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[PMID]:28888983
[Au] Autor:Moncada RM; Blackshear KJ; Garrett TA
[Ad] Endereço:Department of Chemistry, Vassar College, 124 Raymond Avenue, Poughkeepsie, NY 12604, United States.
[Ti] Título:The Arabidopsis thaliana lysophospholipid acyltransferase At1g78690p acylates lysocardiolipins.
[So] Source:Biochem Biophys Res Commun;493(1):340-345, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Arabidopsis thaliana lysophospholipid acyltransferase At1g78690 acylates a variety of lysophospholipids such as lyso phosphatidylglycerol, lyso phosphatidylethanolamine and lyso phosphatidylserine. Despite di-acylate phosphatidylglycerol being a substrate, overexpression of At1g78690 in Escherichia coli leads to the accumulation of acyl-PG. Here we show that cardiolipin also accumulates in cells overexpressing At1g78690. To help try and explain this observation, we show, using a liquid chromatography mass spectrometry (LC-MS) based assay, that At1g78690 utilizes both mono- and di-lyso cardiolipin as an acyl acceptor. Because At1g78690 shares high homology (∼40%) with the cardiolipin remodeling enzyme tafazzin, we also tested whether At1g78690 was able to catalyze a tafazzin-like transacylation reaction. Di-linoleoyl phosphatidylcholine was used as the acyl donor and mono-lyso cardiolipin was used as the acyl acceptor in a reaction and the reaction was monitored by LC-MS. No transfer of the linoleoyl chains was detected in an At1g78690 dependent manner suggesting that, despite the strong homology, these enzymes catalyze unique reactions.
[Mh] Termos MeSH primário: 1-Acilglicerofosfocolina O-Aciltransferase/química
1-Acilglicerofosfocolina O-Aciltransferase/metabolismo
Arabidopsis/enzimologia
Cardiolipinas/química
Cardiolipinas/metabolismo
[Mh] Termos MeSH secundário: Acilação
Proteínas de Arabidopsis/química
Proteínas de Arabidopsis/metabolismo
Sítios de Ligação
Ativação Enzimática
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Cardiolipins); EC 2.3.1.23 (1-Acylglycerophosphocholine O-Acyltransferase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170911
[St] Status:MEDLINE


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[PMID]:28846071
[Au] Autor:Rong X; Wang B; Palladino EN; de Aguiar Vallim TQ; Ford DA; Tontonoz P
[Ad] Endereço:Department of Pathology and Laboratory Medicine, Department of Medicine, UCLA, Los Angeles, California, USA.
[Ti] Título:ER phospholipid composition modulates lipogenesis during feeding and in obesity.
[So] Source:J Clin Invest;127(10):3640-3651, 2017 Oct 02.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sterol regulatory element-binding protein 1c (SREBP-1c) is a central regulator of lipogenesis whose activity is controlled by proteolytic cleavage. The metabolic factors that affect its processing are incompletely understood. Here, we show that dynamic changes in the acyl chain composition of ER phospholipids affect SREBP-1c maturation in physiology and disease. The abundance of polyunsaturated phosphatidylcholine in liver ER is selectively increased in response to feeding and in the setting of obesity-linked insulin resistance. Exogenous delivery of polyunsaturated phosphatidylcholine to ER accelerated SREBP-1c processing through a mechanism that required an intact SREBP cleavage-activating protein (SCAP) pathway. Furthermore, induction of the phospholipid-remodeling enzyme LPCAT3 in response to liver X receptor (LXR) activation promoted SREBP-1c processing by driving the incorporation of polyunsaturated fatty acids into ER. Conversely, LPCAT3 deficiency increased membrane saturation, reduced nuclear SREBP-1c abundance, and blunted the lipogenic response to feeding, LXR agonist treatment, or obesity-linked insulin resistance. Desaturation of the ER membrane may serve as an auxiliary signal of the fed state that promotes lipid synthesis in response to nutrient availability.
[Mh] Termos MeSH primário: Retículo Endoplasmático/metabolismo
Resistência à Insulina
Lipogênese
Obesidade/metabolismo
Fosfolipídeos/metabolismo
[Mh] Termos MeSH secundário: 1-Acilglicerofosfocolina O-Aciltransferase/genética
1-Acilglicerofosfocolina O-Aciltransferase/metabolismo
Animais
Retículo Endoplasmático/genética
Retículo Endoplasmático/patologia
Peptídeos e Proteínas de Sinalização Intracelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Receptores X do Fígado/genética
Receptores X do Fígado/metabolismo
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Camundongos
Camundongos Transgênicos
Obesidade/genética
Obesidade/patologia
Fosfolipídeos/genética
Proteína de Ligação a Elemento Regulador de Esterol 1/genética
Proteína de Ligação a Elemento Regulador de Esterol 1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (Liver X Receptors); 0 (Membrane Proteins); 0 (Phospholipids); 0 (SREBP cleavage-activating protein); 0 (Srebf1 protein, mouse); 0 (Sterol Regulatory Element Binding Protein 1); EC 2.3.1.23 (1-Acylglycerophosphocholine O-Acyltransferase); EC 2.3.1.23 (LPCAT3 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE


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[PMID]:28683445
[Au] Autor:Tanaka H; Zaima N; Sasaki T; Yamamoto N; Inuzuka K; Yata T; Iwaki T; Umemura K; Sano H; Suzuki Y; Urano T; Setou M; Unno N
[Ad] Endereço:Division of Vascular Surgery, Hamamatsu University School of Medicine, Hamamatsu, Japan.
[Ti] Título:Lysophosphatidylcholine Acyltransferase-3 Expression Is Associated with Atherosclerosis Progression.
[So] Source:J Vasc Res;54(4):200-208, 2017.
[Is] ISSN:1423-0135
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Free arachidonic acid (AA) is an important precursor of lipid mediators such as leukotrienes and prostaglandins that induces inflammation and is associated with atherosclerosis progression. Recent studies have shown that lysophosphatidylcholine acyltransferase-3 (LPCAT3) converts lysophosphatidylcholine (LPC) and free AA into phosphatidylcholine (PC)-containing AA (arachidonyl-PC) and thereby can regulate intracellular free-AA levels. However, the association between LPCAT3 and atherosclerosis remains to be established. In this study, we analyzed human and mouse atherosclerotic tissues to gain insight into the arachidonyl-PC metabolism involving LPCAT3 using imaging mass spectrometry. The data revealed a complementary distribution of arachidonyl-PC and LPC in human atherosclerotic tissues with arachidonyl-PC decreasing and LPC increasing as atherosclerosis progressed. Furthermore, we found a homologous distribution of LPCAT3 expression and arachidonyl-PC based on atherosclerotic progression. In contrast, in ApoE-deficient mice, atherosclerosis increased both arachidonyl-PC accumulation and LPCAT3 expression. Taken together, these findings suggest that the regulation of LPCAT3 expression might be associated with atherosclerotic progression in humans.
[Mh] Termos MeSH primário: 1-Acilglicerofosfocolina O-Aciltransferase/metabolismo
Aterosclerose/enzimologia
Músculo Liso Vascular/enzimologia
Miócitos de Músculo Liso/enzimologia
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Animais
Apolipoproteínas E/deficiência
Apolipoproteínas E/genética
Ácido Araquidônico/metabolismo
Artérias/enzimologia
Artérias/patologia
Aterosclerose/genética
Aterosclerose/patologia
Modelos Animais de Doenças
Progressão da Doença
Feminino
Seres Humanos
Lisofosfatidilcolinas/metabolismo
Masculino
Camundongos Endogâmicos BALB C
Camundongos Knockout
Meia-Idade
Músculo Liso Vascular/patologia
Miócitos de Músculo Liso/patologia
Fosfatidilcolinas/metabolismo
Placa Aterosclerótica
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoproteins E); 0 (Lysophosphatidylcholines); 0 (Phosphatidylcholines); 27YG812J1I (Arachidonic Acid); EC 2.3.1.23 (1-Acylglycerophosphocholine O-Acyltransferase); EC 2.3.1.23 (LPCAT3 protein, human); EC 2.3.1.23 (LPCAT3 protein, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170707
[St] Status:MEDLINE
[do] DOI:10.1159/000473879


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[PMID]:28341636
[Au] Autor:Shindou H; Shiraishi S; Tokuoka SM; Takahashi Y; Harayama T; Abe T; Bando K; Miyano K; Kita Y; Uezono Y; Shimizu T
[Ad] Endereço:Department of Lipid Signaling, National Center for Global Health and Medicine, Tokyo, Japan; hshindou-tky@umin.net.
[Ti] Título:Relief from neuropathic pain by blocking of the platelet-activating factor-pain loop.
[So] Source:FASEB J;31(7):2973-2980, 2017 Jul.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neuropathic pain resulting from peripheral neuronal damage is largely resistant to treatment with currently available analgesic drugs. Recently, ATP, lysophosphatidic acid, and platelet-activating factor (PAF) have been reported to play important inductive roles in neuropathic pain. In the present study, we found that pain-like behaviors resulting from partial sciatic nerve ligation (PSL) were largely attenuated by deficiency of lysophosphatidylcholine acyltransferase (LPCAT)2, which is one of the PAF biosynthetic enzymes. By contrast, deficiency of the other PAF biosynthetic enzyme, LPCAT1, did not ameliorate neuropathic pain. With regard to the mechanism of the observed effects, LPCAT2 was detected in wild-type spinal cord microglia, and the absence of LPCAT2 expression precluded spinal PAF expression in LPCAT2-knockout mice. Furthermore, ATP-stimulated PAF biosynthesis in macrophages was decreased by pretreatment with the PAF receptor antagonist ABT-491, indicating the existence of a positive feedback loop of PAF biosynthesis, which we designated the PAF-pain loop. In conclusion, LPCAT2 is a novel therapeutic target for newly categorized analgesic drugs; in addition, our data call for the re-evaluation of the clinical utility of PAF receptor antagonists.-Shindou, H., Shiraishi, S., Tokuoka, S. M., Takahashi Y., Harayama, T., Abe, T., Bando, K., Miyano, K., Kita, Y., Uezono, Y., Shimizu, T. Relief from neuropathic pain by blocking of the platelet-activating factor-pain loop.
[Mh] Termos MeSH primário: 1-Acilglicerofosfocolina O-Aciltransferase/metabolismo
Neuralgia/tratamento farmacológico
Fator de Ativação de Plaquetas/metabolismo
[Mh] Termos MeSH secundário: 1-Acilglicerofosfocolina O-Aciltransferase/genética
Animais
Regulação da Expressão Gênica/fisiologia
Hiperalgesia
Camundongos
Camundongos Knockout
Microglia
Fator de Ativação de Plaquetas/genética
Corno Dorsal da Medula Espinal/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Platelet Activating Factor); EC 2.3.1.23 (1-Acylglycerophosphocholine O-Acyltransferase); EC 2.3.1.23 (LPCAT2 protein, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170326
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601183R


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[PMID]:27932289
[Au] Autor:Fisher AB
[Ad] Endereço:Institute for Environmental Medicine of the Department of Physiology, University of Pennsylvania, 3620 Hamilton Walk, 1 John Morgan Building, Philadelphia, PA, United States. Electronic address: abf@upenn.edu.
[Ti] Título:Peroxiredoxin 6 in the repair of peroxidized cell membranes and cell signaling.
[So] Source:Arch Biochem Biophys;617:68-83, 2017 Mar 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Peroxiredoxin 6 represents a widely distributed group of peroxiredoxins that contain a single conserved cysteine in the protein monomer (1-cys Prdx). The cys when oxidized to the sulfenic form is reduced with glutathione (GSH) catalyzed by the π isoform of GSH-S-transferase. Three enzymatic activities of the protein have been described:1) peroxidase with H O , short chain hydroperoxides, and phospholipid hydroperoxides as substrates; 2) phospholipase A (PLA ); and 3) lysophosphatidylcholine acyl transferase (LPCAT). These activities have important physiological roles in antioxidant defense, turnover of cellular phospholipids, and the generation of superoxide anion via initiation of the signaling cascade for activation of NADPH oxidase (type 2). The ability of Prdx6 to reduce peroxidized cell membrane phospholipids (peroxidase activity) and also to replace the oxidized sn-2 fatty acyl group through hydrolysis/reacylation (PLA and LPCAT activities) provides a complete system for the repair of peroxidized cell membranes.
[Mh] Termos MeSH primário: Peróxido de Hidrogênio/química
Peroxirredoxina VI/química
[Mh] Termos MeSH secundário: 1-Acilglicerofosfocolina O-Aciltransferase/metabolismo
Animais
Catálise
Membrana Celular/química
Dimerização
Glutationa/química
Glutationa Transferase/metabolismo
Seres Humanos
Hidrólise
Camundongos
Camundongos Transgênicos
NADP/química
Estresse Oxidativo
Fosfolipases A2/metabolismo
Fosforilação
Ratos
Proteínas Recombinantes/metabolismo
Transdução de Sinais
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Recombinant Proteins); 53-59-8 (NADP); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.15 (Peroxiredoxin VI); EC 2.3.1.23 (1-Acylglycerophosphocholine O-Acyltransferase); EC 2.5.1.18 (Glutathione Transferase); EC 3.1.1.4 (Phospholipases A2); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161210
[St] Status:MEDLINE


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[PMID]:27913621
[Au] Autor:Singh AB; Liu J
[Ad] Endereço:From the Department of Veterans Affairs Palo Alto Health Care System, Palo Alto, California 94304.
[Ti] Título:Identification of Hepatic Lysophosphatidylcholine Acyltransferase 3 as a Novel Target Gene Regulated by Peroxisome Proliferator-activated Receptor δ.
[So] Source:J Biol Chem;292(3):884-897, 2017 Jan 20.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Peroxisome proliferator-activated receptor δ (PPARδ) regulates many genes involved in lipid metabolism. Hepatic lysophosphatidylcholine acyltransferase 3 (LPCAT3) has critical functions in triglycerides transport and endoplasmic reticulum stress response due to its unique ability to catalyze the incorporation of polyunsaturated fatty acids into phospholipids. Previous studies identified liver X receptor as the transcription factor controlling LPCAT3 expression in mouse liver tissue. Here we show that the hepatic LPCAT3 gene is transcriptionally regulated by PPARδ. Adenovirus-mediated knockdown of PPARδ in cultured hepatic cells and liver tissue reduced LPCAT3 mRNA levels, and exogenous overexpression of PPARδ increased LPCAT3 mRNA expression. Activation of PPARδ in HepG2, Huh7, and Hepa 1-6 cells with its specific agonists increased LPCAT3 mRNA levels in all three hepatic cell lines. Through conducting sequence analysis, LPCAT3 promoter assays, and direct DNA binding assays, we have mapped the functional PPAR-responsive element to a proximal region from -135 to -123 of the LPCAT3 promoter that plays an essential role in mediating PPARδ-induced transactivation of the LPCAT3 gene. Finally, we have provided in vivo evidence showing that activation of PPARδ by agonist L165041 in mice increased hepatic LPCAT3 mRNA abundance and LPCAT enzymatic activity, which is associated with increased incorporations of arachidonate into liver phosphatidylcholine and phosphatidylethanolamine. Furthermore, transient liver-specific knockdown of LPCAT3 in mice affected PPARδ-mediated activation of several hepatic genes involving in FA metabolism. Altogether, our new findings identify LPCAT3 as a direct PPARδ target gene and suggest a novel function of PPARδ in regulation of phospholipid metabolism through LPCAT3.
[Mh] Termos MeSH primário: 1-Acilglicerofosfocolina O-Aciltransferase/metabolismo
Fígado/metabolismo
PPAR delta/metabolismo
Fosfolipídeos/metabolismo
Regiões Promotoras Genéticas/fisiologia
[Mh] Termos MeSH secundário: 1-Acilglicerofosfocolina O-Aciltransferase/genética
Animais
Ácidos Graxos/genética
Ácidos Graxos/metabolismo
Células Hep G2
Seres Humanos
Camundongos
PPAR delta/agonistas
PPAR delta/genética
Fenoxiacetatos/farmacologia
Fosfolipídeos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-(3-(2-propyl-3-hydroxy-4-acetyl)phenoxy)propyloxyphenoxy acetic acid); 0 (Fatty Acids); 0 (PPAR delta); 0 (Phenoxyacetates); 0 (Phospholipids); EC 2.3.1.23 (1-Acylglycerophosphocholine O-Acyltransferase); EC 2.3.1.23 (LPCAT3 protein, human); EC 2.3.1.23 (LPCAT3 protein, mouse)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161204
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.743575


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[PMID]:27706605
[Au] Autor:Sousa CS; Barros BA; Barh D; Ghosh P; Azevedo V; Barros EG; Moreira MA
[Ad] Endereço:Departamento de Bioquímica e Biologia Molecular - BIOAGRO, Universidade Federal de Viçosa, Viçosa, MG, Brasil cassissousa@gmail.com.
[Ti] Título:In silico characterization of 1,2-diacylglycerol cholinephosphotransferase and lysophospha-tidylcholine acyltransferase genes in Glycine max L. Merrill.
[So] Source:Genet Mol Res;15(3), 2016 Aug 26.
[Is] ISSN:1676-5680
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:The enzymes 1,2-diacylglycerol cholinephosphotrans-ferase (CPT) and lysophosphatidylcholine acyltransferase (LPCAT) are important in lipid metabolism in soybean seeds. Thus, understand-ing the genes that encode these enzymes may enable their modification and aid the improvement of soybean oil quality. In soybean, the genes encoding these enzymes have not been completely described; there-fore, this study aimed to identify, characterize, and analyze the in silico expression of these genes in soybean. We identified two gene models encoding CPT and two gene models encoding LPCAT, one of which presented an alternative transcript. The sequences were positioned on the physical map of soybean and the promoter regions were analyzed. Cis-elements responsible for seed-specific expression and responses to biotic and abiotic stresses were identified. Virtual expression analysis of the gene models for CPT and LPCAT indicated that these genes are expressed under different stress conditions, in somatic embryos during differentiation, in immature seeds, root tissues, and calli. Putative ami-no acid sequences revealed the presence of transmembrane domains, and analysis of the cellular localization of these enzymes revealed they are located in the endoplasmic reticulum.
[Mh] Termos MeSH primário: 1-Acilglicerofosfocolina O-Aciltransferase/genética
Diacilglicerol Colinofosfotransferase/genética
Retículo Endoplasmático/enzimologia
Proteínas de Plantas/genética
Feijão de Soja/genética
[Mh] Termos MeSH secundário: 1-Acilglicerofosfocolina O-Aciltransferase/química
1-Acilglicerofosfocolina O-Aciltransferase/metabolismo
Processamento Alternativo
Sequência de Aminoácidos
Simulação por Computador
Diacilglicerol Colinofosfotransferase/química
Diacilglicerol Colinofosfotransferase/metabolismo
Retículo Endoplasmático/química
Retículo Endoplasmático/ultraestrutura
Expressão Gênica
Metabolismo dos Lipídeos/genética
Modelos Genéticos
Mapeamento Físico do Cromossomo
Células Vegetais/enzimologia
Células Vegetais/ultraestrutura
Proteínas de Plantas/química
Proteínas de Plantas/metabolismo
Raízes de Plantas/citologia
Raízes de Plantas/enzimologia
Regiões Promotoras Genéticas
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Sementes/citologia
Sementes/enzimologia
Alinhamento de Sequência
Feijão de Soja/citologia
Feijão de Soja/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (RNA, Messenger); EC 2.3.1.23 (1-Acylglycerophosphocholine O-Acyltransferase); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161006
[St] Status:MEDLINE
[do] DOI:10.4238/gmr.15038974


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[PMID]:27268057
[Au] Autor:Abe M; Hasegawa Y; Oku M; Sawada Y; Tanaka E; Sakai Y; Miyoshi H
[Ad] Endereço:From the Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
[Ti] Título:Mechanism for Remodeling of the Acyl Chain Composition of Cardiolipin Catalyzed by Saccharomyces cerevisiae Tafazzin.
[So] Source:J Biol Chem;291(30):15491-502, 2016 07 22.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Remodeling of the acyl chains of cardiolipin (CL) is responsible for final molecular composition of mature CL after de novo CL synthesis in mitochondria. Yeast Saccharomyces cerevisiae undergoes tafazzin-mediated CL remodeling, in which tafazzin serves as a transacylase from phospholipids to monolyso-CL (MLCL). In light of the diversity of the acyl compositions of mature CL between different organisms, the mechanism underlying tafazzin-mediated transacylation remains to be elucidated. We investigated the mechanism responsible for transacylation using purified S. cerevisiae tafazzin with liposomes composed of various sets of acyl donors and acceptors. The results revealed that tafazzin efficiently catalyzes transacylation in liposomal membranes with highly ordered lipid bilayer structure. Tafazzin elicited unique acyl chain specificity against phosphatidylcholine (PC) as follows: linoleoyl (18:2) > oleoyl (18:1) = palmitoleoyl (16:1) ≫ palmitoyl (16:0). In these reactions, tafazzin selectively removed the sn-2 acyl chain of PC and transferred it into the sn-1 and sn-2 positions of MLCL isomers at equivalent rates. We demonstrated for the first time that MLCL and dilyso-CL have inherent abilities to function as an acyl donor to monolyso-PC and acyl acceptor from PC, respectively. Furthermore, a Barth syndrome-associated tafazzin mutant (H77Q) was shown to completely lack the catalytic activity in our assay. It is difficult to reconcile the present results with the so-called thermodynamic remodeling hypothesis, which premises that tafazzin reacylates MLCL by unsaturated acyl chains only in disordered non-bilayer lipid domain. The acyl specificity of tafazzin may be one of the factors that determine the acyl composition of mature CL in S. cerevisiae mitochondria.
[Mh] Termos MeSH primário: 1-Acilglicerofosfocolina O-Aciltransferase/metabolismo
Cardiolipinas/sangue
Mitocôndrias/metabolismo
Proteínas Mitocondriais/metabolismo
Mutação de Sentido Incorreto
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: 1-Acilglicerofosfocolina O-Aciltransferase/genética
Substituição de Aminoácidos
Cardiolipinas/genética
Mitocôndrias/genética
Proteínas Mitocondriais/genética
Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cardiolipins); 0 (Mitochondrial Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.3.1.23 (1-Acylglycerophosphocholine O-Acyltransferase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160609
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.718510


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[PMID]:27228218
[Au] Autor:Dai X; Zhang H; Han J; He Y; Zhang Y; Qi Y; Pang JJ
[Ad] Endereço:School of Ophthalmology and Optometry, The Eye Hospital, Wenzhou Medical University, Wenzhou, Zhejiang, P.R. China.
[Ti] Título:Effects of Subretinal Gene Transfer at Different Time Points in a Mouse Model of Retinal Degeneration.
[So] Source:PLoS One;11(5):e0156542, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysophosphatidylcholine acyltransferase 1 (LPCAT1) is necessary for photoreceptors to generate an important lipid component of their membranes. The absence of LPCAT1 results in early and rapid rod and cone degeneration. Retinal degeneration 11 (rd11) mice carry a mutation in the Lpcat1 gene, and are an excellent model of early-onset rapid retinal degeneration (RD). To date, no reports have documented gene therapy administration in the rd11 mouse model at different ages. In this study, the AAV8 (Y733F)-smCBA-Lpcat1 vector was subretinally injected at postnatal day (P) 10, 14, 18, or 22. Four months after injection, immunohistochemistry and analysis of retinal morphology showed that treatment at P10 rescued about 82% of the wild-type retinal thickness. However, the diffusion of the vector and the resulting rescue were limited to an area around the injection site that was only 31% of the total retinal area. Injection at P14 resulted in vector diffusion that covered approximately 84% of the retina, and we found that gene therapy was more effective against RD when exposure to light was limited before and after treatment. We observed long-term preservation of electroretinogram (ERG) responses, and preservation of retinal structure, indicating that early treatment followed by limited light exposure can improve gene therapy effectiveness for the eyes of rd11 mice. Importantly, delayed treatment still partially preserved M-cones, but not S-cones, and M-cones in the rd11 retina appeared to have a longer window of opportunity for effective preservation with gene therapy. These results provide important information regarding the effects of subretinal gene therapy in the mouse model of LPCAT1-deficiency.
[Mh] Termos MeSH primário: 1-Acilglicerofosfocolina O-Aciltransferase/biossíntese
Terapia Genética/métodos
Células Fotorreceptoras Retinianas Cones/metabolismo
Degeneração Retiniana/terapia
[Mh] Termos MeSH secundário: 1-Acilglicerofosfocolina O-Aciltransferase/genética
Animais
Modelos Animais de Doenças
Eletrorretinografia
Seres Humanos
Camundongos
Mutação
Degeneração Retiniana/epidemiologia
Degeneração Retiniana/genética
Degeneração Retiniana/fisiopatologia
Transdução Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.1.23 (1-Acylglycerophosphocholine O-Acyltransferase); EC 2.3.1.23 (Lpcat1 protein, mouse)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170706
[Lr] Data última revisão:
170706
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160527
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0156542


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[PMID]:27170177
[Au] Autor:Klein I; Klug L; Schmidt C; Zandl M; Korber M; Daum G; Athenstaedt K
[Ad] Endereço:Institute of Biochemistry, Graz University of Technology, A-8010 Graz, Austria.
[Ti] Título:Regulation of the yeast triacylglycerol lipases Tgl4p and Tgl5p by the presence/absence of nonpolar lipids.
[So] Source:Mol Biol Cell;27(13):2014-24, 2016 Jul 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tgl3p, Tgl4p, and Tgl5p are the major triacylglycerol lipases of the yeast Saccharomyces cerevisiae Recently we demonstrated that properties of Tgl3p are regulated by the formation of nonpolar lipids. The present study extends these investigations to the two other yeast triacylglycerol lipases, Tgl4p and Tgl5p. We show that Tgl4p and Tgl5p, which are localized to lipid droplets in wild type, are partially retained in the endoplasmic reticulum in cells lacking triacylglycerols and localize exclusively to the endoplasmic reticulum in a mutant devoid of lipid droplets. In cells lacking steryl esters, the subcellular distribution of Tgl4p and Tgl5p is unaffected, but Tgl5p becomes unstable, whereas the stability of Tgl4p increases. In cells lacking nonpolar lipids, Tgl4p and Tgl5p lose their lipolytic activity but retain their side activity as lysophospholipid acyltransferases. To investigate the regulatory network of yeast triacylglycerol lipases in more detail, we also examined properties of Tgl3p, Tgl4p, and Tgl5p, respectively, in the absence of the other lipases. Surprisingly, lack of two lipases did not affect expression, localization, and stability of the remaining Tgl protein. These results suggest that Tgl3p, Tgl4p, and Tgl5p, although they exhibit similar functions, act as independent entities.
[Mh] Termos MeSH primário: Lipase/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: 1-Acilglicerofosfocolina O-Aciltransferase/metabolismo
Retículo Endoplasmático/metabolismo
Lipase/genética
Gotículas Lipídicas/metabolismo
Metabolismo dos Lipídeos
Lipídeos/fisiologia
Lipólise
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipids); 0 (Saccharomyces cerevisiae Proteins); 0 (Triglycerides); EC 2.3.1.23 (1-Acylglycerophosphocholine O-Acyltransferase); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (Tgl4 protein, S cerevisiae); EC 3.1.1.3 (Tgl5 protein, S cerevisiae)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160513
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E15-09-0633



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