2008, Number 2
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ABSTRACTMore than half of human proteins are modified (glycosylated) co- and post-translationally with oligosaccharides (glycans) through the action of glycosyltransferases. Glycans play an important role in quality control, traffic and function of these modified proteins (glycoproteins). Several defects in the synthesis of glycans have been described in the main glycosylation pathways: -N and O- glycosylation. The first human congenital disorder of glycosylation (CDG) was reported in 1980, since then more than 35 different subtypes of these disorders have been described. Since hundreds of proteins are involved in these pathways it is likely that new disorders will be identified. Clinical suspicion of a congenital disorder of glycosylation must be established when confronting a multisystemic congenital disease of unknown etiology. The aim of this review is to aid the physician to suspect a CDG and to identify the most plausible subtype in order to request the pertinent molecular studies and to confirm the diagnosis, prescribe and adequate treatment and determine prognosis.
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