Expression of heat shock factor 1, heat shock protein 90 and associated signaling proteins in pregnant rat myometrium: Implications for myometrial proliferation

During pregnancy and labour the myometrium undergoes structural and physiological adaptations as part of a program of development. Heat shock factor 1 (HSF1) is a master regulator of both stress and developmental processes. A noted HSF1-induced gene is the 90 kDa heat shock protein (HSP90), which acts as a chaperone and regulator of cellular processes. Immunoblot analysis demonstrated HSF1 expression levels in pregnant rat myometrium on gestational day (d) 6 were maintained at a significantly higher level compared with d12 to post-partum (PP) time points (P < 0.05), while expression on d12 was significantly higher compared to d15 and d19. The transcriptionally active form pSer230-HSF1 was detected at a significantly greater level at d6 compared with d21 and d23 time points and also at d12 compared with d21, d22 and 23 (labour). Similarly, phosphorylated (P)-HSP90AA1 protein detection was significantly greater on d6 compared to d19 to d23 time points and on d12 compared with d15 to PP time points. In contrast, P-HSP90AB1 showed significantly greater detection levels on d12 compared with d15 while levels on d22 were significantly higher compared to d15, d17 and d19. Immunofluorescence analysis demonstrated that total HSF1 and HSP90 were localized mainly in the cytoplasm of myometrial cells with some detection of HSF1 in nuclei. This work advances our scientific knowledge of the myometrium during pregnancy and the expression profiles of HSF1 and HSP90 within the proliferative phase of myometrial programming suggests a role for them in this period of hyperplasia and myometrial adaptation.