[Hyp3]‐bradykinin and [Hyp3]‐Lys‐bradykinin interact with B2‐bradykinin receptors and stimulate inositol phosphate production in cultured human fibroblasts

FEBS Letters

Dengler, Robert¹  Roscher, Adelbert A.²  Müller-Esterl, Werner¹  Faußner, Alexander² 

[1] Abteilung für Klinische Chemie und Klinische Biochemie in der Chirurgischen Klinik Innenstadt der Universität München, Nußbaumstraße 20, D-8000 München 2, FRG;Kinderklinik im Dr. von Hauner'schen Kinderspital der Universität München, Abteiung für Klinische Biochemie, Lindwurmstraße 4, D-8000 München 2, FRG

关键词: Bradykinin;    Kinin hydroxylation;    B2-receptor;    Cyclic adenosine monophosphate;    Inositol phosphate;    BK;    bradykinin;    IP;    inositol monophosphate;    IP2;    inositol diphosphate;    IP3;    inositol triphosphate;    PI;    phosphatidylinositol;    cAMP;    cyclic 3';    5'-adenosine monophosphate;   

DOI  :  10.1016/0014-5793(90)80166-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The recently isolated, naturally occurring peptide hormones [Hyp³]-bradykinin and [Hyp³]-Lys-bradykinin were investigated for their agonist activity on solubilized binding sites from human fibroblasts. Both ligands competed with [³H]bradykinin binding in a dose-dependent fashion with potencies similar to bradykinin (BK) and Lys-BK. Biological activity was assessed by determination of inositol phosphate accumulation and cyclic 3',5'-adenosine monophosphate synthesis in intact cultured cells. Stimulation by the hydroxylated peptides resulted in a pronounced accumulation of both parameters with similar effectiveness as BK and Lys-BK. These results indicate that [Hyp³]-BK and [Hyp³]-Lys-BK are agonists at the bradykinin receptor system with properties comparable to their non-hydroxylated analogues. This suggests that hydroxylation of kinins does not alter receptor interaction or signal transduction in cultured human fibroblasts.

【 授权许可】

Unknown