Construction of a Physiologically Active Photoaffinity Probe Based on the Structure of Bradykinin: Labelling of Angiotensin Converting Enzyme but Not Candidate Bradykinin Receptors on NG108–15 Cells

Vries, Johannes G. de; Phillips, Elsa; Snell, Christopher R.; Snell, Penelope H.; Webb, M.

doi:10.1111/j.1471-4159.1989.tb09201.x

Cited by 12 publications

(3 citation statements)

References 29 publications

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“…Purification of the BKB2R by classic methods proved elusive (Odya et al, 1980; de Vries et al, 1989; Faussner et al, 1991). However, using the knowledge that the BKB2R is G‐protein coupled resulted in the cloning of the BK receptor from the rat using a Xenopus oocyte assay (McEachern et al, 1991).…”

Section: Cloning and Genetic Characterizationmentioning

confidence: 99%

Mechanisms regulating the expression, self‐maintenance, and signaling‐function of the bradykinin B2 and B1 receptors

Prado

Taylor

Zhou

et al. 2002

Journal Cellular Physiology

157

124

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Bradykinin (BK) is a potent short-lived effector belonging to a class of peptides known as kinins. It participates in inflammatory and vascular regulation and processes including angioedema, tissue permeability, vascular dilation, and smooth muscle contraction. BK exerts its biological effects through the activation of the bradykinin B2 receptor (BKB2R) which is G-protein-coupled and is generally constitutively expressed. Upon binding, the receptor is activated and transduces signal cascades which have become paradigms for the actions of the Gai and Gaq G-protein subunits. Following activation the receptor is then desensitized, endocytosed, and resensitized. The bradykinin B1 (BKB1R) is a closely related receptor. It is activated by desArg 10 -kallidin or desArg 9 -BK, metabolites of kallidin and BK, respectively. This receptor is induced following tissue injury or after treatment with bacterial endotoxins such as lipopolysacharide or cytokines such as interleukin-1 or tumor necrosis factor-a. In this review we will summarize the BKB2R and BKB1R mediated signal transduction pathways. We will then emphasize the relevance of key residues and domains of the intracellular regions of the BKB2R as they relate to modulating its function (signal transduction) and selfmaintenance (desensitization, endocytosis, and resensitization). We will examine the features of the BKB1R gene promoter and its mRNA as these operate in the expression and self-maintenance of this inducible receptor. This communication will not cover areas discussed in earlier reviews pertaining to the actions of peptide analogs. For these we refer you to earlier reviews

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Section: Cloning and Genetic Characterizationmentioning

confidence: 99%

Mechanisms regulating the expression, self‐maintenance, and signaling‐function of the bradykinin B2 and B1 receptors

Prado

Taylor

Zhou

et al. 2002

Journal Cellular Physiology

157

124

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“…Because bradykinin has high affinity for both its receptor and its degradative enzyme, angiotensin converting enzyme, a full characterization of the receptor protein has been difficult (ref. 15; S.B. and K.J., unpublished work).…”

mentioning

confidence: 99%

Expression cloning of a rat B2 bradykinin receptor.

McEachern

Shelton

Bhakta

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

381

224

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A cDNA encoding a functional bradykinin receptor was isolated from a rat uterus library by a clonal selection strategy using Xenopus laevis oocytes to assay for expression of bradykinin responses. The predicted protein is homologous to the seven transmembrane G protein-coupled superfamily of receptors. Bradykinin and its analogs stimulate a Cl current in oocytes expressing the receptor with the rank order of potency: bradykinin Lys-bradykinin > [Tyr8]-bradykinin >> [Phe6Jbradykinin. This is the rank order of potency observed for these compounds in competitive binding assays on soluble receptor from rat uterus. Des-Arg9-bradykinin (10 pAM) elicits no response when applied to oocytes expressing the receptor; thus, the cDNA encodes a B2 type bradykinin receptor. [This8,DPhe7Jbradykinin, where Thi is I3-(2-thienyl)-alanine, is a very weak partial agonist and inhibits the bradykinin-mediated ion flux, suggesting the cDNA encodes a smooth muscle, rather than a neuronal, B2 receptor subtype. Receptor message has a distribution consistent with previous reports of bradykinin function and/or binding in several tissues and is found in rat uterus, vas deferens, kidney, lung, heart, ileum, testis, and brain. Receptor subtypes are a possibility because several tissues contain two or three message species (4.0, 5.7, and 6.5 kilobases). Southern blot highstringency analysis demonstrated that the rat, guinea pig, and human genomes contain a single gene. As bradykinin is a key mediator of pain, knowledge of the primary structure of this receptor will allow a molecular understanding of the receptor and aid the design of antagonists for pain relief.The nonapeptide bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-ProPhe-Arg) is a mediator of pain, inflammation, vascular permeability, smooth muscle tone in vascular and other tissues, and gastrointestinal function (1-5). Bradykinin can serve as a growth factor (2, 6, 7). Bradykinin binds to G proteincoupled receptors that activate phospholipase C or phospholipase A2 and increases synthesis of inositol trisphosphate or arachadonic acid (8-10).Bradykinin receptors have been classified as two major subtypes, B1 and B2 (1). The bradykinin metabolite des-Arg9-bradykinin is a B1 receptor agonist with potency greater than bradykinin, whereas it is inactive at B2 receptors. B2 receptors have been subdivided into two subtypes, a "neuronal" form, which is fully activated by [Thi58,DPhe7]bradykinin, where Thi is 83-(2-thienyl)-alanine, and a "smooth muscle" form, which is weakly activated by [This'8,DPhe7]bradykinin (11,12). Other subtypes of the B2 receptor have also been suggested (13,14).

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“…Compound 12 was first synthesized byDeVries et al (1989). The results are means of two to seven separate determinations.…”

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confidence: 99%

New Photoaffinity Labelled Agonists of Bradykinin

Steinmetzer

Schumann²,

Paegelow³

et al. 1995

Biological Chemistry Hoppe-Seyler

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Several photoaffinity labelled agonists of the peptide hormone bradykinin (BK) were synthesized by solid phase methods. Their biological activities and binding affinities were determined in both the isolated rat uterus (RUT) and guinea pig ileum (GPI). As photoreactive groups p-benzoyl-phenylalanine (Bpa) and the arylazides azidobenzoic acid (ABA) and azidosalicylic acid (ASA) were attached to the N-terminus of the BK agonists. In addition, Bpa was incorporated at different positions of the BK sequence. Three different types of BK agonists were used. Firstly, the photolabels ASA and ABA were attached to BK or to Lys-BK (kallidin). Secondly, tyrosine containing BK analogues, suitable for radioiodination, were labelled. This series is derived from the naturally occurring analogue phyllokinin [BK-Ile-Tyr(SO3H)] and from BK analogues with tyrosine at position 0 and 3. The third series includes several analogues with D-N-methyl-phenylalanine (D-NMe-Phe) at position 7, which selectively discriminate between the RUT and GPI bradykinin B2 receptors. Among the photoaffinity labelled BK agonists, the iodinatable Lys(ASA)-BK (50.8% on RUT, 73.0% on GPI), ASA-BK (26.3% on RUT), Bpa-BK-Ile-Tyr (13.6% on RUT, 14.0% on GPI) and the iodinated [D-Bpa-1, 3-I-Tyr0]-BK (15.5% on RUT, 19.0% on GPI) retained a relatively high biological activity compared with BK (100%). Thus, although BK agonists are known to allow only very restricted modifications without a strong reduction in biological activity, these compounds should be useful candidates for receptor labelling.

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Construction of a Physiologically Active Photoaffinity Probe Based on the Structure of Bradykinin: Labelling of Angiotensin Converting Enzyme but Not Candidate Bradykinin Receptors on NG108–15 Cells

Cited by 12 publications

References 29 publications

Mechanisms regulating the expression, self‐maintenance, and signaling‐function of the bradykinin B2 and B1 receptors

Mechanisms regulating the expression, self‐maintenance, and signaling‐function of the bradykinin B2 and B1 receptors

Expression cloning of a rat B2 bradykinin receptor.

New Photoaffinity Labelled Agonists of Bradykinin

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