Base de dados : MEDLINE
Pesquisa : D08.811.277.656.675 [Categoria DeCS]
Referências encontradas : 2359 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 236 ir para página                         

  1 / 2359 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29465592
[Au] Autor:Bienias B; Sikora P
[Ti] Título:Urinary metalloproteinases and tissue inhibitors of metalloproteinases as potential early biomarkers for renal fibrosis in children with nephrotic syndrome.
[So] Source:Medicine (Baltimore);97(8):e9964, 2018 Feb.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In chronic glomerulopathies, renal fibrosis (RF) results from extracellular matrix remodeling processes regulated by matrix metalloproteinases (MMP) and tissue inhibitors of metalloproteinases (TIMP). We assessed urinary (u-) and serum (s-) MMP-1, -2, -9, TIMP-1, -2 concentrations and MMP-1, -2, -9/TIMP-1, -2 ratios in children with nephrotic syndrome. Steroid-dependent and steroid-resistant nephrotic patients (SDNS-Ps and SRNS-Ps, respectively) were compared with respect to measured parameters. The correlations of measured parameters with magnitude of proteinuria and histopathological diagnosis were determined.The study comprised of 39 children with nephrotic syndrome and 20 healthy controls. Twenty-three patients had SDNS and 16 ones-SRNS. The concentrations MMPs and TIMPs were measured using enzyme-linked immunosorbent assay.In nephrotic patients, higher u-MMP-1, -2, -9/creatinine ratios and u-TIMP-1, -2/creatinine ratios were observed as compared with controls. Nephrotic children were also characterized by lower MMP-1, -2, -9/TIMP-1 ratios. In SRNS-Ps, u-MMP-2/creatinine ratio and u-TIMP-1/creatinine ratio were higher as compared with SDNS-Ps. Magnitude of proteinuria correlated positively with u-MMP-2/creatinine ratio and negatively with u-MMP-2/TIMP-1. In minimal change disease (MCD) patients as compared with those with other glomerulopathies, there was higher u-MMP-2/TIMP-1 ratio. No significant differences in s-MMPs, s-TIMPs, and s-MMPs/TIMPs ratios between nephrotic patients and controls were observed.Children with nephrotic syndrome are characterized by increased u-fibrotic biomarkers excretions. U-MMP-1, -2, -9 excretions and u-MMP-2/TIMP-1 ratio may become potential early biomarkers for RF. SRNS-Ps, those with heavier proteinuria and other than MCD glomerulopathies, seem to be more susceptible to early RF.
[Mh] Termos MeSH primário: Nefropatias/etiologia
Rim/patologia
Metaloproteases/urina
Síndrome Nefrótica/urina
Inibidores Teciduais de Metaloproteinases/urina
[Mh] Termos MeSH secundário: Adolescente
Biomarcadores/urina
Estudos de Casos e Controles
Criança
Pré-Escolar
Creatinina/urina
Feminino
Fibrose
Seres Humanos
Nefropatias/patologia
Masculino
Nefrose Lipoide/complicações
Nefrose Lipoide/urina
Síndrome Nefrótica/complicações
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Tissue Inhibitor of Metalloproteinases); AYI8EX34EU (Creatinine); EC 3.4.- (Metalloproteases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:180222
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000009964


  2 / 2359 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29381728
[Au] Autor:Belousov MV; Bondarev SA; Kosolapova AO; Antonets KS; Sulatskaya AI; Sulatsky MI; Zhouravleva GA; Kuznetsova IM; Turoverov KK; Nizhnikov AA
[Ad] Endereço:Department of Genetics and Biotechnology, St. Petersburg State University, Universitetskaya nab., St. Petersburg, Russian Federation.
[Ti] Título:M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils.
[So] Source:PLoS One;13(1):e0191317, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Amyloids are protein fibrils with a characteristic spatial structure. Amyloids were long perceived as the pathogens involved in a set of lethal diseases in humans and animals. In recent decades, it has become clear that amyloids represent a quaternary protein structure that is not only pathological but also functionally important and is widely used by different organisms, ranging from archaea to animals, to implement diverse biological functions. The greatest biological variety of amyloids is found in prokaryotes, where they control the formation of biofilms and cell wall sheaths, facilitate the overcoming of surface tension, and regulate the metabolism of toxins. Several amyloid proteins were identified in the important model, biotechnological and pathogenic bacterium Escherichia coli. In previous studies, using a method for the proteomic screening and identification of amyloids, we identified 61 potentially amyloidogenic proteins in the proteome of E. coli. Among these proteins, YghJ was the most enriched with bioinformatically predicted amyloidogenic regions. YghJ is a lipoprotein with a zinc metalloprotease M60-like domain that is involved in mucin degradation in the intestine as well as in proinflammatory responses. In this study, we analyzed the amyloid properties of the YghJ M60-like domain and demonstrated that it forms amyloid-like fibrils in vitro and in vivo.
[Mh] Termos MeSH primário: Amiloide/química
Proteínas de Escherichia coli/química
Metaloproteases/química
Multimerização Proteica
[Mh] Termos MeSH secundário: Domínios Proteicos
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amyloid); 0 (Escherichia coli Proteins); EC 3.4.- (Metalloproteases); EC 3.4.- (YghJ protein, E coli)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180131
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191317


  3 / 2359 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28459440
[Au] Autor:Lauinger L; Li J; Shostak A; Cemel IA; Ha N; Zhang Y; Merkl PE; Obermeyer S; Stankovic-Valentin N; Schafmeier T; Wever WJ; Bowers AA; Carter KP; Palmer AE; Tschochner H; Melchior F; Deshaies RJ; Brunner M; Diernfellner A
[Ad] Endereço:Heidelberg University Biochemistry Center, Heidelberg, Germany.
[Ti] Título:Thiolutin is a zinc chelator that inhibits the Rpn11 and other JAMM metalloproteases.
[So] Source:Nat Chem Biol;13(7):709-714, 2017 Jul.
[Is] ISSN:1552-4469
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thiolutin is a disulfide-containing antibiotic and anti-angiogenic compound produced by Streptomyces. Its biological targets are not known. We show that reduced thiolutin is a zinc chelator that inhibits the JAB1/MPN/Mov34 (JAMM) domain-containing metalloprotease Rpn11, a deubiquitinating enzyme of the 19S proteasome. Thiolutin also inhibits the JAMM metalloproteases Csn5, the deneddylase of the COP9 signalosome; AMSH, which regulates ubiquitin-dependent sorting of cell-surface receptors; and BRCC36, a K63-specific deubiquitinase of the BRCC36-containing isopeptidase complex and the BRCA1-BRCA2-containing complex. We provide evidence that other dithiolopyrrolones also function as inhibitors of JAMM metalloproteases.
[Mh] Termos MeSH primário: Quelantes/farmacologia
Inibidores Enzimáticos/farmacologia
Metaloproteases/antagonistas & inibidores
Transativadores/antagonistas & inibidores
Zinco/química
[Mh] Termos MeSH secundário: Quelantes/química
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/química
Células HeLa
Seres Humanos
Metaloproteases/metabolismo
Complexo de Endopeptidases do Proteassoma/metabolismo
Pirrolidinonas/química
Pirrolidinonas/metabolismo
Pirrolidinonas/farmacologia
Relação Estrutura-Atividade
Transativadores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chelating Agents); 0 (Enzyme Inhibitors); 0 (PSMD14 protein, human); 0 (Pyrrolidinones); 0 (Trans-Activators); 02C005Q20B (acetopyrrothine); EC 3.4.- (Metalloproteases); EC 3.4.25.1 (Proteasome Endopeptidase Complex); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1038/nchembio.2370


  4 / 2359 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27778284
[Au] Autor:Prely L; Klein T; Geurink PP; Paal K; Overkleeft HS; Bischoff R
[Ad] Endereço:Department of Pharmacy, Analytical Biochemistry, University of Groningen, Antonius Deusinglaan 1, 9713, AV, Groningen, The Netherlands.
[Ti] Título:Activity-Dependent Photoaffinity Labeling of Metalloproteases.
[So] Source:Methods Mol Biol;1491:103-111, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Metalloproteases, notably members of the matrix metalloprotease (MMP) and A Disintegrin And Metalloprotease (ADAM) families play crucial roles in tissue remodeling, the liberation of growth factors and cytokines from cell membranes (shedding) and cell-cell or cell-matrix interactions. Activity of MMPs or ADAMs must therefore be tightly controlled in time and space by activation of pro-enzymes upon appropriate stimuli and inhibition by endogenous tissue inhibitors of metalloproteases (TIMPs) or α -macroglobulin to prevent irreversible tissue damage due to excessive degradation or uncontrolled release of potent inflammatory mediators, such as tumor necrosis factor-α (TNF-α).Although there is a wide range of methods to measure the amount of metalloproteases based on immunological approaches, relatively little is known about the activation status of a given enzyme at any given time and location. This information is, however, critical in order to understand the function and possible implication of these enzymes in disease. Since metalloproteases use an active-site bound water molecule to cleave the peptide bond, it is not possible to apply known active-site-directed labeling approaches with electrophilic "warheads." We therefore developed novel metalloprotease inhibitors that contain a photoactivatable trifluoromethylphenyldiazirine group and show that such inhibitors are suitable for activity-dependent photoaffinity labeling of MMPs and ADAMs.
[Mh] Termos MeSH primário: Metaloproteases/metabolismo
Marcadores de Fotoafinidade
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Meios de Cultura
Ativação Enzimática
Seres Humanos
Concentração Inibidora 50
Camundongos
Inibidor Tecidual de Metaloproteinase-1/metabolismo
Fator de Necrose Tumoral alfa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 0 (Photoaffinity Labels); 0 (TIMP1 protein, human); 0 (Tissue Inhibitor of Metalloproteinase-1); 0 (Tumor Necrosis Factor-alpha); EC 3.4.- (Metalloproteases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  5 / 2359 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29203373
[Au] Autor:Preciado LM; Rey-Suárez P; Henao IC; Pereañez JA
[Ad] Endereço:Programa de Ofidismo/Escorpionismo, Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia UdeA, Calle 70 No. 52-21, Medellín, Colombia.
[Ti] Título:Betulinic, oleanolic and ursolic acids inhibit the enzymatic and biological effects induced by a P-I snake venom metalloproteinase.
[So] Source:Chem Biol Interact;279:219-226, 2018 Jan 05.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Betulinic acid (BA), Oleanolic acid (OA) and Ursolic acid (UA), are pentacyclic triterpenoids with widespread occurrence throughout the plant kingdom, these compounds are widely recognized by their pharmacological and biological properties, such as, anti-tumoral, anti-inflammatory, anti-microbial and hepatoprotective activity. In this work we determined the inhibitory ability of these compounds on the enzymatic, hemorrhagic, myotoxic and edema-inducing activities of Batx-I, a P-I metalloproteinase isolated from Bothrops atrox venom. BA, UA and OA inhibited the proteolytic activity of Batx-I on gelatin with IC values of 115.3, 223.0 and 357.3 µM, respectively. Additionally, these compounds showed inhibition of the hemorrhagic activity of Batx-I in skin with IC 345.7, 643.5 and 1077.0 µM for BA, UA and OA in preincubation experiments. In studies with independent-injection, in which Batx-I was injected and then, at the same site, a concentration of 600 µM of each compound were administered at either 0, 5 or 10 min, BA showed a significant reduction of hemorrhage at 0 and 5 min. In addition, these compounds inhibited myotoxicity and edema-forming activity of Batx-I at 600 µM concentration. Molecular docking studies suggested that these compounds could occupy part of the substrate binding cleft of the enzyme affecting its catalytic cycle. In this manner, triterpenic acids are candidates for the development of inhibitors for the prevention of local tissue damage in snakebite envenomation.
[Mh] Termos MeSH primário: Venenos de Crotalídeos/enzimologia
Metaloproteases/metabolismo
Ácido Oleanólico/farmacologia
Triterpenos/farmacologia
[Mh] Termos MeSH secundário: Animais
Bothrops/fisiologia
Edema/induzido quimicamente
Edema/prevenção & controle
Hemorragia/induzido quimicamente
Hemorragia/prevenção & controle
Metaloproteases/genética
Camundongos
Estrutura Molecular
Doenças Musculares/induzido quimicamente
Doenças Musculares/prevenção & controle
Ácido Oleanólico/química
Triterpenos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Crotalid Venoms); 0 (Triterpenes); 4G6A18707N (betulinic acid); 6SMK8R7TGJ (Oleanolic Acid); EC 3.4.- (Metalloproteases); P3M2575F3F (ursolic acid)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180103
[Lr] Data última revisão:
180103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE


  6 / 2359 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29049345
[Au] Autor:Stinemetz EK; Gao P; Pinkston KL; Montealegre MC; Murray BE; Harvey BR
[Ad] Endereço:Center for Molecular Imaging, Brown Foundation Institute of Molecular Medicine for the Prevention of Human Diseases, University of Texas Health Science Center, Houston, Texas, United States of America.
[Ti] Título:Processing of the major autolysin of E. faecalis, AtlA, by the zinc-metalloprotease, GelE, impacts AtlA septal localization and cell separation.
[So] Source:PLoS One;12(10):e0186706, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AtlA is the major peptidoglycan hydrolase of Enterococcus faecalis involved in cell division and cellular autolysis. The secreted zinc metalloprotease, gelatinase (GelE), has been identified as an important regulator of cellular function through post-translational modification of protein substrates. AtlA is a known target of GelE, and their interplay has been proposed to regulate AtlA function. To study the protease-mediated post-translational modification of AtlA, monoclonal antibodies were developed as research tools. Flow cytometry and Western blot analysis suggests that in the presence of GelE, surface-bound AtlA exists primarily as a N-terminally truncated form whereas in the absence of GelE, the N-terminal domain of AtlA is retained. We identified the primary GelE cleavage site occurring near the transition between the T/E rich Domain I and catalytic region, Domain II via N-terminal sequencing. Truncation of AtlA had no effect on the peptidoglycan hydrolysis activity of AtlA. However, we observed that N-terminal cleavage was required for efficient AtlA-mediated cell division while unprocessed AtlA was unable to resolve dividing cells into individual units. Furthermore, we observed that the processed AtlA has the propensity to localize to the cell septum on wild-type cells whereas unprocessed AtlA in the ΔgelE strain were dispersed over the cell surface. Combined, these results suggest that AtlA septum localization and subsequent cell separation can be modulated by a single GelE-mediated N-terminal cleavage event, providing new insights into the post-translation modification of AtlA and the mechanisms governing chaining and cell separation.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Enterococcus faecalis/metabolismo
Metaloproteases/metabolismo
Zinco/metabolismo
[Mh] Termos MeSH secundário: Western Blotting
Separação Celular
Citometria de Fluxo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 3.4.- (Metalloproteases); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171020
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186706


  7 / 2359 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Cohen, Moisés
Texto completo
[PMID]:28902861
[Au] Autor:Leal MF; Caires Dos Santos L; Martins de Oliveira A; Santoro Belangero P; Antônio Figueiredo E; Cohen C; de Seixas Alves F; Hiromi Yanaguizawa W; Vicente Andreoli C; de Castro Pochini A; Ejnisman B; Cardoso Smith M; de Seixas Alves MT; Cohen M
[Ad] Endereço:Departamento de Ortopedia e Traumatologia, Universidade Federal de São Paulo, São Paulo, SP, Brazil.
[Ti] Título:Epigenetic regulation of metalloproteinases and their inhibitors in rotator cuff tears.
[So] Source:PLoS One;12(9):e0184141, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rotator cuff tear is a common orthopedic condition. Metalloproteinases (MMP) and their inhibitors (TIMP) seem to play a role in the development of joint injuries and in the failure of tissue healing. However, the mechanisms of regulation of gene expression in tendons are still unknown. Epigenetic mechanisms, such as DNA methylation and microRNAs regulation, are involved in the dynamic control of gene expression. Here, the mRNA expression and DNA methylation status of MMPs (MMP1, MMP2, MMP3, MMP9, MMP13, and MMP14) and TIMPs (TIMP1-3) and the expression of miR-29 family members in ruptured supraspinatus tendons were compared with non-injured tendons of individuals without this lesion. Additionally, the gene expression and methylation status at the edge of the ruptured tendon were compared with macroscopically non-injured rotator cuff tendon samples from the anterior and posterior regions of patients with tendon tears. Moreover, the possible associations between the molecular alterations and the clinical and histologic characteristics were investigated. Dysregulated expression and DNA methylation of MMP and TIMP genes were found across the rotator cuff tendon samples of patients with supraspinatus tears. These alterations were influenced at least in part by age at surgery, sex, smoking habit, tear size, and duration of symptoms. Alterations in the studied MMP and TIMP genes may contribute to the presence of microcysts, fissures, necrosis, and neovascularization in tendons and may thus be involved in the tendon healing process. In conclusion, MMPs and their inhibitors are regulated by epigenetic modifications and may play a role in rotator cuff tears.
[Mh] Termos MeSH primário: Epigênese Genética
Genes Reguladores
Metaloproteases/genética
Lesões do Manguito Rotador/genética
Inibidores Teciduais de Metaloproteinases/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Estudos de Casos e Controles
Metilação de DNA
Feminino
Regulação Enzimológica da Expressão Gênica
Seres Humanos
Masculino
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Tissue Inhibitor of Metalloproteinases); EC 3.4.- (Metalloproteases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184141


  8 / 2359 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28821623
[Au] Autor:Gomes F; Palma FR; Barros MH; Tsuchida ET; Turano HG; Alegria TGP; Demasi M; Netto LES
[Ad] Endereço:From the Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, 05508-090 São Paulo, fernandopgdna@hotmail.com.
[Ti] Título:Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments.
[So] Source:J Biol Chem;292(41):17011-17024, 2017 Oct 13.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Yeast Prx1 is a mitochondrial 1-Cys peroxiredoxin that catalyzes the reduction of endogenously generated H O Prx1 is synthesized on cytosolic ribosomes as a preprotein with a cleavable N-terminal presequence that is the mitochondrial targeting signal, but the mechanisms underlying Prx1 distribution to distinct mitochondrial subcompartments are unknown. Here, we provide direct evidence of the following dual mitochondrial localization of Prx1: a soluble form in the intermembrane space and a form in the matrix weakly associated with the inner mitochondrial membrane. We show that Prx1 sorting into the intermembrane space likely involves the release of the protein precursor within the lipid bilayer of the inner membrane, followed by cleavage by the inner membrane peptidase. We also found that during its import into the matrix compartment, Prx1 is sequentially cleaved by mitochondrial processing peptidase and then by octapeptidyl aminopeptidase 1 (Oct1). Oct1 cleaved eight amino acid residues from the N-terminal region of Prx1 inside the matrix, without interfering with its peroxidase activity Remarkably, the processing of peroxiredoxin (Prx) proteins by Oct1 appears to be an evolutionarily conserved process because yeast Oct1 could cleave the human mitochondrial peroxiredoxin Prx3 when expressed in Altogether, the processing of peroxiredoxins by Imp2 or Oct1 likely represents systems that control the localization of Prxs into distinct compartments and thereby contribute to various mitochondrial redox processes.
[Mh] Termos MeSH primário: Metaloproteases/metabolismo
Mitocôndrias/enzimologia
Peroxidases/metabolismo
Proteólise
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Cisteína Endopeptidases/genética
Cisteína Endopeptidases/metabolismo
Seres Humanos
Metaloproteases/genética
Mitocôndrias/genética
Peroxidases/genética
Transporte Proteico/fisiologia
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Saccharomyces cerevisiae Proteins); 144416-78-4 (LMP-2 protein); EC 1.11.1.- (PRX1 protein, S cerevisiae); EC 1.11.1.- (Peroxidases); EC 3.4.- (Metalloproteases); EC 3.4.22.- (Cysteine Endopeptidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.788588


  9 / 2359 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28813580
[Au] Autor:Tang FY; Ma L; Tam POS; Pang CP; Tham CCY; Chen LJ
[Ad] Endereço:Department of Ophthalmology and Visual Sciences, The Chinese University of Hong Kong, Hong Kong, China.
[Ti] Título:Genetic Association of the PARL-ABCC5-HTR3D-HTR3C Locus With Primary Angle-Closure Glaucoma in Chinese.
[So] Source:Invest Ophthalmol Vis Sci;58(10):4384­4389, 2017 08 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: This study evaluates the associations of haplotype-tagging single nucleotide polymorphisms (SNPs) in the PARL-ABCC5-HTR3D-HTR3C region with primary angle closure glaucoma (PACG), with a view to identify the responsible SNP in this region. Methods: Thirty SNPs from the PARL-ABCC5-HTR3D-HTR3C region were genotyped in a Hong Kong Chinese cohort of 422 PACG patients and 400 control subjects, using TaqMan SNP genotyping assays. Single marker and haplotype-based association analyses were performed. Results: Two synonymous ABCC5 SNPs, namely rs939336 (p.Cys594=; P = 0.013; odds ratio [OR] = 1.46; 95% confidence interval [CI], 1.08 to 1.97) and rs1132776 (p.Ala395=; P = 0.009; OR = 1.47; 95% CI: 1.10 to 1.95), were associated with PACG. Mild associations were detected for ABCC5 rs9838667 (P = 0.024) and HTR3D rs12493550 (P = 0.035). Conditional analysis revealed that no SNPs remained significant after adjusting for other SNPs, suggesting none of these tagging SNPs is fully responsible for the association in this region. In subgroup analysis, ABCC5 SNPs rs939336, rs1132776, and rs983667 and HTR3D rs12493550 were associated only with the chronic form of PACG. However, these associations could not withstand the correction for multiple testing. Conclusions: These findings enrich the allelic spectrum of ABCC5 in PACG. We identified no tagging SNP responsible for the association of the whole region. Further deep sequencing analysis of this region should be warranted to uncover whether there is still disease associated variant in this region.
[Mh] Termos MeSH primário: Estudos de Associação Genética
Glaucoma de Ângulo Fechado/genética
Metaloproteases/genética
Proteínas Mitocondriais/genética
Proteínas Associadas à Resistência a Múltiplos Medicamentos/genética
Polimorfismo de Nucleotídeo Único
Receptores 5-HT3 de Serotonina/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Grupo com Ancestrais do Continente Asiático/genética
Feminino
Frequência do Gene
Predisposição Genética para Doença
Técnicas de Genotipagem
Glaucoma de Ângulo Fechado/diagnóstico
Haplótipos
Seres Humanos
Pressão Intraocular
Região de Controle de Locus Gênico
Masculino
Meia-Idade
Reação em Cadeia da Polimerase em Tempo Real
Tonometria Ocular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCC5 protein, human); 0 (HTR3C protein, human); 0 (HTR3D protein, human); 0 (Mitochondrial Proteins); 0 (Multidrug Resistance-Associated Proteins); 0 (Receptors, Serotonin, 5-HT3); EC 3.4.- (Metalloproteases); EC 3.4.21.105 (PARL protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170817
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-22304


  10 / 2359 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28806058
[Au] Autor:Levytskyy RM; Bohovych I; Khalimonchuk O
[Ad] Endereço:Department of Biochemistry, University of Nebraska-Lincoln , Lincoln, Nebraska 68588-0664, United States.
[Ti] Título:Metalloproteases of the Inner Mitochondrial Membrane.
[So] Source:Biochemistry;56(36):4737-4746, 2017 Sep 12.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The inner mitochondrial membrane (IM) is among the most protein-rich cellular compartments. The metastable IM subproteome where the concentration of proteins is approaching oversaturation creates a challenging protein folding environment with a high probability of protein malfunction or aggregation. Failure to maintain protein homeostasis in such a setting can impair the functional integrity of the mitochondria and drive clinical manifestations. The IM is equipped with a series of highly conserved, proteolytic complexes dedicated to the maintenance of normal protein homeostasis within this mitochondrial subcompartment. Particularly important is a group of membrane-anchored metallopeptidases commonly known as m-AAA and i-AAA proteases, and the ATP-independent Oma1 protease. Herein, we will summarize the current biochemical knowledge of these proteolytic machines and discuss recent advances in our understanding of mechanistic aspects of their functioning.
[Mh] Termos MeSH primário: Metaloproteases/metabolismo
Membranas Mitocondriais/enzimologia
[Mh] Termos MeSH secundário: Animais
Regulação Enzimológica da Expressão Gênica/fisiologia
Homeostase
Metaloproteases/genética
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 3.4.- (Metalloproteases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170815
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00663



página 1 de 236 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde