Endothelin-1-induced arachidonic acid release by cytosolic phospholipase A2 activation in rat vascular smooth muscle via extracellular signal-regulated kinases pathway

Trevisi, Lucia; Bova, Sergio; Cargnelli, Gabriella; Ceolotto, Giulio; Luciani, Sisto

doi:10.1016/s0006-2952(02)01066-3

Cited by 38 publications

(35 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The activation of endothelin receptor, another G protein-coupled receptor, was shown to cause AA release in astrocytes (38) and in smooth muscle cells (39,40). The study with smooth muscle cells further demonstrated the involvement of PKC␣ and p38 MAP kinase in endothelin-1-mediated AA release (39).…”

Section: Response To Receptor Agonistsmentioning

confidence: 88%

Phospholipase A2 in the central nervous system

Sun

Xu²,

Jensen

et al. 2004

Journal of Lipid Research

355

View full text Add to dashboard Cite

Phospholipase A 2 (PLA 2 ) belongs to a family of enzymes that catalyze the cleavage of fatty acids from the sn-2 position of phospholipids. There are more than 19 different isoforms of PLA 2 in the mammalian system, but recent studies have focused on three major groups, namely, the group IV cytosolic PLA 2 , the group II secretory PLA 2 (sPLA 2 ), and the group VI Ca 2 ؉ -independent PLA 2 . These PLA 2 s are involved in a complex network of signaling pathways that link receptor agonists, oxidative agents, and proinflammatory cytokines to the release of arachidonic acid (AA) and the synthesis of eicosanoids. PLA 2 s acting on membrane phospholipids have been implicated in intracellular membrane trafficking, differentiation, proliferation, and apoptotic processes. All major groups of PLA 2 are present in the central nervous system (CNS). Therefore, this review is focused on PLA 2 and AA release in neural cells, especially in astrocytes and neurons. In addition, because many neurodegenerative diseases are associated with increased oxidative and inflammatory responses, an attempt was made to include studies on PLA 2 in cerebral ischemia, Alzheimer's disease, and neuronal injury due to excitotoxic agents. Information from these studies has provided clear evidence for the important role of PLA 2 in regulating physiological and pathological functions in the CNS. Bazan (1) recognized the important role of arachidonic acid (AA) in the central nervous system (CNS) in the '70s when he observed the rapid and transient release of this fatty acid in the brain due to seizure and cerebral ischemia. The "Bazan effect" has since stimulated over 30 years of investigations attempting to unravel mechanisms regulating AA release from membrane phospholipids in the CNS.Phospholipids in CNS membranes are enriched in polyunsaturated fatty acids (PUFAs) (2). Metabolism of PUFA is stringently controlled by phospholipase A 2 (PLA 2 ) and acyltransferases-known as the "deacylation-reacylation cycle" (3-5). Under normal conditions, free fatty acids (FFAs) released by PLA 2 are rapidly taken up by membrane phospholipids through an energy-dependent process involving CoA and ATP (6). To date, limited information is available on the structure and functions of acyltransferases. However, recent advances in molecular biological techniques have aided in the identification of many genes encoding different groups of PLA 2 and have provided new information on the properties and functions of these molecules.PLA 2 (EC3.1.1.4.) belongs to a family of enzymes that catalyze the cleavage of fatty acids from the sn -2 position of phospholipids. These enzymes are not only important for maintenance of cell membrane phospholipids; they also play a key role in regulating the release of AA, a precursor for synthesis of eicosanoids. In the mammalian system, more than 19 different isoforms of PLA 2 have been identified, and different PLA 2 s have been shown to participate in physiological events related to cell injury, inflammation, and apoptosis (7,8). Re...

show abstract

Section: Response To Receptor Agonistsmentioning

confidence: 88%

Phospholipase A2 in the central nervous system

Sun

Xu²,

Jensen

et al. 2004

Journal of Lipid Research

355

View full text Add to dashboard Cite

show abstract

“…It is well established that one characteristic of transformed cells is perturbation of lipid synthetic and degradative pathways (71)(72)(73), suggesting an active role of lipids in oncogenic transformation. Expression of oncogenic Ras correlates with increased levels of phosphocholine and phosphoethanolamine (45,(73)(74)(75), diacylglycerols (76), inositol phosphates (77), and arachidonic acid (78). The stimulated degradation of phospholipids is accompanied by an increased biosynthesis (45,(73)(74)(75), demonstrating an accelerated turnover of lipids in transformed cells.…”

Section: Transient Expression Of Sp3 Increases the Amount Of Both Ct␣mentioning

confidence: 99%

“…The stimulated degradation of phospholipids is accompanied by an increased biosynthesis (45,(73)(74)(75), demonstrating an accelerated turnover of lipids in transformed cells. Increased amounts of phosphocholine and phosphoethanolamine have been implicated in tumor development (78), during which choline/ethanolamine kinases are typically up-regulated, whereas enzymes involved in the subsequent metabolism of phosphocholine and phosphoethanolamine (i.e. CTP:phosphocholine-and phosphoethanolamine cytidylyltransferases) are either up-regulated (47) or down-regulated (45, 46) depending on the cell type.…”

Section: Transient Expression Of Sp3 Increases the Amount Of Both Ct␣mentioning

confidence: 99%

Oncogenic Ha-Ras Transformation Modulates the Transcription of the CTP:Phosphocholine Cytidylyltransferase α Gene via p42/44MAPK and Transcription Factor Sp3

Bakovic¹,

Waite²,

Vance

2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

Phosphatidylcholine (PC)1 is the most abundant phospholipid in mammalian cellular membranes. Besides having a structural role in membranes and lipoproteins (1-3), PC plays an important role in signal transduction as a source of lipid second messengers (1-3). In all nucleated cells, PC is made primarily through the CDP-choline pathway in which the key enzyme is CTP:phosphocholine cytidylyltransferase (CT) (2-6).Two genes that encode CT activity have been identified and characterized. CT␣ is expressed in many cells and tissues (7-13) and has a predicted structure that contains catalytic, phosphorylation, and lipid binding domains as well as a nuclear localization sequence (8, 14 -21). Recently, CT␤ has been identified in human tissues and appears to exist as two splice variants, CT␤1 and CT␤2, differing at their C termini (22, 23). Like CT␣, CT␤1/2 contains catalytic and lipid binding domains. However, CT␤1 lacks the phosphorylation domain, and both CT␤1 and CT␤2 lack the nuclear localization sequence (23).In the last several years, studies have shown that CT can be regulated at both the transcriptional level and post-transcriptionally. CT mRNA is increased after partial hepatectomy in rats (13), after stimulation with colony-stimulating factor 1 in macrophages (24), and during development and growth (25)(26)(27)(28). It remains to be determined whether these increases in the message levels are the result of CT␣ and/or CT␤1/2 mRNA stability, an increase in gene transcription, or a combination of both.The murine CT␣ gene (Ctpct) was cloned and characterized by Tang and co-workers (29). The Ctpct promoter contains several putative elements for binding transcription factors, including Ap1, an overlapping site for nuclear factor-B, E2F, and Elk1, one sterol response element, as well as three elements for Sp-related factors (30). We have shown that Sp1, Sp2, and Sp3 bind competitively to three GC-rich elements and that relative promoter activity depends upon the abundance of these factors (31). We further established that transcription enhancer factor-4 can bind to an upstream regulatory element (Ϫ103/Ϫ82) and enhance the CT␣ gene expression through its interactions with the basal transcriptional machinery (32). In agreement with the finding that lipoprotein deficiency induces the expression of CT␣ mRNA and protein in alveolar type II epithelial cells (33), and our observation that the CT␣ promoter contains a putative sterol response element (30), studies by Kast et al. (34) indicate a role for cholesterol/sterol response element-binding protein and the functionality of the sterol response element in the regulation of CT␣ gene expression in Chinese hamster ovary cells and THP-1 cells. On the other hand, Lagace et al. (35) have shown that cholesterol/sterol response element-binding protein can stimulate PC biosynthe-

show abstract

“…ET-1 induced the phosphorylation of cPLA 2 at ser505 in KCs from BDL and sham animals; however, the effect was significantly greater in KCs from BDL animals. In other cell types, ET-1 has been demonstrated to activate cPLA 2 and the release of various eicosanoids including TXA 2 , via binding to Gq/G11 and Gi coupled ET (A) and ET (B) receptors, subsequently inducing the activation of ERK1/2 or p38 MAPK through PLC or PKC mediated signaling pathways (38,39,41,42,44,45,47,(55)(56)(57)(58)(59)(60)(61). Therefore, the purposes of the present study were to delineate the signaling pathways induced via stimulation of Gq/G11 and Gi coupled ETBRs and the relative roles of intermediates in the activation of cPLA 2 and production of TXA 2 in KCs in response to ET-1, and determine whether the hepatic stress of early stage fibrosis alters the signaling pathways through modifications in the expressions or activities of signaling intermediates.…”

Section: Discussionmentioning

confidence: 99%

“…The stimulation of Gq has been shown to induce the activation of cPLA 2 and production of eicosanoids via the PLC or PKC mediated activation of ERK1/2. Stimulation of Gi coupled receptors have been reported to lead to the phosphorylation of cPLA 2 and release of AA via the activation of p38 MAPK and ERK1/2, although the intermediates involved in the activation of p38 have not been fully elucidated (38)(39)(40)(41)(42)(43)(44)(45)(46)(47). KCs express ET (B) receptors coupled to Gq/G11 and Gi proteins (48)(49)(50)(51), and several reports have supported the initial findings by Qui et al of the requirements of both a transient increase in calcium and phosphorylation of ser505, via p38 MAPK or ERK1/2, for the full activation of cPLA 2 and AA release in macrophages (28,34,35).…”

Section: Introductionmentioning

confidence: 99%

Altered Endothelin-1 Signaling in Production of Thromboxane A2 in Kupffer Cells from Bile Duct Ligated Rats

Miller

Zhang

2009

Cell Mol Immunol

View full text Add to dashboard Cite

Kupffer cells (KCs), the liver resident macrophages accounting for 80-90% of the total population of fixed tissue macrophages in the body, not only play a key role in host defense via removing particulate materials from the portal circulation, but may also contribute to the pathogenesis of various liver diseases. We have previously demonstrated that KCs play an important role in controlling portal hypertension and hepatocellular injury via releasing thromboxane A 2 (TXA 2 ) in early fibrosis induced by one-week bile duct ligation (BDL). Production of TXA 2 is controlled by cytosolic phospholipase A 2 (cPLA 2 ) that is activated by the interaction of entothelin-1 (ET-1) with its G-protein coupled ET receptor B (ETBR). However, the signaling pathways that contribute to the ET-1-induced activation of cPLA 2

show abstract

Endothelin-1-induced arachidonic acid release by cytosolic phospholipase A2 activation in rat vascular smooth muscle via extracellular signal-regulated kinases pathway

Cited by 38 publications

References 39 publications

Phospholipase A2 in the central nervous system

Phospholipase A2 in the central nervous system

Oncogenic Ha-Ras Transformation Modulates the Transcription of the CTP:Phosphocholine Cytidylyltransferase α Gene via p42/44MAPK and Transcription Factor Sp3

Altered Endothelin-1 Signaling in Production of Thromboxane A2 in Kupffer Cells from Bile Duct Ligated Rats

Contact Info

Product

Resources

About