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Cited by 183

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Nuclear Translocation of the Tumor Marker Pyruvate Kinase M2 Induces Programmed Cell Death

Open access
Steták, Attila, Veress, Réka, Ovádi, Judit, Csermely, Péter, Kéri, György, Ullrich, Axel·2007·Cancer Research

Abstract

Cancer cells often fail to respond to stimuli that normally activate their intrinsic apoptotic machinery. Moreover, they are able to adapt to hypoxia by changing their glycolytic rate. Pyruvate kinase (PK) is a rate-limiting enzyme in glycolysis that is converted to a less active dimer form of PKM2 isoenzyme during oncogenesis. Here, we show that both somatostatin and the structural analogue TT-232 interact with the PKM subtype. We further show that the PKM2 is translocated to the nucleus in response to TT-232 and different apoptotic agents. Nuclear translocation of PKM2 is sufficient to induce cell death that is caspase independent, isoform specific, and independent of its enzymatic activity. These results show that the tumor marker PKM2 plays a general role in caspase-independent cell death of tumor cells and thereby defines this glycolytic enzyme as a novel target for cancer therapy development. [Cancer Res 2007;67(4):1602–8]

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Metadata

Authors
Steták, A., Veress, R., Ovádi, J., Csermely, P., Kéri, G., & Ullrich, A.
Venue
Cancer Research
Published
2007-02-15
Volume
67
Issue
4
Pages
1602-1608
ISSN
  • 0008-5472 (ISSN-L)
  • 1538-7445
OpenAlex
W2091672398
Cited by
183
References
1
FWCI
3.95
Type
journal article
Language
en
Open access
bronze

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Steták, A., Veress, R., Ovádi, J., Csermely, P., Kéri, G., & Ullrich, A. (2007). Nuclear Translocation of the Tumor Marker Pyruvate Kinase M2 Induces Programmed Cell Death. Cancer Research. https://doi.org/10.1158/0008-5472.can-06-2870

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