Phospholipid Peroxidation Induces Cytosolic Phospholipase A2Activity: Membrane Effects versus Enzyme Phosphorylation

Rashba-Step, Julia; Tatoyan, Anahit; Duncan, Roger; Ann, David K.; Pushpa-Rehka, Thimmalapura R.; Sevanian, Alex

doi:10.1006/abbi.1997.0134

Cited by 79 publications

(45 citation statements)

References 50 publications

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“…Our experiment on the effect of PKC inhibitors on LacCermediated PLA 2 activation suggests that PLA 2 locates downstream of PKC in the signaling events involved in PECAM-1 expression. Our findings are in agreement with the observation of Rashba-Step (15) in which PKC phosphorylated cPLA 2 and hence increased its activity.…”

Section: Discussionsupporting

confidence: 93%

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Lactosylceramide recruits PKCα/ε and phospholipase A₂to stimulate PECAM-1 expression in human monocytes and adhesion to endothelial cells

Gong

Wei

Chowdhury

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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Despite the importance of platelet͞endothelial cell adhesion molecule-1 (PECAM-1, CD31) in the adhesion and diapedesis of monocytes͞lymphocytes, little is known about the mechanisms by which it is regulated. We explored the role of a glycosphingolipid, lactosylceramide (LacCer), in modulating PECAM-1 expression and cell adhesion in human monocytes. We observed that LacCer specifically exerted a time-dependent increase in PECAM-1 expression in U

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Section: Discussionsupporting

confidence: 93%

“…Because phosphorylation of PLA 2 by PKC enhances its activity (15) and PKC was involved in LacCer-mediated up-regulation of PECAM-1, the question was raised whether PLA 2 was also involved in this process in human monocytes. As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Lactosylceramide recruits PKCα/ε and phospholipase A₂to stimulate PECAM-1 expression in human monocytes and adhesion to endothelial cells

Gong

Wei

Chowdhury

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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“…Thus, cPLA 2 -mediated AA release may be specifically involved in the execution of alternative TNF-induced death pathways that are caspase-independent but reactive oxygen intermediate-dependent in murine fibrosarcoma cells. In line with this, reactive oxygen intermediates have been reported to activate cPLA 2 enzyme via an increase in intracellular calcium and/or lipo-oxygenation (6,34). Butylated hydroxyanisole inhibited TNF-induced AA release in WEHI-S cells, suggesting that reactive oxygen intermediates indeed act upstream of AA release in TNF-treated WEHI-S cells.…”

Section: Figmentioning

confidence: 59%

Cathepsin B Mediates Tumor Necrosis Factor-induced Arachidonic Acid Release in Tumor Cells

Foghsgaard

Lademann

Wissing

et al. 2002

Journal of Biological Chemistry

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Arachidonic acid (AA) generated by cytosolic phospholipase A 2 (cPLA 2 ) has been suggested to function as a second messenger in tumor necrosis factor (TNF)-induced death signaling. Here, we show that cathepsin B-like proteases are required for the TNF-induced AA release in transformed cells. Pharmaceutical inhibitors of cathepsin B blocked TNF-induced AA release in human breast (MCF-7S1) and cervix (ME-180as) carcinoma as well as murine fibrosarcoma (WEHI-S) cells. Furthermore, TNF-induced AA release was significantly reduced in cathepsin B-deficient immortalized murine embryonic fibroblasts. Employing cPLA 2 -deficient MCF-7S1 cells expressing ectopic cPLA 2 or cPLA 2 -deficient immortalized murine embryonic fibroblasts, we showed that cPLA 2 is dispensable for TNF-induced AA release and death in these cells. Furthermore, TNF-induced cathepsin B-dependent AA release could be dissociated from the cathepsin B-independent cell death in MCF-7S1 cells, whereas both events required cathepsin B activity in other cell lines tested. These data suggest that cathepsin B inhibitors may prove useful not only in the direct control of cell death but also in limiting the damageassociated inflammation.

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“…The hydrolysis of glycerophospholipids to liberate fatty acids is in fact regulated by cPLA 2 translocation to membranes and by MAPK-catalyzed phosphorylation (19,25,27). There are several reports indicating that cPLA 2 may be a substrate for PKC phosphorylating activity (17,28). Our recent work has also provided in vitro evidence that PKC upstream activates cPLA 2 after stimulation of ECs by oxidized LDL or of pericytes by b-amyloid peptides (29,30).…”

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confidence: 77%

Endothelial cell-pericyte cocultures induce PLA2 protein expression through activation of PKCα and the MAPK/ERK cascade

Anfuso

Lupo

Romeo

et al. 2007

Journal of Lipid Research

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Little is known about the regulatory mechanisms of endothelial cell (EC) proliferation by retinal pericytes and vice versa. In a model of coculture with bovine retinal pericytes lasting for 24 h, rat brain ECs showed an increase in arachidonic acid (AA) release, whereas Western blot and RT-PCR analyses revealed that ECs activated the protein expression of cytosolic phospholipase A 2 (cPLA 2 ) and its phosphorylated form and calcium-independent intracellular phospholipase A 2 (iPLA 2 ). No activation of the same enzymes was seen in companion pericytes. In ECs, the protein level of phosphorylated extracellular signal-regulated kinase (ERK) 1/2 was also enhanced significantly, a finding not observed in cocultured pericytes. The expression of protein kinase C-a (PKCa) and its phosphorylated form was also enhanced in ECs. Wortmannin, LY294002, and PD98059, used as inhibitors of upstream kinases (the PI3-kinase/Akt/PDK1 or MEK-1 pathway) in cultures, markedly attenuated AA release and the expression of phosphorylated forms of endothelial cPLA 2 , PKCa, and ERK1/2. By confocal microscopy, activation of PKCa in perinuclear regions of ECs grown in coculture as well as strong activation of cPLA 2 in ECs taken from a model of mixed culture were clearly observed. However, no increased expression of both enzymes was found in cocultured pericytes. Our findings indicate that a sequential activation of PKCa contributes to endothelial ERK1/2 and cPLA 2 phosphorylation induced by either soluble factors or direct cell-tocell contact, and that the PKCa-cPLA 2 pathway appears to play a key role in the early phase of EC-pericyte interactions regulating blood retina or blood-brain barrier maturation.-

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Phospholipid Peroxidation Induces Cytosolic Phospholipase A2Activity: Membrane Effects versus Enzyme Phosphorylation

Cited by 79 publications

References 50 publications

Lactosylceramide recruits PKCα/ε and phospholipase A₂to stimulate PECAM-1 expression in human monocytes and adhesion to endothelial cells

Lactosylceramide recruits PKCα/ε and phospholipase A₂to stimulate PECAM-1 expression in human monocytes and adhesion to endothelial cells

Cathepsin B Mediates Tumor Necrosis Factor-induced Arachidonic Acid Release in Tumor Cells

Endothelial cell-pericyte cocultures induce PLA2 protein expression through activation of PKCα and the MAPK/ERK cascade

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Phospholipid Peroxidation Induces Cytosolic Phospholipase A2Activity: Membrane Effects versus Enzyme Phosphorylation

Cited by 79 publications

References 50 publications

Lactosylceramide recruits PKCα/ε and phospholipase A2to stimulate PECAM-1 expression in human monocytes and adhesion to endothelial cells

Lactosylceramide recruits PKCα/ε and phospholipase A2to stimulate PECAM-1 expression in human monocytes and adhesion to endothelial cells

Cathepsin B Mediates Tumor Necrosis Factor-induced Arachidonic Acid Release in Tumor Cells

Endothelial cell-pericyte cocultures induce PLA2 protein expression through activation of PKCα and the MAPK/ERK cascade

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Lactosylceramide recruits PKCα/ε and phospholipase A₂to stimulate PECAM-1 expression in human monocytes and adhesion to endothelial cells

Lactosylceramide recruits PKCα/ε and phospholipase A₂to stimulate PECAM-1 expression in human monocytes and adhesion to endothelial cells