Results 41 to 50 of about 14,270 (217)

Revisiting glucose metabolism in cancer: lessons from a PKM knock-in model

open access: yesMolecular & Cellular Oncology, 2018
Isoform selection of pyruvate kinase M (PKM), a glycolytic enzyme, influences fates of glucose-derived carbons in cellular metabolic networks. We recently developed novel mouse lines to study PKM isoform function and identified PKM1 as a potential target
Taku Sato   +3 more
doaj   +1 more source

PKM2 functions as a histone kinase [PDF]

open access: yesCell Cycle, 2012
In the presence of oxygen, most differentiated cells generate the energy needed for cellular processes primarily by metabolizing glucose to carbon dioxide by oxidation of glycolytic pyruvate in the mitochondrial tricarboxylic acid cycle. When oxygen becomes limited, differentiated cells produce large amounts of lactate.
openaire   +3 more sources

Isoform-specific deletion of PKM2 constrains tumor initiation in a mouse model of soft tissue sarcoma

open access: yesCancer & Metabolism, 2018
Background Alternative splicing of the Pkm gene product generates the PKM1 and PKM2 isoforms of the glycolytic enzyme pyruvate kinase. PKM2 expression is associated with embryogenesis, tissue regeneration, and cancer.
Talya L. Dayton   +7 more
doaj   +1 more source

FOXM1D potentiates PKM2‐mediated tumor glycolysis and angiogenesis [PDF]

open access: yesMolecular Oncology, 2020
Tumor growth, especially in the late stage, requires adequate nutrients and rich vasculature, in which PKM2 plays a convergent role. It has been reported that PKM2, together with FOXM1D, is upregulated in late‐stage colorectal cancer and associated with metastasis; however, their underlying mechanism for promoting tumor progression remains elusive ...
Wei Zhang   +15 more
openaire   +5 more sources

PKM2, STAT3 and HIF-1α [PDF]

open access: yesJAK-STAT, 2012
The M2 isoform of pyruvate kinase, highly expressed in tumor cells, is known to engage a feed forward loop with the glycolysis master transcription factor HIF-1α. Gao and co-authors recently showed that dimeric PKM2 localizes to the nucleus in highly proliferating cancer cells, where it regulates in vivo growth by acting as a protein kinase and ...
DEMARIA, MARCO, POLI, Valeria
openaire   +2 more sources

Pyruvate Kinase M2 Mediates Glycolysis Contributes to Psoriasis by Promoting Keratinocyte Proliferation

open access: yesFrontiers in Pharmacology, 2021
Psoriasis is characterized by keratinocyte proliferation and immune cell infiltration. M2 isoform of pyruvate kinase (PKM2) was reported to have an important role in cell proliferation, which is a rate-limiting enzyme that regulates the final step of ...
Yun-zi Liu   +16 more
doaj   +1 more source

Research progress on the role of PKM2 in the immune response

open access: yesFrontiers in Immunology, 2022
Pyruvate kinase (PK) is a key enzyme that catalyzes the dephosphorylation of phosphoenolpyruvate (PEP) into pyruvate, and is responsible for the production of ATP during glycolysis. As another important isozyme of PK, pyruvate kinase M2 (PKM2) exists in cells with high levels of nucleic acid synthesis, such as normal proliferating cells (e.g ...
Chunyan Liu, Chenchen Liu, Rong Fu
openaire   +3 more sources

PKM2 is not required for colon cancer initiated by APC loss

open access: yesCancer & Metabolism, 2017
Background Cancer cells express the M2 isoform of the glycolytic enzyme pyruvate kinase (PKM2). PKM2 expression is not required for some cancers, and PKM2 loss can promote cancer progression; however, PKM2 has been reported to be essential in other tumor
Allison N. Lau   +10 more
doaj   +1 more source

Please Keep Me 2uned to PKM2 [PDF]

open access: yesMolecular Cell, 2014
In this issue of Molecular Cell, Keller et al. (2014) found that binding of the metabolite SAICAR to PKM2 induces the protein kinase activity of an enzyme normally designed to terminate the glycolytic pathway.
openaire   +3 more sources

Structural insight into mechanisms for dynamic regulation of PKM2 [PDF]

open access: yesProtein & Cell, 2015
Pyruvate kinase isoform M2 (PKM2) converts phosphoenolpyruvate (PEP) to pyruvate and plays an important role in cancer metabolism. Here, we show that post-translational modifications and a patient-derived mutation regulate pyruvate kinase activity of PKM2 through modulating the conformation of the PKM2 tetramer.
Yanhui Xu   +4 more
openaire   +3 more sources

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