JOSE EDUARDO KRIEGER

(Fonte: Lattes)
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Departamento de Cardio-Pneumologia, Faculdade de Medicina - Docente
Instituto do Coração, Hospital das Clínicas, Faculdade de Medicina
LIM/13 - Laboratório de Genética e Cardiologia Molecular, Hospital das Clínicas, Faculdade de Medicina - Líder

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Agora exibindo 1 - 9 de 9
  • conferenceObject
    Selection of candidate genes for hypertension on rat chromosome 4 from shr using expression profilling in kidney and subcongenic strain development
    (2013) TEIXEIRA, Samantha Kuwada; RODRIGUES, Mariliza Velho; MORALES, Marcelo Marcos; KRIEGER, Jose Eduardo
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    Stretch induces CRP3 expression in vein grafts
    (2012) CAMPOS, Luciene Cristina Gastalho; MIYAKAWA, Ayumi Aurea; BARAUNA, Valerio Garrone; BORIN, Thaiz Ferraz; DALLAN, Luis Alberto de Oliveira; KRIEGER, Jose Eduardo
    Cysteine- and glycine- rich protein 3 (CRP3) can act as structural protein and potent transcriptional cofactor during muscle differentiation and vascular remodeling. In this context, we have demonstrated, by real time RT–PCR, that CRP3 expression is 10 times higher in smooth muscle cells (SMCs) from human mammary artery vs. saphenous vein (h-SV) and that CRP3 expression can be induced in arterialized h-SV using an ex vivo flow through system that mimics arterial condition. The upregulation of CRP3 was primarily dependent on stretch stimulus in SMCs, rather than shear stress in ECs. Here, we assessed the induction and localization of CRP3 in SMCs during arterialization. Using a rat vein arterializations model in vivo, 1–14 days after surgery, CRP3 immunostaining was observed predominantly in the inner layer and 28–90 days it appears more scattered in the vessel. Confocal microscopy and western blot analysis showed that CRP3 is expressed in cytoplasm and nucleous of SMCs under stretch and in early stages of rat arterialization model. Later, the localization was restricted to the cytoplasm. Our data provide evidence that CRP3 is primarily expressed in arterial SMCs but upon stretching there is early expression of CRP3 induction in vein SMC cytoplasm and nucleous. These finding support to the idea that CRP3 may influence vascular adaptation to stress via cytoskeleton rearrangement and gene expression reprogramming.
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    Activation of the AT1 receptor-beta-arrestin signaling pathway inhibits NHE3 activity in the renal proximal tubule
    (2014) MORAIS, Carla Carneiro de; OLIVEIRA-SOUZA, Maria; PESSOA, Thaissa; MALNIC, Gerhard; KRIEGER, Jose; GIRARDI, Adriana
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    beta-arrestin-mediated signal transduction participates in laminar shear stress-induced production of nitric oxide in endothelial cells
    (2013) SANTOS, Ana Paula Carneiro dos; BARAUNA, Valerio Garrone; ALANIZ, Miriam Helena Fonseca; GIRARDI, Adriana Castello Costa; KRIEGER, Jose Eduardo
    Endothelial cells are capable of converting mechanical stimuli into intracellular signals generating vasoactive factors such as nitric oxide (NO). A great body of evidence suggests that β-arrestins play a role not only on GPCR desensibilization but also in mechanotransduction. The aim of this study was to test the hypothesis that laminar shear stress (SS)-induced NO production by endothelial cells requires the activation of the β-arrestin signaling pathway. Towards this end, human saphenous vein endothelial cells (SVEC) were transfected with siRNA against the isoforms 1 and 2 of β-arrestins and subsequently subjected to SS (15 dynes/cm2) for 10 minutes. We found that the SS-induced production of nitrite in the cell culture medium was significantly decreased in SVEC silenced for β-arrestin 1 and 2 compared to control cells (326±44 vs. 166±17%; P < 0.001, n=5). Furthermore, silencing of β-arrestin 1 and 2 significantly attenuated the phosphorylation levels of AKT at the serine residue 473 (99±22 vs. 293±42% in control; P <0.001, n=5) and led to a non-significant trend towards an increase of ERK phosphorylation (157±71 vs.107±5% in control; P= 0.3670, n=5). Altogether, we provide evidence that β-arrestins play a role on laminar SS-induced generation of NO associated with AKT activation in endothelial cells.
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    Identifying targets and characterizing the role of aPKCs in murine embryonic stem cells
    (2012) DUARTE, Mariana Lemos; ZERI, Ana Carolina; KRIEGER, Jose Eduardo; SCHECHTMAN, Deborah
    The protein kinase C (PKC) family of isoenzymes plays a pivotal role in maintaining undifferentiated embryonic stem cells (ESC) and in differentiation to specific cell types. We saw that aPKCs are highly expressed in undifferentiated ESC, to elucidate their role in these cells we aimed at identifying direct and indirect aPKC substrates. Using 2-D phosphoproteomics and a {zeta}/{lambda} pseudo-substrate inhibitor peptide we were able to identify 68 proteins whose phosphorylation decreased in the presence of the inhibitor peptide. 34% of the identified proteins were proteins involved in protein folding, stability and synthesis, 27% in metabolism and 13% cytoskeletal elements and associated proteins involved in cell/cell adhesion processes, and cell polarization such as RhoGDI. Most of the identified proteins involved in metabolism were members of the glycolytic pathway. In addition, glucose consumption was reduced in cells treated with the pseudo-substrate peptide. Metabolomic analysis combined with our proteomics results will help elucidate metabolic processes in which aPKC is involved in undifferentiated ESCs. Together our study indicates that aPKC is involved in cell/cell adhesion and glucose metabolism in undifferentiated ESCs, processes which are known to contribute to ESC self-renewal.
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    Rapamycin Activates TGF Receptor Independently of Its Ligands: Implications for Endothelial Dysfunction
    (2015) GIRAO-SILVA, Thais; MIYAKAWA, Ayumi; KRIEGER, Jose; EDELMAN, Elazer
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    Early post-natal ventricle resection is accompained by neoformed cardiomyocytes and maintenance of cardiac function under stress in adult rats
    (2014) ZOGBI, Camila; CARVALHO, Ana Elisa de; NAKAMUTA, Juliana; CACERES, Viviane; ROCHITTE, Carlos; KRIEGER, Jose
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    Markers of acute cardiovascular inflammation induced by angiotensin II in a murine model
    (2013) SANTANA, Andre Bento Chaves; SOUZA-OLIVEIRA, Thais; BARAUNA, Valerio; SOUZA, Leandro; IRIGOYEN, Maria Claudia; CAMPOS, Luciene; KRIEGER, Jose Eduardo; LACCHINI, Silvia
    Angiotensin II has important physiological functions for the homeostasis of the cardiovascular system and may also induce to inflammatory responses. The aim of this study was to evaluate the effetc of subpressor angiotensin II (AngII) on expression of inflammatory markers in cardiac vessels. Were used C57Bl/6J male mice, treated with subpressor dose of AngII (30ng/kg IP), confirmed by carotid catheterization and arterial pressure measure after 10, 30, 60min, and 2 and 6hours of AngII injection (n=5/saline; n=5/AngII). Inflammatory markers were evaluated in cardiac vessels (TGF-beta, IL-6 and iNOS) by western blot, and localized in vessels by immunohistochemistry. Mice were evaluated after 1 and 24 hours to identify acute responses. Results were compared by ANOVA, using p≤0.05 as significant. Blood pressure measurements showed no changes in arterial pressure and heart rate. Protein analysis showed an increase of inflammatory markers in cardiac tissue after 1 hour TGF-beta (84%), IL-6 (90%) and iNOS (70%). However, these markers were unchanged after 24 hours. Immunohistochemistry analysis showed a specific increase in these markers associated to cardiac vessels. The results suggests that, independently on hemodynamic influences, Angiotensin II leads to expression of inflammatory markers in cardiac vessels in a short period, and this may represent a direct pro-inflammatory action mediated by angiotensin II.
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    Molecular mechanisms associated to reversion of proteinuria by RAS antagonists in renovascular hypertensive rats
    (2014) CORREA, Jose; GIRARDI, Adriana; SALLES, Thiago; BOARO, Karoline; LOREDO, Felipe; YOGI, Alvaro; CALLERA, Glaucia; TOUYZ, Rhian; BENDHACK, Lusiane; KRIEGER, Jose