title: Glycosylation related actions of glycodelin: gamete, cumulus cell, immune cell and clinical associations.
abstract: Glycodelin is an example of a glycoprotein whose complex-type glycans mediate biological actions in human reproduction and immune reactions. Being attached to an identical protein backbone, glycodelin oligosaccharides vary significantly from one reproductive tissue to another and have an effect on its own secretion and role in cell communication. For instance, uterine glycodelin-A inhibits sperm-oocyte interaction by binding on the sperm head. This is a glycosylation-dependent phenomenon, in which fucosyltransferase-5 plays a key role. Glycodelin-S from seminal plasma binds evenly around the sperm head and maintains an uncapacitated state in the spermatozoa, until the isoform is detached during sperm passage through the cervix. Glycodelin-F from follicular fluid and Fallopian tube binds to the acrosomal region of the sperm head, thereby inhibiting both the sperm-oocyte binding and premature progesterone-induced acrosome reaction. The cumulus cells surrounding the oocyte can capture glycodelin-A and -F from the surrounding environment and convert these isoforms to a cumulus cell isoform, glycodelin-C. It differs by glycosylation from the other isoforms, and it too attaches on the sperm head, with the highest density in the equatorial region. Glycodelin-C is capable of detaching the sperm-bound inhibitory isoforms so that the sperm-oocyte binding is enhanced. Glycodelin-A also has immunosuppressive actions directed to cellular, humoral and innate immunity. Although these actions depend mainly on the protein backbone, glycosylation also plays a part. Glycosylated glycodelin may be involved in the protection of spermatozoa against maternal immune reactions, and glycodelin also has apoptogenic activity. Some glycosylation patterns of glycodelin may mask its apoptogenic domain. This review updates the recent research and clinical associations of glycodelin, highlighting the role of glycosylation.
authors.affiliation: Department of Clinical Chemistry, University of Helsinki, Helsinki University Central Hospital, Biomedicum Helsinki, 4th Floor, Haartmaninkatu 8, Helsinki, Finland. mseppala@welho.com
authors.forename: M
authors.initials: M
authors.lastname: Seppälä
authors.forename: H
authors.initials: H
authors.lastname: Koistinen
authors.forename: R
authors.initials: R
authors.lastname: Koistinen
authors.forename: P C N
authors.initials: PC
authors.lastname: Chiu
authors.forename: W S B
authors.initials: WS
authors.lastname: Yeung
mesh_terms: D005260:Female; D005854:Germ Cells / Q000276:immunology* / Q000378:metabolism*; D000071816:Glycodelin; D006023:Glycoproteins / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D008214:Lymphocytes / Q000276:immunology / Q000378:metabolism*; D008297:Male; D009865:Oocytes / Q000166:cytology / Q000378:metabolism; D011257:Pregnancy Proteins / Q000378:metabolism*; D013084:Sperm-Ovum Interactions / Q000276:immunology*; D013094:Spermatozoa / Q000166:cytology / Q000378:metabolism
chemical_list: D000071816:Glycodelin; D006023:Glycoproteins; C045246:PAEP protein, human; D011257:Pregnancy Proteins