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Role of Mitochondrial Glycerol-3-Phosphate Dehydrogenase in Metabolic Adaptations of Prostate Cancer

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    SYSNO ASEP0532976
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleRole of Mitochondrial Glycerol-3-Phosphate Dehydrogenase in Metabolic Adaptations of Prostate Cancer
    Author(s) Pecinová, Alena (FGU-C) RID, ORCID, SAI
    Alán, Lukáš (FGU-C) RID, ORCID
    Brázdová, Andrea (FGU-C) ORCID, RID, SAI
    Vrbacký, Marek (FGU-C) RID, ORCID
    Pecina, Petr (FGU-C) RID, ORCID
    Drahota, Zdeněk (FGU-C) RID, ORCID
    Houštěk, Josef (FGU-C) RID, ORCID
    Mráček, Tomáš (FGU-C) RID, ORCID
    Article number1764
    Source TitleCells. - : MDPI
    Roč. 9, č. 8 (2020)
    Number of pages16 s.
    Languageeng - English
    CountryCH - Switzerland
    KeywordsGPD2 gene ; mitochondrial glycerol-3-phosphate dehydrogenase (EC:1.1.5.3) ; prostate cancer ; metabolic adaptation
    Subject RIVCE - Biochemistry
    OECD categoryBiochemistry and molecular biology
    R&D ProjectsGA16-12726S GA ČR - Czech Science Foundation (CSF)
    ED1.1.00/02.0109 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    Method of publishingOpen access
    Institutional supportFGU-C - RVO:67985823
    UT WOS000567281600001
    EID SCOPUS85088811124
    DOI10.3390/cells9081764
    AnnotationProstate cancer is one of the most prominent cancers diagnosed in males. Contrasting with other cancer types, glucose utilization is not increased in prostate carcinoma cells as they employ different metabolic adaptations involving mitochondria as a source of energy and intermediates required for rapid cell growth. In this regard, prostate cancer cells were associated with higher activity of mitochondrial glycerol-3-phosphate dehydrogenase (mGPDH), the key rate limiting component of the glycerophosphate shuttle, which connects mitochondrial and cytosolic processes and plays significant role in cellular bioenergetics. Our research focused on the role of mGPDH biogenesis and regulation in prostate cancer compared to healthy cells. We show that the 42 amino acid presequence is cleaved from N-terminus during mGPDH biogenesis. Only the processed form is part of the mGPDH dimer that is the prominent functional enzyme entity. We demonstrate that mGPDH overexpression enhances the wound healing ability in prostate cancer cells. As mGPDH is at the crossroad of glycolysis, lipogenesis and oxidative metabolism, regulation of its activity by intramitochondrial processing might represent rapid means of cellular metabolic adaptations.
    WorkplaceInstitute of Physiology
    ContactLucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400
    Year of Publishing2021
    Electronic addresshttps://www.mdpi.com/2073-4409/9/8/1764
Number of the records: 1  

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