title: Wisteria floribunda agglutinin-binding glycan expression is decreased in endometriomata.
abstract: BACKGROUND
  Glycosylation is one of the most common post-translational modifications of eukaryotic proteins and is known to undergo dynamic changes in a wide range of biological processes. To date, however, the glycan expression profiles in endometriosis are largely unknown. The objective of the study was to identify the panel of glycans that were aberrantly expressed in endometriosis, a hormone-dependent disease.
  
  
  METHODS
  The glycan expression profiles in primary cultured human endometriotic cyst stromal cells (ECSCs) and normal endometrial stromal cells (NESCs) were determined by lectin microarray analysis. Distribution of Wisteria floribunda agglutinin (WFA)-binding glycans in ovarian endometriotic cysts and eutopic proliferative phase endometrium were assessed by lectin histochemistry. The expressions of N-acetylgalactosaminyl transferases that synthesize WFA-binding glycans were evaluated in ECSCs and NESCs.
  
  
  RESULTS
  We found that the levels of WFA-binding glycans were decreased in ECSCs. Lectin histochemistry revealed that WFA-binding glycans were decreased only in the stromal components of the ovarian endometriotic cysts, but not in the epithelial components, compared to the eutopic proliferative phase endometrium. The expressions of N-acetylgalactosaminyl transferases that synthesize WFA-binding glycans were downregulated in ECSCs.
  
  
  CONCLUSIONS
  Utilizing lectin microarray analysis and lectin histochemistry, we found that WFA-binding glycans were decreased in endometriosis. The synthetic enzymes of WFA-binding glycans were significantly downregulated in ECSCs. It is suggested that reduced expression of N-glycans with WFA-binding properties on ECSCs is a novel characteristics of endometriosis.
authors.forename: Tomoko
authors.initials: T
authors.lastname: Hirakawa
authors.affiliation: Department of Obstetrics and Gynecology, Faculty of Medicine, Oita University, Idaigaoka 1-1, Hasama-machi, Yufu-shi Oita 879-5593, Japan. nasu@oita-u.ac.jp.
authors.forename: Kaei
authors.initials: K
authors.lastname: Nasu
authors.forename: Kentaro
authors.initials: K
authors.lastname: Kai
authors.forename: Yoko
authors.initials: Y
authors.lastname: Aoyagi
authors.forename: Terukazu
authors.initials: T
authors.lastname: Ishii
authors.forename: Tetsuya
authors.initials: T
authors.lastname: Uemura
authors.forename: Mitsutake
authors.initials: M
authors.lastname: Yano
authors.forename: Hisashi
authors.initials: H
authors.lastname: Narahara
mesh_terms: D000328:Adult; D015153:Blotting, Western; D002478:Cells, Cultured; D015536:Down-Regulation; D004715:Endometriosis / Q000201:enzymology / Q000378:metabolism* / Q000473:pathology; D004717:Endometrium / Q000201:enzymology / Q000378:metabolism / Q000473:pathology; D005260:Female; D005498:Follicular Phase; D006801:Humans; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D017350:N-Acetylgalactosaminyltransferases / Q000235:genetics / Q000378:metabolism*; D010048:Ovarian Cysts / Q000201:enzymology / Q000378:metabolism* / Q000473:pathology; D010053:Ovary / Q000201:enzymology / Q000378:metabolism / Q000473:pathology; D037121:Plant Lectins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011134:Polysaccharides / Q000096:biosynthesis* / Q000378:metabolism; D040081:Protein Array Analysis; D012333:RNA, Messenger / Q000378:metabolism; D034781:Receptors, N-Acetylglucosamine / Q000037:antagonists & inhibitors / Q000378:metabolism*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017154:Stromal Cells / Q000201:enzymology / Q000378:metabolism / Q000473:pathology
chemical_list: D007527:Isoenzymes; D037121:Plant Lectins; D011134:Polysaccharides; D012333:RNA, Messenger; D034781:Receptors, N-Acetylglucosamine; C040129:wisteria lectin; D017350:N-Acetylgalactosaminyltransferases