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Department of Medical Research,3 Mackay Memorial Hospital, Tamshui 251, Taiwan
Mackay Medicine, Nursing and Management College,4 Taipei 112, Taiwan
Institute of Biochemical Sciences,5 College of Life Science, National Taiwan University
Institute of Biological Chemistry,6 Academia Sinica, Taipei 106, Taiwan
CEACAM10 was purified from mouse seminal vesicle secretions by a series of purification steps that included ion exchange chromatography on a DEAE-Sephacel column and ion exchange high-performance liquid chromatography on a sulfopropyl column. It was shown to be a 36-kDa glycoprotein with an N-linked carbohydrate moiety. The circular dichromoism spectrum of CEACAM10 in 50 mM phosphate buffer at pH 7.4 appeared as one negative band arising from the ß form at 217 nm. CEACAM10 was expressed predominantly in seminal vesicles of adult mice. 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 castrated mice with testosterone propionate in corn oil restored 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.
male reproductive tract, seminal vesicles, sperm motility and transport
2 Correspondence: Yee-Hsiung Chen, Institute of Biological Chemistry, Academia Sinica, P.O. Box 23-106, Taipei 106, Taiwan. FAX: 886 2 2363 5038; bc304{at}gate.sinica.edu.tw
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