2026-05-29T23:28:52Zhttps://riuma.uma.es/rest/oai/requestoai:riuma.uma.es:10630/328362026-02-03T11:23:11Zcom_10630_2254col_10630_37953
Nuclear Translocation of Glutaminase GLS2 in Human Cancer Cells Associates with Proliferation Arrest and Differentiation
López de la Oliva, Amada
Campos-Sandoval, José A.
Gómez-García, María Carmen
Cardona, Carolina
Martín-Rufián, Mercedes
Sialana, Fernando J.
Castilla, Laura
Bae, Narkhyun
Lobo, Carolina
Peñalver, Ana
García-Frutos, Marina
Carro, David
Enrique, Victoria
Paz-Gutiérrez, José Carlos
Mirmira, Raghavendra G.
Gutiérrez, Antonia
Alonso-Carrión, Francisco José
Segura-Checa, Juan Antonio
Mates-Sánchez, José Manuel
Lubec, Gert
Márquez-Gómez, Javier
Glutaminasa
Glutaminase (GA) catalyzes the first step in mitochondrial glutaminolysis playing a key role in cancer
metabolic reprogramming. Humans express two types of GA isoforms: GLS and GLS2. GLS isozymes
have been consistently related to cell proliferation, but the role of GLS2 in cancer remains poorly
understood. GLS2 is repressed in many tumor cells and a better understanding of its function in
tumorigenesis may further the development of new therapeutic approaches. We analyzed GLS2
expression in HCC, GBM and neuroblastoma cells, as well as in monkey COS-7 cells. We studied GLS2
expression after induction of differentiation with phorbol ester (PMA) and transduction with the fulllength
cDNA of GLS2. In parallel, we investigated cell cycle progression and levels of p53, p21 and c-Myc
proteins. Using the baculovirus system, human GLS2 protein was overexpressed, purified and analyzed
for posttranslational modifications employing a proteomics LC-MS/MS platform. We have demonstrated
a dual targeting of GLS2 in human cancer cells.
2024-09-23T09:42:20Z
2024-09-23T09:42:20Z
2020-02-10
journal article
https://hdl.handle.net/10630/32836
10.1038/s41598-020-58264-4
eng
http://creativecommons.org/licenses/by-nc-nd/4.0/
open access
Attribution-NonCommercial-NoDerivatives 4.0 Internacional
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