Development of a high-throughput assay for human proprotein convertase 5/6 for detecting uterine receptivity

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Abstract

Check for full text(opens in a new window) Library catalogue(opens in a new window) View at Publisher Export Download More... Analytical Biochemistry Volume 475, 15 April 2015, Pages 14-21 Development of a high-throughput assay for human proprotein convertase 5/6 for detecting uterine receptivity (Article) Heng, S.ab, Dynon, K.af, Li, Y.ab, Edgell, T.ab, Walton, K.ab, Rombauts, L.J.cde, Vollenhoven, B.cde, Nie, G.ab a Implantation and Placental Development Laboratory, Centre for Reproductive Health, MIMR-PHI Institute of Medical Research, Clayton, VIC, Australia b Monash University, Clayton, VIC, Australia c Department of Obstetrics and Gynaecology, Monash University, Clayton, VIC, Australia View additional affiliations View references (27) Abstract Embryo implantation requires a healthy embryo and a receptive uterus. In women, the inner lining of the uterus, the endometrium, remains in a hostile state and becomes receptive for embryo implantation for only a short period during each menstrual cycle. Determining endometrial receptivity is vital in in vitro fertilization (IVF) treatment because the timing of embryo transfer needs to be synchronized with endometrial receptivity. We have previously demonstrated that proprotein convertase 5/6A (PC6) is highly expressed in the receptive endometrium and that PC6 is critical for receptivity establishment in women. Furthermore, endometrial PC6 is secreted into the uterine fluid, and levels correlate with receptivity status. Detection of PC6 in uterine fluids, therefore, would provide a nonsurgical assessment of endometrial receptivity. However, to date no assays are available for human PC6. In this study, we produced three PC6 monoclonal antibodies (mAbs) and developed a sandwich enzyme-linked immunosorbent assay (ELISA) for PC6 detection in human uterine fluids. The PC6 mAbs were confirmed to be highly specific to PC6, and the ELISA detected PC6 in human ute
Original languageEnglish
Pages (from-to)14 - 21
Number of pages8
JournalAnalytical Biochemistry
Volume475
DOIs
Publication statusPublished - 15 Apr 2015

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