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Hehir, MP,Morrison, JJ
Journal Of Obstetrics And Gynaecology Research
Paeoniflorin, a novel heat-shock protein inducing compound, and human myometrial contractility in vitro
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heat shock protein labor myometrium paeoniflorin smooth muscle MOLECULAR CHAPERONES SMOOTH-MUSCLE HUMAN UTERINE PREGNANCY KANZO
AimHeat shock proteins (HSPs) are synthesized in virtually all organisms in response to increases in temperature. They are associated with a relaxant effect on the human myometrium and are present in decreased concentration in the myometrium at the time of labor. Paeoniflorin is derived from Paeonia lactiflora and has been shown to induce the synthesis of HSPs in cultured mammalian cells. The purpose of the study was to evaluate the effect of paeoniflorin on human uterine contractility.Material and MethodsSamples of human myometrium were taken at lower segment cesarean section. Dissected muscle strips were suspended under isometric conditions and exposed to cumulative additions of paeoniflorin in concentrations ranging from 1 nmol/L to 10 mol/L. Control experiments were simultaneously performed.ResultsPaeoniflorin was found to exert an inhibitory effect on spontaneous and agonist-induced contractions compared to control strips. The mean maximal inhibition values were: 42.21% 9.26 for spontaneous contractions (n = 6; P < 0.0001) and 47.84% +/- 9.05 for oxytocin-induced contractions (n = 6; P < 0.0001).ConclusionThe HSP inducing compound, paeoniflorin, had a relaxant effect on human uterine contractility in vitro. These results reinforce the fact that HSPs may play a physiological role in the onset of labor and may also provide future targets for novel tocolytic treatments.
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