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Search Results: 1 - 10 of 15775 matches for " Bradykinin B "
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ADRB2, ADRB3, BDKRB2 and MTNR1B Genes Related to Body fat Modulation and Its Interaction with Physical Activity and Blood Pressure  [PDF]
Aline Marcadenti
Open Journal of Endocrine and Metabolic Diseases (OJEMD) , 2015, DOI: 10.4236/ojemd.2015.57012
Abstract: Hypertension (HTN) is the risk factor that most contributes to mortality rates in the world, followed by physical inactivity and obesity. Despite the influence of genetic factors on the genesis of HTN, blood pressure levels are strongly influenced by environmental factors such as physical inactivity and overweight, characterizing it as a polygenic disease. Genetic components and environmental factors such as physical exercise may modulate the phenotype of individuals predisposed to medical conditions such as HTN, independently of modifiable factors such as increased levels of adiposity; however, studies have shown that polymorphic forms detected in genes involved in the mechanisms of blood pressure regulation and also related to body fat modulation may interact with physical activity levels and HTN. The aim of this article is to review the interactions between polymorphisms in ADRB2, ADRB3, BDKRB2 and MTNR1B genes, physical activity and blood pressure.
Functional expression of kinin B1 and B2 receptors in mouse abdominal aorta
Felipe, S.A.;Rodrigues, E.S.;Martin, R.P.;Paiva, A.C.M.;Pesquero, J.B.;Shimuta, S.I.;
Brazilian Journal of Medical and Biological Research , 2007, DOI: 10.1590/S0100-879X2006005000087
Abstract: previous studies have shown that the vascular reactivity of the mouse aorta differs substantially from that of the rat aorta in response to several agonists such as angiotensin ii, endothelin-1 and isoproterenol. however, no information is available about the agonists bradykinin (bk) and desarg9bk (dbk). our aim was to determine the potential expression of kinin b1 and b2 receptors in the abdominal mouse aorta isolated from c57bl/6 mice. contraction and relaxation responses to bk and dbk were investigated using isometric recordings. the kinins were unable to induce relaxation but concentration-contraction response curves were obtained by applying increasing concentrations of the agonists bk and dbk. these effects were blocked by the antagonists icatibant and r-715, respectively. the potency (pd2) calculated from the curves was 7.0 ± 0.1 for bk and 7.3 ± 0.2 for dbk. the efficacy was 51 ± 2% for bk and 30 ± 1% for dbk when compared to 1 μm norepinephrine. the concentration-dependent responses of bk and dbk were markedly inhibited by the arachidonic acid inhibitor indomethacin (1 μm), suggesting a mediation by the cyclooxygenase pathway. these contractile responses were not potentiated in the presence of the nos inhibitor l-name (1 mm) or endothelium-denuded aorta, indicating that the no pathway is not involved. we conclude that the mouse aorta constitutively contains b1 and b2 subtypes of kinin receptors and that stimulation with bk and dbk induces contractile effect mediated by endothelium-independent vasoconstrictor prostanoids.
Regulation of the kinin receptors after induction of myocardial infarction: a mini-review
Tsch?pe, C.;Heringer-Walther, S.;Walther, T.;
Brazilian Journal of Medical and Biological Research , 2000, DOI: 10.1590/S0100-879X2000000600011
Abstract: it is well known that the responses to vasoactive kinin peptides are mediated through the activation of two receptors termed bradykinin receptor b1 (b1r) and b2 (b2r). the physiologically prominent b2r subtype has certainly been the subject of more intensive efforts in structure-function studies and physiological investigations. however, the b1r activated by a class of kinin metabolites has emerged as an important subject of investigation within the study of the kallikrein-kinin system (kks). its inducible character under stress and tissue injury is therefore a field of major interest. although the kks has been associated with cardiovascular regulation since its discovery at the beginning of the last century, less is known about the b1r and b2r regulation in cardiovascular diseases like hypertension, myocardial infarction (mi) and their complications. this mini-review will summarize our findings on b1r and b2r regulation after induction of mi using a rat model. we will develop the hypothesis that differences in the expression of these receptors may be associated with a dual pathway of the kks in the complex mechanisms of myocardial remodeling.
Regulation of the kinin receptors after induction of myocardial infarction: a mini-review
Tsch?pe C.,Heringer-Walther S.,Walther T.
Brazilian Journal of Medical and Biological Research , 2000,
Abstract: It is well known that the responses to vasoactive kinin peptides are mediated through the activation of two receptors termed bradykinin receptor B1 (B1R) and B2 (B2R). The physiologically prominent B2R subtype has certainly been the subject of more intensive efforts in structure-function studies and physiological investigations. However, the B1R activated by a class of kinin metabolites has emerged as an important subject of investigation within the study of the kallikrein-kinin system (KKS). Its inducible character under stress and tissue injury is therefore a field of major interest. Although the KKS has been associated with cardiovascular regulation since its discovery at the beginning of the last century, less is known about the B1R and B2R regulation in cardiovascular diseases like hypertension, myocardial infarction (MI) and their complications. This mini-review will summarize our findings on B1R and B2R regulation after induction of MI using a rat model. We will develop the hypothesis that differences in the expression of these receptors may be associated with a dual pathway of the KKS in the complex mechanisms of myocardial remodeling.
Activation of TRPV1 by capsaicin induces functional Kinin B1 receptor in rat spinal cord microglia
Sébastien Talbot, Jenny Dias, Karim Lahjouji, Maurício Bogo, Maria Campos, Pierrette Gaudreau, Réjean Couture
Journal of Neuroinflammation , 2012, DOI: 10.1186/1742-2094-9-16
Abstract: B1R expression (mRNA, protein and binding sites) was measured in cervical, thoracic and lumbar spinal cord in response to TRPV1 activation by systemic capsaicin (1-50 mg/kg, s.c) in rats pre-treated with TRPV1 antagonists (capsazepine or SB-366791), the antioxidant N-acetyl-L-cysteine (NAC), or vehicle. B1R function was assessed using a tail-flick test after intrathecal (i.t.) injection of a selective B1R agonist (des-Arg9-BK), and its microglial localization was investigated by confocal microscopy with the selective fluorescent B1R agonist, [Nα-bodipy]-des-Arg9-BK. The effect of i.t. capsaicin (1 μg/site) was also investigated.Capsaicin (10 to 50 mg/kg, s.c.) enhanced time-dependently (0-24h) B1R mRNA levels in the lumbar spinal cord; this effect was prevented by capsazepine (10 mg/kg, i.p.; 10 μg/site, i.t.) and SB-366791 (1 mg/kg, i.p.; 30 μg/site, i.t.). Increases of B1R mRNA were correlated with IL-1β mRNA levels, and they were significantly less in cervical and thoracic spinal cord. Intrathecal capsaicin (1 μg/site) also enhanced B1R mRNA in lumbar spinal cord. NAC (1 g/kg/d × 7 days) prevented B1R up-regulation, superoxide anion production and NF-kB activation induced by capsaicin (15 mg/kg). Des-Arg9-BK (9.6 nmol/site, i.t.) decreased by 25-30% the nociceptive threshold at 1 min post-injection in capsaicin-treated rats (10-50 mg/kg) while it was without effect in control rats. Des-Arg9-BK-induced thermal hyperalgesia was blocked by capsazepine, SB-366791 and by antagonists/inhibitors of B1R (SSR240612, 10 mg/kg, p.o.), glutamate NMDA receptor (DL-AP5, 10 μg/site, i.t.), substance P NK-1 receptor (RP-67580, 10 μg/site, i.t.) and nitric oxide synthase (L-NNA, 10 μg/site, i.t.). The B1R fluorescent agonist was co-localized with an immunomarker of microglia (Iba-1) in spinal cord dorsal horn of capsaicin-treated rats.This study highlights a new mechanism for B1R induction via TRPV1 activation and establishes a link between these two pro-nociceptive receptors in
Expression of HER2 and bradykinin B1 receptors in precursor lesions of gallbladder carcinoma
Cesar Toledo,Carola E Matus,Ximena Barraza,Pamela Arroyo
World Journal of Gastroenterology , 2012, DOI: 10.3748/wjg.v18.i11.1208
Abstract: AIM: To determine the expression of HER2 and bradykinin B1 receptors (B1R) in the two pathogenic models of gallbladder cancer: the metaplasia-dysplasia-carcinoma and the adenoma-carcinoma pathways. METHODS: Receptor proteins were visualized by immunohistochemistry on 5-μm sections of paraffin-embedded tissue. Expression of both receptors was studied in biopsy samples from 92 patients (6 males and 86 females; age ranging from 28 to 86 years, mean 56 years). High HER2 expression in specimens was additionally investigated by fluorescence in situ hybridization. Cell proliferation in each sample was assessed by using the Ki-67 proliferation marker. RESULTS: HER2 receptor protein was absent in adenomas and in normal gallbladder epithelium. On the contrary, there was intense staining for HER2 on the basolateral membrane of epithelial cells of intestinal metaplasia (22/24; 91.7%) and carcinoma in situ (9/10; 90%), the lesions that displayed a significantly high proliferation index. Protein up-regulation of HER2 in the epithelium with metaplasia or carcinoma in situ was not accompanied by HER2 gene amplification. A similar result was observed in invasive carcinomas (0/12). The B1R distribution pattern mirrored that of HER2 except that B1R was additionally observed in the adenomas. The B1R appeared either as cytoplasmic dots or labeling on the apical cell membrane of the cells composing the epithelia with intestinal metaplasia (24/24; 100%) and carcinoma in situ (10/10; 100%) and in the epithelial cells of adenomas. In contrast, both HER2 (4/12; 33%) and B1R (1/12; 8.3%) showed a low expression in invasive gallbladder carcinomas. CONCLUSION: The up-regulation of HER2 and B1R in precursor lesions of gallbladder carcinoma suggests cross-talk between these two receptors that may be of importance in the modulation of cell proliferation in gallbladder carcinogenesis.
Activation of kinin B1 receptor evokes hyperthermia through a vagal sensory mechanism in the rat
Talbot Sébastien,De Brito Gariépy Helaine,Saint-Denis Julien,Couture Réjean
Journal of Neuroinflammation , 2012, DOI: 10.1186/1742-2094-9-214
Abstract: Background Kinins are mediators of pain and inflammation. Their role in thermoregulation is, however, unknown despite the fact the B1 receptor (B1R) was found implicated in lipopolysaccharide (LPS)-induced fever. The aim of this study was to investigate the mechanism by which peripheral B1R affects body core temperature in a rat model known to show up-regulated levels of B1R. Methods Male Sprague–Dawley rats received streptozotocin (STZ, 65 mg/kg; i.p.) to enhance B1R expression. Control rats received the vehicle only. One week later, rectal temperature was measured in awake rats after i.p. injection of increasing doses (0.01 to 5 mg/kg) of des-Arg9-Bradykinin (BK) and Sar-[D-Phe8]des-Arg9-BK (B1R agonists) or BK (B2R agonist). The mechanism of B1R-induced hyperthermia was addressed using specific inhibitors and in rats subjected to subdiaphragmatic vagal nerve ligation. B1R mRNA level was measured by quantitative Real Time-polymerase chain reaction (qRT-PCR) and B1R was localized by confocal microscopy. Results B1R agonists (0.1 to 5 mg/kg) showed transient (5- to 30-minute) and dose-dependent increases of rectal temperature (+1.5°C) in STZ-treated rats, but not in control rats. BK caused no effect in STZ and control rats. In STZ-treated rats, B1R agonist-induced hyperthermia was blocked by antagonists/inhibitors of B1R (SSR240612), cyclooxygenase-2 (COX-2) (niflumic acid) and nitric oxide synthase (NOS) (L-NAME), and after vagal nerve ligation. In contrast, COX-1 inhibition (indomethacin) had no effect on B1R agonist-induced hyperthermia. In STZ-treated rats, B1R mRNA was significantly increased in the hypothalamus and the vagus nerve where it was co-localized with calcitonin-gene-related peptide in sensory C-fibers. Conclusion B1R, which is induced in inflammatory diseases, could contribute to hyperthermia through a vagal sensory mechanism involving prostaglandins (via COX-2) and nitric oxide.
Portal hypertensive response to kinin
Kouyoumdjian, Maria;Nagaoka, Marcia R.;Loureiro-Silva, Mauricio R.;Borges, Durval R.;
Anais da Academia Brasileira de Ciências , 2009, DOI: 10.1590/S0001-37652009000300008
Abstract: portal hypertension is the most common complication of chronic liver diseases, such as cirrhosis. the increased intrahepatic vascular resistance seen in hepatic disease is due to changes in cellular architecture and active contraction of stellate cells. in this article, we review the historical aspects of the kallikrein-kinin system, the role of bradykinin in the development of disease, and our main findings regarding the role of this nonapeptide in normal and experimentalmodels of hepatic injury using the isolated rat liver perfusion model (mono and bivascular) and isolated liver cells. we demonstrated that: 1) the increase in intrahepatic vascular resistance induced by bradykinin is mediated by b2 receptors, involving sinusoidal endothelial and stellate cells, and is preserved in the presence of inflammation, fibrosis, and cirrhosis; 2) the hepatic arterial hypertensive response to bradykinin is calcium-independent and mediated by eicosanoids; 3) bradykinin does not have vasodilating effect on the pre-constricted perfused rat liver; and, 4) after exertion of its hypertensive effect, bradykinin is degraded by angiotensin converting enzyme. in conclusion, the hypertensive response to bk is mediated by the b2 receptor in normal and pathological situations. the b1 receptor is expressed more strongly in regenerating and cirrhotic livers, and its role is currently under investigation.
Towards understanding the kallikrein-kinin system: insights from measurement of kinin peptides
Campbell, D.J.;
Brazilian Journal of Medical and Biological Research , 2000, DOI: 10.1590/S0100-879X2000000600008
Abstract: the kallikrein-kinin system is complex, with several bioactive peptides that are formed in many different compartments. kinin peptides are implicated in many physiological and pathological processes including the regulation of blood pressure and sodium homeostasis, inflammatory processes, and the cardioprotective effects of preconditioning. we established a methodology for the measurement of individual kinin peptides in order to study the function of the kallikrein-kinin system. the levels of kinin peptides in tissues were higher than in blood, confirming the primary tissue localization of the kallikrein-kinin system. moreover, the separate measurement of bradykinin and kallidin peptides in man demonstrated the differential regulation of the plasma and tissue kallikrein-kinin systems, respectively. kinin peptide levels were increased in the heart of rats with myocardial infarction, in tissues of diabetic and spontaneously hypertensive rats, and in urine of patients with interstitial cystitis, suggesting a role for kinin peptides in the pathogenesis of these conditions. by contrast, blood levels of kallidin, but not bradykinin, peptides were suppressed in patients with severe cardiac failure, suggesting that the activity of the tissue kallikrein-kinin system may be suppressed in this condition. both angiotensin converting enzyme (ace) and neutral endopeptidase (nep) inhibitors increased bradykinin peptide levels. ace and nep inhibitors had different effects on kinin peptide levels in blood, urine, and tissues, which may be accounted for by the differential contributions of ace and nep to kinin peptide metabolism in the multiple compartments in which kinin peptide generation occurs. measurement of the levels of individual kinin peptides has given important information about the operation of the kallikrein-kinin system and its role in physiology and disease states.
Towards understanding the kallikrein-kinin system: insights from measurement of kinin peptides
Campbell D.J.
Brazilian Journal of Medical and Biological Research , 2000,
Abstract: The kallikrein-kinin system is complex, with several bioactive peptides that are formed in many different compartments. Kinin peptides are implicated in many physiological and pathological processes including the regulation of blood pressure and sodium homeostasis, inflammatory processes, and the cardioprotective effects of preconditioning. We established a methodology for the measurement of individual kinin peptides in order to study the function of the kallikrein-kinin system. The levels of kinin peptides in tissues were higher than in blood, confirming the primary tissue localization of the kallikrein-kinin system. Moreover, the separate measurement of bradykinin and kallidin peptides in man demonstrated the differential regulation of the plasma and tissue kallikrein-kinin systems, respectively. Kinin peptide levels were increased in the heart of rats with myocardial infarction, in tissues of diabetic and spontaneously hypertensive rats, and in urine of patients with interstitial cystitis, suggesting a role for kinin peptides in the pathogenesis of these conditions. By contrast, blood levels of kallidin, but not bradykinin, peptides were suppressed in patients with severe cardiac failure, suggesting that the activity of the tissue kallikrein-kinin system may be suppressed in this condition. Both angiotensin converting enzyme (ACE) and neutral endopeptidase (NEP) inhibitors increased bradykinin peptide levels. ACE and NEP inhibitors had different effects on kinin peptide levels in blood, urine, and tissues, which may be accounted for by the differential contributions of ACE and NEP to kinin peptide metabolism in the multiple compartments in which kinin peptide generation occurs. Measurement of the levels of individual kinin peptides has given important information about the operation of the kallikrein-kinin system and its role in physiology and disease states.
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