Base de dados : LILACS
Pesquisa : D12.644.276.812.654 [Categoria DeCS]
Referências encontradas : 11 [refinar]
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  1 / 11 LILACS  
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Texto completo SciELO Chile
Texto completo
Id: lil-323351
Autor: Leiva-Salcedo, Elias; Perez, Viviana; Acuña-Castillo, Claudio; Walter, Robin; Sierra, Felipe.
Título: T-kininogen inhibits kinin-mediated activation of ERK in endothelial cells
Fonte: Biol. Res;35(2):287-294, 2002. ilus, graf.
Idioma: en.
Projeto: FONDECYT; . FONDAP.
Resumo: Serum levels of T-kininogen increase dramatically as rats approach the end of their lifespan. Stable expression of the protein in Balb/c 3T3 fibroblasts leads to a dramatic inhibition of cell proliferation, as well as inhibition of the ERK signaling pathway. T-kininogen is a potent inhibitor of cysteine proteinases, and we have described that the inhibition of ERK activity occurs, at least in part, via stabilization of the MAP kinase phosphatase, MKP-1. Since fibroblasts are not a physiological target of T-kininogen, we have now purified the protein from rat serum, and used it to assess the effect of T-kininogen on endothelial cells. Adding purified T-kininogen to EAhy 926 hybridoma cells resulted in inhibition of basal ERK activity levels, as estimated using appropriate anti-phospho ERK antibodies. Furthermore, exogenously added T-kininogen inhibited the activation of the ERK pathway induced by either bradykinin or T-kinin. We conclude that the age-related increase in hepatic T-kininogen gene expression and serum levels of the protein could have dramatic consequences on endothelial cell physiology, both under steady state conditions, and after activation by cell-specific stimuli. Our results are consistent with T-kininogen being an important modulator of the senescent phenotype in vivo
Descritores: Inibidores de Cisteína Proteinase
Endotélio
Cininogênios
Proteínas Quinases Ativadas por Mitógeno
-Fatores Etários
Western Blotting
Bradicinina
Divisão Celular
Linhagem Celular
Inibidores de Cisteína Proteinase
Hibridomas
Cininogênios
Cininas
Proteínas Quinases Ativadas por Mitógeno
Ratos Endogâmicos BN
Transdução de Sinais
Limites: Animais
Ratos
Responsável: BR1.1 - BIREME


  2 / 11 LILACS  
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Id: lil-225990
Autor: Schmaier, Alvin H.
Título: Plasma contact activation: a revised hypothesis
Fonte: Biol. Res;31(3):251-62, 1998. ilus, graf.
Idioma: en.
Projeto: NIH.
Descritores: Inibidores de Cisteína Proteinase/metabolismo
Sistema Calicreína-Cinina
Cininogênios/metabolismo
Plasma/metabolismo
-Bradicinina/metabolismo
Endotélio/química
Fibrinólise
Pré-Calicreína/metabolismo
Receptores de Peptídeos
Trombina/antagonistas & inibidores
Tipo de Publ: Revisão
Research Support, U.S. Gov't, P.H.S.
Responsável: BR1.1 - BIREME


  3 / 11 LILACS  
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Id: lil-225984
Autor: Nolly, Hector; Nolly, Alejandro.
Título: Release of endothelial-derived kallikrein, kininogen and kinins
Fonte: Biol. Res;31(3):169-74, 1998. graf.
Idioma: en.
Descritores: Inibidores de Cisteína Proteinase/metabolismo
Endotélio Vascular/metabolismo
Calicreínas/metabolismo
Cininogênios/metabolismo
Cininas/metabolismo
-Sistema Calicreína-Cinina
Ratos Wistar
Limites: Animais
Masculino
Ratos
Responsável: BR1.1 - BIREME


  4 / 11 LILACS  
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Id: lil-225981
Autor: Boric, Mauricio P; Figueiroa, Xavier F; Albertini, Renato; Roblero, Juan S.
Título: Croxatto's fifty-year pursuit: from pepsanurin to the discovery of a new kininogen-derived peptide (PU-D1)
Fonte: Biol. Res;31(3):117-29, 1998.
Idioma: en.
Descritores: Inibidores de Cisteína Proteinase
Cininogênios
Peptídeos
-Fator Natriurético Atrial
Inibidores de Cisteína Proteinase/farmacologia
Hidrólise
Intestinos/metabolismo
Calicreínas
Rim/metabolismo
Cininogênios/farmacologia
Cininas
Pepsina A
Peptídeos/farmacologia
Limites: Animais
Ratos
Tipo de Publ: Revisão
Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


  5 / 11 LILACS  
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Id: lil-225979
Autor: Boric, Mauricio P; Croxatto, Hector R; Moreno, Jose M; Silva, Rosa; Hernandes, Cristin; Roblero, Juan S.
Título: Kinins mediate the inhibition of atrial natriuretic peptide diuretic effect induced by pepsanurin
Fonte: Biol. Res;31(1):33-48, 1998. tab, graf.
Idioma: en.
Projeto: FONDECYT.
Resumo: Pepsanurin is a peptidic fraction resulting from pepsin digestion of plasma globulins, that inhibits ANP renal excretory actions. We studied whether kinin-like peptides mediate the anti-ANP effect by testing if pepsanurin: 1) was blocked by the kinin B12 receptor antagonist HOE-140, 2) was produced from kininogen, and 3) was mimicked by bradykinin. Anti-ANP activity was assessed in anesthetized female rats by comparing the excretory response to two ANP boluses (0.5 mug iv) given before and after ip injection of test samples. Pepsanurin from human or rat plasma (1-5 mL/Kg), and bradykinin (5-20 mug/Kg), dose-relatedly inhibited ANP-induced water, sodium, potassium and cyclic GMP urinary excretion, without affecting arterial blood pressure. The same effect was exerted by pepsin hydrolysates of purified kininogen, whereas hydrolysates of kininogen-free plasma had no effect. HOE-140 (5 mug, iv) did not alter baseline, or ANP-induced excretion, but blocked the anti-ANP effects of pepsanurin. Histamine (15 mug/Kg) plus seroalbumin hydrolysates did not affect ANP response, despite inducing larger peritoneal fluid accumulation as compared with pepsanurin or bradykinin. We concluded that kinins cleaved from kininogen mediate the anti-ANP effects of pepsanurin by activation of kinin B2 receptors, independently of changes in systemic arterial pressure or peritoneal fluid sequestration.
Descritores: Fator Natriurético Atrial/antagonistas & inibidores
Diuréticos/farmacologia
Cininas/farmacologia
Peptídeos/farmacologia
-Antagonistas Adrenérgicos beta/farmacologia
Bradicinina/análogos & derivados
GMP Cíclico/urina
Inibidores de Cisteína Proteinase/sangue
Diurese
Cininogênios/sangue
Ratos Sprague-Dawley
Limites: Animais
Feminino
Ratos
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


  6 / 11 LILACS  
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Texto completo SciELO Brasil
Texto completo
Id: lil-212875
Autor: Veloso, D.
Título: Evidence for the presence of a kininogen-like species in a case of total deficiency of low and high molecular weight kininogens
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;31(7):901-10, jul. 1998. ilus.
Idioma: en.
Resumo: Low and high molecular weight kininogens (LK and HK), containing 409 and 626 amino acids with masses of ~65 and 120120 kDa after glycosylation, respectively, are coded by a single gene mapped to the human chromosome 3 by alternative splicing of the transcribed mRNA. The NH2-termini Glu(1)-Thr(383) region, identical in LK and HK, contains bradykinin (BK) moieties Arg(363)-Arg(371). LK, HK and their kinin products Lys-BK and BK are involved in several biological processes. They are evolutionarily conserved and only 7 patients, all apparently normal, have been reported to lack them. In one of these patients (Williams'trait), a codon mutation (Arg(178) r stop) has been blamed for the absence of LK and HK. However, using Western blots with 2 monoclonal anti-HK antibodies, one that recognizes the region common to LK and HK and the other that recognizes only HK, I detected ~110-kDa bands in the plasma of this LK/HK-deficient patient vs ~120-kDa bands in normal human and ape plasmas. With polyclonal anti-Lys-BK antibody, which strongly detects BK eleaved at its COOH-terminus in purified HK, I detected ~110-kDa bands in the normal and the deficient plasmas. Western blots with a monoclonal anti-prekallikrein (PK) antibody showed that surface activation of PK and distribution of PK activation products, both dependent on HK, were similar in these plasmas. These findings suggest that a mutant gene yielded a kininogen-like species possibly involving aberrant mRNA splicing - structurally different from normal HK, but apparently with the capacity to carry out seemingly vital HK functions.
Descritores: Transtornos da Coagulação Sanguínea/genética
Cininogênio de Alto Peso Molecular/genética
Cininogênio de Baixo Peso Molecular/genética
Cininogênios/genética
Plasma/química
-Anticorpos Monoclonais/isolamento & purificação
Transtornos da Coagulação Sanguínea/imunologia
Western Blotting
Cininogênio de Alto Peso Molecular/imunologia
Cininogênio de Baixo Peso Molecular/imunologia
Cininas/isolamento & purificação
Mutação
RNA Mensageiro/genética
Limites: Feminino
Humanos
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


  7 / 11 LILACS  
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Fotocópia
Id: lil-210414
Autor: Croxatto Rezzio, Héctor; Figueroa F., Xavier; Boric P., Mauricio; Roblero S., Juan; Silva, Rosa; Albertini B., Renato.
Título: La glucosa en conjunto con péptidos derivados de cininógenos podrían actuar desde el aparato digestivo como bloqueadores de la acción diurética-natriurética del péptido natriurético auricular / Glucose in conjunction with peptides derived from kininogens might act from digestive tract as blockers of ANP mediated diuresis-natriuresis
Fonte: Rev. méd. Chile;126(1):88-95, ene. 1998. ilus.
Idioma: es.
Resumo: This paper describes long term research efforts wich have lead: 1) to the identification of peptides present in pepsanurin, a peptidic fraction obtained by pepsin hydrolisis of plasma globulins that inhibits the renal excretory action of atrial natriuretic peptide (ANP) and 2) to the discovery of an unexpected role of glucose, as a requisite, for these inhibitory effects. The active peptides identified in pepsanurin are derived from plasma kininogens, substrates of the kallikrein-kinin system. Pro-kinins of 15, 16 and 18 aminoacids, and bradykinin itself, block ANP-induced diuresis and natriuresis when injected iv, ip or into, the duodenal lumen of anesthetized rats in picomol doses. Furthermore, a novel 20 aminoacids fragment derived from kininogen dominium-1, named PU-D1, is the most potent and longer lasting blocker of ANP renal effects. The anti-ANP effects of those peptides are prevented by B2- kinin receptor antagonists. The inhibition of ANP by kinins and PU-D1 was evident only in rats infused with isotonic glucose; whereas the excretory effect of ANP was not affected in fasted rats not infused, or infused with saline. These findings provide evidence that glucose facilitates liquid retention through a kinin-mediated inhibition of ANP excretory action that may be related to the prandial cycle
Descritores: Fator Natriurético Atrial
Glucose/farmacocinética
Natriurese/efeitos dos fármacos
-Bradicinina/fisiologia
Fator Natriurético Atrial/fisiologia
Hidrólise
Cininogênios
Sistema Calicreína-Cinina/fisiologia
Limites: Animais
Feminino
Ratos
Responsável: CL1.1 - Biblioteca Central


  8 / 11 LILACS  
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Fotocópia
Id: lil-94101
Autor: Cardona Martínez Margarita; Zamacona Ravelo, Guillermo.
Título: Conceptos actuales en fisiopatología de la rinitis alérgica / Current concepts in physiopathology of the alergic rinitis
Fonte: Alergia (Méx.);36(5):217-9, sept.-oct. 1989.
Idioma: es.
Descritores: Rinite Alérgica Sazonal/fisiopatologia
Rinite Alérgica Perene/fisiopatologia
-Ácidos Araquidônicos/metabolismo
Heparina/fisiologia
Histamina/metabolismo
Cininogênios/metabolismo
Tosilarginina Metil Éster/metabolismo
Limites: História do Século XX
Tipo de Publ: Revisão
Responsável: MX1.1 - CENIDSP - Centro de Información para Decisiones en Salud Pública


  9 / 11 LILACS  
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Id: lil-77710
Autor: Chudzinski, A. M; Sampaio, M. U; Oliva, M. L. V; Sampaio, C. A. M.
Título: A Bothrops jararaca plasma cysteine proteinase inhibitor related to Mammalian kininogen
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;22(8):945-8, 1989. ilus.
Idioma: en.
Conferência: Apresentado em: Annual Meeting of the Federaçäo de Sociedades de Biologia Experimental, 4, Caxambu, June 28-July 2, 1989.
Projeto: CNPq; . FINEP; . CAPES.
Resumo: A kininogen-like protein was purified from Bothrops jararaca plasma by DEAE-Sephadex ion-exchange and carboxy-methul-papain-Sepharose affinity chromatography. The molecular weight, estimated by SDS-gel electrophoresis, is about 100,000 and a species of about 75,000 is formed after incubation with hosrse urinary kallikrein. After incubation with rrypsin, only traces of biological activity were detected in tests on guinea pig ileum. The purified protein inhibits papain and bromelain, does not correct the clotting time of a kininogen-depleted human plasma, and does not affect the clotting time ogf plasma from Waglerophis merremii, a nonpoisonous snake; the same type of inhibitor was foind in this nonpoisonous snake. The dissociation cosntant (Ki) for the papain-inhibitor complex is approximately 1.6 nM
Descritores: Cininogênios/farmacologia
Cisteína/sangue
Coagulação Sanguínea
Elapidae/sangue
-Cromatografia por Troca Iônica
Limites: Animais
Humanos
Masculino
Feminino
Responsável: BR26.1 - Biblioteca Central


  10 / 11 LILACS  
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Cunha, S. P
Id: lil-20469
Autor: Silva, R. O; Cunha, S. P; Peracoli, J. C; Duarte, G; Martinez, A. R.
Título: Kininogen, esterase and kininase activities in human peripheral venous plasma and in plasma from the intervillous space of human placenta, before and during labor.
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;17(1):27-34, 1984.
Idioma: en.
Descritores: Esterases
Cininogênios
Parto
Peptidil Dipeptidase A
Placenta
Limites: Gravidez
Humanos
Feminino
Responsável: BR1.1 - BIREME



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