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[Hyp 3 ]‐bradykinin and [Hyp 3 ]‐Lys‐bradykinin interact with B2‐bradykinin receptors and stimulate inositol phosphate production in cultured human fibroblasts
Author(s) -
Dengler Robert,
Faußner Alexander,
Müller-Esterl Werner,
Roscher Adelbert A.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80166-g
Subject(s) - bradykinin , bradykinin receptor , inositol phosphate , receptor , chemistry , agonist , inositol , biochemistry , kallidin , kinin
The recently isolated, naturally occurring peptide hormones [Hyp 3 ]‐bradykinin and [Hyp 3 ]‐Lys‐bradykinin were investigated for their agonist activity on solubilized binding sites from human fibroblasts. Both ligands competed with [ 3 H]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 [Hyp 3 ]‐BK and [Hyp 3 ]‐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.