Mechanical strain induced phospho-proteomic signaling in uterine smooth muscle cells |
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| Institution: | 1. University of Nevada, Reno School of Medicine, Department of Pharmacology, United States;2. University of Nevada, Reno School of Medicine, Mick Hitchcock Proteomics Center, United States;3. University of Nevada, Reno School of Medicine, Department of Biochemistry, United States;1. Department of Engineering, Faculty of Science and Technology, Aarhus University, Finlandsgade 22, 8200 Aarhus N, Denmark;2. Department of Cardiothoracic and Vascular Surgery, Aarhus University Hospital, Palle Juul-Jensens Boulevard 99, 8200 Aarhus N, Denmark;3. Department of Clinical Medicine, Aarhus University Hospital, Palle Juul-Jensens Boulevard 99, 8200 Aarhus N, Denmark;1. Jiangxi Provincial Institute of Hypertension, The First Affiliated Hospital of Nanchang University, Nanchang 330006, China;2. Jiangxi Provincial Key Laboratory of Basic Pharmacology, Nanchang University School of Pharmaceutical Science, Nanchang 330006, China;3. Jiangxi Provincial Key Laboratory of Molecular Medicine, The Second Affiliated Hospital of Nanchang University, Nanchang 330006, China;1. Jiangxi Provincial Institute of Hypertension, The First Affiliated Hospital of Nanchang University, Nanchang 330006, PR China;2. Jiangxi Provincial Key Laboratory of Basic Pharmacology, Nanchang University School of Pharmaceutical Science, Nanchang 330006, PR China;3. Jiangxi Provincial Key Laboratory of Molecular Medicine at the Second Affiliated Hospital, Nanchang University, Nanchang 330006, PR China |
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| Abstract: | Mechanical strain associated with the expanding uterus correlates with increased preterm birth rates. Mechanical signals result in a cascading network of protein phosphorylation events. These signals direct cellular activities and may lead to changes in contractile phenotype and calcium signaling. In this study, the complete phospho-proteome of uterine smooth muscle cells subjected to mechanical strain for 5 min was compared to un-strained controls. Statistically significant, differential phosphorylation events were annotated by Ingenuity Pathway Analysis to elucidate mechanically induced phosphorylation networks. Mechanical strain leads to the direct activation of ERK1/2, HSPB1, and MYL9, in addition to phosphorylation of PAK2, vimentin, DOCK1, PPP1R12A, and PTPN11 at previously unannotated sites. These results suggest a novel network reaction to mechanical strain and reveal proteins that participate in the activation of contractile mechanisms leading to preterm labor. |
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| Keywords: | Proteomics Labor Phosphorylation Preterm Uterus |
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