Disease relevance of Pgk1

• Two versions of the virus were made in which EGFP expression was driven either by the Rous sarcoma virus U3 enhancer or by a combination of sequences from the Syn1 and Pgk-1 promoters [1].
• A similar correlation was found for erythropoietin, phosphoglycerate kinase 1, and aldolase hypoxia response elements, which contain these respective 5' flanking bases [2].
• Lentiviral vectors coding for the first 171, 853, and 1520 amino acids of wild-type (19 CAG) or mutant htt (44, 66, and 82 CAG) driven by either the phosphoglycerate kinase 1 (PGK) or the cytomegalovirus (CMV) promoters were injected in rat striatum [3].

High impact information on Pgk1

• To this end, samples of phosphoglycerate kinase purified from skeletal muscle of young and old rats were unfolded by an 18-hr incubation in a 2 M guanidine hydrochloride solution at 4 degrees C, a treatment that results in extensive loss of the three-dimensional structure of the enzyme [4].
• Class III genes [gadd153, beta-actin, ubiquitin (UbC), phosphoglycerate kinase-1, C/EBP alpha, C/EBP beta] exhibit increased expression in response to amino acid limitation [5].
• Glucose-6-phosphate isomerase, phosphoglycerate kinase, enolase, lactate dehydrogenase, and most of triosephosphate isomerase remained unbound [6].
• Protection of phosphoglycerate kinase against in vitro aging by selective cysteine methylation [7].
• Recent studies have demonstrated that the aging effects in phosphoglycerate kinase (PGK) may be simulated in vitro by prolonged incubation of the enzyme under nonreducing conditions followed by reduction with excess 2-mercaptoethanol [7].

Biological context of Pgk1

• Cloning and cDNA sequence of the rat X-chromosome linked phosphoglycerate kinase [8].
• This cDNA, derived from an X-linked PGK gene transcript, contains a reading frame of 1254 nt and 5' and 3' non coding regions of 40 and 380 nt respectively [8].
• In some stocks the chromosomes carrying the tubulin and phosphoglycerate kinase genes are split into two bands, suggesting that homologous chromosomes may differ substantially in size in trypanosomes [9].
• The kinetics of heat inactivation, which differ markedly between young and old forms of phosphoglycerate kinase, were used as a sensitive probe for the status of the enzyme [10].

Anatomical context of Pgk1

• The N-terminal domain of phosphoglycerate kinase (N-PGK) and domain 1 of the T-cell adhesion protein CD2 (CD2.d1) fold through rapidly formed and transiently populated intermediate states in reactions which have no kinetic complications arising from proline isomerization or disulfide bonding [11].
• Hypoxic-G6PD induction was almost negligible in non-excitable Buffalo rat liver cells, although in these cells PGK1 was strongly upregulated by low PO(2) [12].
• Also unlike the glycolytic enzyme phosphoglycerate kinase, the glycogen metabolizing enzymes had a lower specific activity in synaptosomes than in particle free supernatant fractions of homogenates [13].
• As shown by means of a statistical approach, an increase in bisphosphoglycerate mutase activity and a slight decrease in phosphoglycerate kinase activity is found in erythroid cells as their haemoglobin content increases [14].
• After 1 wk of aortocaval shunt, the hearts were excised and the left ventricle and right ventricle were weighed and used for reverse transcriptase-polymerase chain reaction (RT-PCR) assays for ACE and phosphoglycerate kinase-1 (internal standard) [15].

Associations of Pgk1 with chemical compounds

• These findings strongly support the hypothesis that cysteine oxidation is an essential step in the aging of rat muscle phosphoglycerate kinase [7].
• Under these conditions only about one-quarter of the total triose phosphate dehydrogenase and phosphoglycerate kinase appears in the microsomal fraction [16].
• Loss of NH2- or COOH-terminal amino acids is not responsible for the observed differences in the properties of "young" and "old" muscle phosphoglycerate kinase [17].
• These included hexokinase, phosphofructokinase, aldolase, glyceraldehyde phosphate dehydrogenase, phosphoglycerate kinase, pyruvate kinase, glycerol phosphate dehydrogenase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and phosphorylase [18].
• PCr-dependent labelling, which required creatine kinase, resulted from a shift in the phosphoglycerate kinase equilibrium towards 1,3-bisphosphoglycerate (1,3-biPG) synthesis, ultimately resulting in an increase in available [2-32P]2,3-biPG [19].

Other interactions of Pgk1

• We conclude that, like enolase from aged nematodes, muscle phosphoglycerate kinase becomes altered in conformation in old rats [17].
• 2,3-biPG labelling from [gamma-32P]ATP occurred through the concerted action of phosphoglycerate kinase and 2,3-bisphosphoglycerate mutase [19].
• These three bands were subjected to MALDI-peptide mass fingerprint, showing similarities with phosphoglycerate kinase, elongation factor Tu and enolase molecules, respectively [20].
• Different glycolytic and oxidative capacities were calculated from the ratio of phosphoglycerate kinase and citrate synthase activities, ranging from 25 in m. soleus to 130 in m. tensor fasciae latae [21].

Analytical, diagnostic and therapeutic context of Pgk1

• This paper reports the isolation and the sequence determination of rat phosphoglycerate kinase (PGK) cDNA clones [8].
• Age-related modifications in rat cardiac phosphoglycerate kinase. Rejuvenation of the old enzyme by unfolding-refolding [22].

References