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[PMID]:27157270
[Au] Autor:Sandhoff K
[Ad] Endereço:University of Bonn, LIMES Institute, c/o Kekulé-Institute, Gerhard-Domagk-Str. 1, 53121 Bonn, Germany. Electronic address: sandhoff@uni-bonn.de.
[Ti] Título:Neuronal sphingolipidoses: Membrane lipids and sphingolipid activator proteins regulate lysosomal sphingolipid catabolism.
[So] Source:Biochimie;130:146-151, 2016 Nov.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Glycosphingolipids and sphingolipids of cellular plasma membranes (PMs) reach luminal intra-lysosomal vesicles (LVs) for degradation mainly by pathways of endocytosis. After a sorting and maturation process (e.g. degradation of sphingomyelin (SM) and secretion of cholesterol), sphingolipids of the LVs are digested by soluble enzymes with the help of activator (lipid binding and transfer) proteins. Inherited defects of lipid-cleaving enzymes and lipid binding and transfer proteins cause manifold and fatal, often neurodegenerative diseases. The review summarizes recent findings on the regulation of sphingolipid catabolism and cholesterol secretion from the endosomal compartment by lipid modifiers, an essential stimulation by anionic membrane lipids and an inhibition of crucial steps by cholesterol and SM. Reconstitution experiments in the presence of all proteins needed, hydrolase and activator proteins, reveal an up to 10-fold increase of ganglioside catabolism just by the incorporation of anionic lipids into the ganglioside carrying membranes, whereas an additional incorporation of cholesterol inhibits GM2 catabolism substantially. It is suggested that lipid and other low molecular modifiers affect the genotype-phenotype relationship observed in patients with lysosomal diseases.
[Mh] Termos MeSH primário: Lisossomos/metabolismo
Lipídeos de Membrana/metabolismo
Proteínas Ativadoras de Esfingolipídeos/metabolismo
Esfingolipidoses/metabolismo
Esfingolipídeos/metabolismo
[Mh] Termos MeSH secundário: Colesterol/metabolismo
Endossomos/metabolismo
Seres Humanos
Modelos Biológicos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Membrane Lipids); 0 (Sphingolipid Activator Proteins); 0 (Sphingolipids); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170130
[Lr] Data última revisão:
170130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160510
[St] Status:MEDLINE


  2 / 207 MEDLINE  
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[PMID]:26571594
[Au] Autor:Ikushiro H
[Ti] Título:[Mechanistic enzymology of serine palmitoyltransferase--Stereochemical reaction control revealed by the side reaction of mutant enzymes].
[So] Source:Seikagaku;87(3):298-307, 2015 Jun.
[Is] ISSN:0037-1017
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Mh] Termos MeSH primário: Aciltransferases/metabolismo
Enzimas Multifuncionais/biossíntese
Serina C-Palmitoiltransferase/metabolismo
Proteínas Ativadoras de Esfingolipídeos/biossíntese
Proteínas Ativadoras de Esfingolipídeos/química
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Mutação/fisiologia
Especificidade por Substrato/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Multifunctional Enzymes); 0 (Sphingolipid Activator Proteins); EC 2.3.- (Acyltransferases); EC 2.3.1.50 (Serine C-Palmitoyltransferase)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:170410
[Lr] Data última revisão:
170410
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151118
[St] Status:MEDLINE


  3 / 207 MEDLINE  
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[PMID]:26531285
[Au] Autor:Zhu XY; Ye MY; Zhang AM; Wang WD; Zeng F; Li JL; Fang F
[Ad] Endereço:Department of Pediatrics, Xiangyang Hospital, Hubei University of Medicine, Xiangyang, Hubei, China. 505893788@qq.com.
[Ti] Título:Influence of one-year neurologic outcome of treatment on newborns with moderate and severe hypoxic-ischemic encephalopathy by rhuEP0 combined with ganglioside (GM1).
[So] Source:Eur Rev Med Pharmacol Sci;19(20):3955-60, 2015 Oct.
[Is] ISSN:2284-0729
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To observe the one-year neurologic prognostic outcome of newborns with moderate and severe hypoxic-ischemic encephalopathy (HIE) who received recombinant human erythropoietin (rhuEPO) combined with exogenous monosialotetrahexosylganglioside (GM1) treatment to provide new guidelines for clinical treatment. PATIENTS AND METHODS: Seventy-six newborns with moderate and severe HIE were selected from February 2011 to February 2014 in our hospital. This study received the informed consent of our hospital's Ethics Committee and the newborns' guardians. The newborns were divided to an observation group (n = 34 cases) and a control group (n = 42 cases). All newborns underwent hypothermia and conventional treatment for their conditions. The control group received GMl treatment and observation group received rhuEPO combined with GMl treatment. The curative differences and neural behavior from these two groups were compared. RESULTS: The excellent, efficient proportion and total effective rate of the newborns from the observation group were higher than the control group. The death rate, cerebral palsy and the invalid ratio of the newborns from the observation group were lower than that of the control group. Awareness, muscle tension, primitive reflex and increased intracranial pressure recovery time of the newborns in the observation group were less than those of the control group. The Neonatal Behavior Neurological Assessment (NBNA) score of both groups after the treatment of 7, 14 and 28 days were significantly higher and increased with time (p < 0.05). The MDI, PDI and DQ score of newborns from the two groups all increased after treatment of 3, 6 and 12 months than those of before, which increased with time (p < 0.05). CONCLUSIONS: The rhuEPO + GMl treatment in newborns with HIE improves short-term clinical effects and long-term neurological symptoms.
[Mh] Termos MeSH primário: Eritropoetina/administração & dosagem
Hipóxia-Isquemia Encefálica/diagnóstico
Hipóxia-Isquemia Encefálica/tratamento farmacológico
Proteínas Recombinantes/administração & dosagem
Índice de Gravidade de Doença
Proteínas Ativadoras de Esfingolipídeos/administração & dosagem
[Mh] Termos MeSH secundário: Paralisia Cerebral/diagnóstico
Paralisia Cerebral/tratamento farmacológico
Quimioterapia Combinada
Feminino
Seres Humanos
Recém-Nascido
Masculino
Exame Neurológico/métodos
Prognóstico
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); 0 (Sphingolipid Activator Proteins); 11096-26-7 (Erythropoietin)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:151104
[Lr] Data última revisão:
151104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151105
[St] Status:MEDLINE


  4 / 207 MEDLINE  
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[PMID]:24184515
[Au] Autor:Schulze H; Sandhoff K
[Ad] Endereço:LIMES, Membrane Biology & Lipid Biochemistry Unit, c/o Kekulé-Institut für Organische Chemie und Biochemie, Universität Bonn, Gerhard-Domagk-Str. 1, D-53115 Bonn, Germany.
[Ti] Título:Sphingolipids and lysosomal pathologies.
[So] Source:Biochim Biophys Acta;1841(5):799-810, 2014 May.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Endocytosed (glyco)sphingolipids are degraded, together with other membrane lipids in a stepwise fashion by endolysosomal enzymes with the help of small lipid binding proteins, the sphingolipid activator proteins (SAPs), at the surface of intraluminal lysosomal vesicles. Inherited defects in a sphingolipid-degrading enzyme or SAP cause the accumulation of the corresponding lipid substrates, including cytotoxic lysosphingolipids, such as galactosylsphingosine and glucosylsphingosine, and lead to a sphingolipidosis. Analysis of patients with prosaposin deficiency revealed the accumulation of intra-endolysosmal vesicles and membrane structures (IM). Feeding of prosaposin reverses the storage, suggesting inner membrane structures as platforms of sphingolipid degradation. Water soluble enzymes can hardly attack sphingolipids embedded in the membrane of inner endolysosomal vesicles. The degradation of sphingolipids with few sugar residues therefore requires the help of the SAPs, and is strongly stimulated by anionic membrane lipids. IMs are rich in anionic bis(monoacylglycero)phosphate (BMP). This article is part of a Special Issue entitled New Frontiers in Sphingolipid Biology.
[Mh] Termos MeSH primário: Doenças por Armazenamento dos Lisossomos/metabolismo
Doenças por Armazenamento dos Lisossomos/patologia
Lisossomos/metabolismo
Lisossomos/patologia
Esfingolipídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Proteínas Ativadoras de Esfingolipídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Sphingolipid Activator Proteins); 0 (Sphingolipids)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131105
[St] Status:MEDLINE


  5 / 207 MEDLINE  
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[PMID]:24046456
[Au] Autor:Guillaume E; Comunale F; Do Khoa N; Planchon D; Bodin S; Gauthier-Rouvière C
[Ad] Endereço:Equipe Labellisée Ligue Contre le Cancer, Universités Montpellier 2 et 1, CRBM, CNRS, UMR 5237, 1919 Route de Mende, 34293 Montpellier, France.
[Ti] Título:Flotillin microdomains stabilize cadherins at cell-cell junctions.
[So] Source:J Cell Sci;126(Pt 22):5293-304, 2013 Nov 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cadherins are essential in many fundamental processes and assemble at regions of cell-cell contact in large macromolecular complexes named adherens junctions. We have identified flotillin 1 and 2 as new partners of the cadherin complexes. We show that flotillins are localised at cell-cell junctions (CCJs) in a cadherin-dependent manner. Flotillins and cadherins are constitutively associated at the plasma membrane and their colocalisation at CCJ increases with CCJ maturation. Using three-dimensional structured illumination super-resolution microscopy, we found that cadherin and flotillin complexes are associated with F-actin bundles at CCJs. The knockdown of flotillins dramatically affected N- and E-cadherin recruitment at CCJs in mesenchymal and epithelial cell types and perturbed CCJ integrity and functionality. Moreover, we determined that flotillins are required for cadherin association with GM1-containing plasma membrane microdomains. This allows p120 catenin binding to the cadherin complex and its stabilization at CCJs. Altogether, these data demonstrate that flotillin microdomains are required for cadherin stabilization at CCJs and for the formation of functional CCJs.
[Mh] Termos MeSH primário: Caderinas/metabolismo
Junções Intercelulares/genética
Proteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Caderinas/genética
Cateninas/metabolismo
Membrana Celular/metabolismo
Técnicas de Silenciamento de Genes
Células HCT116
Seres Humanos
Junções Intercelulares/metabolismo
Células MCF-7
Proteínas de Membrana/genética
Estrutura Terciária de Proteína
Proteínas Ativadoras de Esfingolipídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cadherins); 0 (Catenins); 0 (Membrane Proteins); 0 (Sphingolipid Activator Proteins); 0 (delta catenin); 0 (flotillins)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:131118
[Lr] Data última revisão:
131118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130919
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.133975


  6 / 207 MEDLINE  
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[PMID]:23916875
[Au] Autor:Barboza L; Salmen S; Teran-Angel G; Peterson DL; Berrueta L
[Ad] Endereço:Institute of Clinical Immunology, University of Los Andes, Merida, Venezuela.
[Ti] Título:A deficient translocation of CD3ζ, ZAP-70 and Grb2 to lipid raft, as a hallmark of defective adaptive immune response during chronic hepatitis B infection.
[So] Source:Cell Immunol;284(1-2):9-19, 2013 Jul-Aug.
[Is] ISSN:1090-2163
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Hepatitis B is considered to be a worldwide public health problem. An immunosuppressor microenvironment has been proposed to contribute to viral persistence during chronic disease. Understanding the intracellular signaling cascade in T-cells from HBV-infected patients, will contribute to unravel the mechanisms that control the development of immune response during hepatitis B. We analyze lipid rafts formation and early activation signals in chronic HBV infected patients, compared to naturally immune subjects (NIS). Patients show: (1) diminished GM1 clustering, (2) A deficient lipid rafts recruitment of CD3ζ/ZAP-70/Grb2, and (3) these proteins do not merge with GM1 within the lipid rafts. Finally, immunoprecipitation assays proved that ZAP-70 does not associate to CD3ζ. These results show for the first time, defects regarding early key events in T-cell activation, in chronically infected HBV patients, which may contribute not only to understand HBV immune tolerance, but to reveal new potential therapeutic targets to control the infection.
[Mh] Termos MeSH primário: Complexo CD3/imunologia
Proteína Adaptadora GRB2/imunologia
Vírus da Hepatite B/imunologia
Hepatite B Crônica/imunologia
Microdomínios da Membrana/imunologia
Linfócitos T/imunologia
Proteína-Tirosina Quinase ZAP-70/imunologia
[Mh] Termos MeSH secundário: Imunidade Adaptativa
Complexo CD3/metabolismo
Citometria de Fluxo
Proteína Adaptadora GRB2/metabolismo
Hepatite B Crônica/metabolismo
Hepatite B Crônica/virologia
Seres Humanos
Leucócitos Mononucleares/imunologia
Leucócitos Mononucleares/metabolismo
Microdomínios da Membrana/metabolismo
Microscopia de Fluorescência
RNA Viral/química
RNA Viral/genética
Reação em Cadeia da Polimerase em Tempo Real
Proteínas Ativadoras de Esfingolipídeos/imunologia
Linfócitos T/metabolismo
Proteína-Tirosina Quinase ZAP-70/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CD3 Complex); 0 (CD3 antigen, zeta chain); 0 (GRB2 Adaptor Protein); 0 (RNA, Viral); 0 (Sphingolipid Activator Proteins); EC 2.7.10.2 (ZAP-70 Protein-Tyrosine Kinase); EC 2.7.10.2 (ZAP70 protein, human)
[Em] Mês de entrada:1403
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130807
[St] Status:MEDLINE


  7 / 207 MEDLINE  
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[PMID]:23229750
[Au] Autor:Sandhoff K
[Ad] Endereço:LIMES c/o Kekulé-Institut, University of Bonn, Bonn, Germany .sandhoff@uni-bonn.de
[Ti] Título:My journey into the world of sphingolipids and sphingolipidoses.
[So] Source:Proc Jpn Acad Ser B Phys Biol Sci;88(10):554-82, 2012.
[Is] ISSN:1349-2896
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Analysis of lipid storage in postmortem brains of patients with amaurotic idiocy led to the recognition of five lysosomal ganglioside storage diseases and identification of their inherited metabolic blocks. Purification of lysosomal acid sphingomyelinase and ceramidase and analysis of their gene structures were the prerequisites for the clarification of Niemann-Pick and Farber disease. For lipid catabolism, intraendosomal vesicles are formed during the endocytotic pathway. They are subjected to lipid sorting processes and were identified as luminal platforms for cellular lipid and membrane degradation. Lipid binding glycoproteins solubilize lipids from these cholesterol poor membranes and present them to water-soluble hydrolases for digestion. Biosynthesis and intracellular trafficking of lysosomal hydrolases (hexosaminidases, acid sphingomyelinase and ceramidase) and lipid binding and transfer proteins (GM2 activator, saposins) were analyzed to identify the molecular and metabolic basis of several sphingolipidoses. Studies on the biosynthesis of glycosphingolipids yielded the scheme of Combinatorial Ganglioside Biosynthesis involving promiscuous glycosyltransferases. Their defects in mutagenized mice impair brain development and function.
[Mh] Termos MeSH primário: Esfingolipidoses/metabolismo
Esfingolipídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Encéfalo/metabolismo
Encéfalo/patologia
Endocitose
Seres Humanos
Lisossomos/enzimologia
Lisossomos/metabolismo
Proteínas Ativadoras de Esfingolipídeos/química
Proteínas Ativadoras de Esfingolipídeos/metabolismo
Esfingolipidoses/enzimologia
Esfingolipidoses/genética
Esfingolipidoses/patologia
Esfingolipídeos/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Sphingolipid Activator Proteins); 0 (Sphingolipids)
[Em] Mês de entrada:1310
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121212
[St] Status:MEDLINE


  8 / 207 MEDLINE  
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[PMID]:22507308
[Au] Autor:Uncini A
[Ad] Endereço:Department of Neuroscience and Imaging, University G. d'Annunzio, Chieti-Pescara, Italy. uncini@unich.it
[Ti] Título:A common mechanism and a new categorization for anti-ganglioside antibody-mediated neuropathies.
[So] Source:Exp Neurol;235(2):513-6, 2012 Jun.
[Is] ISSN:1090-2430
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Serum antibodies to different gangliosides have been identified in some Guillain-Barré (GBS) subtypes and variants. In the January issue of Experimental Neurology Susuki and colleagues (2012) showed that in experimental neuropathies associated with antibodies to GM1, GD1a and GD1b the common mechanism is a complement mediated dysfunction and disruption of the nodes of Ranvier which causes a pathophysiological continuum from early reversible conduction failure to axonal degeneration. These observations, correlated and integrated with electrophysiological and pathological findings in humans indicate that the GBS subtypes acute motor conduction block neuropathy, acute motor axonal neuropathy, acute motor and sensory neuropathy and acute sensory neuropathy and possibly also a chronic disorder as multifocal motor neuropathy represent a spectrum of the same immunopathologic process. Being the nodal axolemma and the paranode the focus of the nerve injury, these immune mediated neuropathies could be more properly classified as nodo-paranodopathies.
[Mh] Termos MeSH primário: Autoanticorpos/fisiologia
Gangliosídeos/imunologia
Polineuropatias/classificação
Polineuropatias/imunologia
[Mh] Termos MeSH secundário: Animais
Autoanticorpos/classificação
Síndrome de Guillain-Barré/classificação
Síndrome de Guillain-Barré/imunologia
Síndrome de Guillain-Barré/metabolismo
Seres Humanos
Polineuropatias/metabolismo
Proteínas Ativadoras de Esfingolipídeos/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Autoantibodies); 0 (Gangliosides); 0 (Sphingolipid Activator Proteins); 12707-58-3 (ganglioside, GD1a); 19553-76-5 (ganglioside, GD1b)
[Em] Mês de entrada:1206
[Cu] Atualização por classe:120504
[Lr] Data última revisão:
120504
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120418
[St] Status:MEDLINE
[do] DOI:10.1016/j.expneurol.2012.03.023


  9 / 207 MEDLINE  
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[PMID]:20021345
[Au] Autor:Misasi R; Hozumi I; Inuzuka T; Capozzi A; Mattei V; Kuramoto Y; Shimeno H; Soeda S; Azuma N; Yamauchi T; Hiraiwa M
[Ad] Endereço:Department of Geriatric and Neurology, Gifu University, School of Medicine, Gifu, Japan.
[Ti] Título:Biochemistry and neurobiology of prosaposin: a potential therapeutic neuro-effector.
[So] Source:Cent Nerv Syst Agents Med Chem;9(2):119-31, 2009 Jun.
[Is] ISSN:1875-6166
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Prosaposin, a 66 kDa glycoprotein, was identified initially as the precursor of the sphingolipid activator proteins, saposins A-D, which are required for the enzymatic hydrolysis of certain sphingolipids by lysosomal hydrolases. While mature saposins are distributed to lysosomes, prosaposin exists in secretory body fluids and plasma membranes. In addition to its role as the precursor, prosaposin shows a variety of neurotrophic and myelinotrophic activities through a receptor-mediated mechanism. In studies in vivo, prosaposin was demonstrated to exert a variety of neuro-efficacies capable of preventing neuro-degeneration following neuro-injury and promoting the amelioration of allodynia and hyperalgesia in pain models. Collective findings indicate that prosaposin is not a simple house-keeping precursor protein; instead, it is a protein essentially required for the development and maintenance of the central and peripheral nervous systems. Accumulating evidence over the last decade has attracted interests in exploring and developing new therapeutic approaches using prosaposin for human disorders associated with neuro-degeneration. In this review we detail the structure characteristics, cell biological feature, in vivo efficacy, and neuro-therapeutic potential of prosaposin, thereby providing future prospective in clinical application of this multifunctional protein.
[Mh] Termos MeSH primário: Bioquímica
Transporte Biológico/fisiologia
Glicoproteínas/uso terapêutico
Neurobiologia
Sistema Nervoso Periférico/fisiologia
Precursores de Proteínas/metabolismo
Saposinas/fisiologia
Proteínas Ativadoras de Esfingolipídeos/uso terapêutico
[Mh] Termos MeSH secundário: Processamento Alternativo/genética
Sequência de Aminoácidos
Sequência Conservada/genética
Sequência Conservada/fisiologia
Feminino
Seres Humanos
Lactação/metabolismo
Metabolismo dos Lipídeos/fisiologia
Dados de Sequência Molecular
Fatores de Crescimento Neural/fisiologia
Precursores de Proteínas/genética
Saposinas/genética
Saposinas/metabolismo
Proteínas Ativadoras de Esfingolipídeos/metabolismo
Distribuição Tecidual/fisiologia
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Nerve Growth Factors); 0 (Protein Precursors); 0 (Saposins); 0 (Sphingolipid Activator Proteins)
[Em] Mês de entrada:1004
[Cu] Atualização por classe:091221
[Lr] Data última revisão:
091221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:091222
[St] Status:MEDLINE


  10 / 207 MEDLINE  
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[PMID]:19955343
[Au] Autor:Al-Hassnan ZN; Al Dhalaan H; Patay Z; Faqeih E; Al-Owain M; Al-Duraihem A; Faiyaz-Ul-Haque M
[Ad] Endereço:Department of Medical Genetics, King Faisal Specialist Hospital and Research Centre (KFSH&RC), Riyadh, Saudi Arabia. zhassnan@kfshrc.edu.sa
[Ti] Título:Sphingolipid activator protein B deficiency: report of 9 Saudi patients and review of the literature.
[So] Source:J Child Neurol;24(12):1513-9, 2009 Dec.
[Is] ISSN:1708-8283
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutated PSAP gene resulting in sphingolipid activator protein B deficiency is known to cause metachromatic leukodystrophy variant in which arylsulfatase A is normal. Of 16 patients with metachromatic leukodystrophy that were evaluated in our center, 7 patients were diagnosed with arylsulfatase A-deficient metachromatic leukodystrophy, whereas 9 children from 4 unrelated Saudi families were found to have sphingolipid activator protein B deficiency. PSAP analysis found that the 4 families segregate the same homozygous mutation that was a g.722G>C transversion resulting in C241S change, which was previously reported in an Arab patient. Our work, which reports the largest series of patients with sphingolipid activator protein B deficiency, suggests that this variant is likely to be more common than arylsulfatase A-deficient metachromatic leukodystrophy in Arabs, a notion that has potential diagnostic and preventive implications.
[Mh] Termos MeSH primário: Predisposição Genética para Doença/genética
Leucodistrofia Metacromática/genética
Leucodistrofia Metacromática/metabolismo
Mutação/genética
Proteínas Ativadoras de Esfingolipídeos/deficiência
Proteínas Ativadoras de Esfingolipídeos/genética
[Mh] Termos MeSH secundário: Substituição de Aminoácidos/genética
Sistema Nervoso Central/metabolismo
Sistema Nervoso Central/fisiopatologia
Criança
Pré-Escolar
Análise Mutacional de DNA
Feminino
Marcadores Genéticos/genética
Testes Genéticos
Genótipo
Seres Humanos
Lactente
Leucodistrofia Metacromática/fisiopatologia
Masculino
Arábia Saudita
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Genetic Markers); 0 (Sphingolipid Activator Proteins)
[Em] Mês de entrada:1003
[Cu] Atualização por classe:091203
[Lr] Data última revisão:
091203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:091204
[St] Status:MEDLINE
[do] DOI:10.1177/0883073809341269



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