The interaction of phospholipase A2 with oxidized phospholipids at the lipid-water surface with different structural organization

Paradoxical effects of lipolysis on the lipid oxidation in meat and meat products

“…Given its hydrolytic activity, PLA2 has been shown to be involved in lipoxygenase-mediated oxidation of fatty acids to form lipid hydroperoxides and superoxides in skeletal muscles ( Zuo, Christofi, Wright, Bao, & Clanton, 2004 ). However, oxidation of FFA at the sn -2 position of phospholipids by lipoxygenase may as well take place before the hydrolysis by PLA2 ( Chaitidis, Schewe, Sutherland, Kühn, & Nigam, 1998 ), which is aligned with the preference of PLA2 towards oxidized phospholipids ( Litvinko, Skorostetskaya, & Gerlovsky, 2018 ). The uses of phosphatidylcholine-binding protein and PLA2 antibody were tested to alleviate the negative impacts of phospholipid hydrolysis ( Wang et al, 2014 , Chun et al, 2022 ).…”

“…Abilities of FFAs to bind and induce conformational change of heme proteins (myoglobin, hemoglobin) into hemichrome, which is a more inert form of the pro-oxidants, have been demonstrated ( Stewart, 1990 , Wu et al, 2021b ). Litvinko, Skorostetskaya, and Gerlovsky (2018) determined PLA2 activity by monitoring the conversion of hemoglobin into hemichrome upon reacting with FFAs released from the enzymatic hydrolysis of phosphatidylcholine liposomes and micelles.…”

“…In the presence of heme compounds, lipid hydroperoxides can be decomposed into lipid radicals and hypervalent heme species that can initiate further lipid oxidation reactions ( Wu, Richards, & Undeland, 2022 ). Therefore, preferential hydrolysis towards oxidized phospholipids due to presence of membrane defects ( Litvinko, Skorostetskaya, & Gerlovsky, 2018 ) could be the role of PLA2 in depleting the membranes of pre-formed lipid hydroperoxides as illustrated in Fig. 4 .…”

Viper toxins affect membrane characteristics of human erythrocytes

“…According to Devendjiev et al [31] there is no evidence for the complex 'recognition site' involving residues Phe 3 , Trp 31 and Tyr 119 of the molecules of VAC. In the PLA2-subunit the side chains of His 48 , Asp 99 and Tyr 52 for an active site which is conserved in all phospholipases [32]. The positively charged alkylammonium side chain of Lys 69 may satisfy the need for partial neutralisation in the region of the structurally shielded Asp 49 carboxylate in Crotalus atrox [33].…”

“…The phospholipase A2 activity is increased in vesicles containing oxidized soybean phosphatidylcholine compared that the activity in non-oxidized phospholipid membranes[51]. According reports of Litvinko et al[52] PLA2 does not act on the tightly packed lipid bilayers. The exposure of additional negative charged groups of the proteins and lipids on the surface of erythrocytes because of conformational changes and re-organization of membrane components explains the higher net surface charge of erythrocyte membrane upon viper toxin treatment.The interactions of anionic phospholipids and cholesterol and specific sites of Band 3 are situated at the dimeric interface forming and annulus around the protein.…”