Present study shows that non-covalent interaction of kaouthiotoxin (KTX) with their respective pohospholipase A(2) (PLA(2)) from the venom of N. kaouthia displayed marked synergism to exert cytotoxicity without altering the biochemical properties of PLA(2). For example, although NK-PLA(2) or KTX alone did not induce appreciable hemolysis of washed human erythrocytes; however, the hemolytic pote...

Several lines of evidence indicate that phospholipase A(2) (PLA(2)) plays a crucial role in plant cellular responses through production of linolenic acid, the precursor of jasmonic acid, from membrane phospholipids. Here we report the purification and characterization of a 48-kD PLA(2) from the membrane fractions of leaves of broad bean (Vicia faba). The plant PLA(2) was purified to near homoge...

Phospholipase A(2) (PLA(2)) catalyses the hydrolysis of phospholipids into lysophospholipids and free fatty acids. Physiological studies have indicated that PLA(2) is involved in stomatal movement. However, genetic evidence of a role of PLA(2) in guard cell signalling has not yet been reported. To identify PLA(2) gene(s) that is (are) involved in light-induced stomatal opening, stomatal movemen...

Mammalian Group IIA phospholipases A(2) (PLA(2)) potently kill Staphylococcus aureus. Highly cationic properties of these PLA(2) are important for Ca(2+)-independent binding and cell wall penetration, prerequisites for Ca(2+)-dependent degradation of membrane phospholipids and bacterial killing. To further delineate charge properties of the bacterial envelope important in Group IIA PLA(2) actio...

The phospholipase A(2) (PLA(2)) enzymes are activated by binding to phospholipid membranes. Although the N-terminal alpha-helix of group I/II PLA(2)s plays an important role in the productive mode membrane binding of the enzymes, its role in the structural aspects of membrane-induced activation of PLA(2)s is not well understood. In order to elucidate membrane-induced conformational changes in t...

Fourteen kilodalton phospholipase A(2) molecules (PLA(2)) are classified into two groups, I- and II-PLA(2), and only the latter has been considered to play a pathogenetic role in various forms of tissue inflammation. Previously we demonstrated high PLA(2) activity in gingival crevicular fluid (GCF) of patients with periodontal disease, without determining the group of the enzyme involved. In th...

Lipoprotein-associated phospholipase A(2) (Lp-PLA(2)) is an enzyme that is produced by inflammatory cells (macrophages, T-lymphocytes and mast cells) and hydrolyzes oxidized phospholipids in LDL. Several epidemiology studies indicate that Lp-PLA(2) appears to be an independent marker of cardiovascular risk. This study was conducted to define the distribution of Lp-PLA(2) in a large population-b...

Phospholipase A(2) (PLA(2)) hydrolyzes phospholipids at the sn-2 position to yield lysophospholipids and free fatty acids. Of the four paralogs expressed in Arabidopsis, the cellular functions of PLA(2)α in planta are poorly understood. The present study shows that PLA(2)α possesses unique characteristics in terms of spatiotemporal subcellular localization, as compared with the other paralogs t...

Phospholipase A(2) (PLA(2)) from the pyloric ceca of the starfish Asterina pectinifera showed high specific activity and characteristic substrate specificity, compared with commercially available PLA(2) from porcine pancreas. To investigate enzymatic properties of the starfish PLA(2) in further detail, we constructed a bacterial expression system for the enzyme. The starfish PLA(2) cDNA isolate...