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Negative and positive regulatory epitopes in the C-terminal domains of the human B1 and B2 bradykinin receptor subtypes determine receptor coupling efficacy to G9/11-mediated phospholipase Cβ activity

The human B1 bradykinin (BK) receptor (B1R) is more efficacious than the human B2 BK receptor (B2R) in both ligand-independent and agonist-dependent coupling to Gq/11-mediated phospholipase Cβ activity. In fact, B1R is constitutively active, whereas B2R exhibits little if any constitutive activity. To evaluate the role of the C-terminal domain in receptor Gq/11 coupling, we constructed chimeric an

Spontaneous human B2 bradykinin receptor activity determines the action of partial agonists as agonists or inverse agonists. Effect of basal desensitization

In this report, we show that desensitization regulates ligand- independent, spontaneous activity of the human B2 bradykinin (BK) receptor, and the level of spontaneous receptor activity determines the action of the BK antagonists and partial receptor agonists NPC17731 and HOE140 as agonists or inverse agonists. Spontaneous receptor activity was monitored by measuring basal cellular phosphoinositid

Autoregulation of bradykinin receptors : Agonists in the presence of interleukin-1β shift the repertoire of receptor subtypes from B2 to B1 in human lung fibroblasts

Elevated formation of bradykinin (BK) and Lys-BK or kallidin (KD) and their carboxypeptidase metabolites desArg9BK and desArg10KD is evident at sites of inflammation. Moreover, B2 receptors (B2R) which mediate the action of BK and KD, participates in the acute stage of the inflammatory and pain response, whereas B1 receptors (B1R), through which desArg9BK and desArg10KD act, partake in the chronic

A single position in the third transmembrane domains of the human B1 and B2 bradykinin receptors is adjacent to and discriminates between the C- terminal residues of subtype-selective ligands

In order to identify agonist- and antagonist-binding epitopes in the human B1 and B2 bradykinin (BK) receptors, we exploited the ability of these receptors to discriminate between peptide ligands that differ only by the absence (B1) grid presence (B2) of a C-terminal Arg. This was done by constructing chimeric proteins in which specific domains were exchanged between these receptors as recently de

The third transmembrane domains of the human B1 and B2 bradykinin receptor subtypes are involved in discriminating between subtype-selective ligands

The B1 and B2 bradykinin (BK) receptor subtypes belong to the GPCR faro ily, and they discriminate between peptides that differ only by the absence and presence of a C-terminal Arg, To identify receptor residues conferring tigand spe.cificity, chimeric constructs in which TM-III were exchanged between the receptors were expressed and assayed by radioligand binding and fluorescence Ca2+ imaging in

Bradykinin sequesters B2 bradykinin receptors and the receptor-coupled Ga SUBUNITS Gaq and Gai in caveolae

Caveolae are small flask-like invaginations on the plasma membrane that contain both G-proteins aim G-protein coupled receptors. Consequently, these structures have been implicated to serve a role in transmembrane signaling. Bradykinin (BK) is a potent vasoactive peptide that acts through B2 BK receptors to stimulate both Gaq and Gai. DDT1 MF2 smooth muscle cells were used to show that eaveolae co

The sixth transmembrane domains of the human B1 and B2 bradykinin receptors are structurally compatible and involved in discriminating between subtype-selective agonists

In order to investigate the molecular basis for the ability of the human B1 and B2 bradykinin (BK) receptor subtypes to discriminate between subtype- selective ligands, we constructed chimeric proteins in which the sixth transmembrane domains (TM-VI) of these receptors were exchanged. The pharmacological profiles of the constructs were analyzed by radioligand binding in particulate preparations of

Bradykinin sequesters B2 bradykinin receptors and the receptor-coupled gα subunits Gα(q) and Gα(i) in caveolae in DDT1 MF-2 smooth muscle cells

In this report, we show that the vasoactive peptide agonist bradykinin (BK) when bound to B2 BK receptors on DDT1 MF-2 smooth muscle cells promotes the recruitment and sequestration of the occupied receptors and the receptor- coupled G-protein α subunits Gα(q) and Gα(i) in caveolae. Association of ligand receptor complexes and Gα subunits with caveolae was indicated by their co-enrichment on densi

Artificiell intelligens som livsform : Om autonoma vapensystems rättsliga ställning

Artificiell intelligens bryter med invanda sätt att tänka kring å ena sidan objekt, ting, teknologiska artefakter och, å andra sidan, handlande subjekt. Somliga tänker rent av på artificiell intelligens som en ny form av liv. En sfär där artificiell intelligens står inför ett genombrott är i krig. Av förklarliga skäl finns starka åsikter om detta. Utvecklingen förkastas som innebärandes slutet på

Regulation of bradykinin B2 receptors by the ras oncogene : Evidence for multiple mechanisms

The objective of this study was to probe the molecular mechanisms underlying the increase in sensitivity of cells to bradykinin (BK) following expression of a transforming Ha-ras oncogene. We used native NIH3T3 fibroblast (3T3) cells and 3T3 cells transfected with a glucocorticoid-sensitive oncogenic Ha-ras construct (DT cells). DT cells incubated in the presence of 1 μM dexamethasone (DEX) for 24

B1 and B2 kinin receptors mediate distinct patterns of intracellular Ca2+ signaling in single cultured vascular smooth muscle cells

Stimulation of B1 and B2 kinin receptors on cultured rabbit superior mesenteric artery smooth muscle cells with des-Arg9-bradykinin (DBK) and bradykinin (BK), respectively, results in significantly different patterns of intracellular Ca2+ mobilization. Single-cell fluorescence imaging of Fura- 2-loaded cells revealed that although both DBK and BK initially triggered similar rapid increases in cyto

The N terminus of bradykinin when bound to the human bradykinin B2 receptor is adjacent to extracellular Cys20 and Cys277 in the receptor

Chemical cross-linking combined with site-directed mutagenesis was used to evaluate the role of extracellular cysteines and their positions relative to the binding site for the agonist bradykinin (BK) in the human BK B2 receptor. All extracellular cysteines, Cys20, Cys103, Cys184, and Cys277, in the receptor were mutated to serines, and single and double mutants were transfected into COS-7 cells.