidonate. In contrast, platelet aggregation induced by high doses of collagen was strongly inhibited by LM-PLA2 as well as ATP-release. Treatment of the protein with p-bromophenacyl bromide or 2-mercapto-ethanol, as well as thermal inactivation studies, suggested that the platelet inhibitory effect of LM-PLA2 is dependent on its enzymatic activity. Thus, the platelet inhibitory activity of LM-PLA2 was shown to be dependent on the hydrolysis of plasma phospholipids and/or lipoproteins, most probably those rich in phosphatidylcholine. Surprisingly, lyso-phosphatidylcholine released by LM-PLA2 from plasma was shown to preferentially inhibited collagen-induced platelet aggregation, in contrast to other PLA2s, whose plasma hydrolytic products indistinctly affect platelet’s response to several agonists.

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