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[PMID]:28449103
[Au] Autor:Li H; Pei W; Vergarajauregui S; Zerfas PM; Raben N; Burgess SM; Puertollano R
[Ad] Endereço:Cell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
[Ti] Título:Novel degenerative and developmental defects in a zebrafish model of mucolipidosis type IV.
[So] Source:Hum Mol Genet;26(14):2701-2718, 2017 07 15.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mucolipidosis type IV (MLIV) is a lysosomal storage disease characterized by neurologic and ophthalmologic abnormalities. There is currently no effective treatment. MLIV is caused by mutations in MCOLN1, a lysosomal cation channel from the transient receptor potential (TRP) family. In this study, we used genome editing to knockout the two mcoln1 genes present in Danio rerio (zebrafish). Our model successfully reproduced the retinal and neuromuscular defects observed in MLIV patients, indicating that this model is suitable for studying the disease pathogenesis. Importantly, our model revealed novel insights into the origins and progression of the MLIV pathology, including the contribution of autophagosome accumulation to muscle dystrophy and the role of mcoln1 in embryonic development, hair cell viability and cellular maintenance. The generation of a MLIV model in zebrafish is particularly relevant given the suitability of this organism for large-scale in vivo drug screening, thus providing unprecedented opportunities for therapeutic discovery.
[Mh] Termos MeSH primário: Mucolipidoses/genética
Canais de Receptores Transientes de Potencial/genética
Proteínas de Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Autofagossomos/metabolismo
Modelos Animais de Doenças
Técnicas de Inativação de Genes
Mucolipidoses/metabolismo
Mucolipidoses/patologia
Mutação
Canais de Receptores Transientes de Potencial/metabolismo
Peixe-Zebra
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (MCOLN1.1 protein, zebrafish); 0 (Transient Receptor Potential Channels); 0 (Zebrafish Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180225
[Lr] Data última revisão:
180225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddx158


  2 / 967 MEDLINE  
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[PMID]:29289611
[Au] Autor:Kazemi N; Estiar MA; Fazilaty H; Sakhinia E
[Ad] Endereço:Immunology Research Center, Tabriz University of Medical Sciences, Tabriz, Iran; Division of Medical Genetics, Department of Clinical Biochemistry, Faculty of Medicine, Tabriz University of Medical Sciences, Tabriz, Iran.
[Ti] Título:Variants in GNPTAB, GNPTG and NAGPA genes are associated with stutterers.
[So] Source:Gene;647:93-100, 2018 Mar 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Non-syndromic stuttering is a neurodevelopmental disorder characterized by disruptions in normal flow of speech in the form of repetition, prolongation and involuntary halts. Previously, mutations with more severe effects on GNPTAB and GNPTG have been reported to cause Mucolipidosisll (ML-ll) and Mucolipidosislll (ML-lll), two lysosomal storage disorders with multiple pathologies. We used homozygosity mapping and Sanger sequencing to investigate variants of the three genes in 25 Iranian families with at least two first degree related non-syndromic stutterers. Bioinformatic evaluation and Segregation analysis of the found variants helped us define probable consequences. We also compared our findings with those related to Mucolipidosis. 14 variations were found in the three genes 3 of which, including a novel variant within intronic region of GNPTG and a heterozygous 2-bp deletion in coding region of GNPTAB, co-segregated with stuttering in the families they were found. Bioinformatics analysis predicted all three variants causing deleterious effects on gene functioning. Our findings support the role of these three variants in non-syndromic stuttering. This finding may challenge the current belief that variations causing stuttering are at different sites and have less severe consequences than genetic changes that cause ML-ll and ML-lll.
[Mh] Termos MeSH primário: Predisposição Genética para Doença/genética
Mutação/genética
Diester Fosfórico Hidrolases/genética
Gagueira/genética
Transferases (Outros Grupos de Fosfato Substituídos)/genética
[Mh] Termos MeSH secundário: Criança
Pré-Escolar
Feminino
Heterozigoto
Homozigoto
Seres Humanos
Íntrons/genética
Masculino
Mucolipidoses/genética
Fenótipo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.8.- (Transferases (Other Substituted Phosphate Groups)); EC 2.7.8.15 (GNPTAB protein, human); EC 2.7.8.17 (GNPTG protein, human); EC 3.1.4.- (Phosphoric Diester Hydrolases); EC 3.1.4.45 (N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180101
[St] Status:MEDLINE


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[PMID]:28442549
[Au] Autor:Pan X; De Aragão CBP; Velasco-Martin JP; Priestman DA; Wu HY; Takahashi K; Yamaguchi K; Sturiale L; Garozzo D; Platt FM; Lamarche-Vane N; Morales CR; Miyagi T; Pshezhetsky AV
[Ad] Endereço:Sainte-Justine University Hospital Research Center, University of Montreal, Montreal, Quebec, Canada.
[Ti] Título:Neuraminidases 3 and 4 regulate neuronal function by catabolizing brain gangliosides.
[So] Source:FASEB J;31(8):3467-3483, 2017 Aug.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gangliosides (sialylated glycolipids) play an essential role in the CNS by regulating recognition and signaling in neurons. Metabolic blocks in processing and catabolism of gangliosides result in the development of severe neurologic disorders, including gangliosidoses manifesting with neurodegeneration and neuroinflammation. We demonstrate that 2 mammalian enzymes, neuraminidases 3 and 4, play important roles in catabolic processing of brain gangliosides by cleaving terminal sialic acid residues in their glycan chains. In neuraminidase 3 and 4 double-knockout mice, G ganglioside is stored in microglia, vascular pericytes, and neurons, causing micro- and astrogliosis, neuroinflammation, accumulation of lipofuscin bodies, and memory loss, whereas their cortical and hippocampal neurons have lower rate of neuritogenesis Double-knockout mice also have reduced levels of G ganglioside and myelin in neuronal axons. Furthermore, neuraminidase 3 deficiency drastically increased storage of G in the brain tissues of an asymptomatic mouse model of Tay-Sachs disease, a severe human gangliosidosis, indicating that this enzyme is responsible for the metabolic bypass of ß-hexosaminidase A deficiency. Together, our results provide the first evidence that neuraminidases 3 and 4 have important roles in CNS function by catabolizing gangliosides and preventing their storage in lipofuscin bodies.-Pan, X., De Britto Pará De Aragão, C., Velasco-Martin, J. P., Priestman, D. A., Wu, H. Y., Takahashi, K., Yamaguchi, K., Sturiale, L., Garozzo, D., Platt, F. M., Lamarche-Vane, N., Morales, C. R., Miyagi, T., Pshezhetsky, A. V. Neuraminidases 3 and 4 regulate neuronal function by catabolizing brain gangliosides.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Gangliosídeos/metabolismo
Neuraminidase/metabolismo
Neurônios/fisiologia
[Mh] Termos MeSH secundário: Animais
Encéfalo/patologia
Células Cultivadas
Embrião de Mamíferos
Regulação Enzimológica da Expressão Gênica
Camundongos
Camundongos Knockout
Atividade Motora/fisiologia
Mucolipidoses/metabolismo
Neuraminidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gangliosides); EC 3.2.1.18 (Neu3 protein, mouse); EC 3.2.1.18 (Neu4 protein, mouse); EC 3.2.1.18 (Neuraminidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170427
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601299R


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[PMID]:28392473
[Au] Autor:Segal P; Pode-Shakked B; Raas-Rothschild A
[Ad] Endereço:Department of Psychology, Hebrew University, Jerusalem, Israel.
[Ti] Título:Elucidating the behavioral phenotype of patients affected with mucolipidosis IV: What can we learn from the parents?
[So] Source:Eur J Med Genet;60(6):340-344, 2017 Jun.
[Is] ISSN:1878-0849
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Mucolipidosis type IV (ML-IV) is a rare autosomal recessive lysosomal storage disorder which presents with nonspecific developmental delay. Nowadays with the use of new tools such as next generation sequencing, more ML-IV affected patients are diagnosed. Still, identifying the behavioral phenotype might be of help for early diagnosis and anticipatory guidance, as well as for counseling of the families. OBJECTIVE: Identification of the behavioral characteristics of 12 ML-IV patients, aged from 2.5 to 34 years, based on their caregivers' observations. METHODS: The information was gathered from the patients' parents using an extensive semi-structured interview especially designed for this study. Each interview lasted approximately three hours. RESULTS: Patients were uniformly described as friendly and show explicit pleasure from both social interactions and music. They all presented delays in psychomotor development, while their general health was reported as good. Parents reported that the patients present deterioration of motor and communication skills over the years. Episodes of ocular pain, with ipsilateral flushing of the face and tearing were frequently reported, as was shortening of the Achilles tendon. Since the identification of the ML-IV gene, diagnosis is made earlier in life. CONCLUSION: We suggest that ML-IV be considered in the differential diagnosis of patients with developmental delay, who present the behavioral phenotype reported here. This pattern could also be useful for the ancitipatory guidance in the care of ML-IV affected patients. Further clinical research is warranted to confirm these preliminary findings.
[Mh] Termos MeSH primário: Comportamento Infantil
Mucolipidoses/diagnóstico
Fenótipo
[Mh] Termos MeSH secundário: Adolescente
Adulto
Criança
Pré-Escolar
Diagnóstico Diferencial
Feminino
Seres Humanos
Masculino
Destreza Motora
Mucolipidoses/genética
Pais
Comportamento Social
Canais de Receptores Transientes de Potencial/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MCOLN1 protein, human); 0 (Transient Receptor Potential Channels)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE


  5 / 967 MEDLINE  
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[PMID]:28112729
[Au] Autor:Li M; Zhang WK; Benvin NM; Zhou X; Su D; Li H; Wang S; Michailidis IE; Tong L; Li X; Yang J
[Ad] Endereço:Department of Biological Sciences, Columbia University, New York, New York, USA.
[Ti] Título:Structural basis of dual Ca /pH regulation of the endolysosomal TRPML1 channel.
[So] Source:Nat Struct Mol Biol;24(3):205-213, 2017 Mar.
[Is] ISSN:1545-9985
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The activities of organellar ion channels are often regulated by Ca and H , which are present in high concentrations in many organelles. Here we report a structural element critical for dual Ca /pH regulation of TRPML1, a Ca -release channel crucial for endolysosomal function. TRPML1 mutations cause mucolipidosis type IV (MLIV), a severe lysosomal storage disorder characterized by neurodegeneration, mental retardation and blindness. We obtained crystal structures of the 213-residue luminal domain of human TRPML1 containing three missense MLIV-causing mutations. This domain forms a tetramer with a highly electronegative central pore formed by a novel luminal pore loop. Cysteine cross-linking and cryo-EM analyses confirmed that this architecture occurs in the full-length channel. Structure-function studies demonstrated that Ca and H interact with the luminal pore and exert physiologically important regulation. The MLIV-causing mutations disrupt the luminal-domain structure and cause TRPML1 mislocalization. Our study reveals the structural underpinnings of TRPML1's regulation, assembly and pathogenesis.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Endossomos/metabolismo
Lisossomos/metabolismo
Canais de Cátion TRPM/química
Canais de Cátion TRPM/metabolismo
[Mh] Termos MeSH secundário: Aminoácidos/química
Cristalografia por Raios X
Células HEK293
Seres Humanos
Concentração de Íons de Hidrogênio
Modelos Moleculares
Mucolipidoses/genética
Mutação de Sentido Incorreto
Ligação Proteica
Multimerização Proteica
Subunidades Proteicas/metabolismo
Reprodutibilidade dos Testes
Eletricidade Estática
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Protein Subunits); 0 (TRPM Cation Channels); 0 (TRPM1 protein, human); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170124
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3362


  6 / 967 MEDLINE  
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[PMID]:28065440
[Au] Autor:Kubaski F; Suzuki Y; Orii K; Giugliani R; Church HJ; Mason RW; Dung VC; Ngoc CT; Yamaguchi S; Kobayashi H; Girisha KM; Fukao T; Orii T; Tomatsu S
[Ad] Endereço:Nemours/Alfred I. duPont Hospital for Children, Wilmington, DE, United States; Department of Biological Sciences, University of Delaware, Newark, DE, United States; INAGEMP, Porto Alegre, Brazil.
[Ti] Título:Glycosaminoglycan levels in dried blood spots of patients with mucopolysaccharidoses and mucolipidoses.
[So] Source:Mol Genet Metab;120(3):247-254, 2017 Mar.
[Is] ISSN:1096-7206
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mucopolysaccharidoses (MPSs) and mucolipidoses (ML) are groups of lysosomal storage disorders in which lysosomal hydrolases are deficient leading to accumulation of undegraded glycosaminoglycans (GAGs), throughout the body, subsequently resulting in progressive damage to multiple tissues and organs. Assays using tandem mass spectrometry (MS/MS) have been established to measure GAGs in serum or plasma from MPS and ML patients, but few studies were performed to determine whether these assays are sufficiently robust to measure GAG levels in dried blood spots (DBS) of patients with MPS and ML. MATERIAL AND METHODS: In this study, we evaluated GAG levels in DBS samples from 124 MPS and ML patients (MPS I=16; MPS II=21; MPS III=40; MPS IV=32; MPS VI=10; MPS VII=1; ML=4), and compared them with 115 age-matched controls. Disaccharides were produced from polymer GAGs by digestion with chondroitinase B, heparitinase, and keratanase II. Subsequently, dermatan sulfate (DS), heparan sulfate (HS-0S, HS-NS), and keratan sulfate (mono-sulfated KS, di-sulfated KS, and ratio of di-sulfated KS in total KS) were measured by MS/MS. RESULTS: Untreated patients with MPS I, II, VI, and ML had higher levels of DS compared to control samples. Untreated patients with MPS I, II, III, VI, and ML had higher levels of HS-0S; and untreated patients with MPS II, III and VI and ML had higher levels of HS-NS. Levels of KS were age dependent, so although levels of both mono-sulfated KS and di-sulfated KS were generally higher in patients, particularly for MPS II and MPS IV, age group numbers were not sufficient to determine significance of such changes. However, the ratio of di-sulfated KS in total KS was significantly higher in all MPS patients younger than 5years old, compared to age-matched controls. MPS I and VI patients treated with HSCT had normal levels of DS, and MPS I, VI, and VII treated with ERT or HSCT had normal levels of HS-0S and HS-NS, indicating that both treatments are effective in decreasing blood GAG levels. CONCLUSION: Measurement of GAG levels in DBS is useful for diagnosis and potentially for monitoring the therapeutic efficacy in MPS.
[Mh] Termos MeSH primário: Teste em Amostras de Sangue Seco/métodos
Glicosaminoglicanos/sangue
Mucolipidoses/diagnóstico
Mucopolissacaridoses/diagnóstico
[Mh] Termos MeSH secundário: Adolescente
Adulto
Fatores Etários
Criança
Pré-Escolar
Cromatografia Líquida
Dermatan Sulfato/sangue
Feminino
Heparitina Sulfato/sangue
Seres Humanos
Lactente
Recém-Nascido
Sulfato de Ceratano/sangue
Masculino
Mucolipidoses/metabolismo
Mucopolissacaridoses/metabolismo
Sensibilidade e Especificidade
Espectrometria de Massas em Tandem
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycosaminoglycans); 24967-94-0 (Dermatan Sulfate); 9050-30-0 (Heparitin Sulfate); 9056-36-4 (Keratan Sulfate)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170110
[St] Status:MEDLINE


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[PMID]:28062798
[Au] Autor:Markmann S; Krambeck S; Hughes CJ; Mirzaian M; Aerts JM; Saftig P; Schweizer M; Vissers JP; Braulke T; Damme M
[Ad] Endereço:From the ‡Department of Biochemistry, Children's Hospital, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.
[Ti] Título:Quantitative Proteome Analysis of Mouse Liver Lysosomes Provides Evidence for Mannose 6-phosphate-independent Targeting Mechanisms of Acid Hydrolases in Mucolipidosis II.
[So] Source:Mol Cell Proteomics;16(3):438-450, 2017 Mar.
[Is] ISSN:1535-9484
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The efficient receptor-mediated targeting of soluble lysosomal proteins to lysosomes requires the modification with mannose 6-phosphate (M6P) residues. Although the absence of M6P results in misrouting and hypersecretion of lysosomal enzymes in many cells, normal levels of lysosomal enzymes have been reported in liver of patients lacking the M6P-generating phosphotransferase (PT). The identity of lysosomal proteins depending on M6P has not yet been comprehensively analyzed. In this study we purified lysosomes from liver of PT-defective mice and 67 known soluble lysosomal proteins were identified that illustrated quantitative changes using an ion mobility-assisted data-independent label-free LC-MS approach. After validation of various differentially expressed lysosomal components by Western blotting and enzyme activity assays, the data revealed a small number of lysosomal proteins depending on M6P, including neuraminidase 1, cathepsin F, Npc2, and cathepsin L, whereas the majority reach lysosomes by alternative pathways. These data were compared with findings on cultured hepatocytes and liver sinusoid endothelial cells isolated from the liver of wild-type and PT-defective mice. Our findings show that the relative expression, targeting efficiency and lysosomal localization of lysosomal proteins tested in cultured hepatic cells resemble their proportion in isolated liver lysosomes. Hypersecretion of newly synthesized nonphosphorylated lysosomal proteins suggest that secretion-recapture mechanisms contribute to maintain major lysosomal functions in liver.
[Mh] Termos MeSH primário: Hidrolases/metabolismo
Lisossomos/metabolismo
Manosefosfatos/metabolismo
Mucolipidoses/enzimologia
Proteoma/análise
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Cromatografia Líquida
Modelos Animais de Doenças
Regulação da Expressão Gênica
Fígado/metabolismo
Espectrometria de Massas
Camundongos
Mucolipidoses/genética
Fosfotransferases/deficiência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mannosephosphates); 0 (Proteome); 3672-15-9 (mannose-6-phosphate); EC 2.7.- (Phosphotransferases); EC 3.- (Hydrolases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170108
[St] Status:MEDLINE
[do] DOI:10.1074/mcp.M116.063636


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[PMID]:27797444
[Au] Autor:Ferreira CR; Devaney JM; Hofherr SE; Pollard LM; Cusmano-Ozog K
[Ad] Endereço:National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland.
[Ti] Título:Hereditary fructose intolerance mimicking a biochemical phenotype of mucolipidosis: A review of the literature of secondary causes of lysosomal enzyme activity elevation in serum.
[So] Source:Am J Med Genet A;173(2):501-509, 2017 Feb.
[Is] ISSN:1552-4833
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We describe a patient with failure to thrive, hepatomegaly, liver dysfunction, and elevation of multiple plasma lysosomal enzyme activities mimicking mucolipidosis II or III, in whom a diagnosis of hereditary fructose intolerance (HFI) was ultimately obtained. She presented before introduction of solid foods, given her consumption of a fructose-containing infant formula. We present the most extensive panel of lysosomal enzyme activities reported to date in a patient with HFI, and propose that multiple enzyme elevations in plasma, especially when in conjunction with a normal plasma α-mannosidase activity, should elicit a differential diagnosis of HFI. We also performed a review of the literature on the different etiologies of elevated lysosomal enzyme activities in serum or plasma. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Intolerância à Frutose/diagnóstico
Mucolipidoses/diagnóstico
[Mh] Termos MeSH secundário: Biomarcadores/sangue
Diagnóstico Diferencial
Ativação Enzimática
Feminino
Intolerância à Frutose/sangue
Intolerância à Frutose/genética
Seres Humanos
Lactente
Leucócitos/enzimologia
Lisossomos/enzimologia
Mucolipidoses/sangue
Mucolipidoses/genética
Fenótipo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biomarkers)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161101
[St] Status:MEDLINE
[do] DOI:10.1002/ajmg.a.38023


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[PMID]:27532546
[Au] Autor:Gonzales E; Taylor SA; Davit-Spraul A; Thébaut A; Thomassin N; Guettier C; Whitington PF; Jacquemin E
[Ad] Endereço:Pediatric Hepatology and Pediatric Liver Transplantation Unit and National Reference Centre for Rare Pediatric Liver Diseases, Bicêtre University Hospital, University of Paris-Sud, Assistance Publique-Hôpitaux de Paris, Le Kremlin Bicêtre, France.
[Ti] Título:MYO5B mutations cause cholestasis with normal serum gamma-glutamyl transferase activity in children without microvillous inclusion disease.
[So] Source:Hepatology;65(1):164-173, 2017 Jan.
[Is] ISSN:1527-3350
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Some patients with microvillus inclusion disease due to myosin 5B (MYO5B) mutations may develop cholestasis characterized by a progressive familial intrahepatic cholestasis-like phenotype with normal serum gamma-glutamyl transferase activity. So far MYO5B deficiency has not been reported in patients with such a cholestasis phenotype in the absence of intestinal disease. Using a new-generation sequencing approach, we identified MYO5B mutations in five patients with progressive familial intrahepatic cholestasis-like phenotype with normal serum gamma-glutamyl transferase activity without intestinal disease. CONCLUSION: These data show that MYO5B deficiency may lead to isolated cholestasis and that MYO5B should be considered as an additional progressive familial intrahepatic cholestasis gene. (Hepatology 2017;65:164-173).
[Mh] Termos MeSH primário: Colestase Intra-Hepática/sangue
Colestase Intra-Hepática/genética
Mutação
Cadeias Pesadas de Miosina/genética
Miosina Tipo V/genética
gama-Glutamiltransferase/sangue
[Mh] Termos MeSH secundário: Colestase Intra-Hepática/enzimologia
Feminino
Seres Humanos
Lactente
Síndromes de Malabsorção
Masculino
Microvilosidades/patologia
Mucolipidoses
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MYO5B protein, human); EC 2.3.2.2 (gamma-Glutamyltransferase); EC 3.6.1.- (Myosin Type V); EC 3.6.4.1 (Myosin Heavy Chains)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160818
[St] Status:MEDLINE
[do] DOI:10.1002/hep.28779


  10 / 967 MEDLINE  
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[PMID]:27984607
[Au] Autor:Mao M; Guo L; Zhang Z; Wang B; Huang S; Song Y; Chen F; Wen W
[Ad] Endereço:Center of Clinical Laboratory Medicine, The First Affiliated Hospital, Jinan University, Guangzhou, Guangdong 510630, China. songyuanzong@vip.tom.com; . wenwangrong@yeah.net.
[Ti] Título:[Phenotypic and genetic analysis of a family affected with microvillus inclusion disease].
[So] Source:Zhonghua Yi Xue Yi Chuan Xue Za Zhi;33(6):792-796, 2016 Dec 10.
[Is] ISSN:1003-9406
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To explore the clinical features and mutations of MYO5B gene in a family affected with microvillus inclusion disease. METHODS: Clinical data of an infant affected with microvillus inclusion disease was collected. Genomic DNA was extracted from peripheral blood samples from the patient and her parents. PCR amplification and Sanger sequencing were performed to analyze all the exons and their flanking sequences of the MYO5B gene. RESULTS: The patient presented with complicated manifestations including respiratory distress syndrome, dehydration, acidosis, bowel dilatation, liver and kidney dysfunction, and severe and intractable diarrhea. A compound mutation of the MYO5B gene, i.e., IVS37-1G>C/c.2729_2731delC (p.R911Afs916X), was discovered in the patient. The former was a splice-site mutation inherited from the mother, while the latter was a frameshift mutation inherited from the father. Both were not reported previously. CONCLUSION: Based on the clinical and molecular evidence, the patient was diagnosed with microvillus inclusion disease. Above finding has expanded the mutation spectrum of the MYO5B gene, which can provide valuable information for genetic counseling for the family.
[Mh] Termos MeSH primário: Síndromes de Malabsorção/genética
Microvilosidades/patologia
Mucolipidoses/genética
Mutação/genética
[Mh] Termos MeSH secundário: Família
Feminino
Testes Genéticos/métodos
Genótipo
Seres Humanos
Lactente
Masculino
Microvilosidades/genética
Cadeias Pesadas de Miosina/genética
Miosina Tipo V/genética
Fenótipo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MYO5B protein, human); EC 3.6.1.- (Myosin Type V); EC 3.6.4.1 (Myosin Heavy Chains)
[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:161217
[St] Status:MEDLINE



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