Pkc Isoforms
Mostrando 1-12 de 87 artigos, teses e dissertações.
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1. Biochemical and Molecular Mechanisms of Glucose Uptake Stimulated by Physical Exercise in Insulin Resistance State: Role of Inflammation
Resumo A obesidade associada à inflamação sistêmica induz resistência à insulina (RI), com consequente hiperglicemia crônica. Este processo envolve o aumento na liberação de citocinas pró-inflamatórias, ativação da enzima c-Jun N-terminal cinase (JNK), do fator nuclear kappa-B (NF-κB) e dos receptores do tipo Toll 4 (TLR4). Dentre as ferramenta
Arq. Bras. Cardiol.. Publicado em: 21/10/2019
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2. FEZ1 protein : little organizational structure, activities related to elements of the cytoskeleton and generation of the "flower like" phenotype / A proteina FEZ1 : pouca organização estrutural, atividades associadas a elementos do citoesqueleto e formação do fenotipo "flower like"
FEZ1 was identified first as a orthologue of C elegans UNC-76 protein, that plays functions related to neuronal development in this worm. Subsequent studies, shows FEZ1 functions in neuronal development process, cell polarization, transport mechanisms associated to kinesins and vesicular and mitochondrial transports. Other works showed that FEZ1 superexpress
Publicado em: 2009
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3. Papel da proteína quinase C (PKC) na modulação da isoforma 1 do permutador Na+ - H+ (NHE1), em células MDCK. / Role of PKC on exchanger isoform 1 (NHE1), modulation in MDCK cells.
O presente trabalho visa contribuir para o esclarecimento da seqüência de eventos intracelulares produzidos pelas PKCs a e e, na modulação do pHi, via NHE1. Os estudos foram realizados em células MDCK e as medidas de pHi efetuadas por microscopia de fluorescência. A expressão das PKCs a e e, bem como do NHE1 foi investigada por western blot, utilizand
Publicado em: 2008
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4. Análise proteômica comparativa entre neutrófilos não ativados e ativados com PMA, um análogo do diacilglicerol
Neutrophils are the major type of leukocytes in peripheral blood and protect against fungal and bacterial infections. Directed migration in a gradient of chemotactic stimuli enables these cells to rapidly find the site of infection and destroy the invading pathogens. PMNs can exist in three different activation states, namely, resting, primed, and activated
Publicado em: 2007
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5. Hypoxia alters the subcellular distribution of protein kinase C isoforms in neonatal rat ventricular myocytes.
Cardiac myocytes coexpress multiple protein kinase C (PKC) isoforms which likely play distinct roles in signaling pathways leading to changes in contractility, hypertrophy, and ischemic preconditioning. Although PKC has been reported to be activated during myocardial ischemia, the effect of ischemia/hypoxia on individual PKC isoforms has not been determined.
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6. Distribution of Protein Kinase C Isoforms after Infection of Macrophages with Leishmania major
We characterized the effects of Leishmania infection on activation-induced translocation of protein kinase C (PKC) isoforms in murine bone marrow-derived macrophages. Although PKC-dependent gene expression was attenuated by infection, the distribution and translocation of PKC isoforms were unaffected. However, subsequent dissociation from membranes was subst
American Society for Microbiology.
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7. Activation of protein kinase C by tyrosine phosphorylation in response to H2O2
Protein kinase C (PKC) isoforms, α, βI, and γ of cPKC subgroup, δ and ɛ of nPKC subgroup, and ζ of aPKC subgroup, were tyrosine phosphorylated in COS-7 cells in response to H2O2. These isoforms isolated from the H2O2-treated cells showed enhanced enzyme activity to various extents. The enzymes, PKC α and δ, recovered from the cells were independent o
The National Academy of Sciences of the USA.
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8. Activation of Protein Kinase C Triggers Its Ubiquitination and Degradation†
Treatment of cells with tumor-promoting phorbol esters results in the activation but then depletion of phorbol ester-responsive protein kinase C (PKC) isoforms. The ubiquitin-proteasome pathway has been implicated in regulating the levels of many cellular proteins, including those involved in cell cycle control. We report here that in 3Y1 rat fibroblasts, pr
American Society for Microbiology.
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9. Novel Roles of Specific Isoforms of Protein Kinase C in Activation of the c-fos Serum Response Element
Protein kinase C (PKC) is a multigene family of enzymes consisting of at least 11 isoforms. It has been implicated in the induction of c-fos and other immediate response genes by various mitogens. The serum response element (SRE) in the c-fos promoter is necessary and sufficient for induction of transcription of c-fos by serum, growth factors, and the phorbo
American Society for Microbiology.
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10. Characterization of vascular endothelial growth factor's effect on the activation of protein kinase C, its isoforms, and endothelial cell growth.
Vascular endothelial growth factor (VEGF) is a potent endothelial cell mitogen which mediates its effects by binding to tyrosine kinase receptors. We have characterized the VEGF-activated intracellular signal transduction pathway in bovine aortic endothelial cells and correlated this to its mitogenic effects. VEGF induced concentration- and time-dependent in
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11. 1,25-Dihydroxyvitamin D3 and 12-O-tetradecanoyl phorbol 13-acetate cause differential activation of Ca(2+)-dependent and Ca(2+)-independent isoforms of protein kinase C in rat colonocytes.
Considerable evidence that alterations in protein kinase C (PKC) are intimately involved in important physiologic and pathologic processes in many cells, including colonic epithelial cells, has accumulated. In this regard, phorbol esters, a class of potent PKC activators, have been found to induce a number of cellular events in normal or transformed colonocy
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12. Antagonistic Effects of Protein Kinase C α and δ on Both Transformation and Phospholipase D Activity Mediated by the Epidermal Growth Factor Receptor
Downregulation of protein kinase C δ (PKC δ) by treatment with the tumor-promoting phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) transforms cells that overexpress the non-receptor class tyrosine kinase c-Src (Z. Lu et al., Mol. Cell. Biol. 17:3418–3428, 1997). We extended these studies to cells overexpressing a receptor class tyrosine kinase,
American Society for Microbiology.