Differential hydrolysis of molecular species of lipoprotein phosphatidylcholine by groups IIA, V and X secretory phospholipases A

Pruzanski, W.; Lambeau, L.; Lazdunsky, M.; Cho, W.; Kopilov, Julia; Kuksis, A.

doi:10.1016/j.bbalip.2005.07.005

Cited by 50 publications

(115 citation statements)

References 44 publications

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“…4C), was PLA2G10 Ͼ PLA2G5 Ͼ PLA2G3 Ͼ PLA2G2F Ͼ PLA2G2A and PLA2G2E, for both HDL and LDL. In accordance with the preference of PLA2G10 for arachidonate and of PLA2G5 for oleate/linoleate, as noted above and as described recently (49), the release of arachidonic acid from LDL and HDL by PLA2G10 was prominent, and that by PLA2G3 and PLA2G5 was similar (Fig. 4D).…”

Section: Generation Of Pla2g3 Tg Mice-thesupporting

confidence: 63%

“…S6). Although the physiological importance of these observations is unclear at present, similar fatty acid preferences of each sPLA 2 have also been reported in in vitro enzymatic assays (31,62,64) and cellular fatty acid release assays (65), and Pruzanski et al (49) have also reported a similar fatty acid selectivity of PLA2G5 and PLA2G10 toward lipoprotein PC.…”

Section: Discussionmentioning

confidence: 66%

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Analyses of Group III Secreted Phospholipase A2 Transgenic Mice Reveal Potential Participation of This Enzyme in Plasma Lipoprotein Modification, Macrophage Foam Cell Formation, and Atherosclerosis

Sato

Kato²,

Isogai

et al. 2008

Journal of Biological Chemistry

117

136

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Among the many mammalian secreted phospholipase A 2 (sPLA 2 ) enzymes, PLA2G3 (group III secreted phospholipase A 2 ) is unique in that it possesses unusual N-and C-terminal domains and in that its central sPLA 2 domain is homologous to bee venom PLA 2 rather than to other mammalian sPLA 2 s. To elucidate the in vivo actions of this atypical sPLA 2 , we generated transgenic (Tg) mice overexpressing human PLA2G3. Despite marked increases in PLA 2 activity and mature 18-kDa PLA2G3 protein in the circulation and tissues, PLA2G3 Tg mice displayed no apparent abnormality up to 9 months of age. However, alterations in plasma lipoproteins were observed in PLA2G3 Tg mice compared with control mice. In vitro incubation of low density (LDL) and high density (HDL) lipoproteins with several sPLA 2 s showed that phosphatidylcholine was efficiently converted to lysophosphatidylcholine by PLA2G3 as well as by PLA2G5 and PLA2G10, to a lesser extent by PLA2G2F, and only minimally by PLA2G2A and PLA2G2E. PLA2G3-modified LDL, like PLA2G5-or PLA2G10-treated LDL, facilitated the formation of foam cells from macrophages ex vivo. Accumulation of PLA2G3 was detected in the atherosclerotic lesions of humans and apoE-deficient mice. Furthermore, following an atherogenic diet, aortic atherosclerotic lesions were more severe in PLA2G3 Tg mice than in control mice on the apoE-null background, in combination with elevated plasma lysophosphatidylcholine and thromboxane A 2 levels. These results collectively suggest a potential functional link between PLA2G3 and atherosclerosis, as has recently been proposed for PLA2G5 and PLA2G10.

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Section: Generation Of Pla2g3 Tg Mice-thesupporting

confidence: 63%

Section: Discussionmentioning

confidence: 66%

Analyses of Group III Secreted Phospholipase A2 Transgenic Mice Reveal Potential Participation of This Enzyme in Plasma Lipoprotein Modification, Macrophage Foam Cell Formation, and Atherosclerosis

Sato

Kato²,

Isogai

et al. 2008

Journal of Biological Chemistry

117

136

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“…Accumulating evidence suggests that secretory phospholipase A 2 (sPLA 2 ) enzymes may promote atherosclerosis through modification of LDL. Of the 10 sPLA 2 family members that have been described in mammals, group V (GV), GX, and very recently, GIII sPLA 2 have been shown to be potent in hydrolyzing LDL in vitro (8)(9)(10). A role for GV sPLA 2 in atherosclerotic lipid deposition in vivo has recently been substantiated by gain-and loss-of-function studies in LDL receptor-deficient mice (11).…”

mentioning

confidence: 86%

Syndecan-4 mediates macrophage uptake of group V secretory phospholipase A2-modified LDL

Boyanovsky

Shridas

Simons

et al. 2009

Journal of Lipid Research

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We previously reported that LDL modified by group V secretory phospholipase A 2 (GV-LDL) promotes macrophage foam cell formation through a mechanism independent of scavenger receptors SR-A and CD36, and dependent on cellular proteoglycans. This study investigates the role of syndecans, a family of cell surface proteoglycans known to mediate endocytosis through macropinocytosis, in macrophage uptake of GV-LDL. LY 294002, a phosphatidylinositol 3-kinase inhibitor, significantly reduced internalization of 125 I-labeled GV-LDL in J-774 macrophages, consistent with a macropinocytic uptake pathway. Using small, interfering RNA-directed gene silencing, we demonstrated a direct relationship between 125 I-labeled GV-LDL binding and the level of syndecan-3 and syndecan-4 expression in J-774 cells. However, 125 I-labeled GV-LDL uptake was significantly reduced only when syndecan-4 expression was suppressed. Peritoneal macrophages from syndecan-4-deficient mice exhibited markedly reduced uptake of fluorescently labeled GV-LDL compared with wild-type cells. Furthermore, cholesteryl ester accumulation induced by GV-LDL was dependent on syndecan-4 expression. Syndecan-4 expression and GV-LDL binding were significantly increased in J-774 cells treated with lipopolysaccharide, suggesting that GV-LDL uptake via this pathway may be enhanced during inflammation. Taken together, our data point to a novel role for syndecan-4 in mediating the uptake of GV-LDL, a process implicated in atherosclerotic lesion progression.-Boyanovsky, B. B., P. Shridas, M. Simons, D. R. van der Westhuyzen, and N. R. Webb. Syndecan-4 mediates macrophage uptake of group V secretory phospholipase A 2 -modified LDL. J. Lipid Res. 2009. 50: 641-650.

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“…Given that groups IIA, V and X show a differential hydrolysis of molecular species of phosphatidylcholine [44], sPLA 2 modified HDLs with various activities are expected to be formed under inflammatory conditions.…”

Section: Discussionmentioning

confidence: 99%

Neutrophil effector responses are suppressed by secretory phospholipase A2 modified HDL

2015

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Differential hydrolysis of molecular species of lipoprotein phosphatidylcholine by groups IIA, V and X secretory phospholipases A

Cited by 50 publications

References 44 publications

Analyses of Group III Secreted Phospholipase A2 Transgenic Mice Reveal Potential Participation of This Enzyme in Plasma Lipoprotein Modification, Macrophage Foam Cell Formation, and Atherosclerosis

Analyses of Group III Secreted Phospholipase A2 Transgenic Mice Reveal Potential Participation of This Enzyme in Plasma Lipoprotein Modification, Macrophage Foam Cell Formation, and Atherosclerosis

Syndecan-4 mediates macrophage uptake of group V secretory phospholipase A2-modified LDL

Neutrophil effector responses are suppressed by secretory phospholipase A2 modified HDL

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