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Golgi linked protein glycosylation and associated diseases
Authors:Daniel Ungar
Institution:1. Univ. Lille, CNRS, UMR 8576 – UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France;2. LIA GLYCOLAB4CDG France/Belgium (International Associated Laboratory “Laboratory for the Research on Congenital Disorders of Glycosylation – from cellular mechanisms to cure”, France;3. Univ. Lille, CHU Lille, Institut Pasteur de Lille, EA 4483 – IMPECS – IMPact de l''Environnement Chimique sur la Santé humaine, F-59000 Lille, France;4. Center for Human Genetics, KU Leuven, Leuven, Belgium
Abstract:One of the Golgi's main functions is the glycosylation of secreted proteins. A large variety of glycan chains can be synthesized in the Golgi, and it is increasingly clear that these are critical in basic cellular functions as well as the development of multicellular organisms. The structurally best-documented glycans are N-glycans, yet these are also the most enigmatic in their function. In contrast, O-glycan function is far better understood, but here the structures and biosynthetic pathways are very incomplete. The critical importance of glycans is highlighted by the broad spectrum of diseases they are associated with, such as a number of inherited diseases, but also cancers or diabetes. The molecular clues to these, however, are only just being elucidated. Although some glycan structures are known to be involved in signaling or adhesion to the extracellular matrix, for most the functions are not yet known. This review aims at summarizing current knowledge as much as to point out critical areas key for future progress.
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