Disease relevance of PGM1

• METHODS: IHC was performed on cryostat sections of rheumatoid arthritis (RA) and osteoarthritis (OA) synovial membranes using the anti-CD68 mAbs KP1, EBM11, and PGM1, and the fibroblast (FB) markers CD90 and prolyl 4-hydroxylase [1].
• PGM1 revealed normal distribution of macrophages within histologically uninvolved areas and, in addition, also stained granulomas and large numbers of dendritic cells in the inflamed, ulcerated and scarred areas [2].
• Four group systems of serum proteins (Hp, Gc, Gm, Km) and five group systems of erythrocyte enzymes (AP, PGM1, GPT, AK, EsD) were determined in 63 patients with malignant lymphoma [3].
• Isoenzymes of hexokinase, 6-phosphogluconate dehydrogenase, phosphoglucomutase and lactate dehydrogenase in uterine cancer [4].
• Analysis of genetic variance for phosphoglucomutase at the PGM1 locus revealed a highly significant excess of the PGM1-1 phenotype in patients with cancer of the endometrium, which may reflect susceptibility to endometrial cancer in patients with this phenotype [4].

Psychiatry related information on PGM1

• Frequencies of serum groups (Hp and Gc) and red cell enzyme types (PGM1, 6-PGD and ES D) were studied in 195 patients with affective disorders [5].
• These results suggest that phosphoglucomutase activity may be significant in patients with bipolar disorder treated with lithium and carbamazepine [6].

High impact information on PGM1

• Phosphoglucomutase: evidence for a new locus expressed in human milk [7].
• Multiple cell lines derived from the same tumor had identical phosphoglucomutase enzyme phenotype, which suggested a lack of significant cross-contamination between the lines [8].
• Phosphoglucomutase, one of the previously uncharacterized thioredoxin-linked enzymes, has not earlier been considered a target for metabolic control through disulphide reduction [9].
• Data base searches of the deduced amino acid sequence showed that Paramecium parafusin had a 50.7% sequence identity to rabbit muscle phosphoglucomutase, although no detectable phosphoglucomutase activity has been detected in isolated parafusin [10].
• We have now analyzed the whole of the coding region of the human PGM1 gene by DNA sequencing in individuals of known PGM1 protein phenotype [11].

Chemical compound and disease context of PGM1

• Seventy-five isolates from the State of Campeche, Mexico, an area endemic for localized cutaneous leishmaniasis (LCL), were characterized by isoenzyme markers (glucose phosphate isomerase, mannose phospate isomerase, nucleoside hydrolase, phosphoglucomutase, 6-phosphogluconate dehydrogenase, and glucose-6-phosphate dehydrogenase) [12].
• Erythrocyte 6-phosphogluconate dehydrogenase A (PGDA) and phosphoglucomutase 1 (PGM1), phenotypes of unknown relevance to protection against falciparum malaria, were also significantly more prevalent in those claiming resistance to malaria [13].
• Infantile muscle glycogen storage disease: phosphoglucomutase deficiency with decreased muscle and serum carnitine levels [14].
• Role of phosphoglucomutase of Stenotrophomonas maltophilia in lipopolysaccharide biosynthesis, virulence, and antibiotic resistance [15].
• However, this is the first time that phosphoglucomutase has been identified as an important allergen involved in allergic reactions to lamb and beef [16].

Biological context of PGM1

• A physical localization of the human PGM1 gene to chromosome 1p31 has been determined by in situ hybridization [17].
• In 1964, when this genetic polymorphism was first described, two common allelozymes PGM1 and PGM1 2 were identified by starch gel electrophoresis [11].
• A comparison of the nucleotide sequences shows that the homologies between human and rabbit PGM1 mRNAs are 92% and 97% for the coding nucleotide sequence and the amino acid sequence, respectively [17].
• The charge changes predicted by these amino acid substitutions are entirely consistent with the charge intervals calculated from the isoelectric profiles of these four PGM1 isozymes [11].
• We have also used a population genetics approach to map the patterns of linkage disequilibrium across the PGM1 gene in three diverse population samples (Caucasian, Chinese and Vietnamese) [18].

Anatomical context of PGM1

• Significant positive correlations also were found with the following immunohistochemical parameters: PCNA in epithelial cells (r = 0.74) and tubular luminal cells (r = 0.47); tubular lumenal macrophages (r = 0.63) and tubular epithelial cells with acquired PGM1 staining (r = 0.36); and pyknotic tubular epithelial cells (r = 0.47) [19].
• Molecular and cytological investigations of phosphoglucomutase (PGM1) in the K562 cell line [20].
• In contrast, the PGM isozymes of human milk attributed to a fourth locus, PGM4, showed similar cross-reactivity as PGM1 suggesting close structural similarity [21].
• No PGM1 isoenzymes were found in the erythrocytes of the propositus, as demonstrated by the starch gel electrophoresis [22].
• Expression of the human adenylate kinase isozymes, phosphopyruvate hydratase, 6-phosphogluconate dehydrogenase, and phosphoglucomutase-1 in man-rodent somatic cell hybrids [23].

Associations of PGM1 with chemical compounds

• They also suggest a low probability of close linkage to ABO, Rh, Jk, Lu, AK1, PGM1 or C3 [24].
• Micromolar concentrations of fructose 1,6-P2 and glycerate 2,3-P2 inhibit both PGM1 and PGM2 isoenzymes to a similar extent [25].
• Two rapid and reliable electrophoretic techniques for PGM1 and EsD typing on ultrathin polyacrylamide gels are described [26].
• 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 [27].
• Phosphoglucomutase1 (PGM1) and 6-phosphogluconate dehydrogenase (PGD) types in the human hairbulb [28].

Physical interactions of PGM1

• In the reverse experiment, phosphoglucomutase bound to S100A1 and S100B-Sepharose in a calcium-dependent manner [29].

Regulatory relationships of PGM1

• In contrast, S100B stimulated phosphoglucomutase activity in a calcium-dependent manner [29].
• S100A1 inhibited phosphoglucomutase activity in a calcium-dependent manner [29].
• Identification of human calphoglin-induced phosphoglucomutase phosphorylation in Escherichia coli [30].

Other interactions of PGM1

• 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 [31].
• This is in direct conflict with the regional assignments of ACADM to 1p31 by in situ hybridization and of PGM1 to 1p22.1 by somatic cell studies [32].
• In addition, the well-known A variant of ACP1, the Duarte variant of GALT, the 2 variant of Hp and the 2 variant of PGM1 occurred in polymorphic proportions in all three tribes, and the TFDChi variant was present as a polymorphism in the Baniwa [33].
• The organisation of the PGM-RP gene is essentially identical to that of PGM1 [34].
• The gene frequencies observed are: PGM1/1: 0.715, AK1: 0.962 AND ADA1: 0.940 [35].

Analytical, diagnostic and therapeutic context of PGM1

• Review of isoelectric focusing for Gc, PGM1, Tf, and Pi subtypes: population distributions [36].
• Macrophage specificity of three anti-CD68 monoclonal antibodies (KP1, EBM11, and PGM1) widely used for immunohistochemistry and flow cytometry [1].
• Southern blot analysis using a PGM1 cDNA clone as probe suggested that the PGM1 genes had not been subject to any gross structural rearrangements [20].
• Very low levels of PGM1 mRNA which appeared to be full length transcripts were detected in K562 using a reverse transcriptase PCR technique [20].
• The PGM1 and PGM3 phenotypes were examined in extracts of chorionic tissue from 97 spontaneous and 266 induced abortions [37].

References