Artículos de revistas: "Bradykinin B2"

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Ma, Jie, Yu Luo, Lilin Ge, Lei Wang, Mei Zhou, Yingqi Zhang, Jinao Duan, Tianbao Chen y Chris Shaw. "Ranakinestatin-PPF from the Skin Secretion of the Fukien Gold-Striped Pond Frog,Pelophylax plancyi fukienensis: A Prototype of a Novel Class of BradykininB2Receptor Antagonist Peptide from Ranid Frogs". Scientific World Journal 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/564839.

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The defensive skin secretions of many amphibians are a rich source of bradykinins and bradykinin-related peptides (BRPs). Members of this peptide group are also common components of reptile and arthropod venoms due to their multiple biological functions that include induction of pain, effects on many smooth muscle types, and lowering systemic blood pressure. While most BRPs are bradykinin receptor agonists, some have curiously been found to be exquisite antagonists, such as the maximakinin gene-related peptide, kinestatin—a specific bradykinin B2-receptor antagonist from the skin of the giant fire-bellied toad,Bombina maxima. Here, we describe the identification, structural and functional characterization of a heptadecapeptide (DYTIRTRLHQGLSRKIV), named ranakinestatin-PPF, from the skin of the Chinese ranid frog,Pelophylax plancyi fukienensis, representing a prototype of a novel class of bradykinin B2-receptor specific antagonist. Using a preconstricted preparation of rat tail arterial smooth muscle, a single dose of 10−6 M of the peptide effectively inhibited the dose-dependent relaxation effect of bradykinin between 10−11 M and 10−5 M and subsequently, this effect was pharmacologically-characterized using specific bradykinin B1- (desArg-HOE140) and B2-receptor (HOE140) antagonists; the data from which demonstrated that the antagonism of the novel peptide was mediated through B2-receptors. Ranakinestatin—PPF—thus represents a prototype of an amphibian skin peptide family that functions as a bradykinin B2-receptor antagonist herein demonstrated using mammalian vascular smooth muscle.

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2

Dixon, B. S., R. Breckon, J. Fortune, R. J. Vavrek, J. M. Stewart, R. Marzec-Calvert y S. L. Linas. "Effects of kinins on cultured arterial smooth muscle". American Journal of Physiology-Cell Physiology 258, n.º 2 (1 de febrero de 1990): C299—C308. http://dx.doi.org/10.1152/ajpcell.1990.258.2.c299.

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The present study uses various kinin agonists and antagonists to examine the cellular mechanisms of bradykinin's actions on intracellular calcium, prostaglandins, and adenosine 3',5'-cyclic monophosphate (cAMP) accumulation in cultured arterial smooth muscle cells (casmc) obtained from rat mesenteric arteries. Exposure to bradykinin produced a rapid release of calcium (peak less than or equal to 20 s) from intracellular stores and an increase in prostaglandin (PG) E2 and cAMP production in casmc. Compared with bradykinin, the bradykinin B1-agonist [des-Arg9]BK produced only a small increase in intracellular calcium. The bradykinin-mediated increase in intracellular calcium was competitively blocked by the B2 receptor antagonist [D-Arg-O-Hyp3-Thi5,8-D-Phe7]BK (B4307) but not the B1-antagonist ([des-Arg9-Leu8]BK). In addition, the similarity of the dose-response curves for the bradykinin-mediated increase in Ca2+, PGE2, and cAMP (half-maximal stimulation of 12, 11, and 13 nM, respectively) and the ability of the B2-antagonist (B4307) to block each of these effects of bradykinin suggest that all three effects are mediated by the same bradykinin (B2) receptor. Further studies revealed that increases in intracellular calcium are necessary for the bradykinin-mediated increase in PGE2 formation and the subsequent PGE2-dependent formation of cAMP. Taken together, these results suggest that bradykinin acts via a B2-receptor on arterial smooth muscle cells to release calcium from intracellular stores, leading to increases in PGE2 production and the PGE2-dependent activation of adenylate cyclase.

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3

Willars, Gary B., Werner Müller-Esterl y Stefan R. Nahorski. "Receptor phosphorylation does not mediate cross talk between muscarinic M3 and bradykinin B2 receptors". American Journal of Physiology-Cell Physiology 277, n.º 5 (1 de noviembre de 1999): C859—C869. http://dx.doi.org/10.1152/ajpcell.1999.277.5.c859.

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This study examined cross talk between phospholipase C-coupled muscarinic M3 and bradykinin B2 receptors coexpressed in Chinese hamster ovary (CHO) cells. Agonists of either receptor enhanced phosphoinositide signaling (which rapidly desensitized) and caused protein kinase C (PKC)-independent, homologous receptor phosphorylation. Muscarinic M3 but not bradykinin B2 receptors were also phosphorylated after phorbol ester activation of PKC. Consistent with this, muscarinic M3 receptors were phosphorylated in a PKC-dependent fashion after bradykinin B2 receptor activation, but muscarinic M3 receptor activation did not influence bradykinin B2receptor phosphorylation. Despite heterologous phosphorylation of muscarinic M3 receptors, phosphoinositide and Ca2+signaling were unaffected. In contrast, marked heterologous desensitization of bradykinin-mediated responses occurred despite no receptor phosphorylation. This desensitization was associated with a sustained component of muscarinic receptor-mediated signaling, whereas bradykinin's inability to influence muscarinic receptor-mediated responses was associated with rapid and full desensitization of bradykinin responses. Thus the mechanism of functional cross talk most likely involves depletion of a shared signaling component. These data demonstrate that receptor phosphorylation is not a prerequisite for heterologous desensitization and that such desensitization is not obligatory after heterologous receptor phosphorylation.

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4

Regoli, D. "Multiple bradykinin B2 receptors". Trends in Pharmacological Sciences 10, n.º 4 (abril de 1989): 138. http://dx.doi.org/10.1016/0165-6147(89)90163-6.

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5

Pan, H. L., C. L. Stebbins y J. C. Longhurst. "Bradykinin contributes to the exercise pressor reflex: mechanism of action". Journal of Applied Physiology 75, n.º 5 (1 de noviembre de 1993): 2061–68. http://dx.doi.org/10.1152/jappl.1993.75.5.2061.

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This study determined the receptors responsible for mediating bradykinin's effect on skeletal muscle afferents that cause the pressor reflex in anesthetized cats. In eight cats, 1 microgram of bradykinin was injected intra-arterially into the gracilis muscle before and after intravenous injection of a kinin B2-receptor antagonist (NPC 17731, 20 micrograms/kg). Initial injection of bradykinin reflexly increased mean arterial pressure by 23 +/- 7 mmHg, maximal change in pressure over time by 439 +/- 272 mmHg/s, and heart rate by 11 +/- 4 beats/min. The hemodynamic response to bradykinin was abolished by kinin B2-receptor blockade. Similar injection of the kinin B1-receptor agonist des-Arg9-bradykinin caused no cardiovascular responses (n = 6). In eight different animals, mean arterial pressure, maximal change in left ventricular pressure over time, and heart rate responses to 30 s of electrically stimulated hindlimb contraction were attenuated by 50 +/- 6, 55 +/- 7, and 41 +/- 8%, respectively, after kinin B2-receptor blockade. In eight other animals, mean arterial pressure, maximal change in left ventricular pressure over time, and heart rate responses were reduced by 58 +/- 8, 66 +/- 6, and 40 +/- 12%, respectively, after inhibition of prostaglandin synthesis with indomethacin (2.5–3 mg/kg iv) and were then abolished by subsequent B2-receptor blockade. These data suggest that bradykinin contributes to the exercise pressor reflex through its action on kinin B2 receptors located on the nerve endings of the muscle afferents.(ABSTRACT TRUNCATED AT 250 WORDS)

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6

Schanstra, Joost P., Johan Duchene, Françoise Praddaude, Patrick Bruneval, Ivan Tack, Jacques Chevalier, Jean-Pierre Girolami y Jean-Loup Bascands. "Decreased renal NO excretion and reduced glomerular tuft area in mice lacking the bradykinin B2 receptor". American Journal of Physiology-Heart and Circulatory Physiology 284, n.º 6 (1 de junio de 2003): H1904—H1908. http://dx.doi.org/10.1152/ajpheart.01150.2002.

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Bradykinin B2 receptor knockout mice (B2 −/−) have been useful to study the role of bradykinin under pathological conditions. With the use of these mice, it was shown that bradykinin plays an important role in angiogenesis, heart failure, salt-induced hypertension, and kidney fibrosis. Data on the role of the bradykinin B2 receptor under physiological conditions using these mice are controversial and scarce, because these mice have no typical phenotype. For this reason, we have studied, under physiological conditions, renal hemodynamics as well as a number of morphometric glomerular parameters of B2 −/− mice on a homogenized genetic background and on mice bred in a pathogen-free environment. Backcrossed B2 −/− mice had normal blood pressure and normal apparent renal hemodynamics and morphology. However, reduced renal nitrite excretion and glomerular cGMP content were found, which was associated with a reduced glomerular capillary surface area. These differences had, however, no detectable effects on renal hemodynamics. These differences between B2 −/− and wild-type mice might become important under pathological conditions as shown by a number of studies using these bradykinin B2 receptor knockout mice.

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7

Stewart, John M. "Bradykinin B2 receptor antagonists: development and applications". Canadian Journal of Physiology and Pharmacology 73, n.º 7 (1 de julio de 1995): 787–90. http://dx.doi.org/10.1139/y95-106.

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Most physiological and pathophysiological responses to bradykinin are mediated by G-protein-coupled receptors designated B2 receptors. Discovery of antagonists for these receptors has brought about a revolution in research in the kinin field. The chemistry and development of antagonists for B2 kinin receptors are discussed. Uses of the antagonists in biomedical research and potential clinical applications are presented.Key words: bradykinin antagonists, bradykinin inflammation, bradykinin receptors.

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8

Gröger, Moritz, Diane Lebesgue, Didier Pruneau, Jane Relton, Seong-Woong Kim, Jürg Nussberger y Nikolaus Plesnila. "Release of Bradykinin and Expression of Kinin B2 Receptors in the Brain: Role for Cell Death and Brain Edema Formation After Focal Cerebral Ischemia in Mice". Journal of Cerebral Blood Flow & Metabolism 25, n.º 8 (6 de abril de 2005): 978–89. http://dx.doi.org/10.1038/sj.jcbfm.9600096.

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Pharmacological studies using bradykinin B2 receptor antagonists suggest that bradykinin, an early mediator of inflammation and the main metabolite of the kallikrein-kinin system, is involved in secondary brain damage after cerebral ischemia. However, the time-course of bradykinin production and kinin receptor expression as well as the conclusive role of bradykinin B2 receptors for brain damage after experimental stroke have not been elucidated so far. C57/Bl6 mice were subjected to 45 mins of middle cerebral artery occlusion (MCAO) and 2, 4, 8, 24, and 48 h later brains were removed for the analysis of tissue bradykinin concentration and kinin B2 receptor mRNA and protein expression. Brain edema, infarct volume, functional outcome, and long-term survival were assessed in WT and B2−/− mice 24 h or 7 days after MCAO. Tissue bradykinin was maximally increased 12 h after ischemia (three-fold), while kinin B2 receptor mRNA upregulation peaked 24 to 48 h after MCAO (10- to 12-fold versus naïve brain tissue). Immunohistochemistry revealed that kinin B2 receptors were constitutively and widely expressed in mouse brain, were upregulated 2 h after ischemia in cells showing signs of ischemic damage, and remained upregulated in the penumbra up to 24 h after ischemia. B2−/− mice had improved motor function ( P<0.05), smaller infarct volumes (–38%; P<0.01), developed less brain edema (–87%; P<0.05), and survived longer ( P<0.01) as compared with wild-type controls. The current results show that bradykinin is produced in the brain, kinin B2 receptors are upregulated on dying cells, and B2 receptors are involved in cell death and brain edema formation after experimental stroke.

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9

Hess, J. Fred, Patricia J. Hey, Tsing-Bau Chen, Julie OBrien, Stacey S. Omalley, Douglas J. Pettibone y Raymond S. L. Chang. "Molecular Cloning and Pharmacological Characterization of the Canine B1 and B2 Bradykinin Receptors". Biological Chemistry 382, n.º 1 (6 de enero de 2001): 123–29. http://dx.doi.org/10.1515/bc.2001.018.

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Abstract The dog is a valuable animal model in the study of the physiological role of both the B1 and B2 bradykinin receptors. To more thoroughly characterize the pharmacological properties of the canine kinin receptors we isolated the cDNA sequence encoding the B1 and B2 bradykinin receptor subtypes and overexpressed them in Chinese hamster ovary (CHO) cells. The cDNA sequence of the canine B1 bradykinin receptor encodes a protein comprised of 350 amino acids that is 76% identical to the human B1 bradykinin receptor. The cDNA sequence of the canine B2 bradykinin receptor encodes a protein of 392 amino acids that is 81% identical to the human B2 bradykinin receptor. The amino acid sequence of the canine B1 and B2 receptors are 35% identical. Pharmacological studies of the cloned receptors revealed that the agonist affinity of the dog B1 receptor is similar to the rodent B1 receptors, and differs from the human form in that there is no preference for the presence of the Nterminal Lys residue of [desArg10]Lysbradykinin. Significantly, the B1 receptor antagonist [desArg9,Leu8]BK behaves as partial agonist on the cloned dog B1 receptor. The dog B2 receptor exhibits the classical pharmacological properties of this receptor subtype.

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10

Xiao, Hong D., Sebastien Fuchs, Justin M. Cole, Kevin M. Disher, Roy L. Sutliff y Kenneth E. Bernstein. "Role of bradykinin in angiotensin-converting enzyme knockout mice". American Journal of Physiology-Heart and Circulatory Physiology 284, n.º 6 (1 de junio de 2003): H1969—H1977. http://dx.doi.org/10.1152/ajpheart.00010.2003.

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Angiotensin-converting enzyme (ACE) plays a central role in the renin-angiotensin system. Whereas ACE is responsible for the production of angiotensin II, it is also important in the elimination of bradykinin. Constitutively, the biological function of bradykinin is mediated through the bradykinin B2 receptor. ACE knockout mice have a complicated phenotype including very low blood pressure. To investigate the role of bradykinin in the expression of the ACE knockout phenotype, we bred B2 receptor knockout mice with ACE knockout mice, thus generating a line of mice deficient in both the B2 receptor and ACE. Surprisingly, these mice did not differ from ACE knockout mice in blood pressure, urine concentrating ability, renal pathology, and hematocrit. Thus abnormalities of bradykinin accumulation do not play an important role in the ACE knockout phenotype. Rather, this phenotype appears due to the defective production of angiotensin II.

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11

Brew, E. C., M. B. Mitchell, T. F. Rehring, F. Gamboni-Robertson, R. C. McIntyre, A. H. Harken y A. Banerjee. "Role of bradykinin in cardiac functional protection after global ischemia-reperfusion in rat heart". American Journal of Physiology-Heart and Circulatory Physiology 269, n.º 4 (1 de octubre de 1995): H1370—H1378. http://dx.doi.org/10.1152/ajpheart.1995.269.4.h1370.

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We have reported that cardiac preconditioning against ischemia-reperfusion (IR) can be induced by transient ischemia (TI) and alpha 1-adrenoreceptor stimulation, both mediated by protein kinase C (PKC) (Mitchell, M., X. Meng, C. Parker, E. Brew, A. Harken, and A. Banerjee. Circ. Res. 76: 73-81, 1995). Our study objective was to explore the mechanism of endogenous preconditioning and address the role of PKC activation in bradykinin-mediated cardiac functional protection. Isolated rat heart was used to assess the effects of exogenous bradykinin, TI, selective B2-receptor blocker, and PKC antagonism on cardiac functional recovery after a global IR injury. Final recovery of developed pressure was improved in hearts treated with bradykinin and TI compared with controls. Bradykinin- and TI-mediated preconditioning was eliminated with coinfusion of the B2-receptor antagonist. Further evaluation of bradykinin-mediated preconditioning revealed that PKC blockade also eliminated functional protection. Immunofluorescent stains of bradykinin-treated hearts demonstrated translocation and activation of specific PKC isoforms in the preconditioned heart. We conclude that TI-mediated preconditioning involves intrinsic cardiac bradykinin receptor stimulation. Bradykinin, through the B2 receptor, initiates a series of intracellular events culminating in the activation of PKC.

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12

Gieldon, Artur, Jakob J. Lopez, Clemens Glaubitz y Harald Schwalbe. "Theoretical Study of the Human Bradykinin-Bradykinin B2 Receptor Complex". ChemBioChem 9, n.º 15 (13 de octubre de 2008): 2487–97. http://dx.doi.org/10.1002/cbic.200800324.

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13

Regoli, Domenico, Nour-Eddine Rhaleb, Stéphane Dion y Guy Drapeau. "New selective bradykinin receptor antagonists and bradykinin B2 receptor characterization". Trends in Pharmacological Sciences 11, n.º 4 (abril de 1990): 156–61. http://dx.doi.org/10.1016/0165-6147(90)90067-i.

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14

Ji, Bingyuan, Baohua Cheng, Yanyou Pan, Chunmei Wang, Jing Chen y Bo Bai. "Neuroprotection of bradykinin/bradykinin B2 receptor system in cerebral ischemia". Biomedicine & Pharmacotherapy 94 (octubre de 2017): 1057–63. http://dx.doi.org/10.1016/j.biopha.2017.08.042.

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15

Nagaki, M., S. Shimura, T. Irokawa, T. Sasaki, T. Oshiro, M. Nara, Y. Kakuta y K. Shirato. "Bradykinin regulation of airway submucosal gland secretion: role of bradykinin receptor subtype". American Journal of Physiology-Lung Cellular and Molecular Physiology 270, n.º 6 (1 de junio de 1996): L907—L913. http://dx.doi.org/10.1152/ajplung.1996.270.6.l907.

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To clarify the role of bradykinin receptor subtypes, we examined the effect of bradykinin on feline tracheal and human airway submucosal gland secretion using an isolated gland preparation. Bradykinin induced a significant increase in [3H]glycoconjugate secretion in a dose-dependent manner from isolated glands, which was significantly inhibited by D-Arg-(Hyp3, Thi5,8, D-Phe7)-bradykinin (the B2-receptor antagonist), whereas Des-Arg9-(Leu8)-bradykinin (B1-receptor antagonist) or indomethacin did not significantly alter it. Nitric oxide synthase inhibitor (nitro-L-arginine methyl ester) caused a significant inhibition of bradykinin-induced glycoconjugate secretion, which was reversed by the addition of L-arginine. Bradykinin evoked bidirectional current responses, and an initial inward current (Cl- current) was followed by an outward current (K+ current) of the acinar cells in a whole cell configuration by patch-clamp technique. Bradykinin induced an immediate increase in intracellular calcium concentration ([Ca2+]i) of the acinar cells followed by a prolonged plateau, and Ca2+ removal resulted in an initial increase alone. [Ca2+]i rise was significantly inhibited by the B2-receptor antagonist, whereas the B1-receptor antagonist did not significantly alter it. These findings suggest that B2-receptor stimulation and the resultant [Ca2+]i rise induced both mucus glycoprotein and electrolyte secretions, involving NO formation in airway submucosal gland cells.

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16

Kim, Jenny H., Deepika Jain, Omar Tliba, Bei Yang, William F. Jester, Reynold A. Panettieri, Yassine Amrani y Ellen Puré. "TGF-β potentiates airway smooth muscle responsiveness to bradykinin". American Journal of Physiology-Lung Cellular and Molecular Physiology 289, n.º 4 (octubre de 2005): L511—L520. http://dx.doi.org/10.1152/ajplung.00027.2005.

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The molecular mechanisms by which bradykinin induces excessive airway obstruction in asthmatics remain unknown. Transforming growth factor (TGF)-β has been involved in regulating airway inflammation and remodeling in asthma, although it is unknown whether TGF-β can modulate bradykinin-associated bronchial hyperresponsiveness. To test whether TGF-β directly modulates airway smooth muscle (ASM) responsiveness to bradykinin, isolated murine tracheal rings were used to assess whether TGF-β alters ASM contractile responsiveness to bradykinin. Interestingly, we found TGF-β-treated murine rings (12.5 ng/ml, 18 h) exhibited increased expression of bradykinin 2 (B2) receptors and became hyperreactive to bradykinin, as shown by increases in maximal contractile responses and receptor distribution. We investigated the effect of TGF-β on bradykinin-evoked calcium signals since calcium is a key molecule regulating ASM excitation-contraction coupling. We reported that TGF-β, in a dose- (0.5–10 ng/ml) and time- (2–24 h) dependent manner, increased mRNA and protein expression of the B2 receptor in cultured human ASM cells. Maximal B2 receptor protein expression that colocalized with CD44, a marker of membrane cell surface, occurred after 18 h of TGF-β treatment and was further confirmed using fluorescence microscopy. TGF-β (2.5 ng/ml, 18 h) also increased bradykinin-induced intracellular calcium mobilization in fura-2-loaded ASM cells. TGF-β-mediated enhancement of calcium mobilization was not attenuated with indomethacin, a cyclooxygenase inhibitor. These data demonstrate for the first time that TGF-β may play a role in mediating airway hyperresponsiveness to bradykinin seen in asthmatics by enhancing ASM contractile responsiveness to bradykinin, possibly as a result of increased B2 receptor expression and signaling.

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Regoli, D., F. Gobeil, Q. T. Nguyen, D. Jukic, P. R. Seoane, J. M. Salvino y D. G. Sawutz. "Bradykinin receptor types and B2 subtypes". Life Sciences 55, n.º 10 (enero de 1994): 735–49. http://dx.doi.org/10.1016/0024-3205(94)00557-5.

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18

Takano, Masaoki y Shogo Matsuyama. "Intracellular and nuclear bradykinin B2 receptors". European Journal of Pharmacology 732 (junio de 2014): 169–72. http://dx.doi.org/10.1016/j.ejphar.2014.03.011.

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19

Schanstra, Joost, Johan Duchene, Laurence Desmond, Eric Neau, Denis Calise, Serge Estaque, Jean-Pierre Girolami y Jean-Loup Bascands. "The protective effect of angiotensin converting enzyme inhibition in experimental renal fibrosis in mice is not mediated by bradykinin B2 receptor activation". Thrombosis and Haemostasis 89, n.º 04 (2003): 735–40. http://dx.doi.org/10.1055/s-0037-1613580.

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SummaryUnilateral ureteral obstruction (UUO) is an animal model of accelerated renal tubulointerstitial fibrosis. We have recently shown, using this model, that mice lacking the bradykinin B2-receptor (B2-/- ) were more susceptible than control animals to the development of tubulointerstitial fibrosis. Angiotensin converting enzyme (ACE) inhibition slows down UUO-induced renal fibrosis. Since ACE-inhibition increases bradykinin and decreases angiotensin II concentrations we have verified if bradykinin is involved in the antifibrotic effects of ACE-inhibition using the UUO-model and B2-/- mice. Surprisingly, although ACE-inhibition significantly reduced renal fibrosis, no difference was observed between the degree of tubulointerstitial fibrosis, macrophage infiltration and cell proliferation between ACE-inhibitor treated B2+/+ and B2-/- mice suggesting the absence of a role of the B2-receptor in the antifibrotic effects of ACE-inhibition. This was confirmed at the level of bradykinin-induced activity of enzymes involved in the degradation of the extracellular matrix. However in both mouse strains, ACE-inhibitors were more efficient than AT1 receptor antagonists.Theme paper: Part of this paper was originally presented at the joint meetings of the 16th International Congress of the International Society of Fibrinolysis and Proteolysis (ISFP) and the 17th International Fibrinogen Workshop of the International Fibrinogen Research Society (IFRS) held in Munich, Germany, September, 2002.

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Yau, Lorraine, David P. Wilson, Jeffery P. Werner y Peter Zahradka. "Bradykinin receptor antagonists attenuate neointimal proliferation postangioplasty". American Journal of Physiology-Heart and Circulatory Physiology 281, n.º 4 (1 de octubre de 2001): H1648—H1656. http://dx.doi.org/10.1152/ajpheart.2001.281.4.h1648.

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Bradykinin has been linked to the development of restenosis in response to vascular injury. We therefore examined the effect of bradykinin on vascular smooth muscle cell growth and neointimal formation in organ culture. Bradykinin stimulated both RNA and DNA synthesis (by 175%) in smooth muscle cells from either porcine or human coronary arteries and increased cell number in a concentration-dependent manner. Both p42/44 mitogen-activated protein kinase (MAPK) and p38 kinase were also activated. Treatment with [Hyp3,Tyr(Me)8]bradykinin, a B2 receptor agonist, stimulated thymidine incorporation by 146%, whereas B1-selective Lys-des-Arg9-bradykinin had no effect. Addition of the B2 antagonist HOE-140 reduced the stimulation by 56%, whereas B1-selective des-Arg-HOE-140 had no significant effect. Similarly, HOE-140 attenuated angioplasty-induced neointimal formation in organ culture with an efficacy approaching 100% inhibition. These experiments suggest that bradykinin promotes smooth muscle proliferation after vascular injury, presumably via B2 receptor-dependent activation of MAPK family pathways, and may explain the negative outcome of angiotensin converting enzyme inhibitor therapy on restenosis in nonrodent models.

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Jong, Y. J., L. R. Dalemar, B. Wilhelm y N. L. Baenziger. "Human bradykinin B2 receptors isolated by receptor-specific monoclonal antibodies are tyrosine phosphorylated". Proceedings of the National Academy of Sciences 90, n.º 23 (1 de diciembre de 1993): 10994–98. http://dx.doi.org/10.1073/pnas.90.23.10994.

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We report the immunoaffinity isolation of bradykinin B2 receptors in a tyrosine-phosphorylated state from WI-38 human lung fibroblasts. We generated six monoclonal antibodies directed against B2 bradykinin receptor biologic activity mediating prostaglandin E2 production in WI-38. These cells express a repertoire of bradykinin receptor affinity forms with closely correlated biologic activity and [3H]bradykinin binding. Some of the monoclonal antibodies selectively recognize intermediate-affinity (Kd = 5.6 nM) or low-affinity (Kd = 42 nM) receptor forms, whereas others recognize epitopes common to both. The monoclonal antibodies block bradykinin binding and biologic activity. Immunoaffinity chromatography on an immobilized monoclonal antibody of intermediate- plus low-affinity specificity yields WI-38 B2 receptors with intact [3H]bradykinin binding activity and a molecular mass of 78 kDa. The same band is immunoblotted by all the monoclonal antibodies, indicating a similar molecular mass for receptor forms of different affinity. Anti-phosphotyrosine antibodies demonstrate that the receptors are tyrosine phosphorylated, with implications for receptor function and regulation. Genistein completely inhibits bradykinin-mediated prostaglandin E2 production with an IC50 of 8 microM, indicating that tyrosine kinase activity is critical for the signal transduction leading to arachidonic acid release.

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Sawutz, David G., Joseph M. Salvino, Ronald E. Dolle, Peter R. Seoane y Stephen G. Farmer. "Pharmacology and structure – activity relationships of the nonpeptide bradykinin receptor antagonist WIN 64338". Canadian Journal of Physiology and Pharmacology 73, n.º 7 (1 de julio de 1995): 805–11. http://dx.doi.org/10.1139/y95-109.

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A series of competitive, nonpeptide bradykinin receptor antagonists based on an α-amino acid scaffold have been developed and biologically characterized. The lead compound in the series, WIN 64338, demonstrates competitive inhibition of bradykinin-mediated functional responses through B2 receptors in a variety of tissues and species. WIN 64338 is specific for the bradykinin B2 receptor; it is inactive at both the B1and B3 kinin receptors. In conscious guinea pigs, WIN 64338 inhibits kinin-mediated bronchoconstriction but does not attenuate a similar response to acetylcholine. A series of WIN 64338 analogues display a well-defined structure–activity relationship, strongly suggesting binding in a specific manner to the B2 receptor. Structure–activity data suggest that a hydrophobic binding pocket that prefers large aromatic groups in a specific conformational orientation exists in the receptor ligand binding domain. This class of nonpeptide bradykinin receptor antagonists may lead to the design of other compounds with enhanced receptor affinity and optimal in vivo biological activity.Key words: bradykinin, antagonists, nonpeptide.

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Blaukat, Andree, Patrick Micke, Irina Kalatskaya, Alexander Faussner y Werner Müller-Esterl. "Downregulation of bradykinin B2 receptor in human fibroblasts during prolonged agonist exposure". American Journal of Physiology-Heart and Circulatory Physiology 284, n.º 6 (1 de junio de 2003): H1909—H1916. http://dx.doi.org/10.1152/ajpheart.00034.2003.

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Sustained activation of G protein-coupled receptors results in an attenuation of cellular responses, a phenomenon termed desensitization. Whereas mechanisms for rapid desensitization of ligand-receptor-G protein-effector systems are relatively well characterized, much less is known about long-term adaptation processes that occur in the continuous presence of an agonist. Here we have studied the fate of endogenously expressed bradykinin B2 receptors on human fibroblasts during prolonged agonist treatment. Stimulation with bradykinin for up to 24 h resulted in a 50% reduction of surface binding sites that was paralleled by a similar decrease of total B2 receptor protein followed by Western blotting using monoclonal antibodies to the B2 receptor. Whereas B2 receptor mRNA levels did not change during 24 h of agonist treatment, B2receptor de novo synthesis was attenuated by 35–50%, indicating translational control of B2 receptor levels. Furthermore, the half-life of B2 receptor protein was shortened by 20–40% as shown by 35S-labeled pulse-chase and immunoprecipitation experiments. This study demonstrates that bradykinin B2 receptor expression during long-term agonist treatment is primarily regulated on the (post)translational level, i.e., by attenuation of de novo synthesis and by reduction of receptor stability.

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24

HASHII, Minako, Shigeru NAKASHIMA, Shigeru YOKOYAMA, Koh-ichi ENOMOTO, Yoshio MINABE, Yoshinori NOZAWA y Haruhiro HIGASHIDA. "Bradykinin B2 receptor-induced and inositol tetrakisphosphate-evoked Ca2+ entry is sensitive to a protein tyrosine phosphorylation inhibitor in ras-transformed NIH/3T3 fibroblasts". Biochemical Journal 319, n.º 2 (15 de octubre de 1996): 649–56. http://dx.doi.org/10.1042/bj3190649.

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Signal transduction from mouse bradykinin B2 receptors to calcium influx was studied in ras-transformed NIH/3T3 (DT) fibroblasts. DT cells were preloaded with fura-2 and whole-cell voltage-clamped. Activation of B2 receptors resulted in a decrease of cellular fluorescence at the excitation wavelength of 340, or 360 nm after MnCl2 application, in both the presence and absence of external Ca2+ in DT cells, at a holding potential of -40 mV. This Mn2+ entry through the Ca2+ influx pathway increased with membrane hyperpolarization. Internal application of inositol 1,3,4,5-tetrakisphosphate (InsP4), but not of inositol 1,4,5-trisphosphate, mimicked membrane potential-dependent Mn2+ entry. Bradykinin- and InsP4-induced Ca2+ influx was blocked by 10–100 µM genistein, a tyrosine kinase inhibitor. B2 receptor activation induced time-dependent tyrosine phosphorylation of mitogen-activated protein kinase and 120 kDa protein, which was dose-dependently inhibited by genistein. Bradykinin was unable to induce Ca2+ oscillations in genistein-treated DT cells. Our results show that bradykinin-induced Ca2+ influx and oscillations depend upon protein tyrosine phosphorylation. The results suggest that two bradykinin B2 receptor-activated signal pathways, protein tyrosine phosphorylation and formation of InsP4, merge at the Ca2+ influx process in ras-transformed NIH/3T3 fibroblasts.

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25

Yamawaki, I., P. Geppetti, C. Bertrand, B. Chan y J. A. Nadel. "Airway vasodilation by bradykinin is mediated via B2 receptors and modulated by peptidase inhibitors". American Journal of Physiology-Lung Cellular and Molecular Physiology 266, n.º 2 (1 de febrero de 1994): L156—L162. http://dx.doi.org/10.1152/ajplung.1994.266.2.l156.

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We studied the effect of exogenous bradykinin on blood flow in the airway microcirculation of anesthetized F344 rats in vivo. We made three successive determinations of airway blood flow and cardiac output using a modification of the reference sample microsphere technique. Injection of bradykinin into the left ventricle increased airway blood flow in a dose-related manner. Pretreatment with the bradykinin B2 receptor antagonist, Hoe 140, completely abolished bradykinin-, but not histamine-induced vasodilation. A bradykinin B1 receptor agonist, [des-Arg9]bradykinin, did not affect airway blood flow. We also studied the effect of inhibitors of angiotensin-converting enzyme (captopril) and neutral endopeptidase (phosphoramidon) on bradykinin-induced vasodilation. Pretreatment with captopril, but not phosphoramidon, potentiated the bradykinin-induced vasodilation. However, the addition of phosphoramidon further potentiated the effect of captopril. We conclude that injection of bradykinin into the left ventricle produces a dose-related vasodilation in the airway microcirculation mediated via B2 receptors, an effect that is modulated primarily by angiotensin-converting enzyme and, to a lesser extent, by neutral endopeptidase.

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26

Zamorano, Rocio, Sunil Suchindran y James V. Gainer. "3′-Untranslated region of the type 2 bradykinin receptor is a potent regulator of gene expression". American Journal of Physiology-Renal Physiology 290, n.º 2 (febrero de 2006): F456—F464. http://dx.doi.org/10.1152/ajprenal.00009.2005.

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Regulation of the constitutively expressed type 2 bradykinin (B2) receptor, which mediates the principal actions of bradykinin, occurs at multiple levels. The goal of the current study was to determine whether the human B2 3′-untranslated region (UTR) has effects on gene expression, with particular focus on the variable number of tandem repeats (B2-VNTR) polymorphic portion of the 3′-UTR and its flanking AU-rich elements (AREs). When inserted downstream of the luciferase coding region of the pGL3-Promoter vector, the B2-VNTR reduced reporter gene activity by 85% compared with pGL3-Promoter alone (promoter control; P < 0.001), an effect that was not appreciably affected by mutation of the flanking AREs. The negative regulatory effects of the B2-VNTR region were position and orientation dependent and strongly positively correlated with the number of tandem repeats in the B2-VNTR region ( r = 0.85, P < 0.001). With respect to mechanism, quantitative RT-PCR revealed that the B2-VNTR mRNA level was 32% of that of promoter control ( P = 0.008), whereas the number of polyadenylated transcripts was 4% ( P = 0.02). In contrast, the mRNA half-life of the B2-VNTR was increased (B2-VNTR: 14.9 vs. promoter control: 12.2 h, P = 0.009). Transient transfection of human kidney-derived tsA201 cells with the B2-VNTR construct increased transcription of the native B2 receptor mRNA by 43% ( P < 0.05), supporting an endogenous B2 receptor-regulatory capacity of the B2-VNTR. In conclusion, these results identify novel pretranslational effects of the B2-VNTR region to act as a potent negative regulator of heterologous gene expression and support the notion that the bradykinin B2 3′-UTR may impact endogenous receptor regulation.

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27

Tsutsui, Masato, Hisashi Onoue, Yasuhiko Iida, Leslie Smith, Timothy O'Brien y Zvonimir S. Katusic. "B1 and B2 bradykinin receptors on adventitial fibroblasts of cerebral arteries are coupled to recombinant eNOS". American Journal of Physiology-Heart and Circulatory Physiology 278, n.º 2 (1 de febrero de 2000): H367—H372. http://dx.doi.org/10.1152/ajpheart.2000.278.2.h367.

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Our previous ex vivo and in vivo studies reported that expression of the recombinant endothelial nitric oxide (NO) synthase (eNOS) gene in adventitial fibroblasts recovers NO production in arteries without endothelium in response to bradykinin. The present study was designed to characterize subtypes of bradykinin receptors on adventitial fibroblasts coupled to the activation of recombinant eNOS. Endothelium-denuded segments of canine basilar arteries were transduced with β-galactosidase (β-Gal) gene or eNOS gene ex vivo, using a replication-defective adenoviral vector (1010 plaque-forming units/ml) for 30 min at 37°C. Twenty-four hours later, isometric force recording or cGMP measurement was carried out. B1 bradykinin receptor agonist (des-Arg9-bradykinin, 10− 10-10− 8mol/l) did not significantly affect vascular tone in control or β-Gal gene-transduced canine basilar arteries without endothelium. In contrast, this agonist caused concentration-dependent relaxations in recombinant eNOS gene-transduced arteries without endothelium. Relaxations to B1 receptor agonist in the eNOS arteries were abolished by B1 receptor antagonist (des-Arg9-[Leu8]bradykinin, 6 × 10− 9 mol/l) but not by B2 receptor antagonist (Hoe-140, 5 × 10− 8 mol/l). Bradykinin did not significantly alter vascular tone in control or β-gal arteries without endothelium, whereas this peptide (10− 11-10− 8mol/l) induced concentration-dependent relaxations, as well as an increase in cGMP formation in endothelium-denuded eNOS-transduced arteries. Stimulatory effects of bradykinin were prevented in the presence of a B2 receptor antagonist but not in the presence of a B1 receptor antagonist. B1 and B2 receptor antagonists had no effect on relaxations to substance P, confirming the selectivity of the compounds. Our results suggest that B1 and B2 bradykinin receptors are coupled to activation of recombinant eNOS expressed in adventitial fibroblasts.

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28

Haasemann, M., J. Cartaud, W. Muller-Esterl y I. Dunia. "Agonist-induced redistribution of bradykinin B2 receptor in caveolae". Journal of Cell Science 111, n.º 7 (1 de abril de 1998): 917–28. http://dx.doi.org/10.1242/jcs.111.7.917.

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Redistribution of receptors within the plasma membrane as well as between the plasma membrane and various cell compartments presents an important way of regulating the cellular responsiveness to their cognate agonists. We have applied immunocytochemical methods to localize the bradykinin B2 receptor and to examine its agonist induced redistribution in A431 cells. In situ labeling with antibodies to ectodomain-2 of the receptor which do not interfere with bradykinin binding of the receptor showed a random distribution of the B2 receptor on the plasma membrane. Stimulation of cells with 20 nM bradykinin markedly reduced the accessibility of the antibody to its corresponding epitope in non-permeabilized cells. Immuno-electron microscopy revealed the presence of receptors in membrane-near vesicles that are surrounded by an electron-transparent halo. Fluorescence microscopic double labeling co-localized the B2 receptor protein with caveolin-1 by a convergent pattern of punctate staining. At the ultrastructural level the B2 receptor protein was found in vesicles that bear the immunolabel of caveolin-1 and display the morphological characteristics of caveolae. We conclude that stimulation of B2 receptors results in their redistribution and sequestration in caveolae, an event that is likely to be implicated in receptor signaling and/or desensitization. The localization of B2 receptors in endosome-like structures after prolonged exposure to bradykinin might indicate that the internalization through caveolae may communicate with other endocytotic pathways of A431 cells.

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29

Wilkes, B. M. y P. F. Mento. "Bradykinin-induced vasoconstriction and thromboxane release in perfused human placenta". American Journal of Physiology-Endocrinology and Metabolism 254, n.º 6 (1 de junio de 1988): E681—E686. http://dx.doi.org/10.1152/ajpendo.1988.254.6.e681.

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This investigation was performed to study the effects of bradykinin on the human fetoplacental circulation. The artery to a single placental cotyledon was perfused with RPMI medium (0.764 ml/min). Bradykinin caused a dose-related increase in vascular resistance. Because bradykinin is generally a vasodilator, we investigated the possibility that bradykinin-induced vasoconstriction was due to interactions with other pressor systems. Bradykinin and 9,11-dideoxy-9 alpha, 11 alpha-epoxymethanoprostaglandin F2 alpha (a stable thromboxane agonist) caused a dose-related increase in perfusion pressure. The bradykinin response was not mediated by angiotensin II, because bradykinin-induced vasoconstriction was not inhibited by saralasin, a competitive angiotensin antagonist. Bradykinin increased thromboxane B2 production by 62.0%. Prostaglandin E2 levels were increased by 86.7%, but prostaglandin E2 did not affect fetoplacental vascular resistance. Angiotensin II did not stimulate thromboxane B2 production and caused only a slight increase in prostaglandin E2. Indomethacin decreased the pressor response to angiotensin II. SQ29548, a specific thromboxane antagonist, caused a 61.6% inhibition of the bradykinin pressor response but did not change angiotensin II responsiveness. The data demonstrate that thromboxane is an important mediator of bradykinin-induced vasoconstriction in the isolated perfused human placenta.

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30

Rhaleb, Nour-Eddine, Noureddine Rouissi, Guy Drapeau, Daniela Jukic y Domenico Regoli. "Characterization of bradykinin receptors in peripheral organs". Canadian Journal of Physiology and Pharmacology 69, n.º 7 (1 de julio de 1991): 938–43. http://dx.doi.org/10.1139/y91-142.

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Bradykinin (BK) and related kinins are potent stimulants of the rabbit jugular vein, the hamster urinary bladder, and the guinea pig trachea. The characterization of kinin receptors in these tissues was made with agonists and antagonists. Results obtained with agonists indicate that bradykinin and kallidin are much more active than des-Arg9-BK and suggest the presence of B2 receptors in the three organs. Some new agonists were also tested and the BK analogue, [Hyp3,Tyr(Me)8]BK, was found to be a potent and selective stimulant of the three preparations, with pD2 values of 8.56, 8.00, and 8.39, respectively, but inactive on the rabbit aorta (a B1-receptor system). Contractile effects of kinins in the rabbit jugular vein and hamster urinary bladder were reduced or eliminated by B2-receptor antagonists but at different concentration levels; e.g., acetyl-D-Arg[Hyp3,D-Phe7]BK showed pA2 values of 7.78 on the rabbit jugular vein but only 5.72 on hamster urinary bladder. This compound contracted the guinea-pig trachea and was found to be inactive as an antagonist on this preparation. Contractions of the hamster urinary bladder and the guinea-pig trachea in response to bradykinin were markedly reduced or eliminated by indomethacin and by BW 755C, while those of the rabbit jugular vein were not modified. The present findings indicate that the myotropic effect of kinins on the rabbit jugular vein depends on the activation of B2 receptors and suggest that B2 receptors are largely responsible also for the response of the hamster urinary bladder. B2 receptors and (or) a nonreceptor mechanism appear to be involved in the stimulant effects of the kinin agonists and some antagonists in the guinea-pig trachea.Key words: bradykinin, B2 receptors, agonists, antagonists, smooth muscles, arachidonic acid cascade, indomethacin, BW 755C.

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31

Park, Tae-Ju y Kyong-Tai Kim. "Activation of B2 bradykinin receptors by neurotensin". Cellular Signalling 15, n.º 5 (mayo de 2003): 519–27. http://dx.doi.org/10.1016/s0898-6568(02)00136-5.

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32

Buchinger, Peter y Joachim Rehbock. "The Bradykinin B2-Receptor in Human Decidua". Seminars in Thrombosis and Hemostasis 25, n.º 06 (diciembre de 1999): 543–49. http://dx.doi.org/10.1055/s-2007-994963.

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33

Chen, Er-Yun, Dwaine F. Emerich, Raymond T. Bartus y Jeffrey H. Kordower. "B2 bradykinin receptor immunoreactivity in rat brain". Journal of Comparative Neurology 427, n.º 1 (2000): 1–18. http://dx.doi.org/10.1002/1096-9861(20001106)427:1<1::aid-cne1>3.0.co;2-0.

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34

Regoli, D., N. E. Rhaleb, C. Tousignant, N. Rouissi, F. Nantel, D. Jukic y G. Drapeau. "New highly potent bradykinin B2 receptor antagonists". Agents and Actions 34, n.º 1-2 (septiembre de 1991): 138–41. http://dx.doi.org/10.1007/bf01993260.

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35

Lehmberg, Jens, Jürgen Beck, Alexander Baethmann y Eberhard Uhl. "Bradykinin Antagonists Reduce Leukocyte–Endothelium Interactions after Global Cerebral Ischemia". Journal of Cerebral Blood Flow & Metabolism 23, n.º 4 (abril de 2003): 441–48. http://dx.doi.org/10.1097/01.wcb.0000052280.23292.35.

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The aim of the present study was to evaluate the influence of bradykinin on microcirculatory changes and outcome after global cerebral ischemia (15 minute) in Mongolian gerbils. The cerebral microcirculation was investigated by fluorescent intravital microscopy. Survival and functional outcome was evaluated up to 4 d after ischemia. Animals were treated with the selective B1 and B2 receptor antagonists B 9858 and CP 0597, respectively, and the nonselective B1/B2 receptor antagonist B 9430. Leukocyte activation was significantly reduced by all antagonists as indicated by a significant decrease in the number of rolling (33 ± 20, 6 ± 8, 9 ± 10, and 13 ± 10) and adherent leukocytes (9 ± 7, 3 ± 4, 1 ± 1, and 2 ± 3 · 100 μm–1 · min–1 in controls and in animals treated with B1, B2, and B1/B2 antagonist, respectively). Arteriolar diameters were significantly reduced during reperfusion (35 ± 11 before and 27 ± 8 μm 40 minutes after ischemia) in animals treated with the B2 antagonist. The postischemic hypoperfusion, however, was not affected. Mortality was significantly higher in animals treated with the B1 and the B1/B2 antagonist. The authors concluded that bradykinin is involved in postischemic disturbances of cerebral microcirculation. The therapeutic effect of specific bradykinin receptor antagonists on functional outcome, however, remains unclear.

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36

Morgan-Boyd, R., J. M. Stewart, R. J. Vavrek y A. Hassid. "Effects of bradykinin and angiotensin II on intracellular Ca2+ dynamics in endothelial cells". American Journal of Physiology-Cell Physiology 253, n.º 4 (1 de octubre de 1987): C588—C598. http://dx.doi.org/10.1152/ajpcell.1987.253.4.c588.

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The purpose of this study was to investigate the effects of angiotensin II and bradykinin on intracellular Ca2+ dynamics in cultured endothelial cells. We used the "second-generation" fluorescent Ca2+ indicator fura-2, in conjunction with dual-wavelength fluorescence spectroscopy, in cultured adherent pulmonary arterial endothelial cells. Angiotensin II (up to 2 microM) had no consistent effect on intracellular Ca2+ levels. In contrast, bradykinin (10 nM) elicited a transient increase of cytosolic free Ca2+, from the resting value of 37 +/- 5 to 647 +/- 123 nM, followed by a decline to a steady-state value of 113 +/- 14 nM, which was significantly higher than the resting Ca2+ levels. Bradykinin's Ca-stimulatory effect was dose dependent, having a half-maximally effective concentration of approximately 1 nM and a maximally effective concentration of 10 nM. A B1-receptor agonist, Des-Arg9-bradykinin, was much less effective than bradykinin as modulator of cytosolic Ca2+. Moreover, a B1-receptor antagonist, Des-Arg9, [Leu8]-bradykinin, did not significantly affect the increase of cytosolic Ca2+ elicited by bradykinin. On the other hand, the bradykinin-elicited increase of Ca2+ was almost completely inhibited by a novel B2-receptor antagonist, D-Arg-[Hyp3, Thi5,8, D-Phe7]-bradykinin. Bradykinin increased cytosolic free Ca2+ levels in cells maintained in Ca2+-deficient extracellular medium, suggesting that the peptide mobilized Ca2+ from intracellular stores. However, the absence of extra-cellular Ca2+ resulted in an 80-90% attenuation of the transient Ca2+ response, whereas the posttransient steady-state response was completely absent. These findings are consistent with the notion that the bradykinin-elicited transient Ca2+ response is dependent on both extra- and intracellular Ca2+ and that the posttransient steady-state response is entirely dependent on extracellular Ca2+. Endothelial cells were responsive to a second dose of bradykinin after a 10-min interim period of incubation in the absence of the peptide hormone. The absence of extracellular Ca2+ during the interim period, or the pretreatment of cells with ionomycin in the absence of extracellular Ca2+, prevented the response of the cells to a second dose of bradykinin. Bradykinin- or ionomycin-desensitized cells could be resensitized by a brief incubation period in Ca2+-replete medium. The results are consistent with the notions that cellular resensitization requires the replenishment of intracellular Ca2+ and that bradykinin, but not angiotensin II, modulates intracellular Ca2+ dynamics in endothelial cells by interacting with a B2-type receptor.

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37

Figueroa, C. D., C. B. Gonzalez, S. Grigoriev, S. A. Abd Alla, M. Haasemann, K. Jarnagin y W. Müller-Esterl. "Probing for the bradykinin B2 receptor in rat kidney by anti-peptide and anti-ligand antibodies." Journal of Histochemistry & Cytochemistry 43, n.º 2 (febrero de 1995): 137–48. http://dx.doi.org/10.1177/43.2.7822771.

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The kallikrein-kinin system is involved in the inflammatory process, in blood pressure regulation, and in renal homeostasis. The presence of kallikreins, kininogens, and kinins in renal tissues and fluids is well established; however, the occurrence and distribution of the bradykinin (B2) receptor in the kidney are unknown. Using chemically cross-linked conjugates of bovine serum albumin and the B2 agonist bradykinin or the potent B2 antagonist HOE140, followed by antibodies to the respective ligand and the peroxidase-anti-peroxidase system, we were able to detect the B2 receptor. The receptor has been found in straight portions of the proximal tubules, in distal straight tubules, in connecting tubules, and in collecting ducts of rat kidney. The staining patterns produced by the ligand conjugate-antiligand approach are in agreement with those obtained by conventional autoradiography using [125I]-Tyr0-bradykinin. Immunocytochemical localization of B2 receptor by antipeptide antibodies to the receptor confirmed these findings and demonstrated the presence of B2 receptor in the basal infoldings and luminal membranes of the tubule cells, and in smooth muscle cells of the cortical radial artery and of afferent arterioles. Co-localization of the B2 receptor with kallikrein and kininogens in connecting tubule cell and collecting duct cell layers, respectively, provides a structural basis for the hypothesized physiological functions of the kallikrein-kinin system in the kidney.

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38

Lavoie, Julie L. y Louise Béliveau. "Bradykinin facilitates noradrenaline spillover during contraction in the canine gracilis muscle". Canadian Journal of Physiology and Pharmacology 79, n.º 10 (1 de octubre de 2001): 831–35. http://dx.doi.org/10.1139/y01-062.

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Noradrenaline spillover from skeletal muscle vascular areas increases during exercise but the underlying mechanisms are not well understood. Muscle contraction itself causes changes in many factors that could affect noradrenaline spillover. For instance, it has been reported that bradykinin is synthesized in skeletal muscle areas during contraction. Because the B2 bradykinin receptor facilitates noradrenaline spillover, it may be involved in the increase associated with contraction. In this experiment, we studied the effect of bradykinin on noradrenaline spillover in the in situ canine gracilis muscle, using the specific B2 antagonist HOE 140. The drug did not modify noradrenaline spillover at rest, but did cause a significant decrease during muscle contraction, from 558 to 181 pg·min1. As reported previously in the literature, fractional extraction of noradrenaline decreased during muscle contraction. This effect was independent of HOE 140 treatment. In light of our results, it seems that bradykinin formation during muscle contraction may play an important part in the observed increase in noradrenaline spillover but does not affect fractional extraction.Key words: skeletal muscle, fractional extraction, stimulation, HOE 140, B2 receptors.

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39

Trabold, Raimund, Christian Erös, Klaus Zweckberger, Jane Relton, Heike Beck, Juerg Nussberger, Werner Müller-Esterl, Michael Bader, Eric Whalley y Nikolaus Plesnila. "The Role of Bradykinin B1 and B2 Receptors for Secondary Brain Damage after Traumatic Brain Injury in Mice". Journal of Cerebral Blood Flow & Metabolism 30, n.º 1 (23 de septiembre de 2009): 130–39. http://dx.doi.org/10.1038/jcbfm.2009.196.

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Inflammatory mechanisms are known to contribute to the pathophysiology of traumatic brain injury (TBI). Since bradykinin is one of the first mediators activated during inflammation, we investigated the role of bradykinin and its receptors in posttraumatic secondary brain damage. We subjected wild-type (WT), B1-, and B2-receptor-knockout mice to controlled cortical impact (CCI) and analyzed tissue bradykinin as well as kinin receptor mRNA and protein expression up to 48 h thereafter. Brain edema, contusion volume, and functional outcome were assessed 24 h and 7 days after CCI. Tissue bradykinin was maximally increased 2 h after trauma ( P<0.01 versus sham). Kinin B1 receptor mRNA was upregulated up to four-fold 24 h after CCI. Immunohistochemistry showed that B1 and B2 receptors were expressed in the brain and were significantly upregulated in the traumatic penumbra 1 to 24 h after CCI. B2R−/− mice had significantly less brain edema (−51% versus WT, 24 h; P<0.001), smaller contusion volumes (∼50% versus WT 24 h and 7 d after CCI; P<0.05), and better functional outcome 7 days after TBI as compared with WT mice ( P<0.05). The present results show that bradykinin and its B2 receptors play a causal role for brain edema formation and cell death after TBI.

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40

Gauthier, Kathryn M., Cody J. Cepura y William B. Campbell. "ACE inhibition enhances bradykinin relaxations through nitric oxide and B1 receptor activation in bovine coronary arteries". Biological Chemistry 394, n.º 9 (1 de septiembre de 2013): 1205–12. http://dx.doi.org/10.1515/hsz-2012-0348.

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Abstract Bradykinin causes vascular relaxations through release of endothelial relaxing factors including prostacyclin, nitric oxide (NO) and epoxyeicosatrienoic acids (EETs). Bradykinin is metabolized by angiotensin converting enzyme (ACE) and ACE inhibition enhances bradykinin relaxations. Our goal was to characterize the role of bradykinin receptors and endothelial factors in ACE inhibitor-enhanced relaxations in bovine coronary arteries. In U46619 preconstricted arteries, bradykinin (10-11-10-8m) caused concentration-dependent relaxations (maximal relaxation ≥100%, log EC50=-9.8±0.1). In the presence of the NO synthase inhibitor, N-nitro-L-arginine (L-NA, 30 μm) and the cyclooxygenase inhibitor, indomethacin (10 μm), relaxations were reduced by an inhibitor of EET synthesis, miconazole (10 μm) (maximal relaxation=55±10%). Bradykinin relaxations were inhibited by the bradykinin 2 (B2) receptor antagonist, D-Arg0-Hyp3-Thi5,8-D-Phe7-bradykinin (1 μm) (log EC50=-8.5±0.1) but not altered by the B1 receptor antagonist, des-Arg9[Leu8]bradykinin (1 μm). Mass spectrometric analysis of bovine coronary artery bradykinin metabolites revealed a time-dependent increase in bradykinin (1–5) and (1–7) suggesting metabolism by ACE. ACE inhibition with captopril (50 μm) enhanced bradykinin relaxations (log EC50=-10.3±0.1). The enhanced relaxations were eliminated by L-NA or the B1 receptor antagonist but not the B2 receptor antagonist. Our results demonstrate that ACE inhibitor-enhanced bradykinin relaxations of bovine coronary arteries occur through endothelial cell B1 receptor activation and NO.

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41

Maruo, Keishi, Takaaki Akaike, Tomomichi Ono y Hiroshi Maeda. "Involvement of Bradykinin Generation in Intravascular Dissemination of Vibrio vulnificus and Prevention of Invasion by a Bradykinin Antagonist". Infection and Immunity 66, n.º 2 (1 de febrero de 1998): 866–69. http://dx.doi.org/10.1128/iai.66.2.866-869.1998.

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ABSTRACT Involvement of bradykinin generation in bacterial invasion was examined by using a gram-negative bacillus, Vibrio vulnificus, which is known to invade the blood circulatory system and cause septicemia. V. vulnificus was injected intraperitoneally (i.p.) into mice with or without bradykinin or a bradykinin (B2 receptor) antagonist. Dissemination of V. vulnificus from peritoneal septic foci to the circulating blood was assessed by counting of viable bacteria in venous blood by use of the colony-forming assay. Intravascular dissemination of V. vulnificus in mice was significantly potentiated by simultaneous injection with bradykinin but was markedly reduced by coadministration with the B2 antagonist d-Arg,[Hyp3, Thi5,8, d-Phe7]-bradykinin. Furthermore, V. vulnificus lethality was significantly increased when bradykinin was administered simultaneously with the bacillus, whereas it was definitely suppressed by treatment withd-Arg,[Hyp3, Thi5,8,d-Phe7]-bradykinin. Similarly, ovomacroglobulin, a potent inhibitor of the V. vulnificusprotease, showed a strong suppressive effect on the V. vulnificus septicemia. We also confirmed appreciable bradykinin production in the primary septic foci in the mouse peritoneal cavity after i.p. inoculation with V. vulnificus. It is thus concluded that bradykinin generation in infectious foci is critically involved in facilitation of intravascular dissemination of V. vulnificus.

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42

Singh, Padmasana, Amitabh Krishna y Rajagopala Sridaran. "Changes in bradykinin and bradykinin B2-receptor during estrous cycle of mouse". Acta Histochemica 113, n.º 4 (julio de 2011): 436–41. http://dx.doi.org/10.1016/j.acthis.2010.03.008.

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43

Borkowski, Joseph A. y J. Fred Hess. "Targeted disruption of the mouse B2 bradykinin receptor in embryonic stem cells". Canadian Journal of Physiology and Pharmacology 73, n.º 7 (1 de julio de 1995): 773–79. http://dx.doi.org/10.1139/y95-104.

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Two mammalian genes encoding bradykinin (BK) receptors termed B1 and B2 have been identified by molecular cloning techniques. Some pharmacological data suggest the existence of further subtypes of the B2 receptor. To unambiguously determine whether additional genes encoding B2 BK receptors might exist in mammals, steps have been taken toward the generation of mice with a "knockout" of the BK B2 receptor. A genomic clone of the mouse B2 BK receptor was isolated and its coding sequence determined by DNA sequence analysis. A physical map of the DNA flanking this coding sequence was generated. A vector, pBS-KO-1, was constructed for targeted disruption of the mouse B2 receptor gene. This vector contains 1 kb (kilobase) of DNA upstream of the mouse B2 receptor coding sequence, a neomycin resistance gene (neo), and 5.4 kb of DNA downstream of the B2 receptor coding sequence. Thus, the correct homologous recombination event will result in a chromosome in which the coding sequence for the mouse B2 BK receptor is replaced with the neomycin resistance gene. pBS-KO-1 was transfected into embryonic stem cells, and clones containing a targeted disruption of the mouse B2 BK receptor were identified.Key words: bradykinin, G-protein-coupled receptor, embryonic stem cells, gene targeting, homologous recombination.

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44

Yogi, Alvaro, Glaucia E. Callera, Rita Tostes y Rhian M. Touyz. "Bradykinin regulates calpain and proinflammatory signaling through TRPM7-sensitive pathways in vascular smooth muscle cells". American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 296, n.º 2 (febrero de 2009): R201—R207. http://dx.doi.org/10.1152/ajpregu.90602.2008.

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Transient receptor potential melastatin-7 (TRPM7) channels have recently been identified to be regulated by vasoactive agents acting through G protein-coupled receptors in vascular smooth muscle cells (VSMC). However, downstream targets and functional responses remain unclear. We investigated the subcellular localization of TRPM7 in VSMCs and questioned the role of TRPM7 in proinflammatory signaling by bradykinin. VSMCs from Wistar-Kyoto rats were studied. Cell fractionation by sucrose gradient and differential centrifugation demonstrated that in bradykinin-stimulated cells, TRPM7 localized in fractions corresponding to caveolae. Immunofluorescence confocal microscopy revealed that TRPM7 distributes along the cell membrane, that it has a reticular-type intracellular distribution, and that it colocalizes with flotillin-2, a marker of lipid rafts. Bradykinin increased expression of calpain, a TRPM7 target, and stimulated its cytosol/membrane translocation, an effect blocked by 2-APB (TRPM7 inhibitor) and U-73122 (phospholipase C inhibitor), but not by chelerythrine (PKC inhibitor). Expression of proinflammatory mediators VCAM-1 and cyclooxygenase-2 (COX-2) was time-dependently increased by bradykinin. This effect was blocked by Hoe-140 (B2 receptor blocker) and 2-APB. Our data demonstrate that in bradykinin-stimulated VSMCs: 1) TRPM7 is upregulated, 2) TRPM7 associates with cholesterol-rich microdomains, and 3) calpain and proinflammatory mediators VCAM-1 and COX2 are regulated, in part, via TRPM7- and phospholipase C-dependent pathways through B2 receptors. These findings identify a novel signaling pathway for bradykinin, which involves TRPM7. Such phenomena may play a role in bradykinin/B2 receptor-mediated inflammatory responses in vascular cells.

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45

Mio, Tadashi, Xiangde Liu, Myron L. Toews, Yuichi Adachi, Debra J. Romberger, John R. Spurzem y Stephen I. Rennard. "Bradykinin augments fibroblast-mediated contraction of released collagen gels". American Journal of Physiology-Lung Cellular and Molecular Physiology 281, n.º 1 (1 de julio de 2001): L164—L171. http://dx.doi.org/10.1152/ajplung.2001.281.1.l164.

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Bradykinin is a multifunctional mediator of inflammation believed to have a role in asthma, a disorder associated with remodeling of extracellular connective tissue. Using contraction of collagen gels as an in vitro model of wound contraction, we assessed the effects of bradykinin tissue on remodeling. Human fetal lung fibroblasts were embedded in type I collagen gels and cultured for 5 days. After release, the floating gels were cultured in the presence of bradykinin. Bradykinin significantly stimulated contraction in a concentration- and time-dependent manner. Coincubation with phosphoramidon augmented the effect of 10−9 and 10−8 M bradykinin. A B2 receptor antagonist attenuated the effect of bradykinin, whereas a B1 receptor antagonist had no effect, suggesting that the effect is mediated by the B2 receptor. An inhibitor of intracellular Ca2+mobilization abolished the response; addition of EGTA to the culture medium attenuated the contraction of control gels but did not modulate the response to bradykinin. In contrast, the phospholipase C inhibitor U-73122 and the protein kinase C inhibitors staurosporine and GF-109203X attenuated the responses. These data suggest that by augmenting the contractility of fibroblasts, bradykinin may have an important role in remodeling of extracellular matrix that may result in tissue dysfunction in chronic inflammatory diseases, such as asthma.

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46

Santiago, J. A., E. A. Garrison y P. J. Kadowitz. "Analysis of responses to bradykinin: effects of Hoe-140 in the hindquarters vascular bed of the cat". American Journal of Physiology-Heart and Circulatory Physiology 267, n.º 2 (1 de agosto de 1994): H828—H836. http://dx.doi.org/10.1152/ajpheart.1994.267.2.h828.

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The mechanisms and receptor subtype mediating vasodilator responses to bradykinin were investigated in the hindquarters vascular bed of the cat under constant flow conditions. Intraarterial injections of bradykinin in doses of 10–1,000 ng into the hindquarters vascular bed caused dose-related decreases in perfusion pressure that were inhibited by Hoe-140, a bradykinin B2-receptor antagonist. Injections of des-Arg9-bradykinin (in doses 10-fold higher than for bradykinin) caused smaller dose-related decreases in hindquarters perfusion pressure that were not blocked by Hoe-140. Administration of atropine, glibenclamide, or cyclooxygenase inhibitors did not alter vasodilator responses to bradykinin, suggesting that activation of muscarinic receptors, ATP-sensitive K+ channels, or prostaglandin release is not involved in the response to the peptide. Administration of N omega-nitro-L-arginine and its methyl ester reduced vasodilator responses to bradykinin, acetylcholine, and substance P, whereas responses to endothelium-independent vasodilator agents were not attenuated. Decreases in systemic arterial pressure and in hindquarters perfusion pressure in response to bradykinin were enhanced by the angiotensin-converting enzyme inhibitors captopril and enalaprilat. These results suggest that hindquarters vasodilator responses to bradykinin are mediated by activation of kinin B2 receptors and in part by the release of nitric oxide. These data also suggest the presence of bradykinin B1 receptors, mediating vasodilation in the hindquarters vascular bed. These results indicate that bradykinin is rapidly inactivated by angiotensin-converting enzyme in the lung and in the hindquarters vascular bed of the cat.

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47

Feletou, M., M. Germain y B. Teisseire. "Converting-enzyme inhibitors potentiate bradykinin-induced relaxation in vitro". American Journal of Physiology-Heart and Circulatory Physiology 262, n.º 3 (1 de marzo de 1992): H839—H845. http://dx.doi.org/10.1152/ajpheart.1992.262.3.h839.

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Experiments were designed to study the effects of converting-enzyme inhibitors (captopril and S 10211) on the endothelium-dependent relaxation to bradykinin in isolated porcine arteries. Rings of femoral arteries with and without endothelium were suspended in organ chambers to record isometric tension. Rings of coronary arteries without endothelium were used as bioassay tissue to record release of endothelium-derived relaxing factor (EDRF) from perfused femoral arteries. In organ chambers, bradykinin induced endothelium-dependent relaxation and, inconsistently, endothelium-independent contraction of the femoral artery rings. The relaxation is mediated by endothelial B2 bradykinin receptors, the contraction through B1 bradykinin receptors. Converting-enzyme inhibitors induced a weak potentiation of the contractile response and weak or no potentiation of the endothelium-dependent relaxation. In the presence of indomethacin, the response to bradykinin was not modified and no potentiation from the inhibitor could be observed. Blockade of the contractile response with a B1 bradykinin antagonist did not unmask a potentiation of the bradykinin endothelium-dependent relaxation by the converting-enzyme inhibitors. However, in the presence of B2 bradykinin antagonist, when high concentrations of bradykinin are required to induce relaxation, converting-enzyme inhibitors potentiated the effects of bradykinin. In contrast, in bioassay conditions with a perfused vascular segment, converting-enzyme inhibitors selectively enhanced the release of EDRF by bradykinin. This effect is observed in the bioassay tissue and in the donor segment. These results suggest that converting enzyme is indeed a powerful modulator of bradykinin action and that other enzymatic pathways of bradykinin metabolism present in the vascular wall could mask its action.

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48

Kugaevskaya, E. V. y Yu E. Elisseeva. "Ace inhibitors - activators of kinin receptors". Biomeditsinskaya Khimiya 57, n.º 3 (2011): 282–99. http://dx.doi.org/10.18097/pbmc20115703282.

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Angiotensin converting enzyme (ACE) inhibitors are widely used for treatment of cardiovascular diseases. The effects of ACE inhibitors on the human bradykinin receptors were investigated. The mode of action of ACE inhibitors is considered. There is evidence that ACE inhibitors exert effects on the vascular system that cannot be attributed simply to the inhibition of ACE activity and accumulation of locally produced bradykinin. ACE inhibitors augment bradykinin effects on receptors indirectly by inducing cross-talk between ACE and the B2 receptor when enzyme and receptor molecules are sterically close, possibly forming a heterodimer. ACE inhibitors activate B1 receptors directly and independently of ACE via the zink-binding consensus sequence HEXXH, which is present in B1, but not in B2 receptor. Particular structure of B2 and B1 are represented, as well as receptor amino acids coupled with the G-proteins. Activation of kinin receptors by ACE inhibitors leads to clinically beneficial effects of ACE inhibitors.

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49

Asano, Masayuki, Hiroe Sawai, Chie Hatori, Noriaki Inamura, Tatsujiro Fujiwara y Kunio Nakahara. "Effects of a nonpeptide bradykinin B2 receptor antagonist, FR167344, on guinea-pig tracheal smooth muscle bradykinin receptors". Canadian Journal of Physiology and Pharmacology 76, n.º 10-11 (1 de octubre de 1998): 1051–55. http://dx.doi.org/10.1139/y98-098.

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It is speculated that bradykinin may play an important role in asthma. Thus, bradykinin receptor antagonists may have therapeutic potential against asthma. Orally active bradykinin antagonists would be more desirable for the treatment of the disease. In the present study, we examined the effects of a novel, potent, selective, and orally active nonpeptide bradykinin B2 receptor antagonist, FR167344 (N-[N-[3-[(3-bromo-2-methylimidazo[1,2-a]pyridin-8-yl)oxymethyl]- 2,4-dichlorophenyl]-N-methylaminocarbonylmethyl]-4-(dimethylaminocarbonyl)cinnamylamide hydrochloride), on guinea-pig tracheal smooth muscle bradykinin receptors. FR167344 inhibited [3H]bradykinin binding to bradykinin receptors in epithelium-denuded guinea-pig tracheal membrane with an IC50 of 2.1 nM and a Ki of 0.44 nM. This compound also inhibited bradykinin-induced contraction of epithelium-denuded guinea-pig trachea with a pKB of 10.8, but had no effect on carbachol-induced contraction of the trachea even at 10-6 M. These results indicate that FR167344 has the specific antagonistic activity against guinea-pig tracheal smooth muscle bradykinin receptors.Key words: bradykinin, receptor, antagonist, FR167344, trachea.

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50

Shigematsu, Sakuji, Shuji Ishida, Dean C. Gute y Ronald J. Korthuis. "Bradykinin-induced proinflammatory signaling mechanisms". American Journal of Physiology-Heart and Circulatory Physiology 283, n.º 6 (1 de diciembre de 2002): H2676—H2686. http://dx.doi.org/10.1152/ajpheart.00538.2002.

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Intravital microscopic techniques were used to examine the mechanisms underlying bradykinin-induced leukocyte/endothelial cell adhesive interactions (LECA) and venular protein leakage (VPL) in single postcapillary venules of the rat mesentery. The effects of bradykinin superfusion to increase LECA and VPL were prevented by coincident topical application of either a bradykinin-B2 receptor antagonist, a cell-permeant superoxide dismutase (SOD) mimetic or antioxidant, or inhibitors of cytochrome P-450 epoxygenase (CYPE) or protein kinase C (PKC) but not by concomitant treatment with either SOD, a mast cell stabilizer, or inhibitors of nitric oxide synthase, cyclooxygenase, xanthine oxidase, NADPH oxidase, or platelet-activating factor. Immunoneutralizing P-selectin or intercellular adhesion molecule-1 (ICAM-1) completely prevented bradykinin-induced leukocyte adhesion and emigration but did not affect VPL. On the other hand, stabilization of F-actin with phalloidin prevented bradykinin-induced leukocyte emigration and VPL but did not alter leukocyte adhesion. These data indicate that bradykinin induces LECA in rat mesenteric venules via a B2-receptor-initiated, CYPE-, oxidant- and PKC-mediated, P-selectin- and ICAM-1-dependent mechanism. Bradykinin also produced VPL, an effect that was initiated by stimulation of B2receptors and involved CYPE and PKC activation, oxidant generation, and cytoskeletal reorganization but was independent of leukocyte adherence and emigration.

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