Pyruvate Kinase in Selected Human Tumors

Staal, Gerard E.J.; Rijksen, Gert

doi:10.1016/b978-0-12-564498-3.50013-3

Cited by 13 publications

(8 citation statements)

References 56 publications

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“…A number of studies have shown that extracellular chaperonin 10 is associated with various cancers. − ,− Evidence suggests that the extracellular form of chaperonin 10, homologous to the intramitochondrial heat-shock protein, is produced by a separate gene. , This extracellular protein was first discovered as “early pregnancy factor” and was found to be released from the placenta into the blood stream within 6 h of conception. , Our analyses show that extracellular chaperonin 10 carries two post-translational modifications at the N-terminus. , Extracellular chaperonin 10 probably functions as an immunosuppressant 41 and a growth factor in neoplastic cell proliferation. PK-M2 is expressed selectively in metastatic cells, − primarily in its dimeric form. The only expression in healthy tissues is the lung in which PK-M2 is present in the active tetrameric form. , The dimer, but not the tetramer, shows strong immunochemical staining with monoclonal antibodies against PK-M2 .…”

Section: Resultsmentioning

confidence: 99%

“…35,42 Extracellular chaperonin 10 probably functions as an immunosuppressant 41 and a growth factor 43 in neoplastic cell proliferation. PK-M2 is expressed selectively in metastatic cells, [44][45][46][47] primarily in its dimeric form. The only expression in healthy tissues is the lung in which PK-M2 is present in the active tetrameric form.…”

Section: Identification Of Proteins Known To Be Associated With Cancersmentioning

confidence: 99%

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Identification of Candidate Biomarker Proteins Released by Human Endometrial and Cervical Cancer Cells Using Two-Dimensional Liquid Chromatography/Tandem Mass Spectrometry

DeSouza

Ghanny

et al. 2007

J. Proteome Res.

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Section: Resultsmentioning

confidence: 99%

Section: Identification Of Proteins Known To Be Associated With Cancersmentioning

confidence: 99%

Identification of Candidate Biomarker Proteins Released by Human Endometrial and Cervical Cancer Cells Using Two-Dimensional Liquid Chromatography/Tandem Mass Spectrometry

DeSouza

Ghanny

et al. 2007

J. Proteome Res.

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“… 2 – 8 The type M1 and M2 pyruvate kinase isoenzymes are different splice products from the same mRNA transcript, resulting in a difference of 21 amino acids. 9 , 10 Pyruvate kinase M2 (PKM2) has been proposed to be a candidate oncogene that is upregulated in several cancers, including renal cell carcinoma (RCC), 11 , 12 ovarian cancer, 13 , 14 breast cancer, 15 , 16 and lung cancer. 17…”

Section: Introductionmentioning

confidence: 99%

Expression of pyruvate kinase M2 in human bladder cancer and its correlation with clinical parameters and prognosis

Huang¹,

Huang²,

Bai³

et al. 2018

OTT

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BackgroundPyruvate kinase M2 (PKM2) is a key regulator of the Warburg effect and has critical functions in glycolysis, contributing to the Warburg effect, tumor growth, angiogenesis, cell division, metastasis, and apoptosis. The high expression of PKM2 in various solid tumors renders it a potential biomarker of tumorigenesis and tumor invasion, but the expression and role of PKM2 in bladder cancer have not been studied extensively.Patients and methodsWestern blot and immunohistochemistry (IHC) were used to measure the expression of PKM2, and quantitative real-time polymerase chain reaction (PCR) was performed to determine PKM2 mRNA levels. The relationships between PKM2 expression and clinicopathological parameters and prognosis were analyzed using the Kaplan–Meier plots and a Cox proportional hazards regression model.ResultsCompared with paired adjacent normal bladder tissues, PKM2 mRNA and protein levels were found to be higher in urothelial carcinoma of the bladder (UCB) samples by real-time PCR and Western blot. By IHC, high expression of PKM2 was seen in 117 of 215 UCBs (54.4%) and in eight of 90 adjacent normal bladder tissues (8.9%). The expression of PKM2 was significantly associated with grade, stage, and lymph node status (P<0.001). In the univariate survival analysis, a significant association between PKM2 expression and shorter patient survival was observed (P<0.001). In different subsets of UCB patients, we found that PKM2 expression was a prognostic factor in patients with G2 (P=0.009), G3 (P<0.001), pTa/pTis (P=0.006), pT1, pT2–4, and pN− disease (P<0.001). Importantly, PKM2 expression (P=0.003), with tumor histological grade (P<0.001), pT (P<0.001), and pN status (P=0.005), was a significant independent prognostic parameter in the multivariate analysis.ConclusionPKM2 protein and mRNA are upregulated in UCBs and may serve as molecular markers for a poor prognosis in patients with UCB.

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“…Biochem. 107: 293-302, 2009. ß 2009 KEY WORDS: GLYCOLYSIS; PYRUVATE KINASE; PKM2; SUMO-E3 LIGASE; PIAS3; SUMOYLATION P yruvate kinase (PK, ATP/pyruvate O'-phosphotransferase, EC 2.7.1.40) is one of the rate-controlling glycolytic enzymes that catalyze the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, to generate pyruvate and ATP [Staal and Rijksen, 1991]. Four distinct pyruvate kinase isoenzymes (L, R, M1, and M2) occur in mammalian cells.…”

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confidence: 99%

The SUMO‐E3 ligase PIAS3 targets pyruvate kinase M2

Spoden

Morandell

Ehehalt

et al. 2009

J of Cellular Biochemistry

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Pyruvate kinase M2 (M2-PK) controls the rate-limiting step at the end of the glycolytic pathway in normal proliferating and tumor cells. Other functions of M2-PK in addition to its role in glycolysis are little understood. The aim of this study was to identify new cellular interaction partners of M2-PK in order to discover novel links between M2-PK and cellular functions. Here we show that the SUMO-E3 ligase protein PIAS3 (inhibitor of activated STAT3) physically interacts with M2-PK and its isoenzyme M1-PK. Moreover, we demonstrate that endogenous SUMO-1-M2-PK conjugates exist in mammalian cells. Furthermore, we show that transient expression of PIAS3 but not the RING domain mutant PIAS3 (C299S, H301A) is consistent with nuclear localization of M2-PK and PIAS3 and M2-PK partially co-localize in the nucleus of these cells. This study suggests a link between PIAS3 and nuclear pyruvate kinase.

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Pyruvate Kinase in Selected Human Tumors

Cited by 13 publications

References 56 publications

Identification of Candidate Biomarker Proteins Released by Human Endometrial and Cervical Cancer Cells Using Two-Dimensional Liquid Chromatography/Tandem Mass Spectrometry

Identification of Candidate Biomarker Proteins Released by Human Endometrial and Cervical Cancer Cells Using Two-Dimensional Liquid Chromatography/Tandem Mass Spectrometry

Expression of pyruvate kinase M2 in human bladder cancer and its correlation with clinical parameters and prognosis

The SUMO‐E3 ligase PIAS3 targets pyruvate kinase M2

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