Abstract

Furin is a proprotein convertase (PC) implicated in the endoproteolytic maturation of inactive protein precursors of growth factors, hormones, receptors, and viral envelope glycoproteins.1 Two functionally active forms of furin, one membrane-bound containing a C-terminal transmembrane domain (TD) and a cytoplasmic tail (CT), and one soluble without the TD and CT, have been characterised. We have previously shown that PC6, one of the PCs closely related to furin, is expressed in the human endometrium and is closely associated with decidualization of stromal cells during implantation.2 Although furin is ubiquitously expressed, its expression in the human endometrium is unknown. In this study, we investigated the spatial and temporal expression pattern of furin in the human endometrium using RT-PCR and immunohistochemistry. While furin expression is detected throughout the menstrual cycle and during early pregnancy, lowest mRNA levels are seen during the proliferative phase. Using an antibody directed against the C-terminus of the membrane bound form, furin is detected in the stroma, glandular and luminal epithelium, as well as in endothelia and neutrophils throughout the menstrual cycle and during early pregnancy. In the stroma, highest levels of furin are present during menstruation (n = 3), they are also high during the proliferative phase (n = 4), but significantly lower levels are detected during the secretory phase (n = 10, P < 0.05, Tukey HSD). In the first trimester decidua, furin is present in well decidualised stromal cells. The overall expression pattern of furin is different to that of PC6; in particular, furin expression is associated only with well decidualized stromal cells whereas PC6 is involved in the initial stages of decidualization. These data suggest that furin and PC6 play different roles in the human endometrium, especially during embryo implantation. (1)Nakayama K. (1997). Biochem. J. 327, 625–635.(2)Nie et al. (2005). Biol. Reprod. 72, 1029–1036.

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