283-POS

Abstract

Objectives Heat shock proteins (HSPs) are induced in cells as a protective mechanism to cope with cellular stress. The activation of the heat shock response is mediated by heat shock transcription factor 1 (HSF1). HSFs (HSF1-4) bind to the promoter regions of target genes. HSF 1 exists in a complex with HSP40, HSP70 and HSP90 as inactive monomers; after stress HSF 1 is and trimerizes. We reported a spatial expression of HSPs in the placenta and that this is altered in pre-eclampsia (Abdulsid et al., 2013). Aims: To investigate whether expression of HSF-1 alters and may explain the changes in HSP expression. Methods Placental samples were obtained from 8 sites within each placenta: 4 equally spaced apart pieces were sampled from the inner, middle and outer zones of the placenta (Abdulsid et al., 2013). Non-labor, labor, labor pre-eclampsia and non-labor pre-eclampsia were studied. HSF 1 expression was investigated by Western blot analysis and real time PCR. Results Two HSF1 bands were observed which, according to the data sheet represent the phosphorylated 80 kDa and non-phosphorylated 65 kDa forms. HSF1; 65 kDa was significantly increased in both the pre-eclampsia non-labor and labor groups compared to the normal non-labor and labor groups at the inner zone (p = 0.04, p = 0.008 respectively). There was a significant decrease in 65 kDa HSF1 in labor pre-eclampsia compared to the control labor group at the middle zone (p = 0.004). There was no difference in the phosphorylated form of HSF1. No changes at the mRNA level were found when non-labor and labor pre-eclampsia were compared to control groups. When labor and non-labor groups were combined, there was a significant increase in pre-eclampsia compared to the normotensive groups at the inner and middle zones (p = 0.007, p = 0.02 respectively). Conclusions Changes in HSF1 expression occur during labor and pre-eclampsia but at different zones within the placenta. Disclosures A. Abdulsid: None. K. Hanretty: None. F. Lyall: None.