2026-08-29T14:07:38Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/174062024-11-29T17:50:54Zcom_20.500.12105_2173com_20.500.12105_2051col_20.500.12105_19597
Repisalud
author
Kondoh, Hiroshi
author
Lleonart, Matilde E
author
Gil, Jesús
author
Wang, Jing
author
Degan, Paolo
author
Peters, Gordon
author
Martinez Garcia, Maria Dolores
author
Carnero, Amancio
author
Beach, David
funder
Wellcome Trust
2024-02-01T10:59:28Z
2024-02-01T10:59:28Z
2005-01-01
Cancer Res . 2005;65(1):177-85.
10.1158/0008-5472.177.65.1
0008-5472
Cancer research
15665293
http://hdl.handle.net/20.500.12105/17406
An unbiased screen for genes that can immortalize mouse embryonic fibroblasts identified the glycolytic enzyme phosphoglycerate mutase (PGM). A 2-fold increase in PGM activity enhances glycolytic flux, allows indefinite proliferation, and renders cells resistant to ras-induced arrest. Glucosephosphate isomerase, another glycolytic enzyme, displays similar activity and, conversely, depletion of PGM or glucosephosphate isomerase with short interfering RNA triggers premature senescence. Immortalized mouse embryonic fibroblasts and mouse embryonic stem cells display higher glycolytic flux and more resistance to oxidative damage than senescent cells. Because wild-type p53 down-regulates PGM, mutation of p53 can facilitate immortalization via effects on PGM levels and glycolysis.
eng
Glycolytic enzymes can modulate cellular life span.
journal article
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