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  1 / 101 MEDLINE  
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[PMID]:28437447
[Au] Autor:Renner SW; Walker LM; Forsberg LJ; Sexton JZ; Brenman JE
[Ad] Endereço:Genetics and Molecular Biology Curriculum, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
[Ti] Título:Carbonic anhydrase III (Car3) is not required for fatty acid synthesis and does not protect against high-fat diet induced obesity in mice.
[So] Source:PLoS One;12(4):e0176502, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Carbonic anhydrases are a family of enzymes that catalyze the reversible condensation of water and carbon dioxide to carbonic acid, which spontaneously dissociates to bicarbonate. Carbonic anhydrase III (Car3) is nutritionally regulated at both the mRNA and protein level. It is highly enriched in tissues that synthesize and/or store fat: liver, white adipose tissue, brown adipose tissue, and skeletal muscle. Previous characterization of Car3 knockout mice focused on mice fed standard diets, not high-fat diets that significantly alter the tissues that highly express Car3. We observed lower protein levels of Car3 in high-fat diet fed mice treated with niclosamide, a drug published to improve fatty liver symptoms in mice. However, it is unknown if Car3 is simply a biomarker reflecting lipid accumulation or whether it has a functional role in regulating lipid metabolism. We focused our in vitro studies toward metabolic pathways that require bicarbonate. To further determine the role of Car3 in metabolism, we measured de novo fatty acid synthesis with in vitro radiolabeled experiments and examined metabolic biomarkers in Car3 knockout and wild type mice fed high-fat diet. Specifically, we analyzed body weight, body composition, metabolic rate, insulin resistance, serum and tissue triglycerides. Our results indicate that Car3 is not required for de novo lipogenesis, and Car3 knockout mice fed high-fat diet do not have significant differences in responses to various diets to wild type mice.
[Mh] Termos MeSH primário: Anidrase Carbônica III/metabolismo
Dieta Hiperlipídica
Ácidos Graxos/biossíntese
Metabolismo dos Lipídeos/fisiologia
Lipogênese/genética
Obesidade/metabolismo
[Mh] Termos MeSH secundário: Tecido Adiposo Marrom/metabolismo
Tecido Adiposo Branco/metabolismo
Animais
Composição Corporal/fisiologia
Peso Corporal/fisiologia
Anidrase Carbônica III/genética
Resistência à Insulina/fisiologia
Fígado/metabolismo
Masculino
Camundongos
Camundongos Knockout
Músculo Esquelético/metabolismo
Obesidade/etiologia
Obesidade/genética
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Triglycerides); EC 4.2.1.- (Carbonic Anhydrase III)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170425
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0176502


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[PMID]:26847302
[Au] Autor:Min HJ; Hong SC; Yang HS; Mun SK; Lee SY
[Ad] Endereço:Department of Otorhinolaryngology-Head and Neck Surgery, Chung-Ang University College of Medicine, Seoul, Korea.
[Ti] Título:Expression of CAIII and Hsp70 Is Increased the Mucous Membrane of the Posterior Commissure in Laryngopharyngeal Reflux Disease.
[So] Source:Yonsei Med J;57(2):469-74, 2016 Mar.
[Is] ISSN:1976-2437
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:PURPOSE: We tried to evaluate the difference in the expression of carbonic anhydrase (CA) III and heat shock protein (Hsp) 70 between laryngopharyngeal reflux disease (LPRD) and non-LPRD patients. MATERIALS AND METHODS: The study involved 28 patients who underwent laryngeal microsurgery due to benign laryngeal disease from March to August 2008. Reflux symptom index (RSI) and reflux finding score (RFS) were measured for each person, and they were assigned either to the LPRD group (n=10) or non-LPRD group (n=18). Tissue samples were obtained from the mucosa of posterior commissure, and immunohistochemistry (IHC) staining of CAIII and Hsp70 was performed. The IHC scores were measured and compared with clinical features including RSI and RFS. RESULTS: Total 10 patients were assigned as LPRD group, and 18 patients were as control group. The mean IHC score of CAIII and Hsp70 was 1.70 ± 1.06 and 1.90 ± 0.88, respectively, in LPRD patients, whereas the mean IHC score of CAIII and Hsp70 was 0.78 ± 0.73 and 0.94 ± 0.87, respectively, in non-LPRD patients. The difference between two groups was statistically significant (p<0.05). CONCLUSION: CAIII and Hsp70 expressions were higher in LPRD patients that in non-LPRD patients, suggesting the possibility as one of biomomarker in LPRD diagnosis.
[Mh] Termos MeSH primário: Anidrase Carbônica III/metabolismo
Proteínas de Choque Térmico HSP70/metabolismo
Refluxo Laringofaríngeo/diagnóstico
Membrana Mucosa/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Biópsia
Estudos de Casos e Controles
Feminino
Seres Humanos
Imuno-Histoquímica
Refluxo Laringofaríngeo/cirurgia
Laringoscópios
Laringoscopia
Laringe
Masculino
Meia-Idade
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (HSP70 Heat-Shock Proteins); EC 4.2.1.- (Carbonic Anhydrase III)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170104
[Lr] Data última revisão:
170104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160206
[St] Status:MEDLINE
[do] DOI:10.3349/ymj.2016.57.2.469


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[PMID]:26182375
[Au] Autor:Fontana S; Schillaci O; Frinchi M; Giallombardo M; Morici G; Di Liberto V; Alessandro R; De Leo G; Perciavalle V; Belluardo N; Mudò G
[Ad] Endereço:Department of Biopathology and Medical Biotechnology, Section of Biology and Genetics, University of Palermo, I-90127 Palermo, Italy.
[Ti] Título:Reduction in mdx mouse muscle degeneration by low-intensity endurance exercise: a proteomic analysis in quadriceps muscle of exercised compared with sedentary mdx mice.
[So] Source:Biosci Rep;35(3), 2015 May 12.
[Is] ISSN:1573-4935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In our recent study was shown a significant recovery of damaged skeletal muscle of mice with X-linked muscular dystrophy (mdx) following low-intensity endurance exercise, probably by reducing the degeneration of dystrophic muscle. Consequently, in the present work, we aimed to identify proteins involved in the observed reduction in degenerating fibres. To this end, we used proteomic analysis to evaluate changes in the protein profile of quadriceps dystrophic muscles of exercised compared with sedentary mdx mice. Four protein spots were found to be significantly changed and were identified as three isoforms of carbonic anhydrase 3 (CA3) and superoxide dismutase [Cu-Zn] (SODC). Protein levels of CA3 isoforms were significantly up-regulated in quadriceps of sedentary mdx mice and were completely restored to wild-type (WT) mice values, both sedentary and exercised, in quadriceps of exercised mdx mice. Protein levels of SODC were down-regulated in quadriceps of sedentary mdx mice and were significantly restored to WT mice values, both sedentary and exercised, in quadriceps of exercised mdx mice. Western blot data were in agreement with those obtained using proteomic analysis and revealed the presence of one more CA3 isoform that was significantly changed. Based on data found in the present study, it seems that low-intensity endurance exercise may in part contribute to reduce cell degeneration process in mdx muscles, by counteracting oxidative stress.
[Mh] Termos MeSH primário: Proteínas Musculares/metabolismo
Resistência Física/fisiologia
Músculo Quadríceps/metabolismo
Músculo Quadríceps/fisiopatologia
[Mh] Termos MeSH secundário: Animais
Western Blotting
Anidrase Carbônica III/metabolismo
Eletroforese em Gel Bidimensional/métodos
Masculino
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos mdx
Distrofia Muscular de Duchenne/fisiopatologia
Proteômica/métodos
Reprodutibilidade dos Testes
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Muscle Proteins); EC 1.15.1.1 (Superoxide Dismutase); EC 4.2.1.- (Carbonic Anhydrase III)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150717
[St] Status:MEDLINE


  4 / 101 MEDLINE  
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[PMID]:26099944
[Au] Autor:Araujo GR; Vaz ER; Fujimura PT; Fonseca JE; de Lima LM; Canhão H; Venturini G; Cardozo KH; Carvalho VM; Napimoga MH; Goulart LR; Gonçalves J; Ueira-Vieira C
[Ad] Endereço:Laboratory of Nanobiotechnology, Institute of Genetics and Biochemistry, Federal University of Uberlândia, Uberlândia, MG, Brazil. galber.araujo@gmail.com.
[Ti] Título:Improved serological detection of rheumatoid arthritis: a highly antigenic mimotope of carbonic anhydrase III selected in a murine model by phage display.
[So] Source:Arthritis Res Ther;17:168, 2015 Jun 23.
[Is] ISSN:1478-6362
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Rheumatoid arthritis (RA) is a chronic inflammatory autoimmune disease that affects around 1% of the human population worldwide. RA diagnosis can be difficult as there is no definitive test for its detection. Therefore, the aim of this study was to identify biomarkers that could be used for RA diagnosis. METHODS: Sera from a collagen-induced arthritis mouse model were used to select potential biomarkers for RA diagnosis by phage display technology. In silico and in vitro analyses were performed to characterize and validate the selected peptides. Samples were classified into three groups: RA; two other immune-mediated rheumatic diseases (systemic lupus erythematosus (SLE) and ankylosing spondylitis (AS)); and healthy controls (HC). Enzyme-linked immunosorbent assay (ELISA) was carried out to determine antibody levels, and diagnostic parameters were determined by constructing receiver operating characteristic curves. Mass spectrometry and Western blot were performed to identify the putative autoantigen that was mimicked by a highly reactive mimotope. RESULTS: After three rounds of selection, 14 clones were obtained and tested for immunoreactivity analysis against sera from RA and HC groups. The phage-fused peptide with the highest immunoreactivity (M12) was synthesized, and was able to efficiently discriminate RA patients from SLE, AS and HCs (p < 0.0001) by ELISA. The specificity and sensitivity of anti-M12 antibodies for RA diagnosis were 91 % and 84.3 %, respectively. The M12 peptide was identified as one that mimics a predicted antigenic site of the carbonic anhydrase III (CAIII) protein, a ubiquitous biomarker that has been identified in patients with other diseases. CONCLUSION: M12 is the first peptide associated with the CAIII protein that may be used as an antigen for antibody detection to aid in RA diagnosis with high sensitivity and specificity.
[Mh] Termos MeSH primário: Artrite Reumatoide/sangue
Artrite Reumatoide/diagnóstico
Anidrase Carbônica III/sangue
Técnicas de Visualização da Superfície Celular/métodos
Modelos Animais de Doenças
Mimetismo Molecular/fisiologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Sequência de Aminoácidos
Animais
Artrite Reumatoide/genética
Anidrase Carbônica III/genética
Feminino
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos DBA
Meia-Idade
Dados de Sequência Molecular
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 4.2.1.- (Carbonic Anhydrase III)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150624
[St] Status:MEDLINE
[do] DOI:10.1186/s13075-015-0685-3


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[PMID]:25822460
[Au] Autor:Dachy A; Paquot F; Debray G; Bovy C; Christensen EI; Collard L; Jouret F
[Ad] Endereço:Division of Pediatrics, CHC Liège, Liège, Belgium.
[Ti] Título:In-depth phenotyping of a Donnai-Barrow patient helps clarify proximal tubule dysfunction.
[So] Source:Pediatr Nephrol;30(6):1027-31, 2015 Jun.
[Is] ISSN:1432-198X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The megalin/cubilin/amnionless complex is essential for albumin and low molecular weight (LMW) protein reabsorption by renal proximal tubules (PT). Mutations of the LRP2 gene encoding megalin cause autosomal recessive Donnai-Barrow/facio-oculo-acoustico-renal syndrome (DB/FOAR), which is characterized by LMW proteinuria. The pathophysiology of DB/FOAR-associated PT dysfunction remains unclear. CLINICAL CASE: A 3-year-old girl presented with growth retardation and proteinuria. Clinical examination was unremarkable, except for a still-opened anterior fontanel and myopia. Psychomotor development was delayed. At 6, she developed sensorineural hearing loss. Hypertelorism was noted when she turned 12. Blood analyses, including renal function parameters, were normal. Urine sediment was bland. Proteinuria was significant and included albumin and LMW proteins. Immunoblotting analyses detected cubilin and type 3 carbonic anhydrase (CA3) in the urine. Renal ultrasound was unremarkable. Optical examination of a renal biopsy did not disclose any tubular or glomerular abnormality. Electron microscopy revealed that PT apical endocytic apparatus was significantly less developed. Immunostaining for megalin showed a faint signal in PT cytosol contrasting with the distribution of cubilin at the apical membrane. The diagnostic procedure led to identifying two mutations of the LRP2 gene. CONCLUSIONS: The functional loss of megalin in DB/FOAR causes PT dysfunction characterized by increased urinary shedding of CA3 and cubilin.
[Mh] Termos MeSH primário: Agenesia do Corpo Caloso/diagnóstico
Perda Auditiva Neurossensorial/diagnóstico
Hérnias Diafragmáticas Congênitas/diagnóstico
Túbulos Renais Proximais/fisiopatologia
Miopia/diagnóstico
Proteinúria/diagnóstico
Erros Inatos do Transporte Tubular Renal/diagnóstico
[Mh] Termos MeSH secundário: Agenesia do Corpo Caloso/genética
Agenesia do Corpo Caloso/fisiopatologia
Agenesia do Corpo Caloso/urina
Biópsia
Anidrase Carbônica III/urina
Pré-Escolar
Análise Mutacional de DNA
Endocitose
Feminino
Predisposição Genética para Doença
Perda Auditiva Neurossensorial/genética
Perda Auditiva Neurossensorial/fisiopatologia
Perda Auditiva Neurossensorial/urina
Hérnias Diafragmáticas Congênitas/genética
Hérnias Diafragmáticas Congênitas/fisiopatologia
Hérnias Diafragmáticas Congênitas/urina
Seres Humanos
Imuno-Histoquímica
Túbulos Renais Proximais/metabolismo
Túbulos Renais Proximais/ultraestrutura
Proteína-2 Relacionada a Receptor de Lipoproteína de Baixa Densidade/genética
Microscopia Eletrônica
Mutação
Miopia/genética
Miopia/fisiopatologia
Miopia/urina
Fenótipo
Valor Preditivo dos Testes
Prognóstico
Proteinúria/genética
Proteinúria/fisiopatologia
Proteinúria/urina
Receptores de Superfície Celular/metabolismo
Erros Inatos do Transporte Tubular Renal/genética
Erros Inatos do Transporte Tubular Renal/fisiopatologia
Erros Inatos do Transporte Tubular Renal/urina
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (LRP2 protein, human); 0 (Low Density Lipoprotein Receptor-Related Protein-2); 0 (Receptors, Cell Surface); 0 (intrinsic factor-cobalamin receptor); EC 4.2.1.- (Carbonic Anhydrase III)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150331
[St] Status:MEDLINE
[do] DOI:10.1007/s00467-014-3037-7


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[PMID]:25684186
[Au] Autor:Carter WG; Vigneswara V; Newlaczyl A; Wayne D; Ahmed B; Saddington S; Brewer C; Raut N; Gerdes HK; Erdozain AM; Tooth D; Bolt EL; Osna NA; Tuma DJ; Kharbanda KK
[Ad] Endereço:School of Medicine, University of Nottingham, Royal Derby Hospital Centre, Derby, DE22 3DT, UK. Electronic address: wayne.carter@nottingham.ac.uk.
[Ti] Título:Isoaspartate, carbamoyl phosphate synthase-1, and carbonic anhydrase-III as biomarkers of liver injury.
[So] Source:Biochem Biophys Res Commun;458(3):626-31, 2015 Mar 13.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We had previously shown that alcohol consumption can induce cellular isoaspartate protein damage via an impairment of the activity of protein isoaspartyl methyltransferase (PIMT), an enzyme that triggers repair of isoaspartate protein damage. To further investigate the mechanism of isoaspartate accumulation, hepatocytes cultured from control or 4-week ethanol-fed rats were incubated in vitro with tubercidin or adenosine. Both these agents, known to elevate intracellular S-adenosylhomocysteine levels, increased cellular isoaspartate damage over that recorded following ethanol consumption in vivo. Increased isoaspartate damage was attenuated by treatment with betaine. To characterize isoaspartate-damaged proteins that accumulate after ethanol administration, rat liver cytosolic proteins were methylated using exogenous PIMT and (3)H-S-adenosylmethionine and proteins resolved by gel electrophoresis. Three major protein bands of ∼ 75-80 kDa, ∼ 95-100 kDa, and ∼ 155-160 kDa were identified by autoradiography. Column chromatography used to enrich isoaspartate-damaged proteins indicated that damaged proteins from ethanol-fed rats were similar to those that accrued in the livers of PIMT knockout (KO) mice. Carbamoyl phosphate synthase-1 (CPS-1) was partially purified and identified as the ∼ 160 kDa protein target of PIMT in ethanol-fed rats and in PIMT KO mice. Analysis of the liver proteome of 4-week ethanol-fed rats and PIMT KO mice demonstrated elevated cytosolic CPS-1 and betaine homocysteine S-methyltransferase-1 when compared to their respective controls, and a significant reduction of carbonic anhydrase-III (CA-III) evident only in ethanol-fed rats. Ethanol feeding of rats for 8 weeks resulted in a larger (∼ 2.3-fold) increase in CPS-1 levels compared to 4-week ethanol feeding indicating that CPS-1 accumulation correlated with the duration of ethanol consumption. Collectively, our results suggest that elevated isoaspartate and CPS-1, and reduced CA-III levels could serve as biomarkers of hepatocellular injury.
[Mh] Termos MeSH primário: Carbamoil-Fosfato Sintase (Amônia)/análise
Anidrase Carbônica III/análise
Doença Hepática Induzida por Substâncias e Drogas/patologia
Ácido Isoaspártico/análise
Fígado/patologia
Proteína D-Aspartato-L-Isoaspartato Metiltransferase/metabolismo
[Mh] Termos MeSH secundário: Animais
Biomarcadores/análise
Biomarcadores/metabolismo
Carbamoil-Fosfato Sintase (Amônia)/metabolismo
Anidrase Carbônica III/metabolismo
Células Cultivadas
Doença Hepática Induzida por Substâncias e Drogas/etiologia
Doença Hepática Induzida por Substâncias e Drogas/genética
Doença Hepática Induzida por Substâncias e Drogas/metabolismo
Etanol/efeitos adversos
Ácido Isoaspártico/metabolismo
Fígado/efeitos dos fármacos
Fígado/metabolismo
Masculino
Camundongos
Camundongos Knockout
Proteína D-Aspartato-L-Isoaspartato Metiltransferase/genética
Ratos
Ratos Wistar
S-Adenosil-Homocisteína/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Biomarkers); 0 (Isoaspartic Acid); 3K9958V90M (Ethanol); 979-92-0 (S-Adenosylhomocysteine); EC 2.1.1.77 (Protein D-Aspartate-L-Isoaspartate Methyltransferase); EC 4.2.1.- (Carbonic Anhydrase III); EC 6.3.4.16 (Carbamoyl-Phosphate Synthase (Ammonia))
[Em] Mês de entrada:1505
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150217
[St] Status:MEDLINE


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[PMID]:25068727
[Au] Autor:Alzweiri M; Al-Balas Q; Al-Hiari Y
[Ad] Endereço:Department of Pharmaceutical Sciences, Faculty of Pharmacy , The University of Jordan, Amman , Jordan and.
[Ti] Título:Chromatographic evaluation and QSAR optimization for benzoic acid analogues against carbonic anhydrase III.
[So] Source:J Enzyme Inhib Med Chem;30(3):420-9, 2015 Jun.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:An HPLC-size exclusion method was developed as an assay method to evaluate the binding of tested compounds with carbonic anhydrase III (CAIII) enzyme. Inhibition of CAIII by a group of benzoic acid analogues was characterized by vacancy (negative) peak intensity representing the fraction of the compounds bound with CAIII enzyme. Interestingly, p-hydroxyl benzoic acid and aspirin were found potent inhibitors against CAIII with affinity constants of 9954 and 9013 M(-1) respectively. Affinity values of twenty training compounds were modeled against thirty-five descriptors derived from their structures. Strong correlation was obtained between the affinity values and the formal charge of the molecules. Docking studies on training set compounds generated consensus scores having a strong agreement with affinity factors obtained from the chromatographic analysis.
[Mh] Termos MeSH primário: Benzoatos/farmacologia
Anidrase Carbônica III/antagonistas & inibidores
Inibidores da Anidrase Carbônica/farmacologia
Relação Quantitativa Estrutura-Atividade
[Mh] Termos MeSH secundário: Benzoatos/síntese química
Benzoatos/química
Anidrase Carbônica III/metabolismo
Inibidores da Anidrase Carbônica/síntese química
Inibidores da Anidrase Carbônica/química
Cromatografia Líquida de Alta Pressão
Relação Dose-Resposta a Droga
Seres Humanos
Simulação de Acoplamento Molecular
Estrutura Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Benzoates); 0 (Carbonic Anhydrase Inhibitors); EC 4.2.1.- (Carbonic Anhydrase III)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:150713
[Lr] Data última revisão:
150713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140729
[St] Status:MEDLINE
[do] DOI:10.3109/14756366.2014.940939


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[PMID]:25264012
[Au] Autor:Zheng Y; Dai L; Fu W
[Ad] Endereço:Department of Respiratory Medicine, First Hospital, Kunming University School of Medicine, Kunming 650032, China.
[Ti] Título:[Carbonic anhydrase III and mRNA expression levels in quadriceps femoris muscle of chronic obstructive pulmonary disease patients].
[So] Source:Zhonghua Nei Ke Za Zhi;53(7):555-7, 2014 Jul.
[Is] ISSN:0578-1426
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To explore the expression status of carbonic anhydrase III (CAIII) from quadriceps femoris muscle in two kinds of muscle clinical phenotype (skeletal muscle atrophy group and skeletal muscles non-atrophy group) of chronic obstructive pulmonary disease (COPD). METHODS: Totally 37 inpatients from our hospital, were divided into 11 patients without COPD and 26 patients with COPD, in addition, according to body mass index, fat free mass index and quadriceps cross-section diameter, patients with COPD were divided into 14 skeletal muscles non-atrophy patients (SMNA) and 12 skeletal muscle atrophy patients (SMA). CAIII concentration of femoris quadriceps specimens was quantitatively determined using Western blot methods, CAIIImRNA expression levels of femoris quadriceps specimens were also quantitatively measured using RT-PCR, then compared among the 3 groups. RESULTS: There was significant difference in CAIII quantitative concentration and CAIIImRNA expression level in each group (P < 0.05) , further more, CAIII concentration expression level was significantly higher (P < 0.01) in SMA group (1.260 ± 0.068) than in SMNA group (1.110 ± 0.014) , the latter was significantly higher (P < 0.01) than in the control group (1.000 ± 0.062) . CAIIImRNA expression level was significantly higher (P < 0.01) in SMNA group (2.170 ± 0.412) than in the control group (1.000 ± 0.115) , and was significantly lower than in SMA group (3.770 ± 0.788; P < 0.01). CAIII concentration and CAIIImRNA expression level increased at equal pace in SMNA group and SMA group, however, CAIII quantitative concentration and CAIIImRNA expression level were inconsistent in the two groups. CONCLUSION: The expression status of CAIII in quadriceps femoris muscle was different in two kinds of muscle clinical phenotype of COPD.
[Mh] Termos MeSH primário: Anidrase Carbônica III/metabolismo
Doença Pulmonar Obstrutiva Crônica/metabolismo
Músculo Quadríceps/metabolismo
[Mh] Termos MeSH secundário: Índice de Massa Corporal
Seres Humanos
Músculo Esquelético
Músculos
Atrofia Muscular
RNA Mensageiro
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); EC 4.2.1.- (Carbonic Anhydrase III)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:140929
[Lr] Data última revisão:
140929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140930
[St] Status:MEDLINE


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[PMID]:25109532
[Au] Autor:Huang H; Ren HM; Shang XL; Liu XY
[Ad] Endereço:Institute of Neurology, Fudan University, Shanghai 200040, P.R. China.
[Ti] Título:Detection of the phosphatase activity of carbonic anhydrase III on a nitrocellulose membrane following 2D gel electrophoresis.
[So] Source:Mol Med Rep;10(4):1887-92, 2014 Oct.
[Is] ISSN:1791-3004
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Carbonic anhydrase isozyme III (CAIII) is unique among the carbonic anhydrases because it exhibits phosphatase activity. CAIII is relatively specific to skeletal muscles, and may therefore be a useful diagnostic marker for muscular diseases. In the muscles of patients with myasthenia gravis (MG), CAIII is deficient and previous studies have demonstrated that changes in the phosphatase activity of CAIII is a fundamental mechanism underlying the weakness and fatigability of MG. However, there have been no effective analytical methods for investigating its phosphatase activity until now. In the present study, a new method combining two-dimensional electrophoresis (2-DE) and phosphatase staining in situ on a nitrocellulose membrane was reported to detect the phosphatase of CAIII in skeletal muscle extracts. Furthermore, a recombinant CAIII was constructed and its phosphatase activity staining was demonstrated to be positive. This method allows for the effective detection of the phosphatase activity of CAIII following 2-DE and is a promising technique for functional proteomics.
[Mh] Termos MeSH primário: Anidrase Carbônica III/metabolismo
Colódio/química
[Mh] Termos MeSH secundário: Animais
Anidrase Carbônica III/genética
Eletroforese em Gel Bidimensional
Masculino
Músculo Esquelético/enzimologia
Monoéster Fosfórico Hidrolases/metabolismo
Ratos
Ratos Sprague-Dawley
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Recombinant Proteins); 9004-70-0 (Collodion); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 4.2.1.- (Carbonic Anhydrase III)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140812
[St] Status:MEDLINE
[do] DOI:10.3892/mmr.2014.2439


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[PMID]:24887110
[Au] Autor:Hao X; Xing Y; Moore MW; Zhang J; Han D; Schulte BA; Dubno JR; Lang H
[Ad] Endereço:Department of Otolaryngology - Head & Neck Surgery, Beijing Tongren Hospital, Capital Medical University, Beijing, China; Department of Pathology and Laboratory Medicine, Medical University of South Carolina, Charleston, South Carolina, United States of America.
[Ti] Título:Sox10 expressing cells in the lateral wall of the aged mouse and human cochlea.
[So] Source:PLoS One;9(6):e97389, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Age-related hearing loss (presbycusis) is a common human disorder, affecting one in three Americans aged 60 and over. Previous studies have shown that presbyacusis is associated with a loss of non-sensory cells in the cochlear lateral wall. Sox10 is a transcription factor crucial to the development and maintenance of neural crest-derived cells including some non-sensory cell types in the cochlea. Mutations of the Sox10 gene are known to cause various combinations of hearing loss and pigmentation defects in humans. This study investigated the potential relationship between Sox10 gene expression and pathological changes in the cochlear lateral wall of aged CBA/CaJ mice and human temporal bones from older donors. Cochlear tissues prepared from young adult (1-3 month-old) and aged (2-2.5 year-old) mice, and human temporal bone donors were examined using quantitative immunohistochemical analysis and transmission electron microscopy. Cells expressing Sox10 were present in the stria vascularis, outer sulcus and spiral prominence in mouse and human cochleas. The Sox10(+) cell types included marginal and intermediate cells and outer sulcus cells, including those that border the scala media and those extending into root processes (root cells) in the spiral ligament. Quantitative analysis of immunostaining revealed a significant decrease in the number of Sox10(+) marginal cells and outer sulcus cells in aged mice. Electron microscopic evaluation revealed degenerative alterations in the surviving Sox10(+) cells in aged mice. Strial marginal cells in human cochleas from donors aged 87 and older showed only weak immunostaining for Sox10. Decreases in Sox10 expression levels and a loss of Sox10(+) cells in both mouse and human aged ears suggests an important role of Sox10 in the maintenance of structural and functional integrity of the lateral wall. A loss of Sox10(+) cells may also be associated with a decline in the repair capabilities of non-sensory cells in the aged ear.
[Mh] Termos MeSH primário: Envelhecimento/metabolismo
Cóclea/citologia
Cóclea/metabolismo
Fatores de Transcrição SOXE/metabolismo
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Animais
Limiar Auditivo
Anidrase Carbônica III/metabolismo
Cóclea/ultraestrutura
Feminino
Seres Humanos
Masculino
Camundongos Endogâmicos CBA
Meia-Idade
ATPase Trocadora de Sódio-Potássio/metabolismo
Ligamento Espiral da Cóclea/metabolismo
Estria Vascular/metabolismo
Estria Vascular/ultraestrutura
Osso Temporal/metabolismo
Doadores de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (SOXE Transcription Factors); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase); EC 4.2.1.- (Carbonic Anhydrase III)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140603
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0097389



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