Analysis of Two Major Intracellular Phospholipases A2 (PLA2) in Mast Cells Reveals Crucial Contribution of Cytosolic PLA2α, Not Ca2+-independent PLA2β, to Lipid Mobilization in Proximal Mast Cells and Distal Fibroblasts

Ueno, Noriko; Taketomi, Yoshitaka; Yamamoto, Kei; Hirabayashi, Tetsuya; Kamei, Daisuke; Kita, Yoshiaki; Shimizu, Takao; Shinzawa, Koei; Tsujimoto, Yoshihide; Ikeda, Kazutaka; Taguchi, Ryo; Murakami, Makoto

doi:10.1074/jbc.m111.290312

Cited by 26 publications

(28 citation statements)

References 88 publications

(140 reference statements)

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“…The PLA 2 superfamily has been subdivided into several classes. Of these, the intracellular cPLA2 and iPLA2 families and the extracellular sPLA2 family are recognized as the "big three" [23][24][25][26][27]. cPLA 2 is ubiquitously expressed throughout mammalian tissues, with highest levels in immune cells such as macrophages and mast cells [41,42].…”

Section: Discussionmentioning

confidence: 99%

“…cPLA2 plays an important role in the initiation of arachidonic acid metabolism, iPLA2 Chunfeng Xie, Xiaoting Li and Jieshu Wu contributed equally to this work. contributes to membrane homeostasis and energy metabolism, and sPLA2 modulates the extracellular phospholipid milieus [23][24][25][26][27]. During inflammation, activation of PLA 2 releases AA stored in membrane phospholipids [28].…”

Section: Introductionmentioning

confidence: 99%

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Anti-inflammatory Activity of Magnesium Isoglycyrrhizinate Through Inhibition of Phospholipase A2/Arachidonic Acid Pathway

Xie

et al. 2015

Inflammation

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Glycyrrhiza glabra (licorice) has been known to possess various pharmacological properties including anti-inflammatory, antioxidants, antiviral, and hepatoprotective activities. Magnesium isoglycyrrhizinate (MgIG), a magnesium salt of 18-α glycyrrhizic acid stereoisomer, is clinically used for the treatment of inflammatory liver diseases. However, the mechanism by which MgIG exerts its anti-inflammatory effects remains unknown. In the present study, we investigated the inhibitory potential of MgIG in phospholipase A2 (PLA2)/arachidonic acid (AA) pathway and release of the pathway-generated inflammatory lipid mediators in RAW264.7 macrophages. Results revealed that MgIG suppressed LPS-induced activation of PLA2 and production of AA metabolites such as prostaglandin E2 (PGE2), prostacyclin (PGI2), thromboxane 2 (TXB2), and leukotrienes (LTB4) in macrophages. Furthermore, LPS-induced AA-metabolizing enzymes including COX-2, COX-1, 5-LOX, TXB synthase, and PGI2 synthase were significantly inhibited by MgIG. Taken together, our data suggest that modulation of cyclooxygenase (COXs) and 5-lipoxygenase (LOX) pathways in AA metabolism could be a novel mechanism for the anti-inflammatory effects of MgIG.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Anti-inflammatory Activity of Magnesium Isoglycyrrhizinate Through Inhibition of Phospholipase A2/Arachidonic Acid Pathway

Xie

et al. 2015

Inflammation

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“…iPLA 2 ␤ activity has been reported in many components of the immune system, including macrophages ( 6, 401-404 ), monocytes ( 405 ), neutrophils ( 406,407 ), mast cells ( 408 ), and T-cells and Fig. 2.…”

Section: Ipla 2 ␤ and Diseasesmentioning

confidence: 99%

Calcium-independent phospholipases A2 and their roles in biological processes and diseases

Ramanadham

Ali

Ashley

et al. 2015

Journal of Lipid Research

161

172

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The Ca 2+ -independent phospholipases A 2 (iPLA 2 s) are part of a diverse family of PLA 2 s that hydrolyze the sn -2 substituent from membrane phospholipids to release a free fatty acid and a lysolipid ( 1, 2 ). These enzymes are ubiquitously expressed, and in contrast to secretory PLA 2 s (sPLA 2 s) and cytosolic PLA 2 s (cPLA 2 s), do not require Ca 2+ for either translocation or activity. Some of the fi rst descriptions of iPLA 2 activity were in the mid-to late-1980s with the identifi cation of a plasmalogen-selective PLA 2 in Abstract Among the family of phospholipases A 2 (PLA 2 s) are the Ca 2+ -independent PLA 2 s (iPLA 2 s) and they are designated group VI iPLA 2 s. In relation to secretory and cytosolic PLA 2 s, the iPLA 2 s are more recently described and details of their expression and roles in biological functions are rapidly emerging. The iPLA 2 s or patatin-like phospholipases (PNPLAs) are intracellular enzymes that do not require Ca 2+ for activity, and contain lipase (GXSXG) and nucleotide-binding (GXGXXG) consensus sequences. Though nine PNPLAs have been recognized, PNPLA8 (membraneassociated iPLA 2 ␥ ) and PNPLA9 (cytosol-associated iPLA 2 ␤ ) are the most widely studied and understood. The iPLA 2 s manifest a variety of activities in addition to phospholipase, are ubiquitously expressed, and participate in a multitude of biological processes, including fat catabolism, cell differentiation, maintenance of mitochondrial integrity, phospholipid remodeling, cell proliferation, signal transduction, and cell death. As might be expected, increased or decreased expression of iPLA 2 s can have profound effects on the metabolic state, CNS function, cardiovascular performance, and cell survival; therefore, dysregulation of iPLA 2 s can be a critical factor in the development of many diseases. This review is aimed at providing a general framework of the current understanding of the iPLA 2 s and discussion of the potential mechanisms of action of the iPLA 2 s and related involved lipid mediators. -Ramanadham, S

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“…Most cells contain several types of PLA 2 enzymes and studies have suggested that they have distinct functions. For example, a comparison of the function of cPLA 2 ␣ and iPLA 2 ␤ in mast cells and macrophages found that cPLA 2 ␣ , but not iPLA 2 ␤ , selectively hydrolyzes arachidonic acid-containing phospholipids in response to cell stimulation ( 12,13 ).…”

mentioning

confidence: 99%

Cytosolic phospholipase A2: physiological function and role in disease

Leslie

2015

Journal of Lipid Research

329

243

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Analysis of Two Major Intracellular Phospholipases A2 (PLA2) in Mast Cells Reveals Crucial Contribution of Cytosolic PLA2α, Not Ca2+-independent PLA2β, to Lipid Mobilization in Proximal Mast Cells and Distal Fibroblasts

Cited by 26 publications

References 88 publications

Anti-inflammatory Activity of Magnesium Isoglycyrrhizinate Through Inhibition of Phospholipase A2/Arachidonic Acid Pathway

Anti-inflammatory Activity of Magnesium Isoglycyrrhizinate Through Inhibition of Phospholipase A2/Arachidonic Acid Pathway

Calcium-independent phospholipases A2 and their roles in biological processes and diseases

Cytosolic phospholipase A2: physiological function and role in disease

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