Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase, creatine kinase and enolase activity and isoenzymes in breast carcinoma

Durany, Núria; Joseph, Joan; Jiménez, O.; Climent, F.; Fernández, Pilar; Rivera, Francisca; Carreras, José

doi:10.1054/bjoc.1999.0871

Cited by 73 publications

(64 citation statements)

References 56 publications

(76 reference statements)

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“…27 In addition, colorectal, liver, lung and breast carcinoma tissues contain mainly PGM-B and traces of PGM-MB and their PGM enzymatic activities are higher than those of adjacent normal tissues. 28,29 Brain tumours possessed lower PGM activity than normal brain. 30 In fibroblasts, exposure of the cells to hypoxia induces induction of PGM activity, concomitant with elevations of mRNA and the protein levels of PGM-B, indicating that the enzyme activity is regulated mainly at the transcriptional step.…”

Section: Discussionmentioning

confidence: 94%

Purification and identification of monoubiquitin-phosphoglycerate mutase B complex from human colorectal cancer tissues

et al. 2001

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Ubiquitin-conjugated proteins in human colorectal cancer tissues were analyzed by the immunoprecipitation with the antibody FK2 against conjugated ubiquitin followed with SDS-PAGE. In these immunoprecipitable proteins, a 38-kDa protein was abundant in the tumor regions but almost absent in the adjacent normal regions in 17/26 patients, thus we attempted to purify it. Using immunoaffinity chromatography with the antibody FK2 followed by gel filtration and SDS-PAGE, approximately 10 pmol of this protein was separated from 34 g of the pooled cancerous tissue and transferred onto a PVDF membrane. The 38-kDa protein was further digested with Achromobacter protease I, resulting in several peptide fragments. Amino acid sequences of these peptides showed complete sequence identity to those derived from either ubiquitin or phosphoglycerate mutase-B, suggesting that the 38-kDa protein is monoubiquitinated phosphoglycerate mutase-B, whose calculated mass is 37,369 Da. Western blot using an antibody against phosphoglycerate mutase-B revealed the presence of the 38-kDa protein in the anti-ubiquitin immunoprecipitates derived from the tumor regions, but not from normal counterparts. In addition, part of non-ubiquitinated phosphoglycerate mutase-B (29 kDa) was also found in the anti-ubiquitin immunoprecipitates, whose levels were higher in the tumor regions than in the adjacent normal regions. These results suggest that monoubiquitination of phosphoglycerate mutase-B as well as formation of a noncovalent complex containing ubiquitin and phosphoglycerate mutase-B increases in colorectal cancer and novel modification of phosphoglycerate mutase-B might have a pathophysiological role. © 2001 Wiley-Liss, Inc. Key words: phosphoglycerate mutase; monoubiquitination; affinity chromatography; immunoprecipitationThe eukaryotic modifier protein, ubiquitin is involved in degradation and regulation of intracellular substrate proteins. 1,2 This process involves multiple steps. 3,4 First, ubiquitin is activated by the ubiquitin-activating enzyme (E1). Second, 1 of ubiquitinconjugating enzymes (E2s) transfers ubiquitin from E1 to the substrate that is bound to 1 of ubiquitin-protein ligases (E3s). Third, these enzymes catalyze covalent attachment of ubiquitin to the protein substrate, forming the monoubiquitinated protein. In many cases, additional activated ubiquitin moieties are successively transferred to the previously conjugated ubiquitin molecule, forming a multiubiquitin chain adduct. Furthermore, the multiubiquitinated proteins are destined for degradation by 26S proteasome and this proteolytic machinery plays a fundamental role in various cellular events including cell-cycle progression 2,5,6 and apoptosis. 7,8 The monoubiquitin adducts have distinct functions, e.g., a trigger for endocytosis of plasma membrane proteins, thereby regulating growth factor-derived signal input. 9 The ubiquitin-mediated system is often the target of cancer-related deregulation and can underlie carcinogenesis processes 10 and its proteolytic activities ar...

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Section: Discussionmentioning

confidence: 94%

Purification and identification of monoubiquitin-phosphoglycerate mutase B complex from human colorectal cancer tissues

et al. 2001

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“…It has been recently shown that the oncogene P53 may regulate metabolic pathways by several novel genes, including PGAM. Also, PGAM expression levels are altered in brain, colon, breast, lung and liver cancers [6,9,8,7].…”

Section: Important Features For Lymphoma Datamentioning

confidence: 99%

Understanding microarray data through applying competent program evolution

Looks

Goertzel²,

Coelho³

et al. 2007

Proceedings of the 9th Annual Conference on Genetic and Evolutionary Computation

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A number of researchers have used genetic programming (GP) to analyze gene expression microarray data; here it is asked whether the use of an alternate program evolution technique, MOSES (meta-optimizing semantic evolutionary search), can improve upon GP's results in this domain. Based on our results so far, the answer appears to be a resounding yes. We first consider standard supervised classification for two microarray datasets: one involving aging vs. young brains, and the other involving lymphoma types. On these datasets, MOSES is shown to learn classifiers with test accuracies comparable to those obtained by SVMs, and significantly superior to those of GP with a similar configuration (and even more superior to those of GP run under a more standard configuration). Furthermore, unlike SVMs, the classification rules produced by MOSES are still simple and comprehensible to humans -often strikingly simple. Finally, biological interpretation is presented regarding the "important genes" used most often in the ensemble of MOSES models learned; we show that many of the genes identified in this way reflect knowledge available in the literature, and others constitute plausible hypotheses.

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“…is overexpressed in many cancers including lung, colon, liver and breast (Durany et al, 2000;Durany et al, 1997).…”

mentioning

confidence: 99%

Glucose Metabolism and Cancer

Zheng¹,

Li²,

Luo³

2012

Biochemistry

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Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase, creatine kinase and enolase activity and isoenzymes in breast carcinoma

Cited by 73 publications

References 56 publications

Purification and identification of monoubiquitin-phosphoglycerate mutase B complex from human colorectal cancer tissues

Purification and identification of monoubiquitin-phosphoglycerate mutase B complex from human colorectal cancer tissues

Understanding microarray data through applying competent program evolution

Glucose Metabolism and Cancer

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