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Title: Bradykinin-activated contractile signalling pathways in human myometrial cells are differentially regulated by arrestin proteins.
Authors: Willets, Jonathon Mark
Brighton, Paul J.
Windell, LN
Rana, S
Nash, Craig A.
Konje, Justin Chi
First Published: 15-May-2015
Publisher: Elsevier
Citation: Molecular and Cellular Endocrinology, 2015, 407, pp. 57-66
Abstract: Bradykinin is associated with infections and inflammation, which given the strong correlation between uterine infection and preterm labour may imply that it could play a role in this process. Therefore, we investigated bradykinin signalling, and the roles that arrestin proteins play in their regulation in human myometrial cells. Bradykinin induced rapid, transient intracellular Ca[superscript: 2+] increases that were inhibited following B[subscript: 2] receptor (B[subscript: 2]R) antagonism. Arrestin2 or arrestin3 depletion enhanced and prolonged bradykinin-stimulated Ca[superscript: 2+] responses, and attenuated B[subscript: 2]R desensitisation. Knockdown of either arrestin enhanced B[subscript: 2]R-stimulated ERK1/2 signals. Moreover, depletion of either arrestin elevated peak-phase p38-MAPK signalling, yet only arrestin3 depletion prolonged B[subscript: 2]R-induced p38-MAPK signals. Arrestin2-knockdown augmented bradykinin-induced cell movement. Bradykinin stimulates pro-contractile signalling mechanisms in human myometrial cells and arrestin proteins play key roles in their regulation. Our data suggest bradykinin not only acts as an utertonin, but may also have the potential to enhance the contractile environment of the uterus.
DOI Link: 10.1016/j.mce.2015.03.004
eISSN: 1872-8057
Version: Post-review (final submitted)
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2015 Elsevier Ireland Ltd. All rights reserved.
Appears in Collections:Published Articles, Dept. of Cancer Studies and Molecular Medicine

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