Disease relevance of Pgam1

• Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity [1].
• Among the identified proteins, apolipoprotein A-IV may protect lipid peroxidation and atherosclerosis induced by TCDD exposure and the expression level of phosphoglycerate mutase increases due to hyperthyroidism induced by TCDD exposure [2].

High impact information on Pgam1

• Active site sequences of phosphoglycerate mutase and bisphosphoglycerate synthase were highly homologous with the active site of fructose-2,6-bisphosphatase implying a structural similarity and a common evolutionary origin [3].
• Glycolytic enzymes were more active in spermatozoa than in epididymal tissue, being more than 10 times as active in the case of hexokinase, phosphoglycerate kinase and phosphoglycerate mutase [4].
• Extensive oxidation was detected in the hippocampus where we identified 14-3-3 zeta, beta-synuclein, pyruvate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, and phosphoglycerate mutase 1 [5].
• In non-differentiating satellite cells only PGAM-B mRNA was detected, but when cells were differentiated into myotubes, which undergo spontaneous contraction, mRNA for PGAM-M muscle-specific isozyme was also detected [6].
• This finding is in perfect concordance with the transition of PGAM isozymes encountered in the same cell cultures, and strongly supports a transcriptional control of PGAM expression throughout myogenesis independently of nerve influence [6].

Biological context of Pgam1

• A cDNA probe, synthesized by the polymerase chain reaction (PCR) from rat liver cell mRNA using mixed primers specific to the amino acid sequence of human PGAM-B, was used to screen a rat liver cell cDNA library [7].
• cDNA encoding type B subunit of rat phosphoglycerate mutase: its isolation and nucleotide sequence [7].
• Active site sequence of hepatic fructose-2,6-bisphosphatase. Homology in primary structure with phosphoglycerate mutase [3].
• We further investigated the regulatory level(s) at which PGAM-M gene expression is controlled during hindlimb unweighting [8].
• Furthermore, the proximal 400 bp of the PGAM-M promoter contains cis-acting sequences to allow muscle-type-specific expression of a reporter gene and responsiveness to soleus muscle unweighting [8].

Anatomical context of Pgam1

• Location of phosphoglycerate mutase in rat skeletal muscle. An immunocytochemical and biochemical study [9].
• PGAM-M expression is regulated pretranslationally in hindlimb muscles and under altered loading conditions [8].
• Except for PGM, all enzymes showed an increase in total activity, in response to estrogen, in uterus but not in whole brain [10].
• Hypoxia-induced expression of phosphoglycerate mutase B in fibroblasts [11].
• Triiodothyronine (T3) increases phosphoglycerate mutase (PGAM) specific activity in rat skeletal and cardiac muscles [12].

Associations of Pgam1 with chemical compounds

• The deduced amino acid sequence of rat PGAM-B was identical to that of human PGAM-B except for only one substitution at position 251 near the carboxyl terminus (valine for the rat and alanine for the human) [7].
• The 29 kDa protein was identified as phosphoglycerate mutase (PGM), phosphorylated at the active-site histidine residue by 2,3-bisphosphoglycerate (2,3-biPG) [13].
• We studied the effect of electrical stimulation and a sodium channel blocker (tetrodotoxin) on the expression of muscle-specific isozymes of creatine kinase, glycogen phosphorylase, phosphoglycerate mutase, and lactate dehydrogenase in aneurally cultured embryonic rat muscle [14].
• Poly(A)+ mRNA was isolated from rat satellite cell cultures and analyzed by Northern blot analyses for mRNA content of phosphoglycerate mutase (PGAM) isozymes [6].
• CONCLUSION: Thyroid hormone influences PGAM mRNA isozyme levels differently and increases type M mRNA [15].

Analytical, diagnostic and therapeutic context of Pgam1

• Expression of phosphoglycerate mutase mRNA in differentiating rat satellite cell cultures [6].
• The hypothesis that PGAM-M is regulated pretranslationally among muscles of the hindlimb was tested using enzymatic assays, Western blots, and Northern blots [8].
• The subcellular distribution of phosphoglycerate mutase was studied by immunogold techniques [9].
• Only one immunoreactive nuclear band was observed by Western blot experiments and corresponded to that of phosphoglycerate mutase mobility [9].
• Northern blot and in situ hybridization experiments show that in contrast to what happens during skeletal-muscle differentiation, PGAM-M gene expression during spermatogenesis is not coupled to constitutive phosphoglycerate mutase (PGAM-B) gene repression [16].

References