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[PMID]:26141240
[Au] Autor:Kain L; Costanzo A; Webb B; Holt M; Bendelac A; Savage PB; Teyton L
[Ad] Endereço:The Scripps Research Institute, Department of Immunology and Microbial Science, La Jolla, CA 92037, USA.
[Ti] Título:Endogenous ligands of natural killer T cells are alpha-linked glycosylceramides.
[So] Source:Mol Immunol;68(2 Pt A):94-7, 2015 Dec.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The nature of the endogenous ligands for natural killer T (NKT) cells has been debated for more than a decade. Because the mammalian glycosylceramide synthases are invertases, it is believed that in mammals all glycosylceramides are ß anomers. However, the possibility that an alternative enzymatic pathway, an unfaithful enzyme, or unique physico-chemical environments could allow the production of small quantities of α anomers should be entertained. Classic biochemical and chemical analysis approaches are not well suited for this challenge as they lack sensitivity. Using a combination of biological assays and new technological approaches, we have unequivocally demonstrated that α glycosylceramides were constitutively produced by mammalian immune cells, loaded onto CD1d and presented to NKT cells both in the thymus and in the periphery. Their amount is controlled tightly by catabolic enzymes, and can be altered in vitro and in vivo to modify NKT cell behavior.
[Mh] Termos MeSH primário: Células Apresentadoras de Antígenos/imunologia
Ceramidas/imunologia
Células Matadoras Naturais/imunologia
Timócitos/imunologia
[Mh] Termos MeSH secundário: Animais
Apresentação do Antígeno/genética
Células Apresentadoras de Antígenos/citologia
Antígenos CD1d/imunologia
Antígenos CD1d/metabolismo
Ceramidas/química
Ceramidas/classificação
Ceramidas/metabolismo
Glucosiltransferases/genética
Glucosiltransferases/imunologia
Seres Humanos
Células Matadoras Naturais/citologia
N-Acilesfingosina Galactosiltransferase/genética
N-Acilesfingosina Galactosiltransferase/imunologia
Timócitos/citologia
Timo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Antigens, CD1d); 0 (CD1D protein, human); 0 (Ceramides); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.47 (N-Acylsphingosine Galactosyltransferase); EC 2.4.1.80 (ceramide glucosyltransferase)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:161201
[Lr] Data última revisão:
161201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150705
[St] Status:MEDLINE


  2 / 51 MEDLINE  
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[PMID]:25212460
[Au] Autor:Tanaka K; Mikami M; Aoki D; Kiguchi K; Ishiwata I; Iwamori M
[Ad] Endereço:Department of Obstetrics and Gynecology, School of Medicine, Keio University, 35 Shinanomachi, Shinjuku-ku, Tokyo, 160-8582, Japan, kkyokokeio@a5.keio.jp.
[Ti] Título:Expression of sulfatide and sulfated lactosylceramide among histological types of human ovarian carcinomas.
[So] Source:Hum Cell;28(1):37-43, 2015 Jan.
[Is] ISSN:1749-0774
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Among negatively charged lipids, sulfoglycolipids are known to be expressed by specific cell populations and to be involved in their functions, including in adhesion with functional proteins, modification of ion channels and induction of cellular differentiation. Accordingly, we determined their amounts in several histologically defined types of ovarian carcinoma tissues. Sulfoglycolipids were determined by TLC-immunostaining with monoclonal anti-sulfatide antibodies and the gene expression of their synthetic enzymes was by RT-PCR. All types of ovarian carcinomas were revealed to exhibit potential to synthesize sulfoglycolipids, either sulfatide (I(3)SO3-GalCer) or sulfated lactosylceramides (II(3)SO3-LacCer), which were expressed at the following frequencies, 6 out of 6 mucinous cystadenocarcinomas, 4 out of 7 serous cystadenocarcinomas, 2 out of 3 endometrioid carcinomas, and 2 out of 3 clear cell adenocarcinomas. All mucinous cystadenocarcinoma tissues preferentially contained sulfatide in amounts of 0.61-1.13 µg per mg dry weight, the molecular species being similar with those of GalCer. Whereas the other carcinomas contained either sulfatide or sulfated LacCer, the latter being detected in 4 out of 6 specimens with sulfoglycolipids. The expression of sulfatide and sulfated LacCer was found to be positively correlated with the amounts of GalCer and LacCer as substrates for sulfotransferase and expression of the genes for GalCer sulfotransferase and ceramide galactosyltransferase. Sulfoglycolipids in ovarian carcinoma tissues were revealed to be expressed in morphologically defined type-characteristic manners, in contrast to the ubiquitous distribution of GM3.
[Mh] Termos MeSH primário: Adenocarcinoma de Células Claras/metabolismo
Carcinoma Endometrioide/metabolismo
Cistadenocarcinoma Mucinoso/metabolismo
Cistadenocarcinoma Seroso/metabolismo
Glicolipídeos/metabolismo
Lactosilceramidas/metabolismo
Neoplasias Ovarianas/metabolismo
Sulfoglicoesfingolipídeos/metabolismo
Ésteres do Ácido Sulfúrico/metabolismo
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
N-Acilesfingosina Galactosiltransferase/metabolismo
Sulfotransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycolipids); 0 (Lactosylceramides); 0 (Sulfoglycosphingolipids); 0 (Sulfuric Acid Esters); 0 (sulfoglycolipids); EC 2.4.1.47 (N-Acylsphingosine Galactosyltransferase); EC 2.8.2.- (Sulfotransferases)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:171112
[Lr] Data última revisão:
171112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140913
[St] Status:MEDLINE
[do] DOI:10.1007/s13577-014-0100-4


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[PMID]:24821492
[Au] Autor:Okahara K; Kizuka Y; Kitazume S; Ota F; Nakajima K; Hirabayashi Y; Maekawa M; Yoshikawa T; Taniguchi N
[Ad] Endereço:Disease Glycomics Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
[Ti] Título:Ceramide galactosyltransferase expression is regulated positively by Nkx2.2 and negatively by OLIG2.
[So] Source:Glycobiology;24(10):926-34, 2014 Oct.
[Is] ISSN:1460-2423
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Myelin, a multilamellar structure extended from oligodendrocytes or Schwann cells, plays a critical role in maintenance of neuronal function, and damage or loss of myelin causes demyelinating diseases such as multiple sclerosis. For precise alignment of the myelin sheath, there is a requirement for expression of galactosylceramide (GalCer), a major glycosphingolipid in myelin. Synthesis of GalCer is strictly limited in oligodendrocytes in a developmental stage-specific manner. Ceramide galactosyltransferase (CGT), a key enzyme for biosynthesis of GalCer, exhibits restricted expression in oligodendrocytes but the mechanism is poorly understood. Based on our assumption that particular oligodendrocyte-lineage-specific transcription factors regulate CGT expression, we co-expressed a series of candidate transcription factors with the human CGT promoter-driving luciferase expression in oligodendroglioma cells to measure the promoter activity. We found that Nkx2.2 strongly activated the CGT promoter. In addition, we identified a novel repressive DNA element in the first intron of CGT and OLIG2, an oligodendrocyte-specific transcription factor, as a binding protein of this element. Moreover, overexpression of OLIG2 completely canceled the activating effect of Nkx2.2 on CGT promoter activity. Expression of CGT mRNA was also upregulated by Nkx2.2, but this upregulation was cancelled by co-expression of OLIG2 with Nkx2.2. Our study suggests that CGT expression is controlled by balanced expression of the negative modulator OLIG2 and positive regulator Nkx2.2, providing new insights into how expression of GalCer is tightly regulated in cell-type- and stage-specific manners.
[Mh] Termos MeSH primário: Fatores de Transcrição Hélice-Alça-Hélice Básicos/biossíntese
Proteínas de Homeodomínio/biossíntese
Esclerose Múltipla/genética
N-Acilesfingosina Galactosiltransferase/genética
Proteínas do Tecido Nervoso/biossíntese
Fatores de Transcrição/biossíntese
[Mh] Termos MeSH secundário: Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Diferenciação Celular/genética
Galactosilceramidas/biossíntese
Galactosilceramidas/metabolismo
Regulação Enzimológica da Expressão Gênica/genética
Células HeLa
Proteínas de Homeodomínio/metabolismo
Seres Humanos
Esclerose Múltipla/patologia
Bainha de Mielina/metabolismo
Bainha de Mielina/patologia
N-Acilesfingosina Galactosiltransferase/biossíntese
Proteínas do Tecido Nervoso/genética
Fator de Transcrição 2 de Oligodendrócitos
Oligodendroglia/enzimologia
Oligodendroglia/metabolismo
Regiões Promotoras Genéticas
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (Galactosylceramides); 0 (Homeodomain Proteins); 0 (Nerve Tissue Proteins); 0 (Nkx-2.2 homedomain protein); 0 (OLIG2 protein, human); 0 (Oligodendrocyte Transcription Factor 2); 0 (Transcription Factors); EC 2.4.1.47 (N-Acylsphingosine Galactosyltransferase)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140514
[St] Status:MEDLINE
[do] DOI:10.1093/glycob/cwu042


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[PMID]:23933200
[Au] Autor:Miyazaki C; Saitoh M; Itoh M; Yamashita S; Miyagishi M; Takashima S; Moser AB; Iwamori M; Mizuguchi M
[Ad] Endereço:Department of Developmental Medical Sciences, Graduate School of Medicine, University of Tokyo, Japan.
[Ti] Título:Altered phospholipid molecular species and glycolipid composition in brain, liver and fibroblasts of Zellweger syndrome.
[So] Source:Neurosci Lett;552:71-5, 2013 Sep 27.
[Is] ISSN:1872-7972
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:We studied the altered molecular species of lipids in brain and liver tissues, and fibroblasts from patients with Zellweger syndrome (ZS). ZS cerebellum samples contained a higher amount of sphingomyelin with shorter chain fatty acids compared to that in normal controls. The amount of phosphatidylethanolamine (PE) was less than half of that in controls, with the absence of the PE-type of plasmalogen. Gangliosides were accumulated in the brains and fibroblasts of ZS patients. To investigate whether or not impaired beta-oxidation of very long chain fatty acids and/or plasmalogen synthesis affects glycolipids metabolism, RNAi of peroxisomal acylCo-A oxidase (ACOX1) and glyceronephosphate O-acyltransferase (GNPAT) was performed using cultured neural cells. In neuronal F3-Ngn1 cells, ACOX1 and GNPAT silencing up-regulated ceramide galactosyltransferase (UGT8) mRNA expression, and down-regulated UDP-glucose ceramide glucosyltransferase (UGCG). These results suggest that both impaired beta-oxidation of very long chain fatty acids and plasmalogen synthesis affect glycolipid metabolism in neuronal cells.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Fibroblastos/metabolismo
Glicolipídeos/metabolismo
Fígado/metabolismo
Fosfolipídeos/metabolismo
Síndrome de Zellweger/metabolismo
[Mh] Termos MeSH secundário: Aciltransferases/genética
Estudos de Casos e Controles
Criança
Feminino
Inativação Gênica
Glucosiltransferases/biossíntese
Seres Humanos
Lactente
Masculino
N-Acilesfingosina Galactosiltransferase/biossíntese
Neurônios/enzimologia
Neurônios/metabolismo
Oxirredutases/genética
Regulação para Cima/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycolipids); 0 (Phospholipids); EC 1.- (Oxidoreductases); EC 1.3.3.- (peroxisomal acyl-CoA oxidase); EC 2.3.- (Acyltransferases); EC 2.3.1.42 (glycerone-phosphate O-acyltransferase); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.47 (N-Acylsphingosine Galactosyltransferase); EC 2.4.1.80 (ceramide glucosyltransferase)
[Em] Mês de entrada:1405
[Cu] Atualização por classe:130930
[Lr] Data última revisão:
130930
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130813
[St] Status:MEDLINE


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[PMID]:23907947
[Au] Autor:Nowak M; Dziegiel P; Madej J; Ugorski M
[Ad] Endereço:Department of Pathology, Faculty of Veterinary Medicine, Wroclaw University of Environmental and Life Sciences, 50­375 Wroclaw, Poland. marcin.nowak@up.wroc.pl
[Ti] Título:Ceramide galactosyltransferase (UGT8) as a molecular marker of canine mammary tumor malignancy.
[So] Source:Folia Histochem Cytobiol;51(2):164-7, 2013.
[Is] ISSN:1897-5631
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Thirty-two canine mammary tubulopapillary carcinomas and 14 simple adenomas were studied by immunohistochemistry for the expression of UDP-galactose:ceramide galactosyltransferase (UGT8). The majority of tissue specimens (57%) representing adenomas had no or weak reaction with anti-UGT8 antibodies (0-2 pts according to IRS scale) in comparison to the majority of carcinomas (90%) which stained with high intensities (3-9 pts according to IRS scale). When the average values of the reaction intensities (IRS) for malignant and benign tumors were compared, using the Mann-Whitney U-test, significant differences in UGT8 expression between them were found (P < 0.001). Mammary tubulopapillary carcinomas were further analyzed by IHC and the same rabbit polyclonal antibody directed against UGT8 according to their malignancy grade. It was found that the level of UGT8 increased in tumor specimens together with their grading. A comparison of the average values of the reaction intensity (IRS scale) revealed a significant difference (Mann-Whitney U-test, P < 0.05) in UGT8 expression between tumors representing malignancy grades G3 and G1. Based on the obtained results, it is proposed that UGT8 is associated with malignancy of canine mammary gland cells and may have a potential value as a diagnostic marker.
[Mh] Termos MeSH primário: Adenoma/veterinária
Biomarcadores Tumorais/análise
Carcinoma/veterinária
Doenças do Cão/diagnóstico
Glândulas Mamárias Animais/enzimologia
Neoplasias Mamárias Animais/diagnóstico
N-Acilesfingosina Galactosiltransferase/análise
[Mh] Termos MeSH secundário: Adenoma/diagnóstico
Animais
Carcinoma/diagnóstico
Cães
Feminino
Glândulas Mamárias Animais/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); EC 2.4.1.47 (N-Acylsphingosine Galactosyltransferase)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:161020
[Lr] Data última revisão:
161020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130803
[St] Status:MEDLINE
[do] DOI:10.5603/FHC.2013.0024


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[PMID]:23105111
[Au] Autor:Hayashi T; Hayashi E; Fujimoto M; Sprong H; Su TP
[Ad] Endereço:Cellular Stress Signaling Unit, Integrative Neuroscience Branch, Intramural Research Program, NIDA, National Institutes of Health, Baltimore, Maryland 21224, USA. thayashi2r@gmail.com
[Ti] Título:The lifetime of UDP-galactose:ceramide galactosyltransferase is controlled by a distinct endoplasmic reticulum-associated degradation (ERAD) regulated by sigma-1 receptor chaperones.
[So] Source:J Biol Chem;287(51):43156-69, 2012 Dec 14.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The glycosphingolipid biosynthesis is initiated by monoglycosylation of ceramides, the action of which is catalyzed either by UDP-glucose:ceramide glucosyltransferase or by UDP-galactose:ceramide galactosyltransferase (CGalT). CGalT is expressed predominantly at the endoplasmic reticulum (ER) of oligodendrocytes and is responsible for synthesizing galactosylceramides (GalCer) that play an important role in regulation of axon conductance. However, despite the importance of ceramide monoglycosylation enzymes in a spectrum of cellular functions, the mechanism that fine tunes activities of those enzymes is largely unknown. In the present study, we demonstrated that the sigma-1 receptor (Sig-1R) chaperone, the mammalian homologue of a yeast C8-C7 sterol isomerase, controls the protein level and activity of the CGalT enzyme via a distinct ER-associated degradation system involving Insig. The Sig-1R forms a complex with Insig via its transmembrane domain partly in a sterol-dependent manner and associates with CGalT at the ER. The knockdown of Sig-1Rs dramatically prolonged the lifetime of CGalT without affecting the trimming of N-linked oligosaccharides at CGalT. The increased lifetime leads to the up-regulation of CGalT protein as well as elevated enzymatic activity in CHO cells stably expressing CGalT. Knockdown of Sig-1Rs also decreased CGalT degradation endogenously expressed in D6P2T-schwannoma cells. Our data suggest that Sig-1Rs negatively regulate the activity of GalCer synthesis under physiological conditions by enhancing the degradation of CGalT through regulation of the dynamics of Insig in the lipid-activated ER-associated degradation system. The GalCer synthesis may thus be influenced by sterols at the ER.
[Mh] Termos MeSH primário: Degradação Associada com o Retículo Endoplasmático
Chaperonas Moleculares/metabolismo
N-Acilesfingosina Galactosiltransferase/metabolismo
Receptores sigma/metabolismo
[Mh] Termos MeSH secundário: Animais
Células CHO
Cricetinae
Regulação para Baixo
Galactosilceramidas/metabolismo
Técnicas de Silenciamento de Genes
Proteínas de Membrana/metabolismo
Camundongos
Ratos
Frações Subcelulares/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (Galactosylceramides); 0 (Membrane Proteins); 0 (Molecular Chaperones); 0 (Receptors, sigma); 0 (sigma-1 receptor); EC 2.4.1.47 (N-Acylsphingosine Galactosyltransferase)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121030
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M112.380444


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[PMID]:21366909
[Au] Autor:Meixner M; Jungnickel J; Grothe C; Gieselmann V; Eckhardt M
[Ad] Endereço:Institute of Biochemistry and Molecular Biology, University of Bonn, Germany.
[Ti] Título:Myelination in the absence of UDP-galactose:ceramide galactosyl-transferase and fatty acid 2 -hydroxylase.
[So] Source:BMC Neurosci;12:22, 2011 Mar 02.
[Is] ISSN:1471-2202
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The sphingolipids galactosylceramide (GalCer) and sulfatide are major myelin components and are thought to play important roles in myelin function. The importance of GalCer and sulfatide has been validated using UDP-galactose:ceramide galactosyltransferase-deficient (Cgt-/-) mice, which are impaired in myelin maintenance. These mice, however, are still able to form compact myelin. Loss of GalCer and sulfatide in these mice is accompanied by up-regulation of 2-hydroxylated fatty acid containing (HFA)-glucosylceramide in myelin. This was interpreted as a partial compensation of the loss of HFA-GalCer, which may prevent a more severe myelin phenotype. In order to test this hypothesis, we have generated Cgt-/- mice with an additional deletion of the fatty acid 2-hydroxylase (Fa2h) gene. RESULTS: Fa2h-/-/Cgt-/- double-deficient mice lack sulfatide, GalCer, and in addition HFA-GlcCer and sphingomyelin. Interestingly, compared to Cgt-/- mice the amount of GlcCer in CNS myelin was strongly reduced in Fa2h-/-/Cgt-/- mice by more than 80%. This was accompanied by a significant increase in sphingomyelin, which was the predominant sphingolipid in Fa2h-/-/Cgt-/- mice. Despite these significant changes in myelin sphingolipids, compact myelin was formed in Fa2h-/-/Cgt-/- mice, and g-ratios of myelinated axons in the spinal cord of 4-week-old Fa2h-/-/Cgt-/- mice did not differ significantly from that of Cgt-/- mice, and there was no obvious phenotypic difference between Fa2h-/-/Cgt-/- and Cgt-/- mice CONCLUSIONS: These data show that compact myelin can be formed with non-hydroxylated sphingomyelin as the predominant sphingolipid and suggest that the presence of HFA-GlcCer and HFA-sphingomyelin in Cgt-/- mice does not functionally compensate the loss of HFA-GalCer.
[Mh] Termos MeSH primário: Amidoidrolases/deficiência
Bainha de Mielina/metabolismo
N-Acilesfingosina Galactosiltransferase/deficiência
Sistema Nervoso/metabolismo
Regulação para Cima/genética
[Mh] Termos MeSH secundário: Animais
Ceramidas/metabolismo
Cromatografia em Camada Delgada/métodos
Galactosilceramidas/metabolismo
Gangliosídeos/metabolismo
Metabolismo dos Lipídeos/genética
Masculino
Lipídeos de Membrana/metabolismo
Camundongos
Camundongos Knockout
Bainha de Mielina/ultraestrutura
Sistema Nervoso/anatomia & histologia
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ceramides); 0 (Galactosylceramides); 0 (Gangliosides); 0 (Membrane Lipids); EC 2.4.1.47 (N-Acylsphingosine Galactosyltransferase); EC 3.5.- (Amidohydrolases); EC 3.5.1.- (fatty-acid amide hydrolase)
[Em] Mês de entrada:1106
[Cu] Atualização por classe:150204
[Lr] Data última revisão:
150204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110304
[St] Status:MEDLINE
[do] DOI:10.1186/1471-2202-12-22


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[PMID]:20817833
[Au] Autor:Kongmanas K; Xu H; Yaghoubian A; Franchini L; Panza L; Ronchetti F; Faull K; Tanphaichitr N
[Ad] Endereço:Chronic Disease Program, Ottawa Hospital Research Institute, Ottawa, Ontario, Canada.
[Ti] Título:Quantification of seminolipid by LC-ESI-MS/MS-multiple reaction monitoring: compensatory levels in Cgt(+/⁻) mice.
[So] Source:J Lipid Res;51(12):3548-58, 2010 Dec.
[Is] ISSN:1539-7262
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Seminolipid, also known as sulfogalactosylglycerolipid (SGG), plays important roles in male reproduction. Therefore, an accurate and sensitive method for SGG quantification in testes and sperm is needed. Here we compare SGG quantitation by the traditional colorimetric Azure A assay with LC-ESI-MS/MS using multiple reaction monitoring (MRM). Inclusion of deuterated SGG as the internal standard endowed accuracy to the MRM method. The results showed reasonable agreement between the two procedures for purified samples, but for crude lipid extracts, the colorimetric assay significantly overestimated the SGG content. Using ESI-MS/MS MRM, C16:0-alkyl/C16:0-acyl SGG of Cgt(+/⁻) mice was quantified to be 406.06 ± 23.63 µg/g testis and 0.13 ± 0.02 µg/million sperm, corresponding to 78% and 87% of the wild-type values, respectively. CGT (ceramide galactosyltransferase) is a critical enzyme in the SGG biosynthesis pathway. Cgt⁻/⁻ males depleted of SGG are infertile due to spermatogenesis arrest. However, Cgt(+/⁻) males sire offspring. The higher than 50% expression level of SGG in Cgt(+/⁻) animals, compared with the wild-type expression, might be partly due to compensatory translation of the active CGT enzyme. The results also indicated that 78% of SGG levels in Cgt(+/⁻) mice were sufficient for normal spermatogenesis.
[Mh] Termos MeSH primário: Cromatografia Líquida/métodos
Glicolipídeos/análise
Espectrometria de Massas por Ionização por Electrospray/métodos
Espectrometria de Massas em Tandem/métodos
[Mh] Termos MeSH secundário: Animais
Colorimetria/métodos
Feminino
Glicolipídeos/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
N-Acilesfingosina Galactosiltransferase/metabolismo
Sensibilidade e Especificidade
Espermatozoides/metabolismo
Testículo/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glycolipids); 0 (seminolipid); EC 2.4.1.47 (N-Acylsphingosine Galactosyltransferase)
[Em] Mês de entrada:1102
[Cu] Atualização por classe:160307
[Lr] Data última revisão:
160307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100907
[St] Status:MEDLINE
[do] DOI:10.1194/jlr.D010116


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[PMID]:20157020
[Au] Autor:Niimura Y; Moue T; Takahashi N; Nagai K
[Ad] Endereço:Faculty of Medicine, Teikyo University,2-11-1 Kaga Itabashi-ku, Tokyo, Japan. yniimura@med.teikyo-u.ac.jp
[Ti] Título:Modification of sphingoglycolipids and sulfolipids in kidney cell lines under heat stress: activation of monohexosylceramide synthesis as a ceramide scavenger.
[So] Source:Glycobiology;20(6):710-7, 2010 Jun.
[Is] ISSN:1460-2423
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Heat stress on Madin-Darby canine kidney cells increased ceramide content to 187% at 40 degrees C for 24 h, and the de novo synthesis from serine increased to 146%. Glucosylceramide (GlcCer) and galactosylceramide (GalCer) synthesis from ceramide, the first glycosylation step of sphingolipid metabolism in kidney cells, increased to 290% (GalCer) and 143% (GlcCer) after metabolic labeling with (14)C-glucose at 42 degrees C for 20 h. The more complex glycolipid lactosylceramide also increased to 151%, whereas sulfatide and ganglioside GM3 decreased to 21% and 43%, respectively. Sulfatide (SM4s) showed optimal sulfation at 37 degrees C, whereas cholesterol sulfate was optimally sulfated at 40 degrees C. The gene expression of ceramide glucosyltransferase (GluT), ceramide galactosyltransferase, and GalCer sulfotransferase (GST) after 24 h culture at 42 degrees C significantly increased to 714%, 221%, and 174%, respectively. Another kidney cell line, COS7, showed less activation of these transferases by heat stress. Although GST gene expression was higher under heat stress, SM4s synthesis decreased, which may have been due to increased GST sensitivity to a temperature higher than 37 degrees C. When we introduced the HSP70 gene into the expression vector and transfected the plasmid (pCDM-dHSP70) into kidney cells, GlcCer synthesis increased significantly. From these results, we speculated that HSP70 may play a role in GluT gene expression to increase GlcCer and decrease intracellular ceramide level.
[Mh] Termos MeSH primário: Cerebrosídeos/biossíntese
Glicoesfingolipídeos/metabolismo
Temperatura Alta
Rim/citologia
Lipídeos
[Mh] Termos MeSH secundário: Animais
Células COS
Células Cultivadas
Cercopithecus aethiops
Cerebrosídeos/metabolismo
Cães
Glucosiltransferases/genética
Glucosiltransferases/metabolismo
Proteínas de Choque Térmico HSP70/genética
Proteínas de Choque Térmico HSP70/metabolismo
N-Acilesfingosina Galactosiltransferase/genética
N-Acilesfingosina Galactosiltransferase/metabolismo
Sulfotransferases/genética
Sulfotransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cerebrosides); 0 (Glycosphingolipids); 0 (HSP70 Heat-Shock Proteins); 0 (Lipids); 0 (ceramide monohexoside); 0 (sulfolipids); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.47 (N-Acylsphingosine Galactosyltransferase); EC 2.4.1.80 (ceramide glucosyltransferase); EC 2.8.2.- (Sulfotransferases)
[Em] Mês de entrada:1009
[Cu] Atualização por classe:100514
[Lr] Data última revisão:
100514
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100217
[St] Status:MEDLINE
[do] DOI:10.1093/glycob/cwq018


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[PMID]:19878436
[Au] Autor:Fewou SN; Fernandes A; Stockdale K; Francone VP; Dupree JL; Rosenbluth J; Pfeiffer SE; Bansal R
[Ad] Endereço:Departments of Neuroscience, University of Connecticut Health Center, Farmington, Connecticut, USA. sfewou@yahoo.com
[Ti] Título:Myelin protein composition is altered in mice lacking either sulfated or both sulfated and non-sulfated galactolipids.
[So] Source:J Neurochem;112(3):599-610, 2010 Feb.
[Is] ISSN:1471-4159
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Myelin is highly enriched in galactocerebroside (GalCer) and its sulfated form sulfatide. Mice, unable to synthesize GalCer and sulfatide (CGT(null)) or sulfatide alone (CST(null)), exhibit disorganized paranodal structures and progressive dysmyelination. To obtain insights into the molecular mechanisms underlying these defects, we examined myelin composition of these mutants by two-dimensional differential fluorescence intensity gel electrophoresis proteomic approach and immunoblotting. We identified several proteins whose expressions were significantly altered in these mutants. These proteins are known to regulate cytoskeletal dynamics, energy metabolism, vesicular trafficking or adhesion, suggesting a disruption in these physiological processes in the absence of myelin galactolipids. Further analysis of one of these proteins, nucleotide diphosphate kinase (NDK)/Nm23, showed that it was reduced in myelin of CGT(null) and increased in CST(null), but not in whole brain homogenate. Immunostaining showed an increase in its expression in the cell bodies of CGT(null)- and a decrease in CST(null)-oligodenrocytes, together leading to the hypothesis that transport of NDK/Nm23 from oligodenrocyte cell bodies into myelin may be differentially dysregulated in the absence of these galactolipids. This study provides new insights into the changes that occur in the composition/distribution of myelin proteins in mice lacking either unsulfated and/or sulfated galactolipids and reinforces the role of these lipids in intracellular trafficking.
[Mh] Termos MeSH primário: Proteína Básica da Mielina/metabolismo
Bainha de Mielina/metabolismo
N-Acilesfingosina Galactosiltransferase/deficiência
Nucleosídeo NM23 Difosfato Quinases/metabolismo
Sulfotransferases/deficiência
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Astrócitos/efeitos dos fármacos
Astrócitos/metabolismo
Diferenciação Celular/efeitos dos fármacos
Diferenciação Celular/genética
Células Cultivadas
Eletroforese em Gel Bidimensional/métodos
Regulação da Expressão Gênica/efeitos dos fármacos
Regulação da Expressão Gênica/genética
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteína Proteolipídica de Mielina/metabolismo
Neurônios/efeitos dos fármacos
Neurônios/metabolismo
Oligodendroglia/metabolismo
Fator de Crescimento Derivado de Plaquetas/farmacologia
Transporte Proteico/genética
Células-Tronco/efeitos dos fármacos
Células-Tronco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Myelin Basic Protein); 0 (Myelin Proteolipid Protein); 0 (NM23 Nucleoside Diphosphate Kinases); 0 (Platelet-Derived Growth Factor); 0 (Plp1 protein, mouse); EC 2.4.1.47 (N-Acylsphingosine Galactosyltransferase); EC 2.8.2.- (Sulfotransferases)
[Em] Mês de entrada:1002
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:091103
[St] Status:MEDLINE
[do] DOI:10.1111/j.1471-4159.2009.06464.x



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