Disease relevance of GYG2

• Glycogenin-2 was found in Ewing's sarcoma RD-ES cells where, however, it was not associated with high Mr carbohydrate [1].
• Antibodies raised against GN-2 produced in E. coli recognized proteins of Mr approximately 66,000 present in extracts of rat liver and in cultured H4IIEC3 hepatoma cells [2].
• Phenotypic characterization of the isolates was mainly performed with API 20NE and BIOLOG GN2 identification systems; the results were system-dependent, although the presence of representatives of the Pseudomonas genus (for the majority of the isolates) was suggested by both systems [3].

Psychiatry related information on GYG2

• The metabolic profiles produced by the SFN2 and GN2 plates were identical, but the SFN2's narrower range of OD values and significantly longer reaction times made these plates less suitable for differentiation of isolates [4].
• In addition, in Alzheimer's disease we found simple gangliosides (GN2, GM3) to be elevated in the frontal and parietal cortex, which might correlate accelerated lysosomal degradation of gangliosides and/or astrogliosis occurring during neuronal death [5].

High impact information on GYG2

• Mutation of Tyr-196 in glycogenin-2 to a Phe residue abolished the ability of glycogenin-2 to self-glucosylate but not to interact with glycogenin-1 [1].
• Cloning of cDNAs encoding glycogenin-2 indicated the existence of multiple species, including three liver forms (GN-2alpha, GN-2beta, and GN-2gamma) generated in part by alternative splicing [2].
• GYG2 is outside the pseudoautosomal region PAR1 but still in a region of X-Y shared genes [6].
• As is true for several other genes in this location, an inactive remnant of GYG2, consisting of exons 1-3, may be present on the Y chromosome [6].
• Glycogenin-2 maps between the microsatellite anchor markers AFM319te9 (DXS7100) and AFM205tf2 (DXS1060), and its 3' end is 34.5 kb from the 3' end of the arylsulphatase gene ARSD [6].

Biological context of GYG2

• Localization close to the telomere of the short arm of the X chromosome is consistent with mapping information obtained from glycogenin-2 STS sequences [6].
• Overall, GN-2 has 40-45% identity to muscle glycogenin but is 72% identical over a 200-residue segment thought to contain the catalytic domain [2].
• Two tandemly repeated DNA sequences of Gerbillus nigeriae (Rodentia) (GN1 and GN2) were isolated and characterized [7].
• The localization of GN1 and GN2 sequences on metaphase chromosomes of three Gerbillus species, G. nigeriae, G. aureus and G. nanus, was studied by fluorescence in situ hybridization (FISH) [7].

Anatomical context of GYG2

• We describe the characterization of novel forms of glycogenin, designated glycogenin-2 (GN-2), encoded by a second gene that is expressed preferentially in certain tissues, including liver, heart, and pancreas [2].
• The new protein, glycogenin-2, had several properties similar biochemically to the muscle isoform, glycogenin-1, but unlike glycogenin-1, stable expression in fibroblasts led to a significant overaccumulation of glycogen [8].
• Finally, B. cenocepacia and B. pyrrocinia showed generally higher oxidation rates than B. ambifaria on those GN2 substrates that commonly occur in maize root exudates [4].

Associations of GYG2 with chemical compounds

• Glycogenin-2 is one of two self-glucosylating proteins involved in the initiation phase of the synthesis of the storage polysaccharide glycogen [6].

Other interactions of GYG2

• Over regions of protein sequence similarity, the GYG2 gene structure is similar to that of the other glycogenin gene, GYG [6].

Analytical, diagnostic and therapeutic context of GYG2

• A genomic GYG2 clone was used to localize the gene to Xp22.3 by fluorescence in-situ hybridization [6].
• In human liver extracts, most of the glycogenin-2 was only detectable after treatment with alpha-amylase [1].
• Glycogenin-1 and glycogenin-2 interact with one another, based on in vitro interactions and co-immunoprecipitation from liver and cell extracts [1].

References