Abstract
The molecular mechanisms involved in human uterine quiescence during gestation and the induction of labor at term or preterm are not completely known. Preterm delivery is associated with major morbidity and mortality and current efforts to prevent delivery until term are largely ineffective. Identification and semi-quantification of proteomic changes in uterine smooth muscle during pregnancy will allow for targeted research into how quiescence is maintained and what changes are associated with induction of labor. Examining preterm labor in this context will provide potential therapeutic targets for the management of preterm labor. We have recently performed two dimensional liquid chromatography coupled with tandem mass spectrometry on myometrial proteins isolated from pregnant patients in labor, pregnant patients not in labor, and pregnant patients in labor preterm. Using a conservative false discovery rate of 1% we have identified 2132 protein groups using this method and semi-quantitative spectral counting shows 201 proteins that have disparate levels of expression in preterm laboring samples. To our knowledge this is the first large scale proteomic study examining human uterine smooth muscle and this initial work has provided a target list for future experiments that can address how changing protein levels are involved in the induction of labor at term and preterm.
Highlights
Neither human labor nor spontaneous preterm labor is well understood and there is ample evidence that the regulation of contraction-relaxation of the smooth muscle of the uterus is unique [1]
In order to reduce the morbidity and mortality that results from preterm delivery, we need to understand the contraction-relaxation signaling in the smooth muscle of the uterus involved in the induction of labor and how this is disparately activated in preterm labor
We unambiguously identified a total of protein groups with the following breakdown: 1869 proteins identified in term laboring tissue samples, 1963 proteins identified in term nonlaboring tissue samples, and 2102 proteins identified in preterm laboring samples (Figure 2)
Summary
Neither human labor nor spontaneous preterm labor is well understood and there is ample evidence that the regulation of contraction-relaxation of the smooth muscle of the uterus is unique [1]. In order to reduce the morbidity and mortality that results from preterm delivery, we need to understand the contraction-relaxation signaling in the smooth muscle (myometrium) of the uterus involved in the induction of labor and how this is disparately activated in preterm labor The basis of this signaling is the myometrial proteome and its post-translation regulation. We have created a baseline proteome map of human uterine smooth muscle (HUSM) that will allow future research to add more in-depth layers until completing the proteomic profile of HUSM in disparate states of labor in health and disease This will be an immensely useful tool for researchers and clinicians because it will provide ways to prevent preterm delivery, a uniquely human problem with enormous impact on society
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