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-regulatedglycoprotein secreted into uterine luminal cavity by secretory/decidualizedendometrial glands. The other tissues expressing glycodelininclude fallopian tubes, ovary, breast, seminal vesicle, bonemarrow, and eccrine glands. Glycodelin-A potently and dose-dependentlyinhibits human sperm-egg binding, whereas differently glycosylatedglycodelin-S from seminal plasma has no such effect. Absenceof contraceptive glycodelin-A in the uterus during periovulatorymidcycle is consistent with an open "fertile window." Glycodelininduced by local or systemic administration of progestogensmay potentially reduce the fertilizing capacity of sperm inany phase of the menstrual cycle. Glycodelin also has immunosuppressiveactivity. Its high concentration at the fetomaternal interfacemay contribute to protection of the embryonic semiallograft.Besides being an epithelial differentiation marker, glycodelinappears to play a role in glandular morphogenesis, as transfectionof glycodelin cDNA into a glycodelin-negative breast cancercells resulted in formation of gland-like structures, restrictedproliferation, and induction of other epithelial markers. Thesevarious properties, as well as the chemistry, biology, and clinicalaspects of glycodelin, continue to be areas of active investigationreviewed in this communication.
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