Biochemical and immunological arguments for homoology between red cell and liver phosphoglyceromutase isozymes

Prehu, Marie-Odette; Calvin, Marie-Claude; Préhu, Claude; Rosa, R.J. Della

doi:10.1016/0167-4838(84)90319-4

Cited by 14 publications

(7 citation statements)

References 12 publications

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“…Phosphoglycerate mutase is a glycolytic enzyme that catalyses the interconversion of 3‐phosphoglycerate and 2‐phosphoglycerate (26). The brain form of phosphoglycerate mutase is found in brain, liver, kidney, erythrocytes, and early fetal skeletal muscle, while the muscle form of the enzyme is present in adult skeletal and cardiac muscle (27, 28). The down‐regulation of phosphoglycerate mutase in the cells with the altered metabolic state (i.e., low Δ L /Δ G ratio state) was somewhat surprising as it is not a key regulatory enzyme of the glycolytic pathway.…”

Section: Resultsmentioning

confidence: 99%

Proteomic Investigation of Metabolic Shift in Mammalian Cell Culture

et al. 2001

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Mammalian cells, under typical cultivation conditions, produce large quantities of lactate and ammonia that affect cell growth adversely and result in low cell concentration. Controlled nutrient feeding to maintain low concentrations of glucose and glutamine reduces metabolite production drastically, altering the metabolism of the cells. This metabolic shift results in higher cell concentration in continuous cultures and does not affect the specific productivity of the cells. We have taken a proteomics approach to investigate the differential protein expression with metabolic shift. Using two-dimensional gel electrophoresis (2-DE) and mass spectrometry (MS), we have found at least eight differentially expressed spots; two proteins were down-regulated, and the others were up-regulated with metabolic shift. These included metabolic enzymes, the brain form of phosphoglycerate mutase, which was down-regulated, and the precursor of the 23 kDa subunit of NADH-ubiquinone oxidoreductase, which was up-regulated. Another enzyme, the L1 isozyme of ubiquitin carboxyl-terminal hydrolase, which is involved in protein turnover and degradation, was also up-regulated in the metabolically altered cells. The remaining down-regulated spot had been identified as two isoforms of cytoplasmic actins, while three of the up-regulated spots were viral GAG polyproteins from various murine viruses. An unidentified protein was also up-regulated in the cells with altered metabolic state. This study shows the potential of using a proteomics approach in deciphering the intracellular changes in cells with physiological changes such as metabolism shift. The new insight into cell metabolism afforded by this analysis will greatly facilitate process optimization of continuous cell cultures.

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Section: Resultsmentioning

confidence: 99%

Proteomic Investigation of Metabolic Shift in Mammalian Cell Culture

et al. 2001

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Section: Discussionmentioning

confidence: 99%

“…Therefore, in adult mammals, mature sperm cells and skeletal muscle contain almost exclusively type MM-PGM, whereas type BB-PGM is found in most other tissues. Only in heart are the three PGM isoenzymes present in substantial amounts (Omenn and Cheung, 1974;Omenn and Hermodson, 1975;Rosa et al, 1975;Adamson, 1976;Edwards and Hopkinson, 1977;Carreras et al, 1981; Bartrons and Carreras, 1982;Prehu et al, 1984; Pons et al, 1985a,b;Fundele et al, 1987).In addition to PGM isoenzymes, in mammalian tissues there are three other enzyme proteins that have PGM-, BPGM-and 2-phosphoglycolate-stimulated BPGP activities, with a PGM-BPGP and a PGM-BPGM activity ratios lower than those of PGM isoenzymes. One of these enzymes is the 2,3-bisphosphoglycerate synthasephosphatase or 2,3-bisphosphoglycerate mutase (EC 5.4.2.4), which is a homodimer of a subunit that possesses great homology with PGM subunits (Sasaki et al, 1975;Kappel and Hass, 1976;Sasaki et al, 1976;Narita et al, 1979).…”

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confidence: 99%

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

Durany

Joseph²,

Campo³

et al. 1997

Br J Cancer

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SummaryWe have compared the levels of phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activities and the distribution of their isoenzymes in normal colon, liver and lung tissues, and in colon, liver and lung adenocarcinoma, lung squamous cell carcinoma and lung carcinoid. All tumours presented higher phosphoglycerate mutase and enolase activities and lower 2,3-bisphosphoglycerate phosphatase activity than the normal tissues. No changes were observed in the phosphoglycerate mutase isoenzyme patterns analysed by cellulose acetate electrophoresis. All specimens contained mainly type BB isoenzyme, traces of type MB isoenzyme and no type MM isoenzyme. However, the tumours had decreased levels of 2,3-bisphosphoglycerate mutase and 2,3-bisphosphoglycerate mutase-phosphoglycerate mutase hybrid enzyme. Determined by agarose gel electrophoresis, aa-enolase was the isoenzyme predominant in normal lung, colon and liver tissue, although ay-and yy-enolase were also present in all tissues. In colon, liver and non-endocrine lung tumours, the proportions of ay-and yy-enolase decreased. In contrast, in carcinoid tumours of the lung, the proportions of these isoenzymes increased.Keywords: 2,3-bisphosphoglycerate mutase; 2,3-bisphosphoglycerate phosphatase; enolase; phosphoglycerate mutase; isoenzyme; lung, colon and liver adenocarcinoma; lung squamous cell carcinoma; lung carcinoid Phosphoglycerate mutase (D-phosphoglycerate 2,3-phosphomutase, EC 5.4.2.1, PGM) and enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) are glycolytic enzymes that catalyse consecutive reversible reactions connecting the two ATP-generating reactions in the glycolytic pathway. PGM catalyses the conversion of 3-phosphoglycerate, product of the first ATP-generating reaction, into 2-phosphoglycerate in the presence of the cofactor 2,3-bisphosphoglycerate. Enolase catalyses the conversion of 2-phosphoglycerate into phosphoenolpyruvate, substrate of the second ATP-generating reaction. In addition to the main mutase activity, PGM possesses collateral 2,3-bisphosphoglycerate synthase or 2,3-bisphosphoglycerate mutase activity (BPGM: 1,3-bisphosphoglycerate + 3-phosphoglycerate -> 3-phosphoglycerate + 2,3-bisphosphoglycerate) and 2,3-bisphosphoglycerate phosphatase activity (BPGP: 2,3-bisphosphoglycerate --3-phosphoglycerate + Pi), which is stimulated by 2-phosphoglycolate (for reviews, see Fothergill-Gilmore and Watson, 1989;Wold, 1971).In mammalian tissues, there are three isoenzymes of PGM, which result from the homodimeric and the heterodimeric combinations of two different subunits coded by separate genes and designated M (muscle) and B (brain). In early fetal life, type BB-PGM is the only form present. During myogenesis, the isoenzyme phenotype undergoes transition, type BB-PGM being replaced by the MM-form, through the MB isoenzyme. In skeletal muscle, there is an almost complete transition from the BB-to the MM-PGM, but in heart muscle complete transition does not occur (Omenn and Cheung, Omenn and Hermodson, 1975;Adamson, 1...

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“…Mammals express isotypes B and M of cofactor‐dependent PGM (dPGM) genes,3–5 which form either homodimers MM and BB or heterodimer MB 3, 6. The B‐type dPGM (dPGM‐B) is found in the brain, liver, kidney, erythrocytes, and early fetal skeletal muscle, whereas the M‐type is present in adult skeletal and cardiac muscle 7, 8. Enolase is present in vertebrates in three isozymic forms: α, β, and γ 9, 10.…”

Section: Introductionmentioning

confidence: 99%

Molecular dynamics study of interaction and substrate channeling between neuron‐specific enolase and B‐type phosphoglycerate mutase

Hakobyan

Nazaryan

2010

Proteins

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Phosphoglycerate mutase (PGM) and enolase are consecutive enzymes in the glycolytic pathway. We used molecular dynamics simulation to examine the interaction of human B-type PGM (dPGM-B) and neuron-specific enolase (NSE). Specifically, we studied the interactions of 31 orientations of these enzymes by means of the effective energy function implicit solvation method. Interactions between active regions of the enzymes occurred preferentially, although the strongest interactions appeared to be between the back side of NSE and the active regions of dPGM-B. Cleavage of 2PG from dPGM-B was investigated, and the Ser(14)-Leu(30) loop of dPGM-B is suggested as a cleavage site and, likely, another entrance site of a ligand. Substrate channeling between the enzymes was observed when NSE with its active regions Leu(11)-Asn(16), Arg(49)-Lys(59), and Gly(155)-Ala(158) covered the Ser(14)-Leu(30) loop of dPGM-B. Analyses of the results make us believe that the channeling between PGM and enolase "benefits" from weak interaction. The probability of formation of channeling favorable complex is estimated to be up to 5%, while functional interaction between NSE and dPGM-B might be as high as 20%. NSE and dPGM-B functional interaction seems not to be isotype specific.

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Biochemical and immunological arguments for homoology between red cell and liver phosphoglyceromutase isozymes

Cited by 14 publications

References 12 publications

Proteomic Investigation of Metabolic Shift in Mammalian Cell Culture

Proteomic Investigation of Metabolic Shift in Mammalian Cell Culture

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

Molecular dynamics study of interaction and substrate channeling between neuron‐specific enolase and B‐type phosphoglycerate mutase

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