Phosphorylation of proteins during human myometrial contractions: A phosphoproteomic approach

Phasic myometrial contractility is a key component of human parturition and the contractions are driven by reversible phosphorylation of myosin light chains catalyzed by the calcium (Ca2+)-dependent enzyme myosin light chain kinase (MYLK). Other yet unknown phosphorylation or de-phosphorylation even...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2017-01, Vol.482 (4), p.1393-1399
Main Authors: Hudson, Claire A., López Bernal, Andrés
Format: Article
Language:English
Subjects:
Calcium - metabolism
Calcium Signaling
Calmodulin - chemistry
Contractility
Female
Humans
Myometrium
Myometrium - metabolism
Myosin light chain kinase
Myosin-Light-Chain Kinase - metabolism
Oxytocin - physiology
Parturition
Phosphopeptides - chemistry
Phosphoproteomics
Phosphorylation
Proteome
Proteomics
Signal Transduction
Uterine Contraction
Uterus
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Summary:Phasic myometrial contractility is a key component of human parturition and the contractions are driven by reversible phosphorylation of myosin light chains catalyzed by the calcium (Ca2+)-dependent enzyme myosin light chain kinase (MYLK). Other yet unknown phosphorylation or de-phosphorylation events may contribute to myometrial contraction and relaxation. In this study we have performed a global phosphoproteomic analysis of human myometrial tissue using tandem mass tagging to detect changes in the phosphorylation status of individual myometrial proteins during spontaneous and oxytocin-driven phasic contractions. We were able to detect 22 individual phosphopeptides whose relative ratio changed (fold > 2 or 
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2016.12.047