title: Microheterogeneity of serum glycoproteins in patients with chronic alcohol abuse compared with carbohydrate-deficient glycoprotein syndrome type I.
abstract: BACKGROUND
  Chronic alcohol abuse alters the normal N-glycosylation of transferrin, producing the carbohydrate-deficient transferrin isoforms. This alteration could be similar to that present in patients with carbohydrate-deficient glycoprotein syndrome type 1 (CDG1). We thus compared the alterations of N-glycans present in patients with alcoholism and patients with CDG1.
  
  
  METHODS
  The N-glycans of serum glycoproteins were compared in sera of patients with alcoholism, patients with CDG1, and controls by two-dimensional electrophoresis, neuraminidase, peptide:N-glycosidase F, and endoglycosidase F2 treatments. A specific antibody directed against the amino acid sequence surrounding the N-432 N-glycosylation site of transferrin was prepared (SZ-350 antibody).
  
  
  RESULTS
  In patients with alcoholism, the abnormal transferrin and alpha(1)-antitrypsin isoforms were devoid of a variable number of entire N-glycan moieties and were identical with those present in CDG1. In the serum of patients with alcoholism, this finding was less pronounced than in CDG1. In contrast to CDG1, there was no decrease in clusterin or serum amyloid P in patients with alcoholism. The SZ-350 antibody recognized only transferrin isoforms with one or no N-glycan moieties.
  
  
  CONCLUSIONS
  Antibodies directed against specific N-glycosylation sites of glycoproteins could be useful for developing more specific immunochemical tests for the diagnosis of chronic alcohol abuse.
authors.affiliation: Central Clinical Chemistry Laboratory, Centre Hospitalier Universitaire Vaudois, CH-1011 Lausanne, Switzerland. Hugues.Henry@chuv.hospvd.ch
authors.forename: H
authors.initials: H
authors.lastname: Henry
authors.forename: F
authors.initials: F
authors.lastname: Froehlich
authors.forename: R
authors.initials: R
authors.lastname: Perret
authors.forename: J D
authors.initials: JD
authors.lastname: Tissot
authors.forename: B
authors.initials: B
authors.lastname: Eilers-Messerli
authors.forename: D
authors.initials: D
authors.lastname: Lavanchy
authors.forename: C
authors.initials: C
authors.lastname: Dionisi-Vici
authors.forename: J J
authors.initials: JJ
authors.lastname: Gonvers
authors.forename: C
authors.initials: C
authors.lastname: Bachmann
mesh_terms: D000437:Alcoholism / Q000097:blood*; D000581:Amidohydrolases; D000918:Antibody Specificity; D001798:Blood Proteins / Q000032:analysis* / Q000737:chemistry; D018981:Congenital Disorders of Glycosylation / Q000097:blood*; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000097:blood* / Q000737:chemistry; D006031:Glycosylation; D006801:Humans; D015151:Immunoblotting; D009439:Neuraminidase; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D011134:Polysaccharides / Q000378:metabolism; D014168:Transferrin / Q000737:chemistry / Q000276:immunology / Q000378:metabolism
chemical_list: D001798:Blood Proteins; D006023:Glycoproteins; D011134:Polysaccharides; D014168:Transferrin; D009439:Neuraminidase; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase