|Zhuang, Dongyue - WASHINGTON STATE UNIVER|
|Cheevers, William - WASHINGTON STATE UNIVER|
|Sy, Man-Sun - CASE WESTERN RESERVE UNIV|
Submitted to: Journal of Biological Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: March 27, 2001
Publication Date: N/A
Interpretive Summary: This study determined the presence of PrP-C in female reproductive, fetal and placental tissues and fetal fluids. Results showed that PrP-C is present in the ovary, oviduct, endometrium, myometrium, chorioallantois, and allantoic fluid. PrP-C from these locations was truncated, glycosylated and proteinase K sensitive. The results indicate that PrP-C in these locations may play a role in scrapie transmission as well as in reproductive biology in sheep.
Technical Abstract: Scrapie is a naturally occurring prion disease causing fatal neurodegenerative disorders in sheep and goats. PrP-Sc, the presumed causative agent for scrapie, accumulates in brain, lymphoid and placental tissues in sheep. PrP-Sc is derived from the normal isoform of PrP, PrP-C, which as the substrate for conversion to PrP-Sc is necessary for scrapie infection. Natural transmission of scrapie may be primarily through the reproductive tract and fetal-placental tissues/fluids. The objective of this study was to characterize the distribution and biochemical properties of PrP-C in female reproductive, fetal and placental tissues and fetal fluids of normal sheep. The results showed that PrP-C was present in endometrium, myometrium, oviduct and ovary of both pregnant and non-pregnant ewes and cotyledonary chorioallantois, allantoic fluid and fetal bladder. PrP-C was not detectable in the intercotyledonary chorioallantois, amnion, urachus, amniotic fluid, or fetal urine. PrP-C in allantoic fluid and the tissues was glycosylated, N-terminally truncated and proteinase K sensitive. These results are important to a further understanding of scrapie transmission through the reproductive processes and the physiological role of PrP-C in reproduction.