Oxidation of Dilinoleoyl Phosphatidylcholine by Lipoxygenase 1 from Soybeans

Pérez‐Gilabert, Manuela; Veldink, Gerrit A.; Vliegenthart, Johannes F.G.

doi:10.1006/abbi.1998.0673

Cited by 41 publications

(34 citation statements)

References 20 publications

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“…This decrease in LOX expression would lead to a slower rate of supplying the oxygenated fatty acid to AOS, which commits the LOX product for JA synthesis (Figure 1). Additionally, LOX has been reported to utilize fatty acids on glycerolipids (Brash et al, 1987;Perez-Gilabert et al, 1998), and oxidized fatty acids on membrane lipids are more susceptible to cleavage by phospholipases (Banas et al, 1992). Thus, a decrease in LOX could also reduce the release of oxygenated fatty acids from membranes for JA synthesis.…”

Section: Discussionmentioning

confidence: 99%

Involvement of Phospholipase D in Wound-Induced Accumulation of Jasmonic Acid in Arabidopsis

et al. 2000

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Multiple forms of phospholipase D (PLD) were activated in response to wounding, and the expressions of PLD ␣ , PLD ␤ , and PLD ␥ differed in wounded Arabidopsis leaves. Antisense abrogation of the common plant PLD , PLD ␣ , decreased the wound induction of phosphatidic acid, jasmonic acid (JA), and a JA-regulated gene for vegetative storage protein.Examination of the genes involved in the initial steps of oxylipin synthesis revealed that abrogation of the PLD ␣ attenuated the wound-induced expression of lipoxygenase 2 (LOX2) but had no effect on allene oxide synthase (AOS) or hydroperoxide lyase in wounded leaves. The systemic induction of LOX2, AOS, and vegetative storage protein was lower in the PLD ␣ -suppressed plants than in wild-type plants, with AOS exhibiting a distinct pattern. These results indicate that activation of PLD mediates wound induction of JA and that LOX2 is probably a downstream target through which PLD promotes the production of JA. INTRODUCTIONJasmonic acid (JA) and related compounds are a new class of plant hormones that play an important role in regulating many cellular processes, such as wound and defense responses (Farmer and Ryan, 1992;Bell et al., 1995;Creelman and Mullet, 1997;McConn et al., 1997). The production of JA is a tightly regulated process, and the concentrations of JA in unperturbed plant tissues are often very low. However, JA accumulates in wounded plants or in plants and cultured cells treated with pathogen elicitors; it acts as a signal activating the expression of various genes, such as proteinase inhibitors, thionin, and enzymes in phytoalexin metabolism . The pathway for de novo JA biosynthesis, beginning with free ␣ -linolenic acid, has been well elucidated (Vick, 1993;Creelman and Mullet, 1997; also see Figure 1). But when and how linolenic acid is made available for JA synthesis is not well understood. Linolenic acid, the most abundant fatty acid in leaves, is mostly present in esterified glycerolipid form (Browse and Somerville, 1991). Free fatty acids are not generally found in large amounts in healthy, intact plant cells. The release of linolenic acid from membranes has been thought to be an important step in controlling JA synthesis. An increase in free linolenic acid was observed in cultured cells of several plant species after treatment with fungal wall elicitors (Gundlach et al., 1992) and in wounded plants (Conconi et al., 1996;Ryu and Wang, 1998). A phospholipase A (PLA)-like activity has been proposed to mediate the release of linolenic acid from membranes (Farmer and Ryan, 1992), and the presence of such a wound-inducible PLA activity has been noted in tomato and other plant species (Lee et al., 1997;Narváez-Vásquez et al., 1999).Recent studies have suggested that activation of phospholipase D (PLD) also may play an important role in mediating wound-induced lipid hydrolysis Wang, 1996, 1998;Lee et al., 1997). PLD hydrolyzes phospholipids at the terminal phosphoesteric bond, generating phosphatidic acid (PA) and free head groups, such as choline . T...

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Section: Discussionmentioning

confidence: 99%

Involvement of Phospholipase D in Wound-Induced Accumulation of Jasmonic Acid in Arabidopsis

et al. 2000

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“…Indeed, LOX-1 has been shown to utilize phospholipids in lipid bilayers (41), and fatty acids inserted into phospholipid micelles (16), as physiological substrates. Such activity has received increasing interest since the discovery that lipoxygenase forms pore-like structures in biomembranes, thus leading to programmed organelle degradation (42).…”

Section: Discussionmentioning

confidence: 99%

Tryptic Digestion of Soybean Lipoxygenase-1 Generates a 60 kDa Fragment with Improved Activity and Membrane Binding Ability

et al. 2001

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Lipoxygenases are key enzymes in the metabolism of unsaturated fatty acids. Soybean lipoxygenase-1 (LOX-1), a paradigm for lipoxygenases isolated from different sources, is composed of two domains: a ∼30 kDa N-terminal domain and a ∼60 kDa C-terminal domain. We used limited proteolysis and gel-filtration chromatography to generate and isolate a ∼60 kDa fragment of LOX-1 ("mini-LOX"), produced by trypsin cleavage between lysine 277 and serine 278. Mini-LOX was subjected to N-terminal sequencing and to electrophoretic, chromatographic, and spectroscopic analysis. Mini-LOX was found to be more acidic and more hydrophobic than LOX-1, and with a higher content of R-helix. Kinetic analysis showed that mini-LOX dioxygenates linoleic acid with a catalytic efficiency approximately 3-fold higher than that of LOX-1 (33.3 × 10 6 and 10.9 × 10 6 M -1 ‚s -1 , respectively), the activation energy of the reaction being 4.5 ( 0.5 and 8.3 ( 0.9 kJ‚mol -1 for mini-LOX and LOX-1, respectively. Substrate preference, tested with linoleic, R-linolenic, and arachidonic acids, and with linoleate methyl ester, was the same for LOX-1 and mini-LOX, and also identical was the regio-and stereospecificity of the products generated thereof, analyzed by reversed-phase and chiral high-performance liquid chromatography, and by gas chromatography/mass spectrometry. Mini-LOX was able to bind artificial vesicles with higher affinity than LOX-1, but the binding was less affected by calcium ions than was that of LOX-1. Taken together, these results suggest that the N-terminal domain of soybean lipoxygenase-1 might be a built-in inihibitor of catalytic activity and membrane binding ability of the enzyme, with a possible role in physio-(patho)logical conditions.Lipoxygenases are a family of monomeric non-heme, nonsulfur iron dioxygenases which catalyze the conversion of unsaturated fatty acids into conjugated hydroperoxides. Mammalian lipoxygenases have been implicated in the pathogenesis of several inflammatory conditions such as arthritis, psoriasis, and bronchial asthma (1). They have been also implicated in atherosclerosis (2), brain aging (3), HIV infection (4), and kidney disease (5, 6). In plants, lipoxygenases favor germination and participate in the synthesis of traumatin and jasmonic acid and in the response to abiotic stress (7). Recently, they have been also shown to initiate the programmed death (apoptosis) of plant cells (8). Soybean lipoxygenase-1 (LOX-1) 1 is widely used as a prototype for studying the homologous family of lipoxygenases from tissues of different species, both in structural (9-13) and in kinetic (14-18) investigations. The amino acid sequence (19) and three-dimensional structure (9, 10) of LOX-1 have been determined. The overall 839 amino acid residues of LOX-1, with a molecular mass of 93 840 Da, show 2 domains. The first 146 N-terminal amino acid residues form an 8-stranded -barrel, and the remaining 693 residues of the C-terminal domain are organized into 23 helices and 8 -strands. Mammalian lipoxygenases do ...

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“…Conjugated diene formation was a useful monitor of oxidation. However, experiments using soybean lipoxygenase, which produces only conjugated dienes (42), failed to produce enhanced activity, even though the concentration of conjugated dienes formed was equivalent to or greater than that observed in the copper-oxidized phospholipids (data not shown). Although conjugated triene formation appears to correlate with activity in the data presented, this was not always the case (data not shown).…”

Section: Discussionmentioning

confidence: 94%

“…Lipoxygenase Oxidation of Phospholipids-Liposomes (2 mg/ml) were dispersed in 100 mM n-octyl-␤-D-glucopyranoside, 200 mM sodium borate, pH 10, with or without soybean lipoxygenase type I-B (Sigma) at 5000 units/ml (42). The suspensions were vortexed to introduce air into the solutions.…”

Section: Methodsmentioning

confidence: 99%

Lipid Oxidation Enhances the Function of Activated Protein C

Safa¹,

Hensley²,

Smirnov³

et al. 2001

Journal of Biological Chemistry

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Although lipid oxidation products are usually associated with tissue injury, it is now recognized that they can also contribute to cell activation and elicit antiinflammatory lipid mediators. In this study, we report that membrane phospholipid oxidation can modulate the hemostatic balance. Oxidation of natural phospholipids results in an increased ability of the membrane surface to support the function of the natural anticoagulant, activated protein C (APC), without significantly altering the ability to support thrombin generation. Lipid oxidation also potentiated the ability of protein S to enhance APC-mediated factor Va inactivation. Phosphatidylethanolamine, phosphatidylserine, and polyunsaturation of the fatty acids were all required for the oxidation-dependent enhancement of APC function. A subgroup of thrombotic patients with anti-phospholipid antibodies specifically blocked the oxidation-dependent enhancement of APC function. Since leukocytes are recruited and activated at the thrombus or sites of vessel injury, our findings suggest that after the initial thrombus formation, lipid oxidation can remodel the membrane surface resulting in increased anticoagulant function, thereby reducing the thrombogenicity of the thrombus or injured vessel surface. Anti-phospholipid antibodies that block this process would therefore be expected to contribute to thrombus growth and disease.

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Oxidation of Dilinoleoyl Phosphatidylcholine by Lipoxygenase 1 from Soybeans

Cited by 41 publications

References 20 publications

Involvement of Phospholipase D in Wound-Induced Accumulation of Jasmonic Acid in Arabidopsis

Involvement of Phospholipase D in Wound-Induced Accumulation of Jasmonic Acid in Arabidopsis

Tryptic Digestion of Soybean Lipoxygenase-1 Generates a 60 kDa Fragment with Improved Activity and Membrane Binding Ability

Lipid Oxidation Enhances the Function of Activated Protein C

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