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Pesquisa : D08.811.277.040.025.325.875 [Categoria DeCS]
Referências encontradas : 2376 [refinar]
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[PMID]:29311594
[Au] Autor:Nakanishi A; Kishikawa JI; Tamakoshi M; Mitsuoka K; Yokoyama K
[Ad] Endereço:Department of Molecular Biosciences, Kyoto Sangyo University, Motoyama Kamigamo, Kita-ku, Kyoto, 603-8555, Japan.
[Ti] Título:Cryo EM structure of intact rotary H -ATPase/synthase from Thermus thermophilus.
[So] Source:Nat Commun;9(1):89, 2018 01 08.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Proton translocating rotary ATPases couple ATP hydrolysis/synthesis, which occurs in the soluble domain, with proton flow through the membrane domain via a rotation of the common central rotor complex against the surrounding peripheral stator apparatus. Here, we present a large data set of single particle cryo-electron micrograph images of the V/A type H -rotary ATPase from the bacterium Thermus thermophilus, enabling the identification of three rotational states based on the orientation of the rotor subunit. Using masked refinement and classification with signal subtractions, we obtain homogeneous reconstructions for the whole complexes and soluble V domains. These reconstructions are of higher resolution than any EM map of intact rotary ATPase reported previously, providing a detailed molecular basis for how the rotary ATPase maintains structural integrity of the peripheral stator apparatus, and confirming the existence of a clear proton translocation path from both sides of the membrane.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Proteínas de Bactérias/metabolismo
Thermus thermophilus/enzimologia
ATPases Vacuolares Próton-Translocadoras/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/ultraestrutura
Transporte Biológico
Microscopia Crioeletrônica
Hidrólise
Modelos Moleculares
Conformação Proteica
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Prótons
Rotação
ATPases Vacuolares Próton-Translocadoras/química
ATPases Vacuolares Próton-Translocadoras/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Protein Subunits); 0 (Protons); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180110
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02553-6


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[PMID]:29253572
[Au] Autor:Kim YS; Jin HO; Hong SE; Song JY; Hwang CS; Park IC
[Ad] Endereço:Human Resource Biobank, Cheil General Hospital & Women's Healthcare Center, DanKook University College of Medicine, 17, Seoae-ro 1-gil, Jung-gu, Seoul, 04619, Republic of Korea.
[Ti] Título:Silencing of secretory clusterin sensitizes NSCLC cells to V-ATPase inhibitors by downregulating survivin.
[So] Source:Biochem Biophys Res Commun;495(2):2004-2009, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Secretory clusterin (sCLU) is a stress-associated protein that confers resistance to therapy when overexpressed. In this study, we observed that the V-ATPase inhibitors bafilomycin A1 and concanamycin A significantly stimulated sCLU protein expression. Knockdown of sCLU with siRNA sensitized non-small cell lung cancer (NSCLC) cells to bafilomycin A1, suggesting that sCLU expression renders cells resistant to V-ATPase inhibitors. The dual PI3K/AKT and mTOR inhibitor BEZ235 suppressed sCLU expression and enhanced cell sensitivity induced by bafilomycin A1. Notably, sCLU knockdown further decreased the expression of the survivin protein by bafilomycin A1, and the ectopic expression of survivin alleviated the cell sensitivity by bafilomycin A1 and sCLU depletion, suggesting that increased sensitivity to sCLU depletion in the cells with V-ATPase inhibitors is due, at least in part, to the down-regulation of survivin. Taken together, we demonstrated that the depletion of sCLU expression enhances the sensitivity of NSCLC cells to V-ATPase inhibitors by decreasing survivin expression. Inhibition of the PI3K/AKT/mTOR pathway enhances the sensitivity of NSCLC cells to V-ATPase inhibitors, leading to decreased sCLU and survivin expression. Thus, we suggest that a combination of PI3K/AKT/mTOR inhibitors with V-ATPase inhibitors might be an effective approach for NSCLC treatment.
[Mh] Termos MeSH primário: Antineoplásicos/administração & dosagem
Carcinoma Pulmonar de Células não Pequenas/terapia
Clusterina/genética
Terapia Genética/métodos
Proteínas Inibidoras de Apoptose/metabolismo
Neoplasias Pulmonares/terapia
ATPases Vacuolares Próton-Translocadoras/antagonistas & inibidores
[Mh] Termos MeSH secundário: Células A549
Apoptose/efeitos dos fármacos
Carcinoma Pulmonar de Células não Pequenas/genética
Carcinoma Pulmonar de Células não Pequenas/patologia
Sobrevivência Celular/efeitos dos fármacos
Terapia Combinada/métodos
Regulação para Baixo/efeitos dos fármacos
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Regulação Neoplásica da Expressão Gênica/genética
Inativação Gênica
Seres Humanos
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (BIRC5 protein, human); 0 (CLU protein, human); 0 (Clusterin); 0 (Inhibitor of Apoptosis Proteins); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE


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[PMID]:29257951
[Au] Autor:Guo H; Chitiprolu M; Roncevic L; Javalet C; Hemming FJ; Trung MT; Meng L; Latreille E; Tanese de Souza C; McCulloch D; Baldwin RM; Auer R; Côté J; Russell RC; Sadoul R; Gibbings D
[Ad] Endereço:Department of Cellular and Molecular Medicine, University of Ottawa, 3131 Roger Guindon Hall, 451 Smyth Road, Ottawa K1H 8M5, Canada.
[Ti] Título:Atg5 Disassociates the V V -ATPase to Promote Exosome Production and Tumor Metastasis Independent of Canonical Macroautophagy.
[So] Source:Dev Cell;43(6):716-730.e7, 2017 Dec 18.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Autophagy and autophagy-related genes (Atg) have been attributed prominent roles in tumorigenesis, tumor growth, and metastasis. Extracellular vesicles called exosomes are also implicated in cancer metastasis. Here, we demonstrate that exosome production is strongly reduced in cells lacking Atg5 and Atg16L1, but this is independent of Atg7 and canonical autophagy. Atg5 specifically decreases acidification of late endosomes where exosomes are produced, disrupting the acidifying V V -ATPase by removing a regulatory component, ATP6V1E1, into exosomes. The effect of Atg5 on exosome production promotes the migration and in vivo metastasis of orthotopic breast cancer cells. These findings uncover mechanisms controlling exosome release and identify means by which autophagy-related genes can contribute to metastasis in autophagy-independent pathways.
[Mh] Termos MeSH primário: Proteína 5 Relacionada à Autofagia/metabolismo
Neoplasias da Mama/metabolismo
Neoplasias da Mama/patologia
ATPases Vacuolares Próton-Translocadoras/metabolismo
[Mh] Termos MeSH secundário: Animais
Autofagia/fisiologia
Proteína 5 Relacionada à Autofagia/genética
Proteína 7 Relacionada à Autofagia/genética
Proteína 7 Relacionada à Autofagia/metabolismo
Linhagem Celular Tumoral/metabolismo
Endossomos/metabolismo
Exossomos/metabolismo
Feminino
Seres Humanos
Lisossomos/metabolismo
Camundongos
Camundongos Endogâmicos BALB C
Metástase Neoplásica
ATPases Vacuolares Próton-Translocadoras/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autophagy-Related Protein 5); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases); EC 6.2.1.45 (Autophagy-Related Protein 7)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180117
[Lr] Data última revisão:
180117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171220
[St] Status:MEDLINE


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[PMID]:29227610
[Au] Autor:Kovalenko NO; Palladina TA
[Ti] Título:Gene expression of H+-pumps in plasma and vacuolar membranes of corn root cells under the effect of sodium ions and bioactive preparations.
[So] Source:Ukr Biochem J;88(2):89-97, 2016 Mar-Apr.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Four isoforms of H+-ATPase of plasma membrane: MHA1, MHA2, MHA3, MHA4 are expressed in the corn seedling roots with prevalence of genes MHA3 і MHA4. The exposure of seedlings in the presence of 0.1 M NaCl activated the expression of MHA4 gene isoform, that demonstrates its important role in the processes of adaptation to salinization conditions. In vacuolar membrane, where potential is created by two Н+-pumps, sodium ions activated gene expression of only Н+-АТРase of V-type, taking no effect on the expression of Н+-pyrophosphatase. The seeds pretreatment by synthetic preparations Methyure and Ivine did not affect gene expression of Н+-pumps. Thus we can suppose that the ability of the above preparations to activate functioning of Н+-pumps in the presence of sodium ions is realized at the post-tranlation level.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Proteínas de Plantas/genética
Raízes de Plantas/efeitos dos fármacos
Substâncias Protetoras/farmacologia
Pirimidinas/farmacologia
Cloreto de Sódio/farmacologia
ATPases Vacuolares Próton-Translocadoras/genética
[Mh] Termos MeSH secundário: Adaptação Fisiológica/genética
Membrana Celular/efeitos dos fármacos
Membrana Celular/enzimologia
Membranas Intracelulares/efeitos dos fármacos
Membranas Intracelulares/enzimologia
Isoenzimas/genética
Isoenzimas/metabolismo
Células Vegetais/efeitos dos fármacos
Células Vegetais/enzimologia
Proteínas de Plantas/metabolismo
Raízes de Plantas/enzimologia
Raízes de Plantas/crescimento & desenvolvimento
Salinidade
Plântulas/efeitos dos fármacos
Plântulas/enzimologia
Plântulas/crescimento & desenvolvimento
Sódio/metabolismo
ATPases Vacuolares Próton-Translocadoras/metabolismo
Vacúolos/efeitos dos fármacos
Vacúolos/enzimologia
Zea mays/efeitos dos fármacos
Zea mays/enzimologia
Zea mays/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Plant Proteins); 0 (Protective Agents); 0 (Pyrimidines); 451W47IQ8X (Sodium Chloride); 9NEZ333N27 (Sodium); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases)
[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:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.02.089


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[PMID]:28465657
[Au] Autor:Haque R; Iuvone PM; He L; Choi KSC; Ngo A; Gokhale S; Aseem M; Park D
[Ad] Endereço:Department of Ophthalmology, Emory University School of Medicine, Atlanta, GA.
[Ti] Título:The MicroRNA-21 signaling pathway is involved in prorenin receptor (PRR) -induced VEGF expression in ARPE-19 cells under a hyperglycemic condition.
[So] Source:Mol Vis;23:251-262, 2017.
[Is] ISSN:1090-0535
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: MicroRNAs (miRNAs/miRs) are involved in a large number of biological functions and diseases, such as cancer, cardiovascular diseases, and diabetes. MiR-21 has been reported to target Sprouty homolog 1 (SPRY1), SMAD7, and PTEN. In this study, we examined the underlying role of miR-21 in the regulation of prorenin receptor (PRR)-mediated induction of vascular endothelial growth factor (VEGF) expression via targeting SMAD7, SPRY1, and PTEN in a hyperglycemic condition. METHODS: PRR-mediated induction of VEGF under a hyperglycemic condition (high glucose, 33mM) was studied by treating ARPE-19 cells with perindopril (10 µmol/l), which inhibits angiotensin II-mediated signaling. ARPE-19 cells exposed to normal glucose (NG, 5.5 mM) were considered as the control. To examine the role of miR-21 in the regulation of SPRY1, SMAD7, PTEN, and VEGF, ARPE-19 cells cultured in NG or high glucose were transfected with scramble negative control (Scr), a miR-21 mimic, or a miR-21 antagomir. To investigate the role of PRR and the small GTP-binding protein RAC1 in the regulation of miR-21, the expression of PRR and RAC1 was silenced by transfecting ARPE-19 cells with their corresponding siRNAs. RESULTS: Compared with the NG control, high glucose significantly induced the expression of PRR, VEGF, VEGFR2, and miR-21 but significantly suppressed the expression of SPRY1, SMAD7, and PTEN at the transcript and protein levels. In contrast, silencing the expression of PRR significantly abolished the high glucose-induced expression of VEGF, VEGFR2, and miR-21. Knockdown of RAC1 significantly attenuated the high glucose-induced expression of LOX, CTGF, and miR-21, suggesting that PRR and RAC1 are involved in the CTGF/LOX-mediated regulation of miR-21. Furthermore, high glucose dramatically increased the levels of pERK (p44), hypoxia-inducible factor (HIF-1α), and VEGF. However, this effect was antagonized by the miR-21 antagomir, indicative of the involvement of high glucose-induced miR-21 in the regulation of VEGF through ERK signaling. CONCLUSIONS: Our findings, for the first time, showed that the pleiotropic action of miR-21 induced the expression of pERK, HIF-1α, and VEGF in the high glucose condition by simultaneously targeting SPRY1, SMAD7, and PTEN in ARPE-19 cells. Therefore, miR-21 may serve as a potential therapeutic target for diabetes-induced retinal pathology.
[Mh] Termos MeSH primário: Hiperglicemia/metabolismo
MicroRNAs/fisiologia
Receptores de Superfície Celular/metabolismo
Epitélio Pigmentado da Retina/metabolismo
Transdução de Sinais/fisiologia
ATPases Vacuolares Próton-Translocadoras/metabolismo
Fator A de Crescimento do Endotélio Vascular/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Glucose/farmacologia
Seres Humanos
Immunoblotting
Proteínas de Membrana/metabolismo
PTEN Fosfo-Hidrolase/metabolismo
Fosfoproteínas/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Epitélio Pigmentado da Retina/efeitos dos fármacos
Proteína Smad7/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATP6AP2 protein, human); 0 (MIRN21 microRNA, human); 0 (Membrane Proteins); 0 (MicroRNAs); 0 (Phosphoproteins); 0 (Receptors, Cell Surface); 0 (SMAD7 protein, human); 0 (SPRY1 protein, human); 0 (Smad7 Protein); 0 (VEGFA protein, human); 0 (Vascular Endothelial Growth Factor A); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (PTEN protein, human); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


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[PMID]:29237407
[Au] Autor:Ajmal M; Mir A; Wahid S; Khor CC; Foo JN; Siddiqi S; Kauser M; Malik SA; Nasir M
[Ad] Endereço:Institute of Biomedical and Genetic Engineering, 24-Mauve area, G-9/1, Islamabad, 44000, Pakistan.
[Ti] Título:Identification and in silico characterization of a novel p.P208PfsX1 mutation in V-ATPase a3 subunit associated with autosomal recessive osteopetrosis in a Pakistani family.
[So] Source:BMC Med Genet;18(1):148, 2017 12 13.
[Is] ISSN:1471-2350
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Osteopetrosis is a rare inherited bone disorder mainly described as an increased bone density caused by defective osteoclastic bone resorption. To date, genetic variants of eleven genes have been reported so far to be associated with different types of osteopetrosis. However, malignant infantile osteopetrosis, a lethal form of the disease, is mostly (50%) caused by mutation(s) in TCIRG1 gene. In this study, we investigated a consanguineous Pakistani family clinically and genetically to elucidate underlying molecular basis of the infantile osteopetrosis. METHODS: DNA samples from five family members were subjected to SNP-array based whole genome homozygosity mapping. Data was analyzed and potentially pathogenic mutation was identified by Sanger sequencing of two affected as well as three phenotypically healthy individuals in the family. The significance of identified pathogenic variation and its impact on protein structure and function was studied using various bioinformatics tools. RESULTS: DNA samples from five family members were subjected to genome-wide SNP array genotyping and homozygosity mapping which identified ~4 Mb region on chr11 harboring the TCIRG1 gene. Sanger sequencing unveiled a novel homozygous deletion c. 624delC in exon 6 of the TCIRG1 gene encodes a3 subunit of V-ATPase complex. The identified deletion resulted in a frame shift producing a truncated protein of 208 aa. In silico analysis of premature termination of the a3 subunit of V-ATPase complex revealed deleterious effects on the protein structure, predicting impaired or complete loss of V-ATPase function causing infantile osteopetrosis. CONCLUSIONS: Since a3 subunit of V-ATPase complex plays a crucial role in bone resorption process, structurally abnormal a3 subunit might have adversely affected bone resorption process, leading to infantile osteopetrosis in Pakistani family. Therefore, the present study not only expands the genotypic spectrum of osteopetrosis but also improve understandings of the role of V-ATPase a3 subunit in bone resorption process. Moreover, our findings should help in genetic counseling and provide further insight into the disease pathogenesis and potential targeted therapy.
[Mh] Termos MeSH primário: Simulação por Computador
Mutação
Osteopetrose/genética
ATPases Vacuolares Próton-Translocadoras/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Reabsorção Óssea/metabolismo
Pré-Escolar
Análise Mutacional de DNA
Éxons
Genótipo
Homozigoto
Seres Humanos
Lactente
Simulação de Acoplamento Molecular
Osteopetrose/diagnóstico por imagem
Osteopetrose/fisiopatologia
Paquistão
Deleção de Sequência
ATPases Vacuolares Próton-Translocadoras/metabolismo
ATPases Vacuolares Próton-Translocadoras/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (TCIRG1 protein, human); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171231
[Lr] Data última revisão:
171231
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171215
[St] Status:MEDLINE
[do] DOI:10.1186/s12881-017-0506-4


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[PMID]:28899778
[Au] Autor:Konarzewska P; Sherr GL; Ahmed S; Ursomanno B; Shen CH
[Ad] Endereço:Department of Biology, College of Staten Island, City University of New York, 2800 Victory Blvd, Staten Island, NY 10314, USA; PhD Program in Biology, The Graduate Center, City University of New York, 365 Fifth Avenue, New York 10016, USA.
[Ti] Título:Vma3p protects cells from programmed cell death through the regulation of Hxk2p expression.
[So] Source:Biochem Biophys Res Commun;493(1):233-239, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In yeast, the vacuolar proton-pumping ATPase (V-ATPase) acidifies vacuoles to maintain pH of cytoplasm. Yeast cells lacking V-ATPase activity, due to a disruption of any VMA (vacuolar membrane ATPase) gene, remain viable but demonstrate growth defects. Although it has been suggested that VMA genes are critical for phospholipid biosynthesis, the link between VMA genes and phospholipid biosynthesis is still uncertain. Here, we found that cells lacking Vma3p, one of the major V-ATPase assembly genes, had a growth defect in the absence of inositol, suggesting that Vma3p is important in phospholipid biosynthesis. Through real-time PCR, we found that cells lacking Vma3p down-regulated HXK2 expression. Furthermore, acetic acid sensitivity assay showed that cells lacking Vma3p were more sensitive to acetic acid than WT cells. HXK2 encodes hexokinase 2 which can phosphorylate glucose during phospholipid biosynthesis. Since cells lacking HXK2 are sensitive to acetic acid and this is an indicator of programmed cell death, our observations suggest that Vma3p plays an important role in programmed cell death. Taken together, we have proposed a working model to describe how Vma3p protects cells against apoptosis through the regulation of HXK2 expression.
[Mh] Termos MeSH primário: Proteínas Reguladoras de Apoptose/metabolismo
Apoptose/fisiologia
Regulação Fúngica da Expressão Gênica/fisiologia
Hexoquinase/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/fisiologia
ATPases Vacuolares Próton-Translocadoras/metabolismo
[Mh] Termos MeSH secundário: Proliferação Celular/fisiologia
Saccharomyces cerevisiae/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoptosis Regulatory Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.7.1.1 (HXK2 protein, S cerevisiae); EC 2.7.1.1 (Hexokinase); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases); EC 3.6.3.14 (VMA3 protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE


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[PMID]:28791742
[Au] Autor:Mahmud MN; Oda M; Usui D; Inoshima Y; Ishiguro N; Kamatari YO
[Ad] Endereço:The United Graduate School of Veterinary Sciences, Gifu University, Gifu, 501-1193, Japan.
[Ti] Título:A multispecific monoclonal antibody G2 recognizes at least three completely different epitope sequences with high affinity.
[So] Source:Protein Sci;26(11):2162-2169, 2017 Nov.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A monoclonal antibody (mAb) G2 possesses an unusual characteristic of reacting with at least three proteins (ATP6V1C1, SEPT3, and C6H10orf76) other than its original antigen, chicken prion protein (ChPrP). The epitopes on ChPrP and ATP6V1C1 have been identified previously. In this study, we identified the epitope in the third protein, SEPT3. Interestingly, there was no amino acid sequence similarity among the epitopes on the three proteins. These epitopes had high binding affinities to G2 (K = ∼10 M for monovalent binding and K = ∼10 M for divalent binding), as determined using a SPR biosensor. This is the first report on a three-in-one mAb recognizing completely different epitope sequences with high affinity. Additionally, competitive ELISA indicated that the binding sites on G2, specific for the three different epitopes, overlapped, suggesting that the antigen-binding site may be flexible in the free form and capable of adapting to at least three different conformations to enable interactions with three different antigens.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/metabolismo
Epitopos/química
Proteínas Nucleares/química
Proteínas Priônicas/química
Septinas/química
ATPases Vacuolares Próton-Translocadoras/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Anticorpos Monoclonais/biossíntese
Anticorpos Monoclonais/química
Afinidade de Anticorpos
Especificidade de Anticorpos
Reações Antígeno-Anticorpo
Sítios de Ligação
Ligação Competitiva
Galinhas
Clonagem Molecular
Ensaio de Imunoadsorção Enzimática
Mapeamento de Epitopos
Epitopos/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Cinética
Proteínas Nucleares/genética
Proteínas Nucleares/imunologia
Proteínas Priônicas/genética
Proteínas Priônicas/imunologia
Ligação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/imunologia
Septinas/genética
Septinas/imunologia
Ressonância de Plasmônio de Superfície
ATPases Vacuolares Próton-Translocadoras/genética
ATPases Vacuolares Próton-Translocadoras/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Epitopes); 0 (Nuclear Proteins); 0 (Prion Proteins); 0 (Recombinant Proteins); EC 3.6.1.- (Septins); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3263


  9 / 2376 MEDLINE  
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[PMID]:28756231
[Au] Autor:Sherr GL; LaMassa N; Li E; Phillips G; Shen CH
[Ad] Endereço:Department of Biology, College of Staten Island, City University of New York, 2800 Victory Blvd, Staten Island, NY 10314, United States; PhD Program in Biology, The Graduate Center, City University of New York, 365 Fifth Avenue, New York 10016, United States.
[Ti] Título:Pah1p negatively regulates the expression of V-ATPase genes as well as vacuolar acidification.
[So] Source:Biochem Biophys Res Commun;491(3):693-700, 2017 Sep 23.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In yeast, PAH1 plays an important role in cell homeostasis and lipid biosynthesis. PAH1 encodes for the PA phosphatase, Pah1p, which is responsible for de novo TAG and phospholipid synthesis. It has been suggested that the lack of Pah1p causes irregular vacuolar morphology and dysfunctional V-ATPase pump activity. However, the molecular connection between Pah1p and V-ATPase activity has remained unclear. Through real-time PCR, we have shown that PAH1 is maximally induced at the stationary stage in the presence of inositol. We also found that vacuoles were less fragmented when PAH1 is maximally expressed. Subsequently, we observed that vacuoles from pah1Δ cells were more acidic than those in WT cells. Furthermore, V-ATPase genes were upregulated in the absence of Pah1p. These results suggest that Pah1p plays an important role in vacuolar activity by negatively regulating the expression of V-ATPase genes. As such, we provide evidence to show the role of Pah1p in vacuolar acidification and fragmentation.
[Mh] Termos MeSH primário: Inositol/metabolismo
Fosfatidato Fosfatase/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
ATPases Vacuolares Próton-Translocadoras/química
ATPases Vacuolares Próton-Translocadoras/metabolismo
Vacúolos/química
Vacúolos/metabolismo
[Mh] Termos MeSH secundário: Regulação para Baixo/fisiologia
Regulação Enzimológica da Expressão Gênica/fisiologia
Concentração de Íons de Hidrogênio
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Saccharomyces cerevisiae Proteins); 4L6452S749 (Inositol); EC 3.1.3.4 (PAH1 protein, S cerevisiae); EC 3.1.3.4 (Phosphatidate Phosphatase); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170731
[St] Status:MEDLINE


  10 / 2376 MEDLINE  
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[PMID]:28738127
[Au] Autor:Kunkle BW; Vardarajan BN; Naj AC; Whitehead PL; Rolati S; Slifer S; Carney RM; Cuccaro ML; Vance JM; Gilbert JR; Wang LS; Farrer LA; Reitz C; Haines JL; Beecham GW; Martin ER; Schellenberg GD; Mayeux RP; Pericak-Vance MA
[Ad] Endereço:John P. Hussman Institute for Human Genomics, Miller School of Medicine, University of Miami, Miami, Florida.
[Ti] Título:Early-Onset Alzheimer Disease and Candidate Risk Genes Involved in Endolysosomal Transport.
[So] Source:JAMA Neurol;74(9):1113-1122, 2017 Sep 01.
[Is] ISSN:2168-6157
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Importance: Mutations in APP, PSEN1, and PSEN2 lead to early-onset Alzheimer disease (EOAD) but account for only approximately 11% of EOAD overall, leaving most of the genetic risk for the most severe form of Alzheimer disease unexplained. This extreme phenotype likely harbors highly penetrant risk variants, making it primed for discovery of novel risk genes and pathways for AD. Objective: To search for rare variants contributing to the risk for EOAD. Design, Setting, and Participants: In this case-control study, whole-exome sequencing (WES) was performed in 51 non-Hispanic white (NHW) patients with EOAD (age at onset <65 years) and 19 Caribbean Hispanic families previously screened as negative for established APP, PSEN1, and PSEN2 causal variants. Participants were recruited from John P. Hussman Institute for Human Genomics, Case Western Reserve University, and Columbia University. Rare, deleterious, nonsynonymous, or loss-of-function variants were filtered to identify variants in known and suspected AD genes, variants in multiple unrelated NHW patients, variants present in 19 Hispanic EOAD WES families, and genes with variants in multiple unrelated NHW patients. These variants/genes were tested for association in an independent cohort of 1524 patients with EOAD, 7046 patients with late-onset AD (LOAD), and 7001 cognitively intact controls (age at examination, >65 years) from the Alzheimer's Disease Genetics Consortium. The study was conducted from January 21, 2013, to October 13, 2016. Main Outcomes and Measures: Alzheimer disease diagnosed according to standard National Institute of Neurological and Communicative Disorders and Stroke and the Alzheimer Disease and Related Disorders Association criteria. Association between Alzheimer disease and genetic variants and genes was measured using logistic regression and sequence kernel association test-optimal gene tests, respectively. Results: Of the 1524 NHW patients with EOAD, 765 (50.2%) were women and mean (SD) age was 60.0 (4.9) years; of the 7046 NHW patients with LOAD, 4171 (59.2%) were women and mean (SD) age was 77.4 (8.6) years; and of the 7001 NHW controls, 4215 (60.2%) were women and mean (SD) age was 77.4 (8.6) years. The gene PSD2, for which multiple unrelated NHW cases had rare missense variants, was significantly associated with EOAD (P = 2.05 × 10-6; Bonferroni-corrected P value [BP] = 1.3 × 10-3) and LOAD (P = 6.22 × 10-6; BP = 4.1 × 10-3). A missense variant in TCIRG1, present in a NHW patient and segregating in 3 cases of a Hispanic family, was more frequent in EOAD cases (odds ratio [OR], 2.13; 95% CI, 0.99-4.55; P = .06; BP = 0.413), and significantly associated with LOAD (OR, 2.23; 95% CI, 1.37-3.62; P = 7.2 × 10-4; BP = 5.0 × 10-3). A missense variant in the LOAD risk gene RIN3 showed suggestive evidence of association with EOAD after Bonferroni correction (OR, 4.56; 95% CI, 1.26-16.48; P = .02, BP = 0.091). In addition, a missense variant in RUFY1 identified in 2 NHW EOAD cases showed suggestive evidence of an association with EOAD as well (OR, 18.63; 95% CI, 1.62-213.45; P = .003; BP = 0.129). Conclusions and Relevance: The genes PSD2, TCIRG1, RIN3, and RUFY1 all may be involved in endolysosomal transport-a process known to be important to development of AD. Furthermore, this study identified shared risk genes between EOAD and LOAD similar to previously reported genes, such as SORL1, PSEN2, and TREM2.
[Mh] Termos MeSH primário: Doença de Alzheimer/genética
Transporte Biológico/genética
Proteínas de Transporte/genética
Fatores de Troca do Nucleotídeo Guanina/genética
Peptídeos e Proteínas de Sinalização Intracelular/genética
ATPases Vacuolares Próton-Translocadoras/genética
[Mh] Termos MeSH secundário: Idade de Início
Idoso
Idoso de 80 Anos ou mais
Região do Caribe
Estudos de Casos e Controles
Grupo com Ancestrais do Continente Europeu/genética
Exoma
Feminino
Hispano-Americanos/genética
Seres Humanos
Masculino
Meia-Idade
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Guanine Nucleotide Exchange Factors); 0 (Intracellular Signaling Peptides and Proteins); 0 (RIN3 protein, human); 0 (RUFY1 protein, human); 0 (TCIRG1 protein, human); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE
[do] DOI:10.1001/jamaneurol.2017.1518



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