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The most commonly used screening method for CDG, analysis of transferrin glycosylation status by isoelectric focusing, ESI-MS, or other techniques, distinguish between these subtypes in so called Type I and Type II patterns. [31] Currently, over 130 subtypes of CDG have been described. [32] [7]
A major source of transferrin secretion in the brain is the choroid plexus in the ventricular system. [15] The main role of transferrin is to deliver iron from absorption centers in the duodenum and white blood cell macrophages to all tissues. Transferrin plays a key role in areas where erythropoiesis and active cell division occur. [16]
Traditional screening tests utilized for congenital disorders of glycosylation, including carbohydrate deficient transferrin are not diagnostic in NGLY1 deficiency. To date all variants identified as being causative of NGLY1 deficiency have been sequence variants, rather than copy number variants.
ALG1-CDG is an autosomal recessive congenital disorder of glycosylation caused by biallelic pathogenic variants in ALG1. The first cases of ALG1-CDG were described in 2004, and the causative gene was identified at the same time. This disorder was originally designated CDG-IK, under earlier nomenclature for congenital disorders of glycosylation. [1]
SRD5A3-CDG (also known as CDG syndrome type Iq, CDG-Iq, CDG1Q or Congenital disorder of glycosylation type 1q) is a rare, non X-linked congenital disorder of glycosylation (CDG) [1] due to a mutation in the steroid 5 alpha reductase type 3 gene. It is one of over 150 documented types of Congenital disorders of Glycosylation. [2]
Phosphoglucomutase 1 deficiency is both a glycogenosis and a congenital disorder of glycosylation. [39] Individuals with the disease have both a glycolytic block as muscle glycogen cannot be broken down, as well as abnormal serum transferrin (loss of complete N-glycans). [39]
glycosylation, the addition of a glycosyl group to either arginine, asparagine, cysteine, hydroxylysine, serine, threonine, tyrosine, or tryptophan resulting in a glycoprotein. Distinct from glycation, which is regarded as a nonenzymatic attachment of sugars.
The primary sequence of ovotransferrin is similar to that of many serum transferrins found in other species. Recently, scientists have discovered a blood serum transferrin in humans, that binds iron like ovotransferrin and which shows 50% homology to ovotransferrin, i.e., they have similar amino acid composition and carbohydrate content. At the ...