title: Glycosylation of proteins in healthy and neoplastic human salivary glands - a preliminary study.
abstract: BACKGROUND
  In cancer tissue, altered glycosylation of proteins is observed. There are some typical changes; for example, sialyl-Lewis(a/x) glycoforms are more abundant in many types of cancers. The current study investigated the differences in glycosylation of proteins between neoplastic and healthy human salivary glands.
  
  
  METHODS
  Sugar structures on proteins with a molecular mass above 30 kDa were determined by enzyme-linked immunosorbent assay (ELISA) with biotinylated lectins.
  
  
  RESULTS
  The expression of sialic acid in cancer tissues was higher in comparison with healthy ones. The same observations were revealed for Fuc α1-6, α1-2, T, Tn antigens and α1-6 mannose.
  
  
  CONCLUSIONS
  Glycosylation of proteins in cancer salivary gland tissues is altered in comparison with healthy tissue.
authors.affiliation: Department of Pharmaceutical Biochemistry, Medical University of Bialystok, Bialystok, Poland. gocha@umwb.edu.pl
authors.forename: Małgorzata
authors.initials: M
authors.lastname: Borzym-Kluczyk
authors.forename: Iwona
authors.initials: I
authors.lastname: Radziejewska
authors.forename: Marzanna
authors.initials: M
authors.lastname: Cechowska-Pasko
mesh_terms: D000328:Adult; D000368:Aged; D004797:Enzyme-Linked Immunosorbent Assay / Q000379:methods*; D005260:Female; D006031:Glycosylation; D006801:Humans; D008297:Male; D008875:Middle Aged; D008970:Molecular Weight; D037121:Plant Lectins / Q000378:metabolism; D012468:Salivary Gland Neoplasms / Q000378:metabolism* / Q000473:pathology; D012469:Salivary Glands / Q000166:cytology / Q000378:metabolism* / Q000473:pathology; D012471:Salivary Proteins and Peptides / Q000737:chemistry / Q000378:metabolism*
chemical_list: D037121:Plant Lectins; D012471:Salivary Proteins and Peptides