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[PMID]:28527668
[Au] Autor:Gónzalez de San Román E; Manuel I; Giralt MT; Ferrer I; Rodríguez-Puertas R
[Ad] Endereço:Department of Pharmacology, Faculty of Medicine and Nursing, University of the Basque Country (UPV/EHU), B Sarriena s/n, 48940 Leioa, Spain.
[Ti] Título:Imaging mass spectrometry (IMS) of cortical lipids from preclinical to severe stages of Alzheimer's disease.
[So] Source:Biochim Biophys Acta;1859(9 Pt B):1604-1614, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Alzheimer's disease (AD) is a progressive neurodegenerative disease affecting millions of patients worldwide. Previous studies have demonstrated alterations in the lipid composition of lipid extracts from plasma and brain samples of AD patients. However, there is no consensus regarding the qualitative and quantitative changes of lipids in brains from AD patients. In addition, the recent developments in imaging mass spectrometry methods are leading to a new stage in the in situ analysis of lipid species in brain tissue slices from human postmortem samples. The present study uses the matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI-IMS), permitting the direct anatomical analysis of lipids in postmortem brain sections from AD patients, which are compared with the intensity of the lipid signal in samples from matched subjects with no neurological diseases. The frontal cortex samples from AD patients were classified in three groups based on Braak's histochemical criteria, ranging from non-cognitively impaired patients to those severely affected. The main results indicate a depletion of different sulfatide lipid species from the earliest stages of the disease in both white and gray matter areas of the frontal cortex. Therefore, the decrease in sulfatides in cortical areas could be considered as a marker of the disease, but may also indicate neurochemical modifications related to the pathogenesis of the disease. This article is part of a Special Issue entitled: Membrane Lipid Therapy: Drugs Targeting Biomembranes edited by Pablo V. Escribá.
[Mh] Termos MeSH primário: Doença de Alzheimer/metabolismo
Lobo Frontal/química
Lipídeos/análise
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos
[Mh] Termos MeSH secundário: Seres Humanos
Sulfoglicoesfingolipídeos/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Lipids); 0 (Sulfoglycosphingolipids)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170522
[St] Status:MEDLINE


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[PMID]:28526683
[Au] Autor:Stax AM; Tuengel J; Girardi E; Kitano N; Allan LL; Liu V; Zheng D; Panenka WJ; Guillaume J; Wong CH; van Calenbergh S; Zajonc DM; van den Elzen P
[Ad] Endereço:BC Children's Hospital Research Institute, Vancouver, British Columbia V5Z 4H4, Canada.
[Ti] Título:Autoreactivity to Sulfatide by Human Invariant NKT Cells.
[So] Source:J Immunol;199(1):97-106, 2017 Jul 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Invariant NKT (iNKT) cells are innate-like lymphocytes that recognize lipid Ags presented by CD1d. The prototypical Ag, α-galactosylceramide, strongly activates human and mouse iNKT cells, leading to the assumption that iNKT cell physiology in human and mouse is similar. In this article, we report the surprising finding that human, but not mouse, iNKT cells directly recognize myelin-derived sulfatide presented by CD1d. We propose that sulfatide is recognized only by human iNKT cells because of the unique positioning of the 3- -sulfated ß-galactose headgroup. Surface plasmon resonance shows that the affinity of human CD1d-sulfatide for the iNKT cell receptor is relatively low compared with CD1d-α-galactosylceramide ( of 19-26 µM versus 1 µM). Apolipoprotein E isolated from human cerebrospinal fluid carries sulfatide that can be captured by APCs and presented by CD1d to iNKT cells. APCs from patients with metachromatic leukodystrophy, who accumulate sulfatides due to a deficiency in arylsulfatase-A, directly activate iNKT cells. Thus, we have identified sulfatide as a self-lipid recognized by human iNKT cells and propose that sulfatide recognition by innate T cells may be an important pathologic feature of neuroinflammatory disease and that sulfatide in APCs may contribute to the endogenous pathway of iNKT cell activation.
[Mh] Termos MeSH primário: Apresentação do Antígeno
Ativação Linfocitária
Células T Matadoras Naturais/imunologia
Sulfoglicoesfingolipídeos/imunologia
[Mh] Termos MeSH secundário: Animais
Antígenos CD1d/imunologia
Apolipoproteínas E/líquido cefalorraquidiano
Apolipoproteínas E/química
Apolipoproteínas E/imunologia
Linhagem Celular
Cerebrosídeo Sulfatase/deficiência
Cerebrosídeo Sulfatase/metabolismo
Galactosilceramidas/imunologia
Seres Humanos
Leucodistrofia Metacromática/imunologia
Camundongos
Células T Matadoras Naturais/fisiologia
Receptores de Antígenos de Linfócitos T/imunologia
Ressonância de Plasmônio de Superfície
Subpopulações de Linfócitos T/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD1d); 0 (Apolipoproteins E); 0 (CD1D protein, human); 0 (CD1d antigen, mouse); 0 (Galactosylceramides); 0 (Receptors, Antigen, T-Cell); 0 (Sulfoglycosphingolipids); 0 (alpha-galactosylceramide); EC 3.1.6.8 (Cerebroside-Sulfatase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170521
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1601976


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[PMID]:28078602
[Au] Autor:Park KT; Shon JC; Kim JE; Park GH; Choi HJ; Liu KH
[Ad] Endereço:BK21 Plus KNU Multi-Omics Based Creative Drug Research Team, College of Pharmacy and Research Institute of Pharmaceutical Sciences, Kyungpook National University, Daegu, 41566, Korea.
[Ti] Título:Sulfatides Primarily Exist in the Substantia Nigra Region of Mouse Brain Tissue.
[So] Source:Lipids;52(2):179-187, 2017 Feb.
[Is] ISSN:1558-9307
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Lipid distribution in the brain is important for many biological functions and has been associated with some brain diseases. The aim of this study was to investigate lipid distribution in different regions of brain tissue in mice. To this end, substantia nigra (SN), caudate putamen (CPu), hippocampus (Hip), hypothalamus (Hyp), and cortex (Cx) tissues of mice were analyzed using direct infusion nanoelectrospray-ion trap mass spectrometry and multivariate analyses. The SN, CPu, Hip, Hyp, and Cx groups showed clear differences in lipid distribution using principal component analysis and a partial least-squares discriminant analysis score plot, and lipid levels were significantly different in different brain regions. In particular, sulfatides were mainly distributed in the SN region. Our results could be used to help understand the functions and mechanisms of lipids in various brain diseases.
[Mh] Termos MeSH primário: Espectrometria de Massas por Ionização por Electrospray/métodos
Substância Negra/metabolismo
Sulfoglicoesfingolipídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Hipocampo/metabolismo
Hipotálamo/metabolismo
Masculino
Camundongos
Especificidade de Órgãos
Análise de Componente Principal
Distribuição Tecidual
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sulfoglycosphingolipids)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171105
[Lr] Data última revisão:
171105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170113
[St] Status:MEDLINE
[do] DOI:10.1007/s11745-016-4224-z


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[PMID]:27976382
[Au] Autor:Boggs JM
[Ad] Endereço:Department of Molecular Structure and Function, Research Institute, Hospital for Sick Children, Peter Gilgan Centre for Research and Learning, Toronto, Ontario, Canada.
[Ti] Título:Early glycolipid (POA) in pro-oligodendroblasts revealed to be sulfatide: An Editorial Highlight for 'Sulfatide species with various fatty acid chains in oligodendrocytes at different developmental stages determined by imaging mass spectrometry'.
[So] Source:J Neurochem;140(3):356-358, 2017 Feb.
[Is] ISSN:1471-4159
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Read the highlighted article 'Sulfatide species with various fatty acid chains in oligodendrocytes at different developmental stages determined by imaging mass spectrometry' on page 435.
[Mh] Termos MeSH primário: Sulfoglicoesfingolipídeos
[Mh] Termos MeSH secundário: Ácidos Graxos
Espectrometria de Massas
Oligodendroglia
[Pt] Tipo de publicação:EDITORIAL
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Sulfoglycosphingolipids)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161216
[St] Status:MEDLINE
[do] DOI:10.1111/jnc.13893


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[PMID]:27908207
[Au] Autor:Saccomanno D; Tomba C; Magri F; Backelandt P; Roncoroni L; Doneda L; Bardella MT; Comi GP; Bresolin N; Conte D; Elli L
[Ad] Endereço:a Department of Pathophysiology and Transplantation, Neurology Unit , Dino Ferrari Center, University of Milan, Fondazione IRCCS Ca' Granda-Ospedale Maggiore Policlinico , Milan , Italy.
[Ti] Título:Anti-sulfatide reactivity in patients with celiac disease.
[So] Source:Scand J Gastroenterol;52(4):409-413, 2017 Apr.
[Is] ISSN:1502-7708
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To explore a possible significance of the presence of anti-ganglioside and anti-sulfatide antibodies in sera of adult patients with celiac disease (CD) in different clinical scenario. METHODS: We selected 22 adult patients with newly diagnosed CD and 20 age-sex matched non-CD controls. Patients' serum was tested - before and after at least 6 months on a gluten-free diet (GFD) - for anti-GM1, GM2, GM3, GD1a, GD1b, GD3, GT1a, GT1b, GQ1b and sulfatide IgM, IgG and IgA auto-antibodies, by means of a dot blot technique and enzyme-linked immunosorbent assay (ELISA). RESULTS: We found the presence of auto-antibodies in untreated patients. In particular, anti-sulfatide IgG antibodies were present in 8 (36%) patients independently of the presence of neurological symptoms. Anti-sulfatide IgA antibodies were present in 3 (19%) patients. During GFD, anti-sulfatide IgG disappeared in all the patients, whereas IgA were observed in 2 patients. Anti-sulfatide, anti-GM1 and anti-GM2 IgM antibodies were also observed in 2 patients on a GFD. All the other auto-antibodies were absent and no demographic or clinical parameters were associated. Non-CD controls did not present any auto-antibody. CONCLUSIONS: We found anti-sulfatide IgG antibodies in CD patients on a gluten-containing diet. Anti-sulfatide IgA antibodies persisted during GFD together with the occurrence of other IgM auto-antibodies. These data suggest a possible link between gluten and IgG auto-antibodies.
[Mh] Termos MeSH primário: Autoanticorpos/sangue
Doença Celíaca/sangue
Gangliosídeos/imunologia
Isotipos de Imunoglobulinas/sangue
Sulfoglicoesfingolipídeos/imunologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Estudos de Casos e Controles
Doença Celíaca/dietoterapia
Doença Celíaca/imunologia
Dieta Livre de Glúten
Ensaio de Imunoadsorção Enzimática
Feminino
Glutens/efeitos adversos
Seres Humanos
Immunoblotting
Itália
Masculino
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autoantibodies); 0 (Gangliosides); 0 (Immunoglobulin Isotypes); 0 (Sulfoglycosphingolipids); 8002-80-0 (Glutens)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161203
[St] Status:MEDLINE
[do] DOI:10.1080/00365521.2016.1263679


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[PMID]:27861899
[Au] Autor:Hirahara Y; Wakabayashi T; Mori T; Koike T; Yao I; Tsuda M; Honke K; Gotoh H; Ono K; Yamada H
[Ad] Endereço:Department of Anatomy and Cell Science, Kansai Medical University, Osaka, Japan.
[Ti] Título:Sulfatide species with various fatty acid chains in oligodendrocytes at different developmental stages determined by imaging mass spectrometry.
[So] Source:J Neurochem;140(3):435-450, 2017 Feb.
[Is] ISSN:1471-4159
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:HSO3-3-galactosylceramide (Sulfatide) species comprise the major glycosphingolipid components of oligodendrocytes and myelin and play functional roles in the regulation of oligodendrocyte maturation and myelin formation. Although various sulfatide species contain different fatty acids, it is unclear how these sulfatide species affect oligodendrogenesis and myelination. The O4 monoclonal antibody reaction with sulfatide has been widely used as a useful marker for oligodendrocytes and myelin. However, sulfatide synthesis during the pro-oligodendroblast stage, where differentiation into the oligodendrocyte lineage has already occurred, has not been examined. Notably, this stage comprises O4-positive cells. In this study, we identified a sulfatide species from the pro-oligodendroblast-to-myelination stage by imaging mass spectrometry. The results demonstrated that short-chain sulfatides with 16 carbon non-hydroxylated fatty acids (C16) and 18 carbon non-hydroxylated fatty acids (C18) or 18 carbon hydroxylated fatty acids (C18-OH) existed in restricted regions of the early embryonic spinal cord, where pro-oligodendroblasts initially appear, and co-localized with Olig2-positive pro-oligodendroblasts. C18 and C18-OH sulfatides also existed in isolated pro-oligodendroblasts. C22-OH sulfatide became predominant later in oligodendrocyte development and the longer C24 sulfatide was predominant in the adult brain. Additionally, the presence of each sulfatide species in a different area of the adult brain was demonstrated by imaging mass spectrometry at an increased lateral resolution. These findings indicated that O4 recognized sulfatides with short-chain fatty acids in pro-oligodendroblasts. Moreover, the fatty acid chain of the sulfatide became longer as the oligodendrocyte matured. Therefore, individual sulfatide species may have unique roles in oligodendrocyte maturation and myelination. Read the Editorial Highlight for this article on page 356.
[Mh] Termos MeSH primário: Encéfalo/crescimento & desenvolvimento
Ácidos Graxos/análise
Oligodendroglia/química
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Medula Espinal/crescimento & desenvolvimento
Sulfoglicoesfingolipídeos/análise
[Mh] Termos MeSH secundário: Animais
Encéfalo/metabolismo
Bovinos
Ácidos Graxos/metabolismo
Feminino
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Oligodendroglia/metabolismo
Ratos
Ratos Wistar
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos
Medula Espinal/química
Medula Espinal/metabolismo
Sulfoglicoesfingolipídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Sulfoglycosphingolipids)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1111/jnc.13897


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[PMID]:28484173
[Au] Autor:Takahashi T
[Ad] Endereço:Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka.
[Ti] Título:Functional analysis of glyco-molecules that bind with influenza virus.
[So] Source:Uirusu;66(1):101-116, 2016.
[Is] ISSN:0042-6857
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Ab] Resumo:Influenza A virus (IAV) recognizes terminal sialic acid of sialoglyco-conjugates on host cells through the viral envelope glycoprotein hemagglutinin (HA), followed by initiation of entry into the cells. Molecular species of sialic acid are largely divided into two moieties: N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc). A receptor for IAV infection generally means Neu5Ac. Almost all equine IAVs and some human, swine, and duck IAVs bind not only to Neu5Ac but also to Neu5Gc. In nonhuman animals, Neu5Gc has been detected in swine and equine tracheas and the duck colon, which are the main replication sites of mammalian and avian IAVs. Therefore, Neu5Gc in these sites has been suggested to be a functional receptor for IAV infection. Humans cannot synthesize Neu5Gc due to a genetic defect of the Neu5Gc-synthesizing enzyme. We evaluated the receptor function of Neu5Gc in IAV infection in human cells. Our results indicated that Neu5Gc expression on the surface of human cells is not a functional receptor for IAV infection and that it has a negative effect on infectivity of IAV possessing Neu5Gc binding ability. IAV also binds to non-sialo 3-O-sulfated galactosylceramide (sulfatide). Sulfatide has been suggested to be a functional receptor for IAV infection. However, we have shown that sulfatide is not a functional receptor for IAV infection and that the binding of HA with sulfatide enhances progeny virus production. It is expected that functions of these glyco-molecules can be used in prevention and development of new drugs against IAV.
[Mh] Termos MeSH primário: Vírus da Influenza A/metabolismo
Ácido N-Acetilneuramínico/metabolismo
Receptores Virais/metabolismo
Receptores Virais/fisiologia
[Mh] Termos MeSH secundário: Animais
Antivirais
Descoberta de Drogas
Galactosilceramidas/metabolismo
Glicoconjugados/metabolismo
Seres Humanos
Influenza Humana/tratamento farmacológico
Influenza Humana/prevenção & controle
Terapia de Alvo Molecular
Ácido N-Acetilneuramínico/fisiologia
Ácidos Neuramínicos/metabolismo
Sulfoglicoesfingolipídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Galactosylceramides); 0 (Glycoconjugates); 0 (Neuraminic Acids); 0 (Receptors, Virus); 0 (Sulfoglycosphingolipids); 1113-83-3 (N-glycolylneuraminic acid); GZP2782OP0 (N-Acetylneuraminic Acid)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171015
[Lr] Data última revisão:
171015
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170510
[St] Status:MEDLINE
[do] DOI:10.2222/jsv.66.101


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[PMID]:27836184
[Au] Autor:Morikawa M; Kuwahara M; Ueno R; Samukawa M; Hamada Y; Kusunoki S
[Ad] Endereço:Department of Neurology, Kindai University Faculty of Medicine, 377-2 Ohno-Higashi, Osaka-Sayama, Osaka 589-8511, Japan.
[Ti] Título:Serological study using glycoarray for detecting antibodies to glycolipids and glycolipid complexes in immune-mediated neuropathies.
[So] Source:J Neuroimmunol;301:35-40, 2016 Dec 15.
[Is] ISSN:1872-8421
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:We performed a serological investigation using glycoarray in Guillain-Barré syndrome (GBS), chronic inflammatory demyelinating polyradiculoneuropathy (CIDP), and multifocal motor neuropathy (MMN). Antibodies to 10 glycolipids and 45 glycolipid complexes were tested. Anti-GM1/sulfatide and anti-GA1/sulfatide IgG antibodies were common in GBS (20.0% and 19.0%, respectively). Anti-GQ1b/sulfatide IgG antibody was detected in 14.0% of GBS patients. IgG antibodies to antigens containing GQ1b were significantly correlated with ophthalmoplegia in GBS (p<0.01). IgM antibodies to antigens containing GM1 or GalNAc-GD1a were in 50% and 37.5% of MMN patients, respectively. Glycoarray is efficient for detecting antibodies against numerous glycolipid complexes in immune-mediated neuropathies.
[Mh] Termos MeSH primário: Autoanticorpos/sangue
Glicolipídeos/imunologia
Síndrome de Guillain-Barré/sangue
Imunoglobulina G/sangue
Polineuropatias/sangue
Polirradiculoneuropatia Desmielinizante Inflamatória Crônica/sangue
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Ensaio de Imunoadsorção Enzimática
Feminino
Gangliosídeos/imunologia
Seres Humanos
Japão
Masculino
Meia-Idade
Estatísticas não Paramétricas
Sulfoglicoesfingolipídeos/imunologia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autoantibodies); 0 (Gangliosides); 0 (Glycolipids); 0 (Immunoglobulin G); 0 (Sulfoglycosphingolipids); 68652-37-9 (GQ1b ganglioside); 72429-69-7 (IV(4)-galactosyl-N-acetylganglioside GD1a)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161113
[St] Status:MEDLINE


  9 / 1430 MEDLINE  
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[PMID]:27644403
[Au] Autor:Yang Y; Feng Y; Zhang X; Nakajima T; Tanaka N; Sugiyama E; Kamijo Y; Aoyama T
[Ad] Endereço:Department of Metabolic Regulation, Shinshu University Graduate School of Medicine.
[Ti] Título:Activation of PPARα by Fatty Acid Accumulation Enhances Fatty Acid Degradation and Sulfatide Synthesis.
[So] Source:Tohoku J Exp Med;240(2):113-22, 2016 10.
[Is] ISSN:1349-3329
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Very-long-chain acyl-CoA dehydrogenase (VLCAD) catalyzes the first reaction in the mitochondrial fatty acid ß-oxidation pathway. VLCAD deficiency is associated with the accumulation of fat in multiple organs and tissues, which results in specific clinical features including cardiomyopathy, cardiomegaly, muscle weakness, and hepatic dysfunction in infants. We speculated that the abnormal fatty acid metabolism in VLCAD-deficient individuals might cause cell necrosis by fatty acid toxicity. The accumulation of fatty acids may activate peroxisome proliferator-activated receptor (PPAR), a master regulator of fatty acid metabolism and a potent nuclear receptor for free fatty acids. We examined six skin fibroblast lines, derived from VLCAD-deficient patients and identified fatty acid accumulation and PPARα activation in these cell lines. We then found that the expression levels of three enzymes involved in fatty acid degradation, including long-chain acyl-CoA synthetase (LACS), were increased in a PPARα-dependent manner. This increased expression of LACS might enhance the fatty acyl-CoA supply to fatty acid degradation and sulfatide synthesis pathways. In fact, the first and last reactions in the sulfatide synthesis pathway are regulated by PPARα. Therefore, we also measured the expression levels of enzymes involved in sulfatide metabolism and the regulation of cellular sulfatide content. The levels of these enzymes and cellular sulfatide content both increased in a PPARα-dependent manner. These results indicate that PPARα activation plays defensive and compensative roles by reducing cellular toxicity associated with fatty acids and sulfuric acid.
[Mh] Termos MeSH primário: Ácidos Graxos/metabolismo
PPAR alfa/metabolismo
Sulfoglicoesfingolipídeos/metabolismo
[Mh] Termos MeSH secundário: Acil-CoA Desidrogenase de Cadeia Longa/genética
Acil-CoA Desidrogenase de Cadeia Longa/metabolismo
DNA/metabolismo
Fenofibrato/farmacologia
Regulação da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Indóis/farmacologia
Redes e Vias Metabólicas/efeitos dos fármacos
Redes e Vias Metabólicas/genética
Ligação Proteica/efeitos dos fármacos
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Sulfoglicoesfingolipídeos/química
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Indoles); 0 (PPAR alpha); 0 (RNA, Messenger); 0 (Sulfoglycosphingolipids); 0 (Triglycerides); 080626SQ8C (MK-886); 9007-49-2 (DNA); EC 1.3.8.8 (Acyl-CoA Dehydrogenase, Long-Chain); U202363UOS (Fenofibrate)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160921
[St] Status:MEDLINE
[do] DOI:10.1620/tjem.240.113


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[PMID]:27417284
[Au] Autor:Palavicini JP; Wang C; Chen L; Ahmar S; Higuera JD; Dupree JL; Han X
[Ad] Endereço:Center for Metabolic Origins of Disease, Sanford Burnham Prebys Medical Discovery Institute, Orlando, Florida, USA.
[Ti] Título:Novel molecular insights into the critical role of sulfatide in myelin maintenance/function.
[So] Source:J Neurochem;139(1):40-54, 2016 Oct.
[Is] ISSN:1471-4159
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cerebroside sulfotransferase (CST) catalyzes the production of sulfatide, a major class of myelin-specific lipids. CST knockout (CST(-/-) ) mice in which sulfatide is completely depleted are born healthy, but display myelin abnormalities and progressive tremors starting at 4-6 weeks of age. Although these phenotypes suggest that sulfatide plays a critical role in myelin maintenance/function, the underlying mechanisms remain largely unknown. We analyzed the major CNS myelin proteins and the major lipids enriched in the myelin in a spatiotemporal manner. We found a one-third reduction of the major compact myelin proteins (myelin basic protein, myelin basic protein, and proteolipid protein, PLP) and an equivalent post-developmental loss of myelin lipids, providing the molecular basis behind the thinner myelin sheaths. Our lipidomics data demonstrated that the observed global reduction of myelin lipid content was not because of an increase of lipid degradation but rather to the reduction of their synthesis by oligodendrocytes. We also showed that sulfatide depletion leads to region-specific effects on non-compact myelin, dramatically affecting the paranode (neurofascin 155) and the major inner tongue myelin protein (myelin-associated glycoprotein). Moreover, we demonstrated that sulfatide promotes the interaction between adjacent PLP extracellular domains, evidenced by a progressive decline of high molecular weight PLP complexes in CST(-/-) mice, providing an explanation at a molecular level regarding the uncompacted myelin sheaths. Finally, we proposed that the dramatic losses of neurofascin 155 and PLP interactions are responsible for the progressive tremors and eventual ataxia. In summary, we unraveled novel molecular insights into the critical role of sulfatide in myelin maintenance/function. Cerebroside sulfotransferase (CST) catalyzes the production of sulfatide, a major class of myelin-specific lipids. CST knockout (CST(-/-) ) mice in which sulfatide is completely depleted are born healthy, but display myelin abnormalities We show in our study that sulfatide depletion leads to losses of myelin proteins and lipids, and impairment of myelin functions, unraveling novel molecular insights into the critical role of sulfatide in myelin maintenance/function.
[Mh] Termos MeSH primário: Proteínas da Mielina/genética
Proteínas da Mielina/metabolismo
Bainha de Mielina/fisiologia
Sulfoglicoesfingolipídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Axônios/metabolismo
Axônios/ultraestrutura
Homeostase
Metabolismo dos Lipídeos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteína Proteolipídica de Mielina/metabolismo
Bainha de Mielina/metabolismo
Bainha de Mielina/ultraestrutura
Glicoproteína Associada a Mielina/metabolismo
Oligodendroglia/metabolismo
Fenótipo
Sulfotransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Myelin Proteins); 0 (Myelin Proteolipid Protein); 0 (Myelin-Associated Glycoprotein); 0 (Sulfoglycosphingolipids); EC 2.8.2.- (Sulfotransferases); EC 2.8.2.11 (galactosylceramide sulfotransferase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171001
[Lr] Data última revisão:
171001
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160716
[St] Status:MEDLINE
[do] DOI:10.1111/jnc.13738



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