Format

Send to

Choose Destination
Semin Cell Dev Biol. 2009 Sep;20(7):762-9. doi: 10.1016/j.semcdb.2009.03.004.

Golgi linked protein glycosylation and associated diseases.

Author information

1
University of York, Department of Biology (area 9), PO Box 373, York YO10 5YW, UK. du500@york.ac.uk

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.

PMID:
19508859
DOI:
10.1016/j.semcdb.2009.03.004
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center