小白鼠附屬性腺所分泌蛋白酶 (P12) 和精子作用之機制(2/3)

CEACAM10 was purified from mouse seminal vesicle secretion by a series of purification
steps including ion exchange chromatography on a DEAE-Sephacel column and ion exchange
HPLC on an SP column. It was shown to be a 36-kDa glycoprotein with an N-linked
carbohydrate moiety. The CD spectrum of CEACAM10 in 50 mM phosphate buffer at pH 7.4
appeared as one negative band arising from the β-form at 217 nm. In the reproductive glands of
adult mice, CEACAM10 was expressed predominantly in seminal vesicles. Both CEACAM10
and its mRNA were demonstrated on the luminal epithelium of the mucosal folds in the seminal
vesicle. The amount of Ceacam10 mRNA in the seminal vesicle was correlated with the stage of
animal maturation. Castration of adult mice resulted in cessation of Ceacam10 expression, while
treatment of the castrated mice with testosterone propionate in corn oil restored the Ceacam10
expression in the seminal vesicle. During the entire course of pregnancy, Ceacam10 might be
silent in the embryo. A cytochemical study illustrated the presence of the CEACAM10-binding
region on the entire surface of mouse sperm. CEACAM10-sperm binding greatly enhanced
sperm motility in vitro.