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Emerging roles of cytosolic phosphoenolpyruvate kinase 1 (PCK1) in cancer

Although it was traditionally believed that gluconeogenesis enzymes were absent from cancers that did not originate in gluconeogenic organs, numerous investigations have shown that they are functionally expressed in a variety of tumors as mediators of shortened forms of Gluconeogenesis. One of the i...

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Published in:Biochemistry and biophysics reports 2023-09, Vol.35, p.101528-101528, Article 101528
Main Authors: Abate, Ebsitu, Mehdi, Mohammed, Addisu, Sisay, Degef, Maria, Tebeje, Solomon, Kelemu, Tsehayneh
Format: Article
Language:English
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Summary:Although it was traditionally believed that gluconeogenesis enzymes were absent from cancers that did not originate in gluconeogenic organs, numerous investigations have shown that they are functionally expressed in a variety of tumors as mediators of shortened forms of Gluconeogenesis. One of the isomers of PEPCK, the first-rate limiting enzyme in gluconeogenesis, is PCK 1, which catalyzes the conversion of oxaloacetate (OAA) and GTP into PEP, CO2, and GDP. It is also known as PEPCK-C or PCK1, and it is cytosolic. Despite being paradoxical, it has been demonstrated that, in addition to its enzymatic role in normal metabolism, this enzyme also plays a role in tumors that arise in gluconeogenic and non-gluconeogenic organs. According to newly available research, it has metabolic and non-metabolic roles in tumor progression and development. Thus, this review will give insight into PCK1 relationship, function, and mechanism in or with different types of cancer using contemporary findings. •PCK 1 is one of the isomers of PEPCK.•PEPCK is the first-rate limiting enzyme of gluconeogenesis.•It catalyzes the conversion of oxaloacetate (OAA) and GTP into phosphoenolpyruvate (PEP) and CO2.•Some cancer cells use PCK1 as a novel metabolic regulator.•PCK1 has controversial role in cancer cells.•It has a tumor suppressor or oncogenic role in different types of human malignancies.
ISSN:2405-5808
2405-5808
DOI:10.1016/j.bbrep.2023.101528