Elucidation of Complement C3 Degradation in Mouse Uterine Fluid by CEACAM10 from Seminal Vesicle Secretion
Date Issued
2008
Date
2008
Author(s)
Wang, Hsi-Chao
Abstract
Innate immunity plays an essential role in the defense of the invaders in the female genital tract. Spermatozoa must therefore evade immunity attack in order to reach the ampulla of oviduct for fertilization. A 36-kDa has been demonstrated carcinoembryonic antigen-related cell adhesion molecule 10（CEACAM10）from adult mouse seminal vesicle secretions. Among the sexual glands of male and female mice, it is exclusively expressed in seminal vesicle. Although, it is able to bind on the entire surface of mouse spermatozoa and enhance sperm motility in vitro, its role in murine female reproductive system has no yet understood. This work aimed to that direction, I incubated purified CEACAM10 with uterine luminal fluid collected from adult female mice during estrus and resolved the protein components by nonreduced SDS-PAGE. A 180-kDa protein was markedly decrease by CEACAM10. This protein was demonstrated to be complement 3 component（C3）based on the peptide sequences determined by LC/MS/MS analysis. Further, I illustrated the degradation of β chain of C3 in the uterine fluid by CEACAM10. As a result, C3b、iC3b、C3c、C3dg became incomplete. In the preimplantation period, CEACAM10 was determined in the uterine fluid and only on day 1. It was accomplished with the degradation of C3 β chain. Taken together, the presence of CEACAM10 in the uterine fluid caused the loss of C3 activity via the degradation of its β chain to prevent the ejaculated spermatozoa in the uterine lumen from the immunity, attacked by the complement system. C3 was highly conserved and I studied the effect of CEACAM10 in the human C3 activity. These results were summarized：（1）Incubation of human C3 and mouse CEACAM10 didn’t cause the C3 degradation；（2）Addition of the human C3 deficient serum to the incubation of human C3 and CEACAM10 caused the human C3 β chain degradation;（3）CEACAM10 was able to inhibit the lysis of sheep blood by human C3 and the C3 deficient serum together.
Subjects
mouse
seminal vesicle secretion
C3
complement activity
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