ANALYSIS OF N-LINKED GLYCOFORM VARIANTS IN CONGENITAL DISORDERS OF GLYCOSYLATION

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. More than half of the proteins in mammals, specifically in humans, are glycosylated through linkages to asparagine (N-linked glycans) or serine/threonine (O-linked glycans) and ocassionally other sites as well. The absence or diminished expression of glycosidases and glycosyl transfereases that are involved in the assembly of glycans can lead to severe disease, now generically referred to as "congenital disorders of glycosylation (CDGs). The aberrant pathways in some CDGs have been defined, but numerous new cases are being recognized. It is sometimes difficult to determine the specific structures of the resulting glycans, especially when the modification or presence of multiple pathways or incomplete penetrance of the disorder leads to the production of glycosylation mixtures. The Resource collaborated with Prof. Freeze and his colleagues to unravel the glycan structures and thereby to deduce the genetic aberration in a recent case that resulted in the definintion of a new congenital disorder of glycosylation, type IIh, that involves a deficiency of COG8.