Roles of glycodelin in modulating sperm function

MOLECULAR AND CELLULAR ENDOCRINOLOGY

卷:250

Article

Yeung, William S. B. ; Lee, Kai-Fai ; Koistinen, Riitta ; Koistinen, Hannu ; Seppala, Markku ; Ho, P. C. ; Chiu, Philip C. N.

关键词: acrosome reaction;    capacitation;    glycodelin;    spermatozoa;    zona pellucida;   

DOI  :  10.1016/j.mce.2005.12.038

来源: Elsevier

【 摘 要 】

Glycodelin is a glycoprotein with three well-defined isoforms. They are named as glycodelin-S, glycodelin-A and glycodelin-F. The three isoforms have similar protein core but different carbohydrate moieties. Glycodelin-S is abundant in the human seminal plasma. It suppresses sperm capacitation and in doing so, it maintains the spermatozoa in an uncapacitated state before they enter into the uterine cavity. Glycodelin-A is abundant in the amniotic fluid. It is also secreted from endometrial glands into uterine fluid and is produced by the fallopian tube. Glycodelin-A is the first endogenous glycoprotein that was found to inhibit the binding of spermatozoa to the zona pellucida. The immunosuppressive properties of glycodelin-A suggest that the molecule may protect the spermatozoa from immune attack in the maternal reproductive tract. Glycodelin-F was first found in the follicular fluid, hence its name. It also inhibits spermatozoa-zona pellucida binding. In addition, glycodelin-F suppresses progesterone-induced acrosome reaction, and may serve to prevent premature acrosome reaction. Preliminary findings suggest possible presence of yet another glycodelin isoform in the extracellular matrix of cumulus oophorus. Unlike glycodelin-A and -F, it stimulates spermatozoa-zona pellucida binding. In summary, different isoforms of glycodelin have different biological roles on sperm function, and they act in succession to contribute to the success of fertilization. (c) 2005 Elsevier Ireland Ltd. All rights reserved.

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