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Articles |
1
Central Clinical Chemistry Laboratory and
2
Division of Immunology and Allergology, Centre Hospitalier Universitaire Vaudois, CH-1011 Lausanne, Switzerland.
3
Division of Gastroenterology, Policlinique
Médicale Universitaire, Lausanne, Switzerland.
4
Red Cross Transfusion Center, Lausanne, Switzerland.
5
Department of Metabolism, Bambino Gesu Hospital, Rome,
Italy.
a Address correspondence to this author at: Laboratoire Central de Chimie Clinique, Centre Hospitalier Universitaire Vaudois, CH-1011 Lausanne, Switzerland. Fax 41-21-3144288; e-mail Hugues.Henry{at}chuv.hospvd.ch
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 
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.
Conclusion: 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.
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L. Dibbelt Does Trisialo-Transferrin Provide Valuable Information for the Laboratory Diagnosis of Chronically Increased Alcohol Consumption by Determination of Carbohydrate-deficient Transferrin? Clin. Chem., August 1, 2000; 46(8): 1203 - 1205. [Full Text] [PDF]
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 E. Korvatska, H. Henry, Y. Mashima, M. Yamada, C. Bachmann, F. L. Munier, and D. F. Schorderet Amyloid and Non-amyloid Forms of 5q31-linked Corneal Dystrophy Resulting from Kerato-epithelin Mutations at Arg-124 Are Associated with Abnormal Turnover of the Protein J. Biol. Chem., April 6, 2000; 275(15): 11465 - 11469. [Abstract] [Full Text] [PDF]
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