title: Genetic defects in the human glycome.
abstract: The spectrum of all glycan structures--the glycome--is immense. In humans, its size is orders of magnitude greater than the number of proteins that are encoded by the genome, one percent of which encodes proteins that make, modify, localize or bind sugar chains, which are known as glycans. In the past decade, over 30 genetic diseases have been identified that alter glycan synthesis and structure, and ultimately the function of nearly all organ systems. Many of the causal mutations affect key biosynthetic enzymes, but more recent discoveries point to defects in chaperones and Golgi-trafficking complexes that impair several glycosylation pathways. As more glycosylation disorders and patients with these disorders are identified, the functions of the glycome are starting to be revealed.
authors.affiliation: Burnham Institute for Medical Research, 10901 North Torrey Pines Road, La Jolla, California 92037, USA. hudson@burnham.org
authors.forename: Hudson H
authors.initials: HH
authors.lastname: Freeze
mesh_terms: D000818:Animals; D002236:Carbohydrate Conformation; D002239:Carbohydrate Metabolism, Inborn Errors / Q000235:genetics* / Q000378:metabolism*; D002240:Carbohydrate Sequence; D006031:Glycosylation; D006801:Humans; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism
chemical_list: D011134:Polysaccharides