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Tyrosine phosphorylation levels in primary human myometrial cells


Gao, Lu (2019), Tyrosine phosphorylation levels in primary human myometrial cells, Dryad, Dataset,


Context. Preterm birth is one of the most common complications during human pregnancy and labor, and associated with a dramatic switch within the uterus from quiescence to contractility. However, the mechanisms underlying uterine remodeling are largely unknown.

Objective. To define the roles of src-homology phosphatase type-1 (SHP-1, PTPN6) in regulating the phosphorylation of proteins involved in the uterine smooth muscle cell functions.

Design and Setting. Human myometrial tissues, primary uterine smooth muscle cells, and myometrium-specific Ptpn6-KO mice were used to study SHP-1 regulation of uterine remodeling and labor.

Patients. Patients who underwent elective cesarean section (n=20) and emergency cesarean section at term (37-42 wks, n=20) were recruited with no evidence of underlying diseases.

Results. We found that SHP-1 was significantly decreased in human myometrium in labor compared with that not in labor. Timed-pregnant mice injected intraperitoneally with the specific SHP-1 inhibitor, PTPI-1, or those with a myometrium-specific Ptpn6-KO manifested significantly preterm labor, with enriched plasmalemmal dense plaques between myometrial cells and increased phosphorylation at Tyr397 and Tyr576/577 sites of focal adhesion kinase (FAK), which remained to the time of labor. Knockdown of SHP-1 dramatically increased the spontaneous contraction of HUSMCs, which was reversed by co-infection of a FAK-knockdown lentivirus. PGF2a could downregulate SHP-1 via PI3K-NF-kB pathway.

Conclusions. SHP-1 plays important roles in uterine remodeling and plasticity by activating focal adhesion pathway. The aberrant decrease of SHP-1 may be one of the reasons for spontaneous preterm labor, and interventions for modulation of SHP-1 provide a potential strategy for preventing preterm birth.