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Endocrine Reviews 23 (4): 401-430
Copyright © 2002 by The Endocrine Society

Glycodelin: A Major Lipocalin Protein of the Reproductive Axis with Diverse Actions in Cell Recognition and Differentiation

Markku Seppälä, Robert N. Taylor, Hannu Koistinen, Riitta Koistinen and Edwin Milgrom

Department of Obstetrics and Gynecology (M.S., H.K., R.K.), Helsinki University Central Hospital, Haartmaninkatu 2, 00029 HUS, Helsinki, Finland; Department of Obstetrics, Gynecology and Reproductive Sciences (R.N.T.), University of California, San Francisco, California 94143-0132; and Laboratoire d’Hormonologie et de Biologie Moleculaire (E.M.), Institute National de la Santé et de la Recherche Médicale Unité 135, Hormones, Genes et Reproduction, Hopital de Bicetre, 94275 Le Kremlin-Bicetre, France

Correspondence: Address all correspondence and requests for reprints to: Markku Seppälä, Pihlajatie 20 B 15, 00270 Helsinki, Finland. E-mail: mseppala{at}pp.htv.fi

Glycodelin is a glycoprotein that belongs to the lipocalin superfamily. Depending on glycosylation, glycodelin appears in various isoforms. In the uterus, glycodelin-A is the major progesterone-regulated glycoprotein secreted into uterine luminal cavity by secretory/decidualized endometrial glands. The other tissues expressing glycodelin include fallopian tubes, ovary, breast, seminal vesicle, bone marrow, and eccrine glands. Glycodelin-A potently and dose-dependently inhibits human sperm-egg binding, whereas differently glycosylated glycodelin-S from seminal plasma has no such effect. Absence of contraceptive glycodelin-A in the uterus during periovulatory midcycle is consistent with an open "fertile window." Glycodelin induced by local or systemic administration of progestogens may potentially reduce the fertilizing capacity of sperm in any phase of the menstrual cycle. Glycodelin also has immunosuppressive activity. Its high concentration at the fetomaternal interface may contribute to protection of the embryonic semiallograft. Besides being an epithelial differentiation marker, glycodelin appears to play a role in glandular morphogenesis, as transfection of glycodelin cDNA into a glycodelin-negative breast cancer cells resulted in formation of gland-like structures, restricted proliferation, and induction of other epithelial markers. These various properties, as well as the chemistry, biology, and clinical aspects of glycodelin, continue to be areas of active investigation reviewed in this communication.




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