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[PMID]:27775687
[Au] Autor:Iwata H; Kamaguchi M; Ujiie H; Nishimura M; Izumi K; Natsuga K; Shinkuma S; Nishie W; Shimizu H
[Ad] Endereço:Department of Dermatology, Hokkaido University Graduate School of Medicine, Sapporo, Japan.
[Ti] Título:Macropinocytosis of type XVII collagen induced by bullous pemphigoid IgG is regulated via protein kinase C.
[So] Source:Lab Invest;96(12):1301-1310, 2016 12.
[Is] ISSN:1530-0307
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Macropinocytosis is an endocytic pathway that is involved in the nonselective fluid uptake of extracellular fluid. Bullous pemphigoid (BP) is an autoimmune subepidermal blistering disease associated with autoantibodies to type XVII collagen (COL17), which is a component of hemidesmosome. When keratinocytes are treated with BP-IgG, COL17 internalizes into cells by way of the macropinocytosis. We investigated the mechanism of COL17 macropinocytosis using DJM-1 cells, a cutaneous squamous cell carcinoma cell line. First, non-hemidesmosomal COL17 was preferentially depleted by stimulation with the BP-IgG in the DJM-1 cells. To investigate the signaling involved in COL17-macropinocytosis, the inhibition of small GTPase family members Rac1 and Cdc42 was found to strongly repress COL17 internalization; in addition, the Rho inhibitor also partially blocked that internalization, suggesting these small GTPases are involved in signaling to mediate COL17-macropinocytosis. Western blotting using Phostag-SDS-PAGE demonstrated high levels of COL17 phosphorylation in DJM-1 cells under steady-state condition. Treatment with BP-IgG increased the intracellular calcium level within a minute, and induced the overabundant phosphorylation of COL17. The overabundant phosphorylation of COL17 was suppressed by a protein kinase C (PKC) inhibitor. In addition, PKC inhibitor repressed COL17 endocytosis using cell culture and organ culture systems. Finally, the depletion of COL17 was not observed in the HEK293 cells transfected COL17 without intracellular domain. These results suggest that COL17 internalization induced by BP-IgG may be mediated by a PKC pathway. In summary, BP-IgG initially binds to COL17 distributed on the plasma membrane, and COL17 may be internalized by means of a macropinocytic pathway related to the phosphorylation of the intracellular domain by PKC.
[Mh] Termos MeSH primário: Autoanticorpos/farmacologia
Autoantígenos/metabolismo
Imunoglobulina G/farmacologia
Queratinócitos/efeitos dos fármacos
Colágenos não Fibrilares/metabolismo
Penfigoide Bolhoso/imunologia
Pinocitose/efeitos dos fármacos
Proteína Quinase C/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/farmacologia
Autoantígenos/química
Autoantígenos/genética
Sinalização do Cálcio/efeitos dos fármacos
Linhagem Celular Tumoral
Células HEK293
Seres Humanos
Queratinócitos/imunologia
Queratinócitos/metabolismo
Queratinócitos/patologia
Camundongos
Colágenos não Fibrilares/química
Colágenos não Fibrilares/genética
Penfigoide Bolhoso/metabolismo
Penfigoide Bolhoso/patologia
Fragmentos de Peptídeos
Fosforilação/efeitos dos fármacos
Domínios e Motivos de Interação entre Proteínas
Proteína Quinase C/antagonistas & inibidores
Inibidores de Proteínas Quinases/farmacologia
Processamento de Proteína Pós-Traducional/efeitos dos fármacos
Proteínas Recombinantes
Técnicas de Cultura de Tecidos
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Autoantibodies); 0 (Autoantigens); 0 (Immunoglobulin G); 0 (Non-Fibrillar Collagens); 0 (Peptide Fragments); 0 (Protein Kinase Inhibitors); 0 (Recombinant Proteins); 0 (collagen type XVII); EC 2.7.11.13 (Protein Kinase C)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE
[do] DOI:10.1038/labinvest.2016.108


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[PMID]:28458776
[Au] Autor:Stein J; Steven S; Bros M; Sudowe S; Hausding M; Oelze M; Münzel T; Grabbe S; Reske-Kunz A; Daiber A
[Ad] Endereço:Department of Dermatology, Medical Center of the Johannes Gutenberg University, Mainz, Germany.
[Ti] Título:Role of Protein Kinase C and Nox2-Derived Reactive Oxygen Species Formation in the Activation and Maturation of Dendritic Cells by Phorbol Ester and Lipopolysaccharide.
[So] Source:Oxid Med Cell Longev;2017:4157213, 2017.
[Is] ISSN:1942-0994
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:. Activation/maturation of dendritic cells (DCs) plays a central role in adaptive immune responses by antigen processing and (cross-) activation of T cells. There is ongoing discussion on the role of reactive oxygen species (ROS) in these processes and with the present study we investigated this enigmatic pathway. . DCs were cultured from precursors in the bone marrow of mice (BM-DCs) and analyzed for ROS formation, maturation, and T cell stimulatory capacity upon stimulation with phorbol ester (PDBu) and lipopolysaccharide (LPS). LPS stimulation of BM-DCs caused maturation with moderate intracellular ROS formation, whereas PDBu treatment resulted in maturation with significant ROS formation. The NADPH oxidase inhibitors apocynin/VAS2870 and genetic gp91phox deletion both decreased the ROS signal in PDBu-stimulated BM-DCs without affecting maturation and T cell stimulatory capacity of BM-DCs. In contrast, the protein kinase C inhibitors chelerythrine/Gö6983 decreased PDBu-stimulated ROS formation in BM-DCs as well as maturation. . Obviously Nox2-dependent ROS formation in BM-DCs is not always required for their maturation or T cell stimulatory potential. PDBu/LPS-triggered BM-DC maturation rather relies on phosphorylation cascades. Our results question the role of oxidative stress as an essential "danger signal" for BM-DC activation, although we cannot exclude contribution by other ROS sources.
[Mh] Termos MeSH primário: Células da Medula Óssea/enzimologia
Células Dendríticas/enzimologia
Lipopolissacarídeos/farmacologia
NADPH Oxidase 2/metabolismo
Proteína Quinase C/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Acetato de Tetradecanoilforbol/farmacologia
[Mh] Termos MeSH secundário: Animais
Células Dendríticas/patologia
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Knockout
NADPH Oxidase 2/antagonistas & inibidores
NADPH Oxidase 2/genética
Estresse Oxidativo/efeitos dos fármacos
Proteína Quinase C/antagonistas & inibidores
Proteína Quinase C/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipopolysaccharides); 0 (Reactive Oxygen Species); EC 1.6.3.- (Cybb protein, mouse); EC 1.6.3.- (NADPH Oxidase 2); EC 2.7.11.13 (Protein Kinase C); NI40JAQ945 (Tetradecanoylphorbol Acetate)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1155/2017/4157213


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[PMID]:29247648
[Au] Autor:Deng B; Zhu X; Zhao Y; Zhang D; Pannu A; Chen L; Niu W
[Ad] Endereço:Department of Immunology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Key Laboratory of Hormones and Development (Ministry of Health), Tianjin Metabolic Diseases Hospital, Tianjin Medical University, Tianjin, 300070, China.
[Ti] Título:PKC and Rab13 mediate Ca signal-regulated GLUT4 traffic.
[So] Source:Biochem Biophys Res Commun;495(2):1956-1963, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Exercise/muscle contraction increases cell surface glucose transporter 4 (GLUT4), leading to glucose uptake to regulate blood glucose level. Elevating cytosolic Ca mediates this effect, but the detailed mechanism is not clear yet. We used calcium ionophore ionomycin to raise intracellular cytosolic Ca level to explore the underlying mechanism. We showed that in L6 myoblast muscle cells stably expressing GLUT4myc, ionomycin increased cell surface GLUT4myc levels and the phosphorylation of AS160, TBC1D1. siPKCα and siPKCθ but not siPKCδ and siPKCε inhibited the ionomycin-increased cell surface GLUT4myc level. siPKCα, siPKCθ inhibited the phosphorylation of AS160 and TBC1D1 induced by ionomycin. siPKCα and siPKCθ prevented ionomycin-inhibited endocytosis of GLUT4myc. siPKCθ, but not siPKCα inhibited ionomycin-stimulated exocytosis of GLUT4myc. siRab13 but not siRab8a, siRab10 and siRab14 inhibited the exocytosis of GLUT4myc promoted by ionomycin. In summary, ionomycin-promoted exocytosis of GLUT4 is partly reversed by siPKCθ, whereas ionomycin-inhibited endocytosis of GLUT4 requires both siPKCα and siPKCθ. PKCα and PKCθ contribute to ionomycin-induced phosphorylation of AS160 and TBC1D1. Rab13 is required for ionomycin-regulated GLUT4 exocytosis.
[Mh] Termos MeSH primário: Sinalização do Cálcio/fisiologia
Endocitose/fisiologia
Exocitose/fisiologia
GTP Fosfo-Hidrolases/metabolismo
Transportador de Glucose Tipo 4/metabolismo
Mioblastos/fisiologia
Proteína Quinase C/metabolismo
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Ionóforos de Cálcio/administração & dosagem
Sinalização do Cálcio/efeitos dos fármacos
Linhagem Celular
Endocitose/efeitos dos fármacos
Exocitose/efeitos dos fármacos
Regulação da Expressão Gênica/efeitos dos fármacos
Regulação da Expressão Gênica/fisiologia
Ionomicina/administração & dosagem
Mioblastos/efeitos dos fármacos
Transporte Proteico/fisiologia
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium Ionophores); 0 (Glucose Transporter Type 4); 0 (Slc2a4 protein, rat); 56092-81-0 (Ionomycin); EC 2.7.11.13 (Protein Kinase C); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (Rab13 protein, rat); SY7Q814VUP (Calcium)
[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:171217
[St] Status:MEDLINE


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[PMID]:28461572
[Au] Autor:Upadhyay K; Park JE; Yoon TW; Halder P; Kim YI; Metcalfe V; Talati AJ; English BK; Yi AK
[Ad] Endereço:Department of Pediatrics, The University of Tennessee Health Science Center, Memphis, TN 38163.
[Ti] Título:Group B Streptococci Induce Proinflammatory Responses via a Protein Kinase D1-Dependent Pathway.
[So] Source:J Immunol;198(11):4448-4457, 2017 06 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Group B streptococci (GBS) are one of the leading causes of life-threatening illness in neonates. Proinflammatory responses to GBS mediated through host innate immune receptors play a critical role in the disease manifestation. However, the mechanisms involved in proinflammatory responses against GBS, as well as the contribution of signaling modulators involved in host immune defense, have not been fully elucidated. In the present study, we investigated the role of protein kinase D (PKD)1 in the proinflammatory responses to GBS. We found that both live and antibiotic-killed GBS induce activation of PKD1 through a pathway that is dependent on the TLR signaling adaptor MyD88 and its downstream kinase IL-1R-associated kinase 1, but independent of TNFR-associated factor 6. Our studies using pharmacological PKD inhibitors and PKD1-knockdown macrophages revealed that PKD1 is indispensable for GBS-mediated activation of MAPKs and NF-κB and subsequent expression of proinflammatory mediators. Furthermore, systemic administration of a PKD inhibitor protects d-galactosamine-sensitized mice from shock-mediated death caused by antibiotic-killed GBS. These findings imply that PKD1 plays a critical regulatory role in GBS-induced proinflammatory reactions and sepsis, and inhibition of PKD1 activation together with antibiotic treatment in GBS-infected neonates could be an effective way to control GBS diseases.
[Mh] Termos MeSH primário: Inflamação/imunologia
Proteína Quinase C/metabolismo
Infecções Estreptocócicas/imunologia
Infecções Estreptocócicas/metabolismo
Streptococcus agalactiae/imunologia
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Recém-Nascido
Proteína Antagonista do Receptor de Interleucina 1/imunologia
Proteína Antagonista do Receptor de Interleucina 1/metabolismo
Macrófagos/imunologia
Macrófagos/microbiologia
Camundongos
Fator 88 de Diferenciação Mieloide
NF-kappa B/metabolismo
Proteína Quinase C/antagonistas & inibidores
Proteína Quinase C/deficiência
Sepse/microbiologia
Transdução de Sinais
Fator de Necrose Tumoral alfa/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Il1rn protein, mouse); 0 (Interleukin 1 Receptor Antagonist Protein); 0 (Myeloid Differentiation Factor 88); 0 (NF-kappa B); 0 (Tumor Necrosis Factor-alpha); EC 2.7.10.- (protein kinase D); EC 2.7.11.13 (Protein Kinase C)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180127
[Lr] Data última revisão:
180127
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1601089


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[PMID]:29244935
[Au] Autor:Voronkov AV; Mamleev AV
[Ti] Título:Endothelial dysfunction and Protein kinase C activity development interrelation at ischemic injury of a brain.
[So] Source:Patol Fiziol Eksp Ter;60(4):134-42, 2016 Oct-Dec.
[Is] ISSN:0031-2991
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:The ischemic stroke is the reason of high mortality and population disability worldwide and it is closely connected with endothelium dysfunction (ED). The endothelium carries out regulation of specific functions, generally the universal modulator - nitrogen oxide. A number of enzymes participates in a production of nitric oxide, but specific for an endothelium is endothelial NO synthase (eNOS), which violation of regulation is observed at an ischemic stroke. Significant role in activity of eNOS regulation plays protein kinase C (PKC). In this review the following processes were investigated: ED and nitric oxide interrelation at an ischemic stroke; some features of biological activity of nitric oxide depending on a place of synthesis and on time of ischemic damage; eNOS activity regulation by means of PKC; interrelation between ED and PKC activity at oxidative stress; the main alarm ways including activation of eNOS and PKC which regulate microvascular permeability and a tone of vessels of a brain. Being guided by the carried-out analysis of theoretical data, it should be noted that at development of ED the PKC hyperactivity is observed, therefore, the search of the substances possessing inhibiting influence on activity of PKC for treatment of the majority of cardiovascular diseases and an ischemic stroke has become particularly important and perspective.
[Mh] Termos MeSH primário: Isquemia Encefálica/enzimologia
Endotélio Vascular/enzimologia
Estresse Oxidativo
Proteína Quinase C/metabolismo
Acidente Vascular Cerebral/enzimologia
[Mh] Termos MeSH secundário: Animais
Isquemia Encefálica/patologia
Isquemia Encefálica/fisiopatologia
Endotélio Vascular/patologia
Endotélio Vascular/fisiopatologia
Seres Humanos
Óxido Nítrico Sintase Tipo III/metabolismo
Acidente Vascular Cerebral/patologia
Acidente Vascular Cerebral/fisiopatologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 1.14.13.39 (NOS3 protein, human); EC 1.14.13.39 (Nitric Oxide Synthase Type III); EC 2.7.11.13 (Protein Kinase C)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE


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[PMID]:29176328
[Au] Autor:Xie Y; Liu S; Hu S; Wei Y
[Ti] Título:Cardiomyopathy-Associated Gene 1-Sensitive PKC-Dependent Connexin 43 Expression and Phosphorylation in Left Ventricular Noncompaction Cardiomyopathy.
[So] Source:Cell Physiol Biochem;44(2):828-842, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Cardiomyopathy-associated gene 1 (CMYA1) plays an important role in embryonic cardiac development, postnatal cardiac remodeling and myocardial injury repair. Abnormal CMYA1 expression may be involved in cardiac dysplasia and primary cardiomyopathy. Our study aims to establish the relationship between CMYA1 and Left ventricular noncompaction cardiomyopathy (LVNC) pathogenesis. METHODS: We explored the effects of CMYA1 on connexins (Cx), which contribute to gap junction intercellular communication (GJIC), and the underlying signaling pathway in human normal tissues, LVNC myocardial tissues and HL1 cells by means of western blotting, RT-qPCR, immunohistochemistry, immunofluorescence, co-immunoprecipitation and scrape loading-dye transfer. RESULTS: CMYA1 expression was inversely associated with Cx43 and Cx40 expression, as determined by gap junction PCR array analysis. An increased expression and disordered distribution of CMYA1 at the intercalated discs in LVNC myocardial tissue was also observed. CMYA1 and Cx43 are co-expressed and interact in myocardial cells. CMYA1 expression was positively correlated with p-Cx43 (S368) via the Protein kinase C (PKC) signaling pathway in myocardial tissue and HL1 cells. The diffusion distance of Lucifer Yellow in the HL1 cells in which CMYA1 was over-expressed or knocked down was significantly less or more than that of the control group, respectively. CONCLUSION: Abnormal CMYA1 expression affects the expression and phosphorylation of Cx43 through the PKC signaling pathway, which is involved in the regulation of GJIC. CMYA1 participates in the molecular mechanism of LVNC pathogenesis.
[Mh] Termos MeSH primário: Conexina 43/metabolismo
Proteínas de Ligação a DNA/metabolismo
Proteínas Nucleares/metabolismo
Proteína Quinase C/metabolismo
[Mh] Termos MeSH secundário: Cardiomiopatias/metabolismo
Cardiomiopatias/patologia
Comunicação Celular
Linhagem Celular
Conexina 43/genética
Conexinas/genética
Conexinas/metabolismo
Proteínas de Ligação a DNA/antagonistas & inibidores
Proteínas de Ligação a DNA/genética
Junções Comunicantes/metabolismo
Ventrículos do Coração/fisiopatologia
Seres Humanos
Imuno-Histoquímica
Imunoprecipitação
Microscopia de Fluorescência
Miocárdio/metabolismo
Miocárdio/patologia
Proteínas Nucleares/antagonistas & inibidores
Proteínas Nucleares/genética
Fosforilação
Ligação Proteica
Interferência de RNA
RNA Interferente Pequeno/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Connexin 43); 0 (Connexins); 0 (DNA-Binding Proteins); 0 (Nuclear Proteins); 0 (RNA, Small Interfering); 0 (XIRP1 protein, human); 0 (connexin 40); EC 2.7.11.13 (Protein Kinase C)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1159/000485348


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[PMID]:29175450
[Au] Autor:Albano GD; Bonanno A; Moscato M; Anzalone G; Di Sano C; Riccobono L; Wenzel SE; Profita M
[Ad] Endereço:Institute of Biomedicine and Molecular Immunology "A. Monroy" (IBIM), National Research Council of Italy (CNR), Palermo, Italy.
[Ti] Título:Crosstalk between mAChRM3 and ß2AR, via acetylcholine PI3/PKC/PBEP1/Raf-1 MEK1/2/ERK1/2 pathway activation, in human bronchial epithelial cells after long-term cigarette smoke exposure.
[So] Source:Life Sci;192:99-109, 2018 Jan 01.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Cigarette smoke extract (CSE) affects the expression of non-neuronal components of cholinergic system in bronchial epithelial cells and, as PEBP1/Raf-mediated MAPK1/2 and ERK1/2 pathway, promotes inflammation and oxidative stress. AIMS: We studied whether Acetylcholine (ACh) is involved in the mechanism of crosstalk between mAChRM3 and ß2Adrenergic receptors (ß2AR) promoting, via PI3/PKC/PBEP1/Raf/MEK1/2/ERK1/2 activation, ß2AR desensitization, inflammation and, oxidative stress in a bronchial epithelial cell line (16HBE) after long-term exposure to cigarette smoke extract (LECSE). METHODS: We evaluated mAChRM3 and Choline Acetyltransferase (ChAT) expression, ACh production, PEBP1, ERk1/2, and ß2AR phosphorylation, as well as NOX-4, ROS production and IL-8 release in 16HBE after LECSE. The inhibitory activity of Hemicholinium (HCh-3) (a potent choline uptake blocker), LY294002 (a highly selective inhibitor of PI3 kinase), Tiotropium (Spiriva®) (anticholinergic drug) and Olodaterol (ß AR agonist), were tested in 16HBE after LECSE. RESULTS: mAChRM3, ChAT, ACh activity, pPEBP1, pß2AR, pERK1/2, ROS, NOX-4 and IL-8 increased after LECSE in 16HBE LECSE compared to untreated cells. HCh-3 and LY294002 (alone or in combination) as well as Tiotropium (Spiriva®) or Olodaterol (alone or in combination) all reduced the levels of pPEBP1, pß2AR, pERK1/2, ROS, NOX-4, and IL-8 in 16HBE LECSE compared to untreated cells. CONCLUSIONS: LECSE promotes ACh production which enhances PI3/PKC/PEBP1/Raf-ERK1/2 pathway activation, heterologous ß2AR desensitization, as well as release of inflammatory and oxidative mediators in bronchial epithelial cells. The use of anticholinergic drugs and long-acting ß2-agonists, alone or in combination may be dampen these inflammatory mechanisms when used in combination in some epithelial cell types.
[Mh] Termos MeSH primário: Acetilcolina/metabolismo
Brônquios/patologia
Células Epiteliais/efeitos dos fármacos
Quinase 2 de Receptor Acoplado a Proteína G
Receptor Cross-Talk/efeitos dos fármacos
Receptores Adrenérgicos beta 2
Transdução de Sinais/efeitos dos fármacos
Fumaça/efeitos adversos
Fumar/patologia
Tabaco/química
[Mh] Termos MeSH secundário: Brônquios/citologia
Brônquios/efeitos dos fármacos
Citocinas/biossíntese
Seres Humanos
MAP Quinase Quinase Quinases/antagonistas & inibidores
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
Fosfatidilinositol 3-Quinases/antagonistas & inibidores
Fosfatidilinositol 3-Quinases/metabolismo
Proteína Quinase C/antagonistas & inibidores
Proteína Quinase C/metabolismo
Inibidores de Proteínas Quinases/farmacologia
Quinases raf/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ADRB2 protein, human); 0 (Cytokines); 0 (Protein Kinase Inhibitors); 0 (Receptors, Adrenergic, beta-2); 0 (Smoke); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (raf Kinases); EC 2.7.11.13 (Protein Kinase C); EC 2.7.11.15 (muscarinic receptor kinase); EC 2.7.11.16 (G-Protein-Coupled Receptor Kinase 2); EC 2.7.11.25 (MAP Kinase Kinase Kinases); N9YNS0M02X (Acetylcholine)
[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:171128
[St] Status:MEDLINE


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[PMID]:29211809
[Au] Autor:Yang H; Chen Q; Sun F; Zhao N; Wen L; Li L; Ran G
[Ad] Endereço:Department of Clinical Nutrition, Kecheng People's Hospital, Quzhou, Zhejiang Province, China.
[Ti] Título:Down-regulation of the klf5-c-Myc interaction due to klf5 phosphorylation mediates resveratrol repressing the caveolin-1 transcription through the PI3K/PKD1/Akt pathway.
[So] Source:PLoS One;12(12):e0189156, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Resveratrol (RSV), a natural polyphenol, has been reported to produce effect on genes transcription in lipid metabolism. In this study, we aim to explore the novel mechanisms of RSV on the regulation of caveolin-1 (Cav-1) transcription. Via body weight, blood glucose, serum lipid, and liver pathology detection, we found that RSV decreased body weight, blood glucose and lipid accumulation in rats fed high-fat diet. Based on co-immunoprecipitation (Co-IP) and western blotting assay, we found that RSV up-regulated klf5 phosphorylation and decreased the interaction of klf5 with c-Myc, which were accompanied by down-regulation of Cav-1 expression in livers of rats fed with high-fat diet. Moreover, in HEK293 cells, we observed RSV enhanced klf5 phosphorylation and separated the interaction of klf5 with c-Myc through inhibiting the activation of PI3K/PKD1/Akt pathway, which maybe promoted c-Myc binding to the promoter to inhibit Cav-1 expression. The results of the present study demonstrated that RSV activated klf5 phosphorylation by inhibiting PI3K/PKD1/Akt pathway, and then attenuated the interaction of klf5 with c-Myc, subsequently probably promoted the c-Myc binding to the promoter to repress Cav-1 expression.
[Mh] Termos MeSH primário: Caveolina 1/genética
Regulação para Baixo
Fatores de Transcrição Kruppel-Like/metabolismo
Fosfatidilinositol 3-Quinases/metabolismo
Proteína Quinase C/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
Proteínas Proto-Oncogênicas c-myc/metabolismo
Estilbenos/farmacologia
Transcrição Genética/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Glicemia/metabolismo
Peso Corporal/efeitos dos fármacos
Dieta Hiperlipídica
Células HEK293
Seres Humanos
Lipídeos/sangue
Fígado/efeitos dos fármacos
Fígado/enzimologia
Fígado/metabolismo
Masculino
Fosforilação
Regiões Promotoras Genéticas
Ratos
Ratos Wistar
Reação em Cadeia da Polimerase em Tempo Real
Fator de Crescimento Transformador beta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Caveolin 1); 0 (Klf5 protein, rat); 0 (Kruppel-Like Transcription Factors); 0 (Lipids); 0 (Proto-Oncogene Proteins c-myc); 0 (Stilbenes); 0 (Transforming Growth Factor beta); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.10.- (protein kinase D); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.13 (Protein Kinase C); Q369O8926L (resveratrol)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189156


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[PMID]:27774775
[Au] Autor:Park HJ; Jeon EJ; Lee JS; Hong SH; Cho AN; Lee J; Moon JS; Jung KE; Oh JW; Lee H; Cho SW
[Ad] Endereço:Department of Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-guSeoul, 120-749, South Korea.
[Ti] Título:Galactosylated Lipidoid Nanoparticles for Delivery of Small Interfering RNA to Inhibit Hepatitis C Viral Replication In Vivo.
[So] Source:Adv Healthc Mater;5(22):2931-2941, 2016 Nov.
[Is] ISSN:2192-2659
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Small interfering RNA (siRNA) delivery can provide an effective therapy for treating viral diseases by silencing genes involved in viral replication. In this study, a liver-targeting formulation of lipidoid nanoparticle for delivery of siRNA that targets protein kinase C-related kinase 2 (PRK2) to inhibit hepatitis C virus (HCV) replication is reported. The most effective, minimally cytotoxic lipidoid for siRNA delivery to hepatic cells is identified from a small library of alkyl epoxide-polyamine conjugates. In vitro transfection of PRK2 siRNA (siPRK2) using this lipidoid induces significant silencing of PRK2 (≈80%), suppressing HCV replication in human hepatic cells transfected with the HCV subgenomic replicon. Systemic administration of siPRK2 using the lipidoid nanoparticles results in significant reduction of host PRK2 in the mouse liver (≈60%). This treatment significantly suppresses HCV replication in an HCV-xenograft mouse model. siRNA delivery to the liver is further improved via galactosylation of the lipidoid. Compared with the unmodified lipidoid formulation, galactosylated lipidoids induce greater silencing of host PRK2 in mouse livers (≈80%) and more rapid suppression of HCV replication in an HCV-xenograft mouse. This study suggests that galactosylated lipidoid nanoparticles could provide a treatment for hepatitis C by mediating delivery of anti-viral RNA interference therapeutics to the liver.
[Mh] Termos MeSH primário: Antivirais/administração & dosagem
Hepacivirus/efeitos dos fármacos
Nanopartículas/administração & dosagem
RNA Interferente Pequeno/administração & dosagem
Replicação Viral/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Hepatite C/tratamento farmacológico
Hepatite C/virologia
Hepatócitos/efeitos dos fármacos
Hepatócitos/virologia
Seres Humanos
Fígado/efeitos dos fármacos
Fígado/virologia
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Proteína Quinase C/metabolismo
Interferência de RNA/fisiologia
Transfecção/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (RNA, Small Interfering); EC 2.7.1.- (protein kinase N); EC 2.7.11.13 (Protein Kinase C)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171130
[Lr] Data última revisão:
171130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE
[do] DOI:10.1002/adhm.201600416


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[PMID]:29058721
[Au] Autor:Löf-Öhlin ZM; Nyeng P; Bechard ME; Hess K; Bankaitis E; Greiner TU; Ameri J; Wright CV; Semb H
[Ad] Endereço:The Danish Stem Cell Center, University of Copenhagen, Blegdamsvej 3B, Building 6, 4th floor, DK-2200 Copenhagen N, Denmark.
[Ti] Título:EGFR signalling controls cellular fate and pancreatic organogenesis by regulating apicobasal polarity.
[So] Source:Nat Cell Biol;19(11):1313-1325, 2017 Nov.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Apicobasal polarity is known to affect epithelial morphogenesis and cell differentiation, but it remains unknown how these processes are mechanistically orchestrated. We find that ligand-specific EGFR signalling via PI(3)K and Rac1 autonomously modulates apicobasal polarity to enforce the sequential control of morphogenesis and cell differentiation. Initially, EGF controls pancreatic tubulogenesis by negatively regulating apical polarity induction. Subsequently, betacellulin, working via inhibition of atypical protein kinase C (aPKC), causes apical domain constriction within neurogenin3 endocrine progenitors, which results in reduced Notch signalling, increased neurogenin3 expression, and ß-cell differentiation. Notably, the ligand-specific EGFR output is not driven at the ligand level, but seems to have evolved in response to stage-specific epithelial influences. The EGFR-mediated control of ß-cell differentiation via apical polarity is also conserved in human neurogenin3 cells. We provide insight into how ligand-specific EGFR signalling coordinates epithelial morphogenesis and cell differentiation via apical polarity dynamics.
[Mh] Termos MeSH primário: Polaridade Celular/fisiologia
Células Secretoras de Insulina/metabolismo
Células Secretoras de Insulina/fisiologia
Organogênese/fisiologia
Receptor do Fator de Crescimento Epidérmico/metabolismo
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Animais
Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Diferenciação Celular/fisiologia
Células Epiteliais/metabolismo
Camundongos
Camundongos Knockout
Morfogênese/fisiologia
Proteínas do Tecido Nervoso/metabolismo
Neuropeptídeos/metabolismo
Fosfatidilinositol 3-Quinases/metabolismo
Proteína Quinase C/metabolismo
Proteínas rac1 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (Nerve Tissue Proteins); 0 (Neurog3 protein, mouse); 0 (Neuropeptides); 0 (Rac1 protein, mouse); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.10.1 (EGFR protein, mouse); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 2.7.11.13 (PKC-3 protein); EC 2.7.11.13 (Protein Kinase C); EC 3.6.5.2 (rac1 GTP-Binding Protein)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171024
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3628



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