Disease relevance of PGM2

• Genetic investigations reveal that: (1) inbreeding does not increase risk of lymphoma; (2) there is a weak association between the PGM2 locus and lymphoma; (3) based upon path analysis, there is evidence of a significant transmissible component (genetic predisposition) passed from the parental to the next generation [1].

High impact information on PGM2

• The genes for PGM2 and malic enzyme-1 map in region 6p2100 leads to 6qter [2].
• PGM-2 is a variant of the transplantable PGM-1 leukemia of strain C3H/HeJ [3].
• Lithium stress causes an increase of the phosphoglucomutase activity due to an induction of transcription of the PGM2 gene, and its overexpression confers lithium tolerance in galactose medium [4].
• In humans, there are three well-described isozymes, PGMI, PGM2, and PGM3 [5].
• Indeed, an amino acid sequence, derived from a partial human cDNA, that fell within the second cross-kingdom lineage bears several characteristics expected for PGM2 [5].

Biological context of PGM2

• Previous studies have shown that two homologs of genes on HSA4, PGM2 and PEPS, are located in bovine syntenic group U15 (chromosome 6) [6].
• In screening of the PGM system by isoelectric focusing a heterozygote with a rare allele of PGM2 was detected [7].
• One rare phenotype was found at each of the PGM1 AND PGM2 loci [8].
• Baseline data are presented on phenotype and gene frequency distributions of nine red-cell enzyme systems (ADA, AK, EsD, GLO I, PGM1, AP, GPI, PGM2, SOD) in the Sunni Muslims of Kashmir valley in the northernmost Indian border state of Jammu and Kashmir [9].
• These forms have the same kinetic properties, but from the substrate specificity experiments we have found that PGM2 forms are more effective for catalyzing the phosphoribomutase and glucose 1,6-bisphosphate synthase reaction than PGM1 forms [10].

Anatomical context of PGM2

• At the PGM2 locus, samples of malignant cervix were deficient in "Band f" compared with normal cervix samples, all of which showed this band [11].
• With regard to the phosphoglucomutase PGM1 and PGM2 isoenzymes, the latter appear to be more important in erythrocyte metabolism owing to their ability to mutate ribose monophosphates and synthetize glucose-1,6-bisphosphate [12].
• Analysis of 13 isozymes showed 12 to be asyntenic and on epair (PGD-PGM2) to be syntenic This system will allow extensive somatic cell hybrid gene mapping in the mouse and permit a comparison of human and mouse linkage relationships [13].
• The recently described PGM-2 leukemia displays a hierarchical structure with bipotential stem cells, B-lymphocyte and macrophage progenitor cells, and post-mitotic end cells [14].

Associations of PGM2 with chemical compounds

• Micromolar concentrations of fructose 1,6-P2 and glycerate 2,3-P2 inhibit both PGM1 and PGM2 isoenzymes to a similar extent [15].
• Other salient findings were the variability observed in the PGM2 and C3 systems, and the low prevalence of Bfs [16].
• This cannot be achieved on human hemolysates where glycerate 1,3-P2-dependent glucose 1,2-bisphosphate synthesis is displayed only by multifunctional PGM2 isoenzymes [17].

Other interactions of PGM2

• Of the two prokaryotic/eukaryotic lineages, one contained bacterial, yeast, slimemold, invertebrate, and vertebrate homologs to human PGM1 and the second contained likely homologs to human PGM2 [5].
• PGM2 and SOD1 could not be assigned [18].
• Variants were observed in ADA, PGM1 and PGM2 [19].
• Mitochondrial aconitate hydratase, alpha-glucosidase, glyceraldehyde-3-phosphate dehydrogenase, phosphogluconate dehydrogenase, and phosphoglucomutase-2 are unlinked to other loci [20].
• The corresponding alleles are designated AK1 3 Wayampi, PGM1 (4/10) Wayampi, PGM2 6 Wayampi, and TfD [21].

References