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Clinical Chemistry 46: 795-805, 2000;
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(Clinical Chemistry. 2000;46:795-805.)
© 2000 American Association for Clinical Chemistry, Inc.

Articles

Protein Glycosylation and Diseases: Blood and Urinary Oligosaccharides as Markers for Diagnosis and Therapeutic Monitoring

Geneviève Durand1,2 and Nathalie Seta1,3,a

1 Biochimie A, Hôpital Bichat-Claude Bernard AP-HP, 75877 Paris Cedex 18, France.

2 Laboratoire de Biochimie Générale, UFR Sciences Pharmaceutiques et Biologiques–Paris XI, 92260 Châtenay-Malabry Cedex, France.

3 Faculté de Pharmacie, Université Paris V, 75270 Paris Cedex 06, France.
a Address correspondence to this author at: Laboratoire de Biochimie A, Hôpital Bichat-Claude Bernard, 46, Rue H. Huchard, 75877 Paris Cedex, France. Fax 33-1-4025-8821; e-mail nathalie.seta{at}bch.ap-hop-paris.fr

Background: N- and O-oligosaccharide variants on glycoproteins (glycoforms) can lead to alterations in protein activity or function that may manifest themselves as overt disease.

Approach: This review summarizes those diseases that are known to be the result of an inherited or acquired glycoprotein oligosaccharide structural alteration and that are diagnosed in blood or urine by chemical characterization of that oligosaccharide alteration.

Content: The biochemical synthesis steps and catabolic pathways important in determining glycoprotein function are outlined with emphasis on alterations that lead to modified function. Clinical and biochemical aspects of the diagnosis are described for inherited diseases such as I-cell disease, congenital disorders of glycosylation, leukocyte adhesion deficiency type II, hereditary erythroblastic multinuclearity with a positive acidified serum test, and Wiskott-Aldrich syndrome. We also review the laboratory use of measurements of glycoforms related to acquired diseases such as alcoholism and cancer.

Conclusions: Identification of glycoprotein glycoforms is becoming an increasingly important laboratory contribution to the diagnosis and management of human diseases as more diseases are found to result from glycan structural alterations.




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eLetters:

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PROTEIN GLYCOSYLATION AND DISEASES
S Vivekanandan
Clinical Chemistry Online, 13 Sep 2000 [Full text]

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