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  1 / 1215 MEDLINE  
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[PMID]:29243276
[Au] Autor:Baldassini WA; Ramsey JJ; Hagopian K; Lanna DPD
[Ad] Endereço:Department of Animal Science, "Luiz de Queiroz" College of Agriculture (ESALQ), University of São Paulo (USP), Piracicaba, São Paulo, Brazil.
[Ti] Título:The influence of Shc proteins and high-fat diet on energy metabolism of mice.
[So] Source:Cell Biochem Funct;35(8):527-537, 2017 Dec.
[Is] ISSN:1099-0844
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The purpose of this study was to determine if Shc proteins influence the metabolic response to acute (7 days) feeding of a high-fat diet (HFD). To this end, whole animal energy expenditure (EE) and substrate oxidation were measured in the Shc knockout (ShcKO) and wild-type (WT) mice fed a control or HFD. The activities of enzymes of glycolysis, the citric acid cycle, electron transport chain (ETC), and ß-oxidation were also investigated in liver and skeletal muscle of ShcKO and WT animals. The study showed that ShcKO increases (P < .05) EE adjusted for either total body weight or lean mass. This change in EE could contribute to decreases in weight gain in ShcKO versus WT mice fed an HFD. Thus, our results indicate that Shc proteins should be considered as potential targets for developing interventions to mitigate weight gain on HFD by stimulating EE. Although decreased levels of Shc proteins influenced the activity of some enzymes in response to high-fat feeding (eg, increasing the activity of acyl-CoA dehydrogenase), it did not produce concerted changes in enzymes of glycolysis, citric acid cycle, or the ETC. The physiological significance of observed changes in select enzyme activities remains to be determined. SIGNIFICANCE OF THE STUDY: We report higher EE in ShcKO versus WT mice when consuming the HFD. Although decreased levels of Shc proteins influenced the activity of a central enzyme of ß-oxidation in response to high-fat feeding, it did not produce concerted changes in enzymes of glycolysis, citric acid cycle, or the ETC. Thus, an increase in EE in response to consumption of an HFD may be a mechanism that leads to decreased weight gain previously reported in ShcKO mice with long-term consumption of an HFD.
[Mh] Termos MeSH primário: Dieta Hiperlipídica/efeitos adversos
Metabolismo Energético
Proteínas Adaptadoras da Sinalização Shc/metabolismo
[Mh] Termos MeSH secundário: Animais
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteínas Adaptadoras da Sinalização Shc/deficiência
Ganho de Peso
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Shc Signaling Adaptor Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180101
[Lr] Data última revisão:
180101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1002/cbf.3310


  2 / 1215 MEDLINE  
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[PMID]:28213521
[Au] Autor:Wills MK; Keyvani Chahi A; Lau HR; Tilak M; Guild BD; New LA; Lu P; Jacquet K; Meakin SO; Bisson N; Jones N
[Ad] Endereço:From the Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
[Ti] Título:Signaling adaptor ShcD suppresses extracellular signal-regulated kinase (Erk) phosphorylation distal to the Ret and Trk neurotrophic receptors.
[So] Source:J Biol Chem;292(14):5748-5759, 2017 Apr 07.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proteins of the Src homology and collagen (Shc) family are typically involved in signal transduction events involving Ras/MAPK and PI3K/Akt pathways. In the nervous system, they function proximal to the neurotrophic factors that regulate cell survival, differentiation, and neuron-specific characteristics. The least characterized homolog, ShcD, is robustly expressed in the developing and mature nervous system, but its contributions to neural cell circuitry are largely uncharted. We now report that ShcD binds to active Ret, TrkA, and TrkB neurotrophic factor receptors predominantly via its phosphotyrosine-binding (PTB) domain. However, in contrast to the conventional Shc adaptors, ShcD suppresses distal phosphorylation of the Erk MAPK. Accordingly, genetic knock-out of mouse ShcD enhances Erk phosphorylation in the brain. In cultured cells, this capacity is tightly aligned to phosphorylation of ShcD CH1 region tyrosine motifs, which serve as docking platforms for signal transducers, such as Grb2. Erk suppression is relieved through independent mutagenesis of the PTB domain and the CH1 tyrosine residues, and successive substitution of these tyrosines breaks the interaction between ShcD and Grb2, thereby promoting TrkB-Grb2 association. Erk phosphorylation can also be restored in the presence of wild type ShcD through Grb2 overexpression. Conversely, mutation of the ShcD SH2 domain results in enhanced repression of Erk. Although the SH2 domain is a less common binding interface in Shc proteins, we demonstrate that it associates with the Ptpn11 (Shp2) phosphatase, which in turn regulates ShcD tyrosine phosphorylation. We therefore propose a model whereby ShcD competes with neurotrophic receptors for Grb2 binding and opposes activation of the MAPK cascade.
[Mh] Termos MeSH primário: MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Sistema de Sinalização das MAP Quinases/fisiologia
Glicoproteínas de Membrana/metabolismo
Proteínas Tirosina Quinases/metabolismo
Proteínas Proto-Oncogênicas c-ret/metabolismo
Receptor trkA/metabolismo
Proteínas Adaptadoras da Sinalização Shc/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Linhagem Celular
MAP Quinases Reguladas por Sinal Extracelular/genética
Proteína Adaptadora GRB2/genética
Proteína Adaptadora GRB2/metabolismo
Seres Humanos
Glicoproteínas de Membrana/genética
Fosforilação/fisiologia
Proteína Tirosina Fosfatase não Receptora Tipo 11/genética
Proteína Tirosina Fosfatase não Receptora Tipo 11/metabolismo
Proteínas Tirosina Quinases/genética
Proteínas Proto-Oncogênicas c-ret/genética
Receptor trkA/genética
Receptor trkB
Proteínas Adaptadoras da Sinalização Shc/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GRB2 Adaptor Protein); 0 (GRB2 protein, human); 0 (Membrane Glycoproteins); 0 (SHC4 protein, human); 0 (Shc Signaling Adaptor Proteins); 0 (TRKA protein, human); EC 2.7.10.1 (Protein-Tyrosine Kinases); EC 2.7.10.1 (Proto-Oncogene Proteins c-ret); EC 2.7.10.1 (RET protein, human); EC 2.7.10.1 (Receptor, trkA); EC 2.7.10.1 (Receptor, trkB); EC 2.7.10.1 (tropomyosin-related kinase-B, human); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 3.1.3.48 (PTPN11 protein, human); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 11)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170219
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.770511


  3 / 1215 MEDLINE  
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[PMID]:27830506
[Au] Autor:Hammerling U
[Ad] Endereço:Member Emeritus, Immunology Program, Sloan-Kettering Institute for Cancer Research, 10065, New York, NY, USA. uhammerling@gmail.com.
[Ti] Título:Vitamin A as PKC Co-factor and Regulator of Mitochondrial Energetics.
[So] Source:Subcell Biochem;81:201-230, 2016.
[Is] ISSN:0306-0225
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:For the past century, vitamin A has been considered to serve as a precursor for retinoids that facilitate vision or as a precursor for retinoic acid (RA), a signaling molecule that modulates gene expression. However, vitamin A circulates in plasma at levels that far exceed the amount needed for vision or the synthesis of nanomolar levels of RA, and this suggests that vitamin A alcohol (i.e. retinol) may possess additional biological activity. We have pursued this question for the last 20 years, and in this chapter, we unfold the story of our quest and the data that support a novel and distinct role for vitamin A (alcohol) action. Our current model supports direct binding of vitamin A to the activation domains of serine/threonine kinases, such as protein kinase C (PKC) and Raf isoforms, where it is involved in redox activation of these proteins. Redox activation of PKCs was first described by the founders of the PKC field, but several hurdles needed to be overcome before a detailed understanding of the biochemistry could be provided. Two discoveries moved the field forward. First, was the discovery that the PKCδ isoform was activated by cytochrome c, a protein with oxidoreduction activity in mitochondria. Second, was the revelation that both PKCδ and cytochrome c are tethered to p66Shc, an adapter protein that brings the PKC zinc-finger substrate into close proximity with its oxidizing partner. Detailed characterization of the PKCδ signalosome complex was made possible by the work of many investigators. Our contribution was determining that vitamin A is a vital co-factor required to support an unprecedented redox-activation mechanism. This unique function of vitamin A is the first example of a general system that connects the one-electron redox chemistry of a heme protein (cytochrome c) with the two-electron chemistry of a classical phosphoprotein (PKCδ). Furthermore, contributions to the regulation of mitochondrial energetics attest to biological significance of vitamin A alcohol action.
[Mh] Termos MeSH primário: Mitocôndrias/metabolismo
Proteína Quinase C-delta/metabolismo
Vitamina A/fisiologia
[Mh] Termos MeSH secundário: Animais
Citocromos c/metabolismo
Metabolismo Energético
Ativação Enzimática/efeitos dos fármacos
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/fisiologia
Previsões
Proteínas de Choque Térmico/química
Proteínas de Choque Térmico/fisiologia
Seres Humanos
Mitocôndrias/enzimologia
Oxirredução
Estresse Oxidativo
Ligação Proteica
Isoformas de Proteínas/metabolismo
Proteína Quinase C-épsilon/fisiologia
Proteínas Adaptadoras da Sinalização Shc/fisiologia
Vitamina A/análogos & derivados
Dedos de Zinco
Quinases raf/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (HSP33 protein, E coli); 0 (Heat-Shock Proteins); 0 (Protein Isoforms); 0 (Shc Signaling Adaptor Proteins); 11103-57-4 (Vitamin A); 235BBF3K97 (anhydrovitamin A); 9007-43-6 (Cytochromes c); EC 2.7.11.1 (raf Kinases); EC 2.7.11.13 (Protein Kinase C-delta); EC 2.7.11.13 (Protein Kinase C-epsilon)
[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:161111
[St] Status:MEDLINE


  4 / 1215 MEDLINE  
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[PMID]:27129942
[Au] Autor:Feng W; Li HC; Xu K; Chen YF; Pan LY; Mei Y; Cai H; Jiang YM; Chen T; Feng DX
[Ad] Endereço:Department of General Surgery, Putuo Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai 200062, China.
[Ti] Título:SHCBP1 is over-expressed in breast cancer and is important in the proliferation and apoptosis of the human malignant breast cancer cell line.
[So] Source:Gene;587(1):91-7, 2016 Aug 01.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: SHC SH2-binding protein 1, a member of Src homolog and collagen homolog (Shc) family, has been recently identified in different contexts in unbiased screening assays. It has been reported to be over-expressed in several malignant cancers. METHODS: Immunohistochemistry of SHCBP1 on 128 breast cancer tissues and adjacent normal tissues were used to evaluate the prognostic significance of SHCBP1. Survival analyses were performed by Kaplan-Meier method. CRISPR/CAS9 method was used to knockout SHCBP1 expression. CRISPR/CAS9 technology was used to knockout SHCBP1 in 2 breast cancer cell lines. MTT assay, BrdU assay, colony formation assay, cell cycle assay and apoptosis analysis in MCF-7 and MDA-MB-231 cell lines were carried out to evaluate the effects of SHCBP1 on breast cancer in vitro. RESULTS: Immunohistochemical analysis revealed SHCBP1 was significantly up-regulated in breast cancer tissues compared with adjacent normal tissues (82 of 128, 64%). Over-expressed SHCBP1 was correlated with advanced clinical stage and poorer survival. Ablation of SHCBP1 inhibited the proliferation in vitro. SHCBP1 knockout increased cyclin-dependent kinase inhibitor p21, and decreased the Cyclin B1 and CDK1. CONCLUSION: Our study suggests SHCBP1 is dysregulated expressed in breast cancer and plays a critical role in cancer progression, which can be a potential prognosis predictor of breast cancer.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Neoplasias da Mama/patologia
Proteínas Adaptadoras da Sinalização Shc/metabolismo
[Mh] Termos MeSH secundário: Adulto
Apoptose
Biomarcadores/metabolismo
Neoplasias da Mama/diagnóstico
Linhagem Celular Tumoral
Proliferação Celular
Feminino
Técnicas de Inativação de Genes
Seres Humanos
Meia-Idade
Prognóstico
Proteínas Adaptadoras da Sinalização Shc/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (SHCBP1 protein, human); 0 (Shc Signaling Adaptor Proteins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170111
[Lr] Data última revisão:
170111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160501
[St] Status:MEDLINE


  5 / 1215 MEDLINE  
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[PMID]:27059956
[Au] Autor:Tomilov A; Tomilova N; Shan Y; Hagopian K; Bettaieb A; Kim K; Pelicci PG; Haj F; Ramsey J; Cortopassi G
[Ad] Endereço:From the Departments of ‡Molecular Biosciences.
[Ti] Título:p46Shc Inhibits Thiolase and Lipid Oxidation in Mitochondria.
[So] Source:J Biol Chem;291(24):12575-85, 2016 Jun 10.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although the p46Shc isoform has been known to be mitochondrially localized for 11 years, its function in mitochondria has been a mystery. We confirmed p46Shc to be mitochondrially localized and showed that the major mitochondrial partner of p46Shc is the lipid oxidation enzyme 3-ketoacylCoA thiolase ACAA2, to which p46Shc binds directly and with a strong affinity. Increasing p46Shc expression inhibits, and decreasing p46Shc stimulates enzymatic activity of thiolase in vitro Thus, we suggest p46Shc to be a negative mitochondrial thiolase activity regulator, and reduction of p46Shc expression activates thiolase. This is the first demonstration of a protein that directly binds and controls thiolase activity. Thiolase was thought previously only to be regulated by metabolite balance and steady-state flux control. Thiolase is the last enzyme of the mitochondrial fatty acid beta-oxidation spiral, and thus is important for energy metabolism. Mice with reduction of p46Shc are lean, resist obesity, have higher lipid oxidation capacity, and increased thiolase activity. The thiolase-p46Shc connection shown here in vitro and in organello may be an important underlying mechanism explaining the metabolic phenotype of Shc-depleted mice in vivo.
[Mh] Termos MeSH primário: Acetil-CoA C-Aciltransferase/metabolismo
Metabolismo dos Lipídeos
Mitocôndrias/metabolismo
Proteínas Mitocondriais/metabolismo
Proteínas Adaptadoras da Sinalização Shc/metabolismo
Proteína 1 de Transformação que Contém Domínio 2 de Homologia de Src/metabolismo
[Mh] Termos MeSH secundário: Acetil-CoA C-Aciltransferase/genética
Animais
Ligação Competitiva
Western Blotting
Linhagem Celular
Metabolismo Energético
Ácidos Graxos/metabolismo
Células HEK293
Células HeLa
Seres Humanos
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteínas Mitocondriais/genética
Células NIH 3T3
Oxirredução
Ligação Proteica
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Interferência de RNA
Proteínas Adaptadoras da Sinalização Shc/genética
Proteína 1 de Transformação que Contém Domínio 2 de Homologia de Src/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Mitochondrial Proteins); 0 (Protein Isoforms); 0 (Shc Signaling Adaptor Proteins); 0 (Shc1 protein, mouse); 0 (Src Homology 2 Domain-Containing, Transforming Protein 1); EC 2.3.1.- (Acaa2 protein, mouse); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160410
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.695577


  6 / 1215 MEDLINE  
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[PMID]:27004682
[Au] Autor:Shi H; Zhang T; Yi Y; Ma Y
[Ad] Endereço:College of Animal Science and Technology, Northwest A&F University, Yangling, Shaanxi 712100, P.R. China.
[Ti] Título:Inhibition of the Ras-ERK pathway in mitotic COS7 cells is due to the inability of EGFR/Raf to transduce EGF signaling to downstream proteins.
[So] Source:Oncol Rep;35(6):3593-9, 2016 Jun.
[Is] ISSN:1791-2431
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Although previous studies have shown that Ras-ERK signaling in mitosis is closed due to the inhibition of signal transduction, the events involved in the molecular mechanisms are still unclear. In the present study, we investigated the Ras-ERK signaling pathway in mitotic COS7 cells. The results demonstrated that treatment with epidermal growth factor (EGF) failed to increase the endocytosis of EGF-EGFR (EGF receptor) complexes in mitotic COS7 cells, although a large amount of endosomes were found in asynchronous COS7 cells. Clathrin expression levels in mitotic COS7 cells were inhibited whereas caveolin expression levels in mitotic COS7 cells were almost unaffected. Y1068 and Y1086 residues of EGFR in the mitotic COS7 cells were activated. However, Grb2 and Shc in the mitotic COS7 cells did not bind to activated EGFR. Ras activity was inhibited in the mitotic COS7 cells whereas its downstream protein, Raf, was obviously phosphorylated by EGF in mitosis. Treatment with phorbol 12-myristate 13-acetate (PMA) also increased the phosphorylation levels of Raf in the mitotic COS7 cells. Nevertheless, Raf phosphorylation in mitosis was significantly inhibited by AG1478. Lastly, activation of EGF-mediated MEK and ERK in the mitotic COS7 cells was obviously inhibited. In summary, our results suggest that the Ras-ERK pathway is inhibited in mitotic COS7 cells which may be the dual result of the difficulty in the transduction of EGF signaling by EGFR or Raf to downstream proteins.
[Mh] Termos MeSH primário: Fator de Crescimento Epidérmico/metabolismo
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Proteínas Proto-Oncogênicas c-raf/metabolismo
Proteínas Proto-Oncogênicas p21(ras)/metabolismo
Receptor do Fator de Crescimento Epidérmico/metabolismo
Quinases raf/metabolismo
[Mh] Termos MeSH secundário: Animais
Células COS
Caveolinas/biossíntese
Linhagem Celular
Cercopithecus aethiops
Clatrina/biossíntese
Endocitose/fisiologia
Endossomos/fisiologia
Proteína Adaptadora GRB2/metabolismo
Sistema de Sinalização das MAP Quinases
Nocodazol/farmacologia
Fosforilação/efeitos dos fármacos
Quinazolinas/farmacologia
Proteínas Adaptadoras da Sinalização Shc/metabolismo
Acetato de Tetradecanoilforbol/farmacologia
Tirfostinas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caveolins); 0 (Clathrin); 0 (GRB2 Adaptor Protein); 0 (Quinazolines); 0 (Shc Signaling Adaptor Proteins); 0 (Tyrphostins); 170449-18-0 (tyrphostin AG 1478); 62229-50-9 (Epidermal Growth Factor); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 2.7.11.1 (raf Kinases); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 3.6.5.2 (Proto-Oncogene Proteins p21(ras)); NI40JAQ945 (Tetradecanoylphorbol Acetate); SH1WY3R615 (Nocodazole)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170313
[Lr] Data última revisão:
170313
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160324
[St] Status:MEDLINE
[do] DOI:10.3892/or.2016.4696


  7 / 1215 MEDLINE  
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[PMID]:26874853
[Au] Autor:Siala-Sahnoun O; Dhieb D; Ben Thabet A; Hmida N; Belguith N; Fakhfakh F
[Ad] Endereço:Live Sciences Department, Faculty of Sciences of Sfax, Sfax, Tunisia. olfasiala9@gmail.com.
[Ti] Título:First molecular diagnosis of Donohue syndrome in Africa: novel unusual insertion/deletion mutation in the INSR gene.
[So] Source:Mol Biol Rep;43(3):165-73, 2016 Mar.
[Is] ISSN:1573-4978
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Donohue syndrome (DS) is a very rare autosomal recessive disease affecting less than one in a million life births. It represents the most severe form of insulin resistance due to mutations involving the insulin receptor (IR) gene "INSR". DS is characterized by pre- and postnatal growth retardation with failure-to-thrive, lipoatrophy, acanthosis nigricans, hypertrichosis, and dysmorphic features. An exhaustive INSR gene sequencing was performed after PCR amplification of coding exons and introns boundaries. Bioinformatic tools, including ESEfinder, MFOLD and Proter software were also used to predict the impact of INSR mutation on INSR on gene expression as well as on the protein structure and function. The results have shown a novel unusual c.3003_3012delinsGGAAG (p.S1001_D1004delinsRE) insertion/deletion (indel) mutation within the exon 16 in the three patients, which represent the fourth indel mutation within the INSR gene. The mutation modifies the secondary structure of DNA and RNA, as well as the composition of exonic splicing enhancers of exon 16. Moreover, despite the conservation of the secondary structure of the IR, the p.S1001_D1004delinsRE in-frame mutation is accompanied by the loss of four amino acids replaced by two residues of different nature and hydrophobicity level in the juxtamembrane domain of the receptor. The results have confirmed the role of the juxtamembrane domain of IR involved in a crucial interaction of the IR with cellular effectors essentially the IR substrate 1 (IRS-1), the SHC and the Nck proteins that ensure the signal mediated by the insulin transduction pathway in target cells. Our findings have also proven the genotype/phenotype correlation between INSR mutation and DS phenotype severity.
[Mh] Termos MeSH primário: Antígenos CD/genética
Síndrome de Donohue/metabolismo
Mutação INDEL
Receptor de Insulina/genética
Transdução de Sinais
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
África
Sequência de Aminoácidos
Antígenos CD/metabolismo
Síndrome de Donohue/genética
Feminino
Expressão Gênica
Seres Humanos
Lactente
Recém-Nascido
Proteínas Substratos do Receptor de Insulina/metabolismo
Masculino
Dados de Sequência Molecular
Proteínas Oncogênicas/metabolismo
Estrutura Secundária de Proteína
Receptor de Insulina/metabolismo
Alinhamento de Sequência
Análise de Sequência de DNA
Proteínas Adaptadoras da Sinalização Shc/metabolismo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Antigens, CD); 0 (IRS1 protein, human); 0 (Insulin Receptor Substrate Proteins); 0 (Nck protein); 0 (Oncogene Proteins); 0 (Shc Signaling Adaptor Proteins); EC 2.7.10.1 (INSR protein, human); EC 2.7.10.1 (Receptor, Insulin)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160215
[St] Status:MEDLINE
[do] DOI:10.1007/s11033-016-3951-9


  8 / 1215 MEDLINE  
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[PMID]:26804443
[Au] Autor:Chen SD; Ji BB; Yan YX; He X; Han KY; Dai QX; Zhang MX; Mo YC; Wang JL
[Ad] Endereço:Department of Anesthesiology, The First Affiliated Hospital of Wen Zhou Medical University, Wenzhou, Zhejiang 325000, China.
[Ti] Título:Carnosic acid attenuates neuropathic pain in rat through the activation of spinal sirtuin1 and down-regulation of p66shc expression.
[So] Source:Neurochem Int;93:95-102, 2016 Feb.
[Is] ISSN:1872-9754
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: It has been reported that carnosic acid (CA) exhibits a range of biological activities including hepatoprotective, antioxidant and anti-inflammatory. However, the effect of carnosic acid in neuropathic pain remained elusive. METHODS: A neuropathic pain model of chronic constriction injury (CCI) was established in adult male Sprague-Dawley rats. Mechanical withdrawal threshold (MWT) and thermal withdrawal latency (TWL) were recorded, and western blot was performed to detect sirtuin1 and p66shc content. RESULTS: Intrathecal administration of carnosic acid attenuated mechanical allodynia and thermal hyperalgesia in rats following chronic constriction injury. Interestingly, carnosic acid analgesic effect was positively associated with spinal sirtuin1 activation; however, p66shc was inhibited by carnosic acid in the spinal cord. In additional, sirtuin1 inhibitor EX-527 reversed the anti-nociceptive effect of carnosic acid. CONCLUSIONS: Carnosic acid is effective in the treatment of the established CCI-induced pain. It may be possible that spinal sirtuin1 activition by carnosic acid attenuates neuropathic pain through a mechanism involving the down-regulation of p66shc expression.
[Mh] Termos MeSH primário: Diterpenos Abietanos/farmacologia
Neuralgia/prevenção & controle
Proteínas Adaptadoras da Sinalização Shc/metabolismo
Sirtuína 1/metabolismo
Medula Espinal/metabolismo
[Mh] Termos MeSH secundário: Animais
Regulação para Baixo
Masculino
Ratos
Ratos Sprague-Dawley
Proteína 1 de Transformação que Contém Domínio 2 de Homologia de Src
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Diterpenes, Abietane); 0 (Shc Signaling Adaptor Proteins); 0 (Shc1 protein, rat); 0 (Src Homology 2 Domain-Containing, Transforming Protein 1); EC 3.5.1.- (Sirtuin 1); LI791SXT24 (salvin)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170103
[Lr] Data última revisão:
170103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160126
[St] Status:MEDLINE


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[PMID]:26802937
[Au] Autor:Yamagata K; Suzuki S; Tagami M
[Ad] Endereço:Department of Food Bioscience and Biotechnology, College of Bioresource Sciences, Nihon University (NUBS), Fujisawa, Japan. Electronic address: kyamagat@brs.nihon-u.ac.jp.
[Ti] Título:Docosahexaenoic acid prevented tumor necrosis factor alpha-induced endothelial dysfunction and senescence.
[So] Source:Prostaglandins Leukot Essent Fatty Acids;104:11-8, 2016 Jan.
[Is] ISSN:1532-2823
[Cp] País de publicação:Scotland
[La] Idioma:eng
[Ab] Resumo:We investigated how docosahexaenoic acid (DHA) regulated tumor necrosis factor-alpha (TNF-α)-induced senescence and dysfunction in endothelial cells (EC). We used RT-PCR to examine the expression of several genes related to senescence and dysfunction in EC. TNF-α-induced p21 protein levels were investigated by Western blot (WB) and fluorescence antibody techniques. TNF-α induced the senescence marker ß-galactosidase and the expression of several senescence and endothelial dysfunction-related genes, e.g., CDKN1A, SHC1 and GLB1. DHA attenuated TNF-α-induced senescence-related gene expression and p21 protein expression. DHA attenuated TNF-α-induced gene expression related to dysfunction of EC, such as plasminogen activator inhibitor 1 (SERPINE1), lectin-like oxidized low-density lipoprotein receptor-1 (OLR1), thromboxane A2 receptor (TXA2R) and p38 MAPK (MAPK14). DHA reversed the TNF-α-mediated reduction of endothelial nitric oxide synthase (NOS3) gene expression. TNF-α-mediated upregulation of these genes was inhibited by allopurinol and apocynin. These results indicated that DHA regulated the expression of several genes that are associated with senescence and dysfunction of EC.
[Mh] Termos MeSH primário: Senescência Celular/efeitos dos fármacos
Ácidos Docosa-Hexaenoicos/farmacologia
Células Endoteliais/efeitos dos fármacos
Células Endoteliais/metabolismo
Fator de Necrose Tumoral alfa/farmacologia
[Mh] Termos MeSH secundário: Linhagem Celular
Inibidor de Quinase Dependente de Ciclina p21/metabolismo
Seres Humanos
Óxido Nítrico Sintase Tipo III/metabolismo
Inibidor 1 de Ativador de Plasminogênio/metabolismo
Receptores Depuradores Classe E/metabolismo
Proteínas Adaptadoras da Sinalização Shc/metabolismo
Proteína 1 de Transformação que Contém Domínio 2 de Homologia de Src
beta-Galactosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CDKN1A protein, human); 0 (Cyclin-Dependent Kinase Inhibitor p21); 0 (OLR1 protein, human); 0 (Plasminogen Activator Inhibitor 1); 0 (SERPINE1 protein, human); 0 (SHC1 protein, human); 0 (Scavenger Receptors, Class E); 0 (Shc Signaling Adaptor Proteins); 0 (Src Homology 2 Domain-Containing, Transforming Protein 1); 0 (Tumor Necrosis Factor-alpha); 25167-62-8 (Docosahexaenoic Acids); EC 1.14.13.39 (NOS3 protein, human); EC 1.14.13.39 (Nitric Oxide Synthase Type III); EC 3.2.1.23 (GLB1 protein, human); EC 3.2.1.23 (beta-Galactosidase)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160124
[St] Status:MEDLINE


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[PMID]:26798412
[Au] Autor:Wu H; Li R; Wei ZH; Zhang XL; Chen JZ; Dai Q; Xie J; Xu B
[Ad] Endereço:Department of Cardiology, Drown Tower Hospital, Nanjing University Medical School, Nanjing 210008, China.
[Ti] Título:Diabetes-Induced Oxidative Stress in Endothelial Progenitor Cells May Be Sustained by a Positive Feedback Loop Involving High Mobility Group Box-1.
[So] Source:Oxid Med Cell Longev;2016:1943918, 2016.
[Is] ISSN:1942-0994
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oxidative stress is considered to be a critical factor in diabetes-induced endothelial progenitor cell (EPC) dysfunction, although the underlying mechanisms are not fully understood. In this study, we investigated the role of high mobility group box-1 (HMGB-1) in diabetes-induced oxidative stress. HMGB-1 was upregulated in both serum and bone marrow-derived monocytes from diabetic mice compared with control mice. In vitro, advanced glycation end productions (AGEs) induced, expression of HMGB-1 in EPCs and in cell culture supernatants in a dose-dependent manner. However, inhibition of oxidative stress with N-acetylcysteine (NAC) partially inhibited the induction of HMGB-1 induced by AGEs. Furthermore, p66shc expression in EPCs induced by AGEs was abrogated by incubation with glycyrrhizin (Gly), while increased superoxide dismutase (SOD) activity in cell culture supernatants was observed in the Gly treated group. Thus, HMGB-1 may play an important role in diabetes-induced oxidative stress in EPCs via a positive feedback loop involving the AGE/reactive oxygen species/HMGB-1 pathway.
[Mh] Termos MeSH primário: Diabetes Mellitus Experimental/patologia
Células Progenitoras Endoteliais/patologia
Retroalimentação Fisiológica
Proteína HMGB1/metabolismo
Estresse Oxidativo
[Mh] Termos MeSH secundário: Acetilcisteína/farmacologia
Animais
Glicemia/metabolismo
Peso Corporal/efeitos dos fármacos
Células da Medula Óssea/efeitos dos fármacos
Células da Medula Óssea/patologia
Células Cultivadas
Células Progenitoras Endoteliais/efeitos dos fármacos
Células Progenitoras Endoteliais/metabolismo
Produtos Finais de Glicação Avançada/metabolismo
Ácido Glicirrízico/farmacologia
Proteína HMGB1/sangue
Masculino
Camundongos Endogâmicos C57BL
Modelos Biológicos
Monócitos/patologia
Estresse Oxidativo/efeitos dos fármacos
Proteínas Adaptadoras da Sinalização Shc/metabolismo
Proteína 1 de Transformação que Contém Domínio 2 de Homologia de Src
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Glycation End Products, Advanced); 0 (HMGB1 Protein); 0 (Shc Signaling Adaptor Proteins); 0 (Shc1 protein, mouse); 0 (Src Homology 2 Domain-Containing, Transforming Protein 1); 6FO62043WK (Glycyrrhizic Acid); WYQ7N0BPYC (Acetylcysteine)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160123
[St] Status:MEDLINE
[do] DOI:10.1155/2016/1943918



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