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Structure of the Bradykinin B2 Receptors' Amino Terminus†

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Institute of Physiological Chemistry and Pathobiochemsitry, the University at Mainz, Duesbergweg 6, 55099 Mainz, Germany, Institute of Molecular Biotechnology e. V., Beutenbergstrasse 11, 07745 Jena, Germany, Children's Hospital, Department of Clinical Chemistry and Biochemistry, University of Munich, Lindwurmstrasse 4, 80337, Germany, and Institute of Pharmacology and Toxicology, the University at Würzburg, Versbacherstrasse 9, 97078 Würzburg, Germany
Cite this: Biochemistry 1996, 35, 23, 7514–7519
Publication Date (Web):June 11, 1996
https://doi.org/10.1021/bi9601060
Copyright © 1996 American Chemical Society
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    Abstract

    The peptide hormone bradykinin exerts important biological functions by binding to and activating bradykinin B2 receptors. B2 receptors belong to the seven transmembrane domain (7TM) receptor family. Cloning of the cDNA sequences for the rat, human, and mouse bradykinin B2 receptor revealed several in-frame AUG triplets as potential initiation sites for translation. Due to “Kozak-like” consensus nucleotides, the AUG codon closest to transmembrane domain 1 was assumed the preferred initiation site for translation, but the real amino terminus of the B2 receptor protein was unknown. The amino terminus of several 7TM receptors has been shown to be essentially involved in receptor activation and/or ligand binding. Therefore we determined the amino terminus of the human and of the rat B2 receptor using domain-specific antipeptide antibodies, amino acid sequence analysis, and in vitro transcription/translation. We report that the human and rat B2 receptor protein start with the methionine which is translated from the first in-frame AUG. This start site extends the known amino terminus of the human and rat B2 receptors by 27 or 30 amino acid residues, respectively. Antibodies raised against a peptide of the initial 27 amino acids of the human B2 receptor stained B2 receptors on intact cells. This finding excludes the existence of a signal sequence for this receptor.

    †

     This work was supported in part by the Deutsche Forschungsgemeinschaft Grant Mu 598/3-2.

    ‡

     University at Mainz.

    §

     Institute of Molecular Biotechnology.

    ‖

     University of Munich.

    *

     Address correspondence to this author at Institute of Pharmacology and Toxicology, the University at Würzburg, Versbacherstrasse 9, 97078 Würzburg, Germany. Phone:  0049-931-201-3982. Fax:  0049-931-201-3539.

    #

     University of Würzburg.

    ✗

     Abstract published in Advance ACS Abstracts, May 15, 1996.

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    11. R. Couture, C.J. Lindsey. Chapter VII Brain kallikrein–kinin system: from receptors to neuronal pathways and physiological functions. 2000, 241-300. https://doi.org/10.1016/S0924-8196(00)80009-3
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    17. J.B. Pesquero, M. Bader. Molecular biology of the kallikrein-kinin system: from structure to function. Brazilian Journal of Medical and Biological Research 1998, 31 (9) , 1197-1203. https://doi.org/10.1590/S0100-879X1998000900013
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