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[PMID]:27293319
[Au] Autor:Silva CR; Biselli-Périco JM; Zampieri BL; Silva WA; de Souza JE; Bürger MC; Goloni-Bertollo EM; Pavarino ÉC
[Ad] Endereço:Unit of Research in Genetics and Molecular Biology (UPGEM), Department of Molecular Biology, Medical School of São José do Rio Preto (FAMERP), 15090-000 São José do Rio Preto, SP, Brazil.
[Ti] Título:Differential Expression of Inflammation-Related Genes in Children with Down Syndrome.
[So] Source:Mediators Inflamm;2016:6985903, 2016.
[Is] ISSN:1466-1861
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: The aim of the study was to investigate the expression patterns of a specific set of genes involved in the inflammation process in children with Down Syndrome (DS) and children without the syndrome (control group) to identify differences that may be related to the immune abnormalities observed in DS individuals. METHOD: RNA samples were obtained from peripheral blood, and gene expression was quantified using the TaqMan® Array Plate Human Inflammation Kit, which facilitated the investigation into 92 inflammation-related genes and four reference genes using real-time polymerase chain reaction (qPCR). RESULTS: Twenty genes showed differential expression in children with DS; 12 were overexpressed (PLA2G2D, CACNA1D, ALOX12, VCAM1, ICAM1, PLCD1, ADRB1, HTR3A, PDE4C, CASP1, PLA2G5, and PLCB4), and eight were underexpressed (LTA4H, BDKRB1, ADRB2, CD40LG, ITGAM, TNFRSF1B, ITGB1, and TBXAS1). After statistically correcting for the false discovery rate, only the genes BDKRB1 and LTA4H showed differential expression, and both were underexpressed within the DS group. CONCLUSION: DS children showed differential expression of inflammation-related genes that were not located on chromosome 21 compared with children without DS. The BDKRB1 and LTA4H genes may differentiate the case and control groups based on the inflammatory response, which plays an important role in DS pathogenesis.
[Mh] Termos MeSH primário: Síndrome de Down/genética
Inflamação/genética
[Mh] Termos MeSH secundário: Antígeno CD11b/genética
Canais de Cálcio Tipo L/genética
Caspase 1/genética
Criança
Pré-Escolar
Nucleotídeo Cíclico Fosfodiesterase do Tipo 4/genética
Síndrome de Down/imunologia
Feminino
Perfilação da Expressão Gênica
Fosfolipases A2 do Grupo II/genética
Fosfolipases A2 do Grupo V/genética
Seres Humanos
Inflamação/imunologia
Molécula 1 de Adesão Intercelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/genética
Masculino
Proteínas de Membrana/genética
Fosfolipase C beta/genética
Fosfolipase C delta/genética
Reação em Cadeia da Polimerase em Tempo Real
Receptores Adrenérgicos beta 1/genética
Receptores Adrenérgicos beta 2/genética
Receptores 5-HT3 de Serotonina/genética
Receptores Tipo II do Fator de Necrose Tumoral/genética
Proteínas Recombinantes de Fusão/genética
Molécula 1 de Adesão de Célula Vascular/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ADRB1 protein, human); 0 (ADRB2 protein, human); 0 (CACNA1D protein, human); 0 (CD11b Antigen); 0 (CD40Ig protein, recombinant); 0 (Calcium Channels, L-Type); 0 (HTR3A protein, human); 0 (ICAM1 protein, human); 0 (ITGAM protein, human); 0 (ITGB1BP1 protein, human); 0 (Intracellular Signaling Peptides and Proteins); 0 (Membrane Proteins); 0 (Receptors, Adrenergic, beta-1); 0 (Receptors, Adrenergic, beta-2); 0 (Receptors, Serotonin, 5-HT3); 0 (Receptors, Tumor Necrosis Factor, Type II); 0 (Recombinant Fusion Proteins); 0 (TNFRSF1B protein, human); 0 (Vascular Cell Adhesion Molecule-1); 126547-89-5 (Intercellular Adhesion Molecule-1); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.1.4 (Group V Phospholipases A2); EC 3.1.1.4 (PLA2G2D protein, human); EC 3.1.1.4 (PLA2G5 protein, human); EC 3.1.4.11 (PLCB4 protein, human); EC 3.1.4.11 (PLCD1 protein, human); EC 3.1.4.11 (Phospholipase C beta); EC 3.1.4.11 (Phospholipase C delta); EC 3.1.4.17 (Cyclic Nucleotide Phosphodiesterases, Type 4); EC 3.1.4.17 (PDE4C protein, human); EC 3.4.22.36 (Caspase 1)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160614
[St] Status:MEDLINE
[do] DOI:10.1155/2016/6985903


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[PMID]:26936936
[Au] Autor:Yamaguchi M; Zacharia J; Laidlaw TM; Balestrieri B
[Ad] Endereço:Department of Medicine, Harvard Medical School, Boston Massachusetts, USA; and the Jeff and Penny Vinik Center for Allergic Disease Research, Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Boston, Massachusetts, USA.
[Ti] Título:PLA2G5 regulates transglutaminase activity of human IL-4-activated M2 macrophages through PGE2 generation.
[So] Source:J Leukoc Biol;100(1):131-41, 2016 Jul.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phospholipases A2 are enzymes that liberate membrane-bound lipids in a tissue and cell-specific fashion. Group V secretory phospholipase A2 is necessary for the development of M2 macrophages and their effector functions in a mouse model of the T-helper-2 allergic airway inflammation. However, the function of group V phospholipase A2 in human M2 activation and T-helper-2 inflammation is ill-defined. Transglutaminase-2, a protein cross-linking enzyme, is a newly identified marker of both human and mouse interleukin-4-activated M2 macrophages and is also found in the lungs of patients with asthma. We report that group V phospholipase A2 and transglutaminase-2 colocalized in macrophages of human nasal polyp tissue obtained from patients with T-helper-2 eosinophilic inflammation, and their coexpression positively correlated with the number of eosinophils in each tissue specimen. We demonstrate that in human monocyte-derived macrophages activated by interleukin-4, group V phospholipase A2 translocated and colocalized with transglutaminase-2 in the cytoplasm and on the membrane of macrophages. Moreover, knocking down group V phospholipase A2 with small interfering ribonucleic acid reduced macrophage transglutaminase activity, whereas mass spectrometry analysis of lipids also showed reduced prostaglandin E2 production. Finally, exogenous prostaglandin E2 restored transglutaminase activity of group V phospholipase A2-small interfering ribonucleic acid-treated macrophages. Thus, our study shows a novel function of group V phospholipase A2 in regulating the transglutaminase activity of human interleukin-4-activated M2 macrophages through prostaglandin E2 generation and suggests that group V phospholipase A2 is a functionally relevant enzyme that may have therapeutic value for the treatment of human T-helper-2 inflammatory disorders.
[Mh] Termos MeSH primário: Dinoprostona/metabolismo
Fosfolipases A2 do Grupo V/metabolismo
Inflamação/patologia
Interleucina-4/farmacologia
Macrófagos/patologia
Pólipos Nasais/metabolismo
Transglutaminases/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Estudos de Casos e Controles
Células Cultivadas
Eosinófilos/imunologia
Eosinófilos/metabolismo
Eosinófilos/patologia
Seres Humanos
Inflamação/imunologia
Inflamação/metabolismo
Macrófagos/imunologia
Macrófagos/metabolismo
Meia-Idade
Pólipos Nasais/patologia
Adulto Jovem
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
207137-56-2 (Interleukin-4); EC 2.3.2.13 (Transglutaminases); EC 3.1.1.4 (Group V Phospholipases A2); EC 3.1.1.4 (PLA2G5 protein, human); K7Q1JQR04M (Dinoprostone)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160304
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.3A0815-372R


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[PMID]:26820468
[Au] Autor:Silva-Filho JL; Peruchetti DB; Moraes-Santos F; Landgraf SS; Silva LS; Sirtoli GM; Zamith-Miranda D; Takiya CM; Pinheiro AA; Diaz BL; Caruso-Neves C
[Ad] Endereço:Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
[Ti] Título:Group V Secretory Phospholipase A2 Is Involved in Tubular Integrity and Sodium Handling in the Kidney.
[So] Source:PLoS One;11(1):e0147785, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Group V (GV) phospholipase A2 (PLA2) is a member of the family of secreted PLA2 (sPLA2) enzymes. This enzyme has been identified in several organs, including the kidney. However, the physiologic role of GV sPLA2 in the maintenance of renal function remains unclear. We used mice lacking the gene encoding GV sPLA2 (Pla2g5-/-) and wild-type breeding pairs in the experiments. Mice were individually housed in metabolic cages and 48-h urine was collected for biochemical assays. Kidney samples were evaluated for glomerular morphology, renal fibrosis, and expression/activity of the (Na+ + K+)-ATPase α1 subunit. We observed that plasma creatinine levels were increased in Pla2g5-/- mice following by a decrease in creatinine clearance. The levels of urinary protein were higher in Pla2g5-/- mice than in the control group. Markers of tubular integrity and function such as γ-glutamyl transpeptidase, lactate dehydrogenase, and sodium excretion fraction (FENa+) were also increased in Pla2g5-/- mice. The increased FENa+ observed in Pla2g5-/- mice was correlated to alterations in cortical (Na+ + K+) ATPase activity/ expression. In addition, the kidney from Pla2g5-/- mice showed accumulation of matrix in corticomedullary glomeruli and tubulointerstitial fibrosis. These data suggest GV sPLA2 is involved in the maintenance of tubular cell function and integrity, promoting sodium retention through increased cortical (Na+ + K+)-ATPase expression and activity.
[Mh] Termos MeSH primário: Fosfolipases A2 do Grupo V/fisiologia
Túbulos Renais Distais/enzimologia
Rim/enzimologia
Sódio/metabolismo
[Mh] Termos MeSH secundário: Animais
Homeostase
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
ATPase Trocadora de Sódio-Potássio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
9NEZ333N27 (Sodium); EC 3.1.1.4 (Group V Phospholipases A2); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160129
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0147785


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[PMID]:26715269
[Au] Autor:Menschikowski M; Hagelgans A; Nacke B; Jandeck C; Mareninova OA; Asatryan L; Siegert G
[Ad] Endereço:Institute of Clinical Chemistry and Laboratory Medicine, Carl Gustav Carus University Hospital, Technical University of Dresden, Fetscherstr. 74, D-01307, Dresden, Germany. Mario.Menschikowski@uniklinikum-dresden.de.
[Ti] Título:Epigenetic control of group V phospholipase A2 expression in human malignant cells.
[So] Source:Tumour Biol;37(6):8097-105, 2016 Jun.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Secreted phospholipases A2 (sPLA2) are suggested to play an important role in inflammation and tumorigenesis. Different mechanisms of epigenetic regulation are involved in the control of group IIA, III and X sPLA2s expression in cancer cells, but group V sPLA2 (GV-PLA2) in this respect has not been studied. Here, we demonstrate the role of epigenetic mechanisms in regulation of GV-PLA2 expression in different cell lines originating from leukaemia and solid cancers. In blood leukocytes from leukaemic patients, levels of GV-PLA2 transcripts were significantly lower in comparison to those from healthy individuals. Similarly, in DU-145 and PC-3 prostate and CAL-51 and MCF-7 mammary cancer cell lines, levels of GV-PLA2 transcripts were significantly lower in relation to those found in normal epithelial cells of prostate or mammary. By sequencing and methylation-specific high-resolution melting (MS-HRM) analyses of bisulphite-modified DNA, distinct CpG sites in the GV-PLA2 promoter region were identified that were differentially methylated in cancer cells in comparison to normal epithelial and endothelial cells. Spearman rank order analysis revealed a significant negative correlation between the methylation degree and the cellular expression of GV-PLA2 (r = -0.697; p = 0.01). The effects of demethylating agent (5-aza-2'-deoxycytidine) and histone deacetylase inhibitor (trichostatin A) on GV-PLA2 transcription in the analysed cells confirmed the importance of DNA methylation and histone modification in the regulation of the GV-PLA2 gene expression in leukaemic, prostate and mammary cancer cell lines. The exposure of tumour cells to human recombinant GV-PLA2 resulted in a reduced colony forming activity of MCF-7, HepG2 and PC-3 cells, but not of DU-145 cells suggesting a cell-type-dependent effect of GV-PLA2 on cell growth. In conclusion, our results suggest that epigenetic mechanisms such as DNA methylation and histone modification play an important role in downregulation of GV-PLA2 expression in cancer cells.
[Mh] Termos MeSH primário: Metilação de DNA
Epigênese Genética
Regulação Neoplásica da Expressão Gênica
Fosfolipases A2 do Grupo V/genética
Neoplasias/genética
Neoplasias/patologia
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Proliferação Celular
Células Cultivadas
Seres Humanos
Regiões Promotoras Genéticas/genética
RNA Mensageiro/genética
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Sulfitos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Sulfites); EC 3.1.1.4 (Group V Phospholipases A2); EC 3.1.1.4 (PLA2G5 protein, human); OJ9787WBLU (hydrogen sulfite)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151231
[St] Status:MEDLINE
[do] DOI:10.1007/s13277-015-4670-x


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[PMID]:26711221
[Au] Autor:Pruzanski W; Kopilov J; Kuksis A
[Ad] Endereço:St. Michael's Hopital, Toronto, Canada; University of Toronto, Toronto, Canada. Electronic address: drwpruzanski@bellnet.ca.
[Ti] Título:Hydrolysis of lipoproteins by sPLA2's enhances mitogenesis and eicosanoid release from vascular smooth muscle cells: Diverse activity of sPLA2's IIA, V and X.
[So] Source:Prostaglandins Other Lipid Mediat;122:64-8, 2016 Jan.
[Is] ISSN:1098-8823
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitogenesis of Vascular Smooth Muscle Cells (VSMC) plays an important role in atherogenesis. Until recently, the effect of lipid subfractions has not been clarified. Secretory phospholipases A2 (sPLA2's) hydrolyse glycerophospholipids and release pro-inflammatory lyso-lipids, oxidized and non-oxidized fatty acids and isoprostanes. They localize in the vascular wall. We hypothesized that structurally similar sPLA2's may exert different impact on VSMC. The influence of sPLA2's, IIA, V, X, HDL, LDL, and hydrolysis products was tested on mitogenesis of VSMC, i.e., the early effect on the cell membrane phospholipids, and on PGE2 and LTB4 release, i.e., late effect of Cyclooxygenase and 5-lipooxygenase activity in VSMC. Mitogenesis was significantly enhanced by HDL and LDL, and by products of sPLA2 hydrolysis. Hydrolysis of HDL or LDL enhanced mitogenic activity in order V>X>IIA. The release of PGE2 was enhanced by group X sPLA2 and by HDL hydrolyzed by groups V and X. LDL and its hydrolysis products enhanced the release of PGE2 in order X>V>IIA. The release of LTB4 was markedly increased by LDL and HDL, and by hydrolytic products of group V and X, but not group IIA sPLA2. Our study demonstrates a diverse interaction of pro-inflammatory sPLA2's with HDL and LDL affecting both mitogenesis and eicosanoid release from VSMC, therefore potentially enhancing their pro-atherogenic activity.
[Mh] Termos MeSH primário: Eicosanoides/secreção
Lipoproteínas/metabolismo
Miócitos de Músculo Liso/metabolismo
Fosfolipases A2 Secretórias/metabolismo
[Mh] Termos MeSH secundário: Araquidonato 5-Lipoxigenase/metabolismo
Células Cultivadas
Dinoprostona/secreção
Fosfolipases A2 do Grupo II/metabolismo
Fosfolipases A2 do Grupo V/metabolismo
Fosfolipases A2 do Grupo X/metabolismo
Seres Humanos
Hidrólise
Leucotrieno B4/secreção
Lipoproteínas HDL/metabolismo
Lipoproteínas LDL/metabolismo
Mitose
Músculo Liso Vascular/citologia
Prostaglandina-Endoperóxido Sintases/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eicosanoids); 0 (Lipoproteins); 0 (Lipoproteins, HDL); 0 (Lipoproteins, LDL); 1HGW4DR56D (Leukotriene B4); EC 1.13.11.34 (Arachidonate 5-Lipoxygenase); EC 1.14.99.1 (Prostaglandin-Endoperoxide Synthases); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.1.4 (Group V Phospholipases A2); EC 3.1.1.4 (Group X Phospholipases A2); EC 3.1.1.4 (PLA2G2A protein, human); EC 3.1.1.4 (PLA2G5 protein, human); EC 3.1.1.4 (Phospholipases A2, Secretory); K7Q1JQR04M (Dinoprostone)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151230
[St] Status:MEDLINE


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[PMID]:25725101
[Au] Autor:Rubio JM; Rodríguez JP; Gil-de-Gómez L; Guijas C; Balboa MA; Balsinde J
[Ad] Endereço:Instituto de Biología y Genética Molecular, Consejo Superior de Investigaciones Científicas, Universidad de Valladolid, 47003 Valladolid, Spain; Centro de Investigación Biomédica en Red de Diabetes y Enfermedades Metabólicas Asociadas, 28029 Madrid, Spain; and.
[Ti] Título:Group V secreted phospholipase A2 is upregulated by IL-4 in human macrophages and mediates phagocytosis via hydrolysis of ethanolamine phospholipids.
[So] Source:J Immunol;194(7):3327-39, 2015 Apr 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Studies on the heterogeneity and plasticity of macrophage populations led to the identification of two major polarization states: classically activated macrophages or M1, induced by IFN-γ plus LPS, and alternatively activated macrophages, induced by IL-4. We studied the expression of multiple phospholipase A2 enzymes in human macrophages and the effect that polarization of the cells has on their levels. At least 11 phospholipase A2 genes were found at significant levels in human macrophages, as detected by quantitative PCR. None of these exhibited marked changes after treating the cells with IFN-γ plus LPS. However, macrophage treatment with IL-4 led to strong upregulation of the secreted group V phospholipase A2 (sPLA2-V), both at the mRNA and protein levels. In parallel with increasing sPLA2-V expression levels, IL-4-treated macrophages exhibited increased phagocytosis of yeast-derived zymosan and bacteria, and we show that both events are causally related, because cells deficient in sPLA2-V exhibited decreased phagocytosis, and cells overexpressing the enzyme manifested higher rates of phagocytosis. Mass spectrometry analyses of lipid changes in the IL-4-treated macrophages suggest that ethanolamine lysophospholipid (LPE) is an sPLA2-V-derived product that may be involved in regulating phagocytosis. Cellular levels of LPE are selectively maintained by sPLA2-V. By supplementing sPLA2-V-deficient cells with LPE, phagocytosis of zymosan or bacteria was fully restored in IL-4-treated cells. Collectively, our results show that sPLA2-V is required for efficient phagocytosis by IL-4-treated human macrophages and provide evidence that sPLA2-V-derived LPE is involved in the process.
[Mh] Termos MeSH primário: Fosfolipases A2 do Grupo V/genética
Interleucina-4/metabolismo
Macrófagos/imunologia
Macrófagos/metabolismo
Fagocitose/genética
Fagocitose/imunologia
Fosfatidiletanolaminas/metabolismo
[Mh] Termos MeSH secundário: Regulação da Expressão Gênica/efeitos dos fármacos
Fosfolipases A2 do Grupo V/deficiência
Fosfolipases A2 do Grupo V/metabolismo
Voluntários Saudáveis
Seres Humanos
Hidrólise
Interleucina-4/farmacologia
Isoenzimas
Metabolismo dos Lipídeos
Macrófagos/efeitos dos fármacos
Masculino
Fagocitose/efeitos dos fármacos
Fosfatidiletanolaminas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Phosphatidylethanolamines); 207137-56-2 (Interleukin-4); EC 3.1.1.4 (Group V Phospholipases A2)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:150321
[Lr] Data última revisão:
150321
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:150301
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1401026


  7 / 100 MEDLINE  
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[PMID]:25716287
[Au] Autor:Nakamura H; Wakita S; Yasufuku K; Makiyama T; Waraya M; Hashimoto N; Murayama T
[Ad] Endereço:Laboratory of Chemical Pharmacology, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, 260-8675, Japan.
[Ti] Título:Sphingomyelin Regulates the Activity of Secretory Phospholipase A2 in the Plasma Membrane.
[So] Source:J Cell Biochem;116(9):1898-907, 2015 Sep.
[Is] ISSN:1097-4644
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We examined the effect of the cellular sphingolipid level on the release of arachidonic acid (AA) and the activity of secretory phospholipase A2 (sPLA2 ) using two Chinese hamster ovary (CHO)-K1 cell mutants, LY-B and LY-A cells, deficient in sphingolipid synthesis. In LY-B cells, deficiency of sphingolipids enhanced the release of AA induced by bee venom sPLA2-III or human sPLA2-V. These alterations were reversed by replenishment of exogenous sphingomyelin (SM). In LY-A cells, deficiency of SM increased the release of AA induced by sPLA2. In CHO-K1 cells, decrease and increase of SM level in the plasma membrane by pharmacological methods increased and inhibited the release of AA, respectively. SM inhibited the activity of sPLA2 in vitro. Niemann-Pick disease type C (NPC) is a lysosomal storage disorder caused by mutation of either the NPC1 or NPC2 gene, and is characterized by accumulation of cholesterol and sphingolipids including SM in late endosomes/lysosomes. Increased levels of AA and sPLA2 activity are involved in various neurodegenerative diseases. In CHO cells lacking NPC1 (A101 cells), SM level was lower in the plasma membrane, while it was higher in late endosomes/lysosomes. The release of AA induced by sPLA2 was increased in A101 cells than that in parental cells (JP17 cells), which was attenuated by adding exogenous SM. In addition, sPLA2 -III-induced cytotoxicity in A101 cells was much higher than that in JP17 cells. These results suggest that SM in the plasma membrane plays important roles in regulating sPLA2 activity and the enzyme-induced cytotoxicity in A101 cells.
[Mh] Termos MeSH primário: Ácido Araquidônico/biossíntese
Membrana Celular/metabolismo
Doença de Niemann-Pick Tipo C/enzimologia
Fosfolipases A2 Secretórias/metabolismo
Esfingomielinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Células CHO
Cricetinae
Cricetulus
Fosfolipases A2 do Grupo III/metabolismo
Fosfolipases A2 do Grupo III/farmacologia
Fosfolipases A2 do Grupo V/metabolismo
Fosfolipases A2 do Grupo V/farmacologia
Seres Humanos
Glicoproteínas de Membrana/deficiência
Modelos Biológicos
Fosfolipases A2 Secretórias/farmacologia
Esfingomielinas/deficiência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Glycoproteins); 0 (Sphingomyelins); 27YG812J1I (Arachidonic Acid); EC 3.1.1.4 (Group III Phospholipases A2); EC 3.1.1.4 (Group V Phospholipases A2); EC 3.1.1.4 (PLA2G5 protein, human); EC 3.1.1.4 (Phospholipases A2, Secretory)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:150724
[Lr] Data última revisão:
150724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150227
[St] Status:MEDLINE
[do] DOI:10.1002/jcb.25145


  8 / 100 MEDLINE  
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[PMID]:25549071
[Au] Autor:Bin NJ; Heng HM; Poh R; Noor SM; Subrayan V
[Ad] Endereço:*Department of Biomedical Science, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia; and †Department of Ophthalmology, University Malaya Medical Center, Kuala Lumpur, Malaysia.
[Ti] Título:Phospholipase A2 group v in benign familial fleck retina in a set of triplets.
[So] Source:Retina;35(6):1266-72, 2015 Jun.
[Is] ISSN:1539-2864
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To evaluate the association of phospholipase A2, Group V (PLA2G5), with benign familial fleck retina in a consanguineous family with triplets. METHODS: Clinical eye examination, including fundus examination and spectral domain optical coherence tomography, was performed for all the family members. After blood sample collection and DNA extraction, polymerase chain reaction was performed to amplify regions spanning Exons 2, 3, 4, and 5 of PLA2G5. The amplified products were sequenced to observe the presence of any mutations. RESULTS: Fundus examination in two of the triplets revealed discrete yellow-white flecks and both had good vision and absence of night blindness, consistent with benign familial fleck retina. The flecks were hyperautofluorescent. Furthermore, spectral domain optical coherence tomography showed focal thickening of the retinal pigment epithelium because of the presence of these flecks. Molecular investigations showed that PLA2G5 Exons 2, 4, and 5 harbored no misalignments among all family members. However, PLA2G5 Exon 3 showed a p.Gly45Cys mutation for the father and the third triplet who was affected. CONCLUSION: The clinical findings in this family suggest a diagnosis of benign familial fleck retina with excellent prognosis, in which the PLA2G5 gene may play a role.
[Mh] Termos MeSH primário: Oftalmopatias Hereditárias/genética
Fosfolipases A2 do Grupo V/genética
Mutação Puntual
Doenças Retinianas/genética
Trigêmeos/genética
[Mh] Termos MeSH secundário: Adulto
Pareamento Incorreto de Bases
Criança
Consanguinidade
Eletrorretinografia
Éxons/genética
Oftalmopatias Hereditárias/diagnóstico
Seres Humanos
Masculino
Linhagem
Reação em Cadeia da Polimerase
Doenças Retinianas/diagnóstico
Tomografia de Coerência Óptica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.1.1.4 (Group V Phospholipases A2); EC 3.1.1.4 (PLA2G5 protein, human)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:150603
[Lr] Data última revisão:
150603
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141231
[St] Status:MEDLINE
[do] DOI:10.1097/IAE.0000000000000446


  9 / 100 MEDLINE  
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[PMID]:25224632
[Au] Autor:Vijaya Mohan Rao L
[Ad] Endereço:Department of Cellular and Molecular Biology, The University of Texas Health Science Center at Tyler, Tyler, TX, USA.
[Ti] Título:Secretory group V phospholipase A2 : a new player in thrombosis?
[So] Source:J Thromb Haemost;12(11):1918-20, 2014 Nov.
[Is] ISSN:1538-7836
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Estenose das Carótidas/enzimologia
Fosfolipases A2 do Grupo V/biossíntese
Fígado/enzimologia
Proteína C/metabolismo
Receptores de Superfície Celular/metabolismo
Trombose/enzimologia
[Mh] Termos MeSH secundário: Animais
Receptor de Proteína C Endotelial
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Endothelial Protein C Receptor); 0 (Procr protein, mouse); 0 (Protein C); 0 (Receptors, Cell Surface); EC 3.1.1.4 (Group V Phospholipases A2); EC 3.1.1.4 (PLA2G5 protein, human)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140917
[St] Status:MEDLINE
[do] DOI:10.1111/jth.12729


  10 / 100 MEDLINE  
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[PMID]:25132377
[Au] Autor:Suzuki K; Takahashi S; Watanabe K; Fujioka D; Nakamura T; Obata JE; Kawabata K; Katoh R; Matsumoto M; Kugiyama K
[Ad] Endereço:Department of Internal Medicine II, University of Yamanashi, Faculty of Medicine.
[Ti] Título:The expression of groups IIE and V phospholipase A2 is associated with an increased expression of osteogenic molecules in human calcified aortic valves.
[So] Source:J Atheroscler Thromb;21(12):1308-25, 2014.
[Is] ISSN:1880-3873
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:AIM: Eicosanoids play various pathogenic roles in aortic valve calcification. Eicosanoids are derived from the arachidonic acid generated by phospholipase A2 (PLA2). We therefore sought to determine whether PLA2s are expressed in human aortic valves and, if so, whether the expression of PLA2s is related to the expression of osteogenic molecules in these tissues. METHODS: Histological and gene expression analyses of 38 non-rheumatic aortic valves obtained at the time of cardiac valve replacement surgery were conducted. Moreover, gene expression analyses were performed using valve interstitial cells (VICs) obtained from human aortic valves. RESULTS: Among the PLA2s examined, the degree of immunoreactivity for PLA2s-IIE and -V was found to significantly correlate with the grade of calcification in the aortic valves. The degree of immunoreactivity and gene expression levels of PLA2s-IIE and -V significantly correlated with those of bone morphogenetic protein (BMP)-2, osteopontin and alkaline phosphatase (ALP). In addition, immunoreactivity for cyclooxygenase (COX)-1, COX-2 and 5-lipoxygenase, downstream enzymes of PLA2 in the arachidonic acid cascade, was co-localized with that for PLA2s-IIE and -V in cells expressing α-smooth muscle actin and macrophages expressing CD68. Furthermore, in the in vitro experiments using cultured VICs, the mRNA expression levels of BMP-2, osteopontin and ALP were suppressed by the inhibition of the expression of PLA2s-IIE or -V with specific siRNAs. CONCLUSIONS: The expression of PLA2s-IIE and -V correlates with the development of calcification as well as the expression of pro-osteogenic molecules in human aortic valves, and inhibiting the expression of PLA2s-IIE and -V suppresses the induction of osteogenic molecules in cultured cells. Therefore, PLA2s-IIE and -V may play a role in the pathogenesis of valve calcification.
[Mh] Termos MeSH primário: Estenose da Valva Aórtica/metabolismo
Valva Aórtica/patologia
Calcinose/metabolismo
Regulação Enzimológica da Expressão Gênica
Fosfolipases A2 do Grupo II/metabolismo
Fosfolipases A2 do Grupo V/metabolismo
[Mh] Termos MeSH secundário: Idoso
Antígenos CD/metabolismo
Antígenos de Diferenciação Mielomonocítica/metabolismo
Valva Aórtica/metabolismo
Araquidonato 5-Lipoxigenase/metabolismo
Índice de Massa Corporal
LDL-Colesterol/metabolismo
Ciclo-Oxigenase 1/metabolismo
Ciclo-Oxigenase 2/metabolismo
Feminino
Perfilação da Expressão Gênica
Seres Humanos
Imuno-Histoquímica
Masculino
Microscopia de Fluorescência
Meia-Idade
Osteogênese
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/metabolismo
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Antigens, Differentiation, Myelomonocytic); 0 (CD68 antigen, human); 0 (Cholesterol, LDL); 0 (RNA, Messenger); 0 (RNA, Small Interfering); EC 1.13.11.34 (Arachidonate 5-Lipoxygenase); EC 1.14.99.1 (Cyclooxygenase 1); EC 1.14.99.1 (Cyclooxygenase 2); EC 1.14.99.1 (PTGS1 protein, human); EC 1.14.99.1 (PTGS2 protein, human); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.1.4 (Group V Phospholipases A2); EC 3.1.1.4 (PLA2G5 protein, human)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:141218
[Lr] Data última revisão:
141218
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140819
[St] Status:MEDLINE



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