Kinin receptors: functional aspects

Marceau, François; Sabourin, Thierry; Houle, Steeve; Fortin, Jean‐Philippe; Petitclerc, Éric; Molinaro, Giuseppe A.; Adam, Albert

doi:10.1016/s1567-5769(02)00189-3

Cited by 61 publications

(56 citation statements)

References 37 publications

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“…Thus, bradykinin clearance, mainly by angiotensin I-converting enzyme (ACE) present in the serum-containing culture medium of HEK 293 cells expressing B 2 R-GFP, was sufficient for the recycling of the receptor construction at the cell surface in ϳ60 min (Bachvarov et al, 2001). Pharmacological ACE inhibition with captopril or the use of a carboxypeptidase-and ACE-resistant bradykinin analog, [Phe 8 ⌿(CH 2 NH)Arg 9 ]bradykinin (Drapeau et al, 1988), led to a prolonged period (3 h) of B 2 R-GFP endocytosis in HEK 293 cells, but without degradation (down-regulation) (Bachvarov et al, 2001;Marceau et al, 2002;. Multiple cycles of receptor endocytosis and recycling may be suspected in these experiments.…”

mentioning

confidence: 99%

B-9972 (D-Arg-[Hyp³,Igl⁵,Oic⁷,Igl⁸]-bradykinin) Is an Inactivation-Resistant Agonist of the Bradykinin B₂Receptor Derived from the Peptide Antagonist B-9430 (D-Arg-[Hyp³,Igl⁵,D-Igl⁷,Oic⁸]-bradykinin): Pharmacologic Profile and Effective Induction of Receptor Degradation

Bawolak

Gera²,

Morissette³

et al. 2007

J Pharmacol Exp Ther

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confidence: 99%

B-9972 (D-Arg-[Hyp³,Igl⁵,Oic⁷,Igl⁸]-bradykinin) Is an Inactivation-Resistant Agonist of the Bradykinin B₂Receptor Derived from the Peptide Antagonist B-9430 (D-Arg-[Hyp³,Igl⁵,D-Igl⁷,Oic⁸]-bradykinin): Pharmacologic Profile and Effective Induction of Receptor Degradation

Bawolak

Gera²,

Morissette³

et al. 2007

J Pharmacol Exp Ther

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“…Such information could help to decide whether to fight against fever or to accept the temperature rise as therapeutically useful. As kinin receptors are the mediators of the effects of the proinflammatory kinin peptide hormones under inflammatory pathological conditions (e.g., sepsis) (Marceau et al, 2002;Leeb-Lundberg et al, 2005), these receptors appeared to be ideal to perform investigations on the temperature sensitivity of membrane receptors.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, unlike B 2 R, B 1 R does not become desensitized and responds in some cell types to activation with an increase in surface receptor number rather than internalization, e.g., in IMR 90 cells (Phagoo et al, 2000;Leeb-Lundberg et al, 2005). As both kinin receptors participate in inflammatory processes by mediating the release of proinflammatory cytokines and recruitment of immune cells (McLean et al, 2000;Leeb-Lundberg et al, 2005;Ehrenfeld et al, 2006), the properties of the B 1 R indicate sustained signaling and thus a role in the prolonged phase of the immune response with amplification of inflammatory processes (Blaukat et al, 1996;Austin et al, 1997;Marceau et al, 1998;Faussner et al, 1999;Phagoo et al, 2000;Marceau et al, 2002;Leeb-Lundberg et al, 2005). Inflammation is characterized by five cardinal symptoms: pain, redness, swelling, loss of function, and heat (Elliott et al, 1960).…”

Section: Introductionmentioning

confidence: 99%

Fever-like temperature modification differentially affects in vitro signaling of bradykinin B₁ and B₂ receptors

Leschner

Ring²,

Feierler

et al. 2011

BCHM

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The bradykinin (BK) B 2 and B 1 receptors (B 2 R, B 1 R) belong to the rhodopsin-like G protein-coupled receptors (GPCRs) and are involved in (patho)physiological processes such as blood pressure regulation or inflammation. They mediate the effects of the pro-inflammatory peptides bradykinin/kallidin and desArg 9 -BK/desArg 10 -kallidin, respectively. Whereas the B 2 R is constitutively expressed and gets internalized upon activation, the B 1 R is especially induced by inflammatory mediators and responds to stimulation with increased surface receptor numbers. Stimulation of both receptors activates phospholipase Cb (PLCb) and mitogen activated protein kinase (MAPK) signaling. Because inflammatory processes are characterized by heat (fever), we analyzed the effect of increased temperature (418C vs. 378C) on B 1 R and B 2 R signaling in HEK 293 and IMR 90 cells. Our results show that signaling of both receptors is temperature-sensitive, however to a different extent and with regard to the investigated pathways. Comparing PLCb activity and Ca 2q -regulated signals, a temperature-dependent increase was only observed for B 1 R but not for B 2 R activation, whereas MAPK activities were doubled at 418C for both receptors. Taken together, our findings suggest that the observed temperature sensitivity of B 1 R-induced PLCb activation is B 1 R-specific. In contrast, the enhanced stimulation of MAPK activity under hyperthermic conditions appears to be a common phenomenon for GPCRs.

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“…19 Serum-free medium from rat hepatomas was also immunoblotted using anti-rat ␣-fetoprotein polyclonal antibodies (gift from Prof. L. Bélanger, CHUQ) to confirm the identity and phenotype of the cells. Poly(ADP-ribose)-polymerase I (PARP) is a caspase substrate cleaved in apoptotic cells; immunoblot detection of PARP and cleaved PARP was carried out in extracts of rat vascular rings preincubated for 17 hr with CM, further pulverized in liquid N 2 and extracted with the lysis buffer.…”

Section: Immunoblots For Inos ␣-Fetoprotein Poly(adp-ribose)polymermentioning

confidence: 99%

“…Poly(ADP-ribose)-polymerase I (PARP) is a caspase substrate cleaved in apoptotic cells; immunoblot detection of PARP and cleaved PARP was carried out in extracts of rat vascular rings preincubated for 17 hr with CM, further pulverized in liquid N 2 and extracted with the lysis buffer. 19 The detection was based on a polyclonal anti-PARP antibody from Cell Signaling Technologies, Inc. (Beverly, MA).…”

Section: Immunoblots For Inos ␣-Fetoprotein Poly(adp-ribose)polymermentioning

confidence: 99%

Loss of function of vascular smooth muscle cells by nitric oxide‐dependent and ‐independent interactions with tumorigenic cells

Morissette

Petitclerc

Marceau

2004

Intl Journal of Cancer

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Key words: vascular smooth muscle; nitric oxide synthase; Morris hepatoma; M-21 melanoma; tumor vessel maturationThe host tissue reaction to tumor invasion involves many nonmalignant cell types and stromal reactions (angiogenesis and grossly increased vascular permeability in the tumor; accelerated matrix synthesis and degradation; leukocyte infiltrate; secretion by nonmalignant cells of factors that affect the growth of malignant cells, etc.). 1,2 Solid tumors induce the formation of a blood supply from the neighboring vasculature that exhibits certain features relative to the two main vascular cell types. Angiogenesis driven by endothelial cell protease release, migration and mitosis is observed; the permeability of the microcirculation to macromolecules remains high, with such consequences as elevated tumor interstitial fluid pressure and flow and peritumoral edema. 3 In some tumors, the feeder vessels contain little vascular smooth muscle cells (VSMCs) and apparently no innervation. 4 Possibly correlated to these structural findings, hemodynamic studies show that the blood supply of primary tumors or metastases is remarkably resistant to the infusion of various pharmacological vasoconstrictor agents relatively to surrounding normal tissues, 5-9 suggesting that the tumor resistance vessels were in a state of maximal vasodilation or anergy. Other tumor blood vessels, however, exhibit differentiation, with recruitment of ␣-actin positive periendothelial cells (e.g., VSMCs ϩ pericytes) around tumor vessels. 10,11 Further, pericyte/VSMC presence indicates a maturation process in tumor neovessels, with a decreased dependence on vascular endothelial cell growth factor (VEGF), a greater histological stability relative to microvessels formed of endothelial cells alone and a greater resistance to anti-angiogenic therapy. 12,13 Whereas considerable efforts have been devoted to the analysis of the endothelial cell-tumor interactions, less is known about the behavior of VSMCs in tumor biology. To detect and model such an interaction, we have attempted reconstitution experiments where tumorigenic cell lines of rat or human origin were cultured in the presence of rat aortic rings as a source of differentiated and functional arterial VSMCs, to evaluate the consequences of coculture on the vascular tone by performing contractility assays. MATERIAL AND METHODS Cell linesThe rat Morris 7777 hepatocarcinoma cell line, subclone 7.6 14 was a gift from Professor L. Bélanger, CHUQ, Québec. This cell line is tumorigenic in syngeneic Buffalo rats. The human melanoma M-21 cell line was a gift of Dr. David Cheresh (Scripps Research Institute, San Diego, CA). It is tumorigenic in immunodeficient mice. 10,15 RBL (rat basophilic leukemia) cells were a gift from Dr. Julia Ember (Scripps Clinic Research Institute). Other cells lines were originally obtained from the ATTC and subcultured in our laboratories: the rat hepatoma H4-II-E-C3, the human hepatomas HEP-3B and HEP G2, and the human breast cancer line MDA-MB-231. All cell lines were pr...

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Kinin receptors: functional aspects

Cited by 61 publications

References 37 publications

B-9972 (D-Arg-[Hyp³,Igl⁵,Oic⁷,Igl⁸]-bradykinin) Is an Inactivation-Resistant Agonist of the Bradykinin B₂Receptor Derived from the Peptide Antagonist B-9430 (D-Arg-[Hyp³,Igl⁵,D-Igl⁷,Oic⁸]-bradykinin): Pharmacologic Profile and Effective Induction of Receptor Degradation

B-9972 (D-Arg-[Hyp³,Igl⁵,Oic⁷,Igl⁸]-bradykinin) Is an Inactivation-Resistant Agonist of the Bradykinin B₂Receptor Derived from the Peptide Antagonist B-9430 (D-Arg-[Hyp³,Igl⁵,D-Igl⁷,Oic⁸]-bradykinin): Pharmacologic Profile and Effective Induction of Receptor Degradation

Fever-like temperature modification differentially affects in vitro signaling of bradykinin B₁ and B₂ receptors

Loss of function of vascular smooth muscle cells by nitric oxide‐dependent and ‐independent interactions with tumorigenic cells

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Kinin receptors: functional aspects

Cited by 61 publications

References 37 publications

B-9972 (D-Arg-[Hyp3,Igl5,Oic7,Igl8]-bradykinin) Is an Inactivation-Resistant Agonist of the Bradykinin B2Receptor Derived from the Peptide Antagonist B-9430 (D-Arg-[Hyp3,Igl5,D-Igl7,Oic8]-bradykinin): Pharmacologic Profile and Effective Induction of Receptor Degradation

B-9972 (D-Arg-[Hyp3,Igl5,Oic7,Igl8]-bradykinin) Is an Inactivation-Resistant Agonist of the Bradykinin B2Receptor Derived from the Peptide Antagonist B-9430 (D-Arg-[Hyp3,Igl5,D-Igl7,Oic8]-bradykinin): Pharmacologic Profile and Effective Induction of Receptor Degradation

Fever-like temperature modification differentially affects in vitro signaling of bradykinin B1 and B2 receptors

Loss of function of vascular smooth muscle cells by nitric oxide‐dependent and ‐independent interactions with tumorigenic cells

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B-9972 (D-Arg-[Hyp³,Igl⁵,Oic⁷,Igl⁸]-bradykinin) Is an Inactivation-Resistant Agonist of the Bradykinin B₂Receptor Derived from the Peptide Antagonist B-9430 (D-Arg-[Hyp³,Igl⁵,D-Igl⁷,Oic⁸]-bradykinin): Pharmacologic Profile and Effective Induction of Receptor Degradation

B-9972 (D-Arg-[Hyp³,Igl⁵,Oic⁷,Igl⁸]-bradykinin) Is an Inactivation-Resistant Agonist of the Bradykinin B₂Receptor Derived from the Peptide Antagonist B-9430 (D-Arg-[Hyp³,Igl⁵,D-Igl⁷,Oic⁸]-bradykinin): Pharmacologic Profile and Effective Induction of Receptor Degradation

Fever-like temperature modification differentially affects in vitro signaling of bradykinin B₁ and B₂ receptors