Tyrosine Phosphorylation in Nitric Oxide–Mediated Signaling Events

Monteiro, Hugo P.; Oliveira, Carlos Jorge Rocha; Curcio, Marli F.; Moraes, Miriam S.; Arai, Roberto Jun

doi:10.1016/s0076-6879(05)96029-1

Cited by 8 publications

(5 citation statements)

References 23 publications

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“…EGF (10 ng/ml, 10 min, 358C) was used as control. Medium was removed, the cells were washed with ice-cold PBS and lysed in ice-cold lysis buffer (20 mM HEPES [pH 7.5], 150 mM NaCl, 10% glycerol, 1% Triton X-100, 1.5 mM MgCl 2 , 1 mM EGTA, 1 lg/ml aprotinin, 1 lg/ml leupeptin, 1 mM PMSF, 2 mM Na 3 VO 4 , 50 mM NaF, and 10 mM Na 4 P 2 0 7 ), as previously described [52]. Total cellular proteins (60 lg per lane) were incubated with sample buffer containing b-mercaptoethanol and subjected to 10% SDS/PAGE.…”

Section: Western Blot For Detection Of Estrogen Receptorsmentioning

confidence: 99%

17Beta-Estradiol Induces the Translocation of the Estrogen Receptors ESR1 and ESR2 to the Cell Membrane, MAPK3/1 Phosphorylation and Proliferation of Cultured Immature Rat Sertoli Cells1

Lucas

Siu

Esteves

et al. 2008

Biology of Reproduction

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141

143

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The aim of the present study was to determine the mechanisms involved in estrogen actions in cultured rat Sertoli cells. RT-PCR detected transcripts for the estrogen receptors ESR1 and ESR2 in cultured immature Sertoli cells and in the testis of 15-, 28-, and 120-day-old rats. The expression of ESR1 and ESR2 was confirmed in Sertoli cells by immunofluorescence and Western blot. Immunohistochemistry with cryosections of testes from immature and adult rats revealed that ESR1 is present in Sertoli, Leydig, and some peritubular myoid cells, and ESR2 is present in multiple cell types, including germ cells. Treatment of Sertoli cells with 17beta-estradiol (E(2)) induced a translocation of ESR1 and ESR2 to the plasma membrane and a concomitant phosphorylation of MAPK3/1. Both effects reached a maximum after 10 min and were blocked by PP2, an inhibitor of the SRC family of protein tyrosine kinases, and by the antiestrogen ICI 182,780 (ICI). MAPK3/1 phosphorylation was also decreased in the presence of AG 1478, an inhibitor of the epidermal growth factor receptor (EGFR) kinase, and in the presence of MAP2K1/2 inhibitor UO126. Treatment with E(2) for 24 h increased the incorporation of [methyl-(3)H]thymidine, which was blocked by ICI. These results indicate that E(2) activates an SRC-mediated translocation of estrogen receptors to the plasma membrane, which results in the activation of EGFR and the mitogen-activated protein kinase signaling pathway. In addition, activation of ESR1 and/or ESR2 by E(2) is involved in proliferation of immature Sertoli cells. The estrogen actions in Sertoli cells might be a key step mediating cellular events important for spermatogenesis and fertility.

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Section: Western Blot For Detection Of Estrogen Receptorsmentioning

confidence: 99%

17Beta-Estradiol Induces the Translocation of the Estrogen Receptors ESR1 and ESR2 to the Cell Membrane, MAPK3/1 Phosphorylation and Proliferation of Cultured Immature Rat Sertoli Cells1

Lucas

Siu

Esteves

et al. 2008

Biology of Reproduction

Self Cite

141

143

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“…Presently, a direct effect of iNOS activation on the activity of these kinases has not been proved. However, NO enhances EGF receptor-and cGMP/protein kinase G (PKG) -dependent protein tyrosine phosphorylation of substrates [4]. Further studies are needed to confirm whether NO phosphorylation of AJ proteins is mediated by EGFR or cGMP/PKG signalling pathways.…”

Section: Discussionmentioning

confidence: 99%

“…Chronic inflammatory diseases such as diabetes, arthritis, ulcerative colitis, Crohn’s disease, septic shock, and atherosclerosis are associated with excessive production of NO and its derivatives [2], [3]. NO exerts many of its functions through post-translational modification of proteins, affecting signalling pathways by modifying protein-protein interactions [4], [5]. Protein tyrosine phosphorylation and nitration are among the NO-mediated protein modifications that accompany inflammatory processes [6].…”

Section: Introductionmentioning

confidence: 99%

iNOS Activation Regulates β-catenin Association with Its Partners in Endothelial Cells

et al. 2012

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BackgroundSignals that disrupt β-catenin association to cadherins may influence the translocation of β-catenin to the nucleus to regulate transcription. Post-translational modification of proteins is a signalling event that may lead to changes in structural conformation, association or function of the target proteins. NO and its derivatives induce nitration of proteins during inflammation. It has been described that animals treated with NO donors showed increased permeability due to modulation of VE-cadherin/catenin complex. We, therefore, aim to evaluate the effect of iNOS activation on the expression, nuclear localisation and function of β-catenin in endothelial cells.Methodology/Principal FindingsExpression, nuclear localisation, post-translational modifications and function of β-catenin was analysed by cell fractionation, immunoprecipitation, immunoblots, QRT-PCR and permeability assays in murine endothelial cells (H5V). Influence of macrophage activation on expression of VE-cadherin/p120-catenin/β-catenin complex in co-cultured H5V cells was also assessed. Activation of macrophages to produce NO provoked a decrease in VE-cadherin/p120-catenin/β-catenin expression in H5V cells. Phosphorylation of β-catenin, p120-catenin and VE-cadherin, and reduction in the barrier properties of the cell monolayer was associated with iNOS induction. Moreover, high NO levels provoked nitration of β-catenin, and induced its translocation to the nucleus. In the nucleus of NOS activated cells, nitration levels of β-catenin influenced its association with TCF4 and p65 proteins. High levels of NO altered β-catenin mediated gene expression of NFκB and Wnt target genes without affecting cell viability.ConclusionsNOS activity modulates β-catenin post-translational modifications, function and its association with different partners to promote endothelial cell survival. Therapeutic manipulation of iNOS levels may remove a critical cytoprotective mechanism of importance in tumour angiogenesis.

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“…Chronic sustained hypoxia increases the levels of NO in the CB ( Ye et al, 2002 ) due to an augmented expression of endothelial and inducible nitric oxide synthase ( Ye et al, 2002 ). An increased NO levels evoked by CSH may change the oxidative state and/or produce protein nitrosylation in type-I cells ( Monteiro et al, 2005 ). It is possible that increased levels of NO induced by CSH may contribute to enhances the oxygen sensitivity in the CB.…”

Section: Chronic Sustained Hypoxia (Csh)mentioning

confidence: 99%

Carotid Body Type-I Cells Under Chronic Sustained Hypoxia: Focus on Metabolism and Membrane Excitability

et al. 2018

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Chronic sustained hypoxia (CSH) evokes ventilatory acclimatization characterized by a progressive hyperventilation due to a potentiation of the carotid body (CB) chemosensory response to hypoxia. The transduction of the hypoxic stimulus in the CB begins with the inhibition of K+ currents in the chemosensory (type-I) cells, which in turn leads to membrane depolarization, Ca2+ entry and the subsequent release of one- or more-excitatory neurotransmitters. Several studies have shown that CSH modifies both the level of transmitters and chemoreceptor cell metabolism within the CB. Most of these studies have been focused on the role played by such putative transmitters and modulators of CB chemoreception, but less is known about the effect of CSH on metabolism and membrane excitability of type-I cells. In this mini-review, we will examine the effects of CSH on the ion channels activity and excitability of type-I cell, with a particular focus on the effects of CSH on the TASK-like background K+ channel. We propose that changes on TASK-like channel activity induced by CSH may contribute to explain the potentiation of CB chemosensory activity.

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Tyrosine Phosphorylation in Nitric Oxide–Mediated Signaling Events

Cited by 8 publications

References 23 publications

17Beta-Estradiol Induces the Translocation of the Estrogen Receptors ESR1 and ESR2 to the Cell Membrane, MAPK3/1 Phosphorylation and Proliferation of Cultured Immature Rat Sertoli Cells1

17Beta-Estradiol Induces the Translocation of the Estrogen Receptors ESR1 and ESR2 to the Cell Membrane, MAPK3/1 Phosphorylation and Proliferation of Cultured Immature Rat Sertoli Cells1

iNOS Activation Regulates β-catenin Association with Its Partners in Endothelial Cells

Carotid Body Type-I Cells Under Chronic Sustained Hypoxia: Focus on Metabolism and Membrane Excitability

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