Group IIA and group V secretory phospholipase A2: quantitative analysis of expression and secretion and determination of the localization and routing in rat mesangial cells

Helm, Hester A. van der; Buijtenhuijs, P; Bosch, H. van den

doi:10.1016/s1388-1981(00)00171-2

Cited by 10 publications

(9 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…19 Although it is not known whether vimentin and HSPGs colocalize in these membrane microdomains, these proteins may play a role in the intracellular distribution of hGIIA in activated cells. 19,81 The interaction of hGIIA with vimentin in conjunction with the crucial role of HSPG for its activity could provide regulatory mechanisms for its activation and its intracellular colocalization with proteins involved in the metabolism of AA.…”

Section: Discussionmentioning

confidence: 99%

Identification of an autoantigen on the surface of apoptotic human T cells as a new protein interacting with inflammatory group IIA phospholipase A2

Boilard

Bourgoin

Bernatchez

et al. 2003

Blood

100

View full text Add to dashboard Cite

One of the most studied secreted phospholipases A 2 (sPLA 2 ), the group IIA sPLA 2 , is found at high levels in inflammatory fluids of patients with autoimmune diseases. A characteristic of group IIA sPLA 2 is its preference for negatively charged phospholipids, which become exposed on the extracellular leaflet of apoptotic cell membranes. We recently showed that low molecular weight heparan sulfate proteoglycans (HSPGs) and uncharacterized detergent-insoluble binding site(s) contribute to the enhanced binding of human group IIA PLA 2 (hGIIA) to apoptotic human T cells. Using matrixassisted laser desorption/ionization time of flight (MALDI-TOF) mass spectrometry we now identify vimentin as the major HSPG-independent binding protein of hGIIA on apoptotic primary T lymphocytes. Vimentin is partially exposed on the surface of apoptotic T cells and binds hGIIA via its rod domain in a calciumindependent manner. Studies with hGIIA mutants showed that specific motifs in the interfacial binding surface are in- IntroductionPhospholipases A 2 (PLA 2 ) hydrolyze membrane phospholipids to produce free fatty acids and lysophospholipids. 1,2 PLA 2 provide precursors for the biosynthesis of proinflammatory lipid mediators such as prostaglandins, leukotrienes, and lipoxins when the hydrolyzed fatty acid is arachidonic acid (AA) and platelet-activating factor when the lysophospholipid is 1-alkyl-2-lyso-phosphatidylcholine. Several high molecular weight intracellular mammalian PLA 2 and a family of 14-to 19-kDa PLA 2 , referred to as secretory PLA 2 (sPLA 2 ), have been identified. 2,3 Mammalian sPLA 2 are classified into 10 different groups. 3,4 sPLA 2 can interact with external cell membranes through direct binding to phospholipids or specific cell surface receptors. 3,5,6 The M-type receptor present on skeletal muscle 7 and human neutrophils 8 belongs to the superfamily of C-type lectins and binds with high affinity to the snake venom sPLA 2 OS 1 and OS 2 , pancreatic group IB PLA 2 , and rabbit and mouse group IIA PLA 2 but not to bee venom group III PLA 2 and very weakly to human group IIA PLA 2 (hGIIA). 7,[9][10][11][12][13] The N-type receptors identified in rat brain have high affinity for OS 2 and bee venom group III PLA 2 . 14 Venom and mammalian sPLA 2 also bind to a number of cell soluble proteins, such as pentraxins, 15 reticulocalbins, 16 calmodulin, 17 heparin, and to the serum coagulation factor Xa. 18 Several mammalian sPLA 2 such as group II and V enzymes also bind to heparan sulfate proteoglycans (HSPGs) like glypican-1 19 and decorin. 20 hGIIA is found in high concentrations in the circulation of patients with acute pancreatitis and certain cancers and in the synovial fluid from patients with rheumatoid arthritis. 1,2,[21][22][23] hGIIA has been proposed to release AA for the generation of prostaglandins in certain conditions. 19,[24][25][26][27][28][29][30][31] The binding of hGIIA to HSPGs is required for exogenous hGIIA-catalyzed AA release from apoptotic human T cells and from HEK-293 cells overexpressin...

show abstract

Section: Discussionmentioning

confidence: 99%

Identification of an autoantigen on the surface of apoptotic human T cells as a new protein interacting with inflammatory group IIA phospholipase A2

Boilard

Bourgoin

Bernatchez

et al. 2003

Blood

100

View full text Add to dashboard Cite

show abstract

“…Alternatively, it is possible that GX sPLA 2 , like BPI (88), is a membrane-associated protein in azurophilic granules and is not released into the extracellular fluid after exposure to fMLP or OZ. It may be noted that recent studies with rat mesangial cells show that ϳ80% of the GIIA sPLA 2 in these cells is secreted after agonist stimulation, whereas most of the GV sPLA 2 remains in an intracellular compartment (91). Thus, it would appear that not all sPLA 2 s are secreted to the extracellular space following agonist-induced cell activation.…”

Section: Fig 4 Neutrophils Contain Gv and Gx Splamentioning

confidence: 94%

Groups IV, V, and X Phospholipases A2s in Human Neutrophils

Dégousée¹,

Ghomashchi²,

Stefanski³

et al. 2002

Journal of Biological Chemistry

165

View full text Add to dashboard Cite

The bacterial tripeptide formyl-Met-Leu-Phe (fMLP) induces the secretion of enzyme(s) with phospholipase A 2 (PLA 2 ) activity from human neutrophils. We show that circulating human neutrophils express groups V and X sPLA 2 (GV and GX sPLA 2 ) mRNA and contain GV and GX sPLA 2 proteins, whereas GIB, GIIA, GIID, GIIE, GIIF, GIII, and GXII sPLA 2 s are undetectable. GV sPLA 2 is a component of both azurophilic and specific granules, whereas GX sPLA 2 is confined to azurophilic granules. Exposure to fMLP or opsonized zymosan results in the release of GV but not GX sPLA 2 and most, if not all, of the PLA 2 activity in the extracellular fluid of fMLPstimulated neutrophils is due to GV sPLA 2 . GV sPLA 2 does not contribute to fMLP-stimulated leukotriene B 4 production but may support the anti-bacterial properties of the neutrophil, because 10 -100 ng per ml concentrations of this enzyme lead to Gram-negative bacterial membrane phospholipid hydrolysis in the presence of human serum. By use of a recently described and specific inhibitor of cytosolic PLA 2 -␣ (group IV PLA 2 ␣), we show that this enzyme produces virtually all of the arachidonic acid used for the biosynthesis of leukotriene B 4 in fMLP-and opsonized zymosan-stimulated neutrophils, the major eicosanoid produced by these pro-inflammatory cells.

show abstract

“…These responses were abrogated by pretreatment with both heparitinase and phosphatidylinositol‐specific phospholipase C, thus suggesting that a glysophosphatidylinositol‐anchored platelet‐membrane heparan sulfate proteoglycan is the binding site for sPLA 2 ‐IIA in human platelets, and also that the engagement of this structure leads to the release of the arachidonic acid needed for thromboxane A 2 production [31]. As regards mesangial cells, early studies showing cross‐talk between sPLA 2 ‐IIA and cPLA 2 [32] have been recently enlarged by the description of a synergistic effect of peroxisome proliferator‐activated receptor and tumor necrosis factor‐α (TNF‐α) on sPLA 2 ‐IIA expression [33], and by the finding that interleukin‐1β enhances the expression of both sPLA 2 ‐IIA and group V sPLA 2 in rat mesangial cells [34], thus pointing to the positive modulation of sPLA 2 ‐IIA expression as a relevant factor for kidney pathology.…”

Section: Spla2‐iia Elicits a Mitogenic Response And Activates Arachidmentioning

confidence: 99%

Biological effects of group IIA secreted phosholipase A₂

Fuentes¹,

Hernández²,

Nieto³

et al. 2002

FEBS Letters

View full text Add to dashboard Cite

Group IIA secreted phospholipase A 2 (sPLA 2 -IIA) is the most abundant element in human tissues of a large family of low molecular weight phospholipases A 2 , which shows properties di¡erent from those displayed by the cytosolic phospholipase A 2 involved in the release of arachidonic acid. sPLA 2 -IIA behaves as a ligand for a group of receptors inside the C-type multilectin mannose receptor family and also interacts with heparan sulfate proteoglycans such as glypican, the dermatan/chondroitin sulfate-rich decorin, and the chondroitin sulfate-rich versican, thus being able to internalize to speci¢c compartments within the cell and producing biological responses. This review provides a short summary of the biological actions of sPLA 2 -IIA on intracellular signaling pathways. Phospholipases A 2 (PLA 2 ) are a large family of related enzymes that have been classi¢ed into groups I^XII according to several criteria which include catalysis of the hydrolysis of the sn-2 ester bond of glycerophospholipids, complete protein sequence, existence of homologous enzymes, and ¢nding of active splice variants [1^4]. Group I, II, V, and X PLA 2 are closely related enzymes, which can be collectively termed secreted phospholipases (sPL), are characterized by a low molecular mass of 13^18 kDa, several disul¢de bonds, a requirement for millimolar amounts of Ca 2þ for catalytic activity, and a low selectivity for phospholipids with di¡erent polar heads and fatty acids. They share a common mechanism for cleaving the sn-2 ester bond of phospholipids, involving a catalytic histidine, but show a di¡erent pattern of expression among the di¡erent tissues. Thus, group IIE PLA 2 has been detected in human brain, lung and placenta [5]. Group V sPLA 2 is expressed in human heart and, less abundantly, in lung [6], and group X sPLA 2 is expressed in spleen, thymus and blood leukocytes [7].Group IIA PLA 2 (also known as in£ammatory PLA 2 , sPLA 2 -IIA) has been considered the main human element of the large family of sPLA 2 for several reasons: (i) its early characterization as a secreted enzyme from synovial £uid [8,9]; (ii) its broad expression pattern in human tissues as compared to other elements of group II enzymes [5]; (iii) the induction of its synthesis by endotoxin and cytokines via paracrine and/or autocrine processes during in£ammatory processes of clinical relevance, which have allowed the characterization of this enzyme as a newly recognized acute phase protein [10]; (iv) its potent bactericidal e¡ects, which support a role for this enzyme in the innate immunity against Staphylococcus aureus infection [11]. In this connection, studies intended to address the physiological relevance of sPLA 2 -IIA in vivo have shown that its concentration in plasma may reach V1 Wg/ml after injection of bacteria in experimental animals [12], thus agreeing with the range of concentrations which display antibacterial e¡ects in vitro [13,14].At present, there are several ¢elds where the functional relevance of sPLA 2 -IIA is a subject of activ...

show abstract

Group IIA and group V secretory phospholipase A2: quantitative analysis of expression and secretion and determination of the localization and routing in rat mesangial cells

Cited by 10 publications

References 32 publications

Identification of an autoantigen on the surface of apoptotic human T cells as a new protein interacting with inflammatory group IIA phospholipase A2

Identification of an autoantigen on the surface of apoptotic human T cells as a new protein interacting with inflammatory group IIA phospholipase A2

Groups IV, V, and X Phospholipases A2s in Human Neutrophils

Biological effects of group IIA secreted phosholipase A₂

Contact Info

Product

Resources

About

Group IIA and group V secretory phospholipase A2: quantitative analysis of expression and secretion and determination of the localization and routing in rat mesangial cells

Cited by 10 publications

References 32 publications

Identification of an autoantigen on the surface of apoptotic human T cells as a new protein interacting with inflammatory group IIA phospholipase A2

Identification of an autoantigen on the surface of apoptotic human T cells as a new protein interacting with inflammatory group IIA phospholipase A2

Groups IV, V, and X Phospholipases A2s in Human Neutrophils

Biological effects of group IIA secreted phosholipase A2

Contact Info

Product

Resources

About

Biological effects of group IIA secreted phosholipase A₂