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Sagot :
Enzymatic activation of pyruvate kinase increases cytosolic oxaloacetate to inhibit the Warburg effect is a research paper written by Elizabeth K Wiese, Sadae Hitosugi, Sharon T Loa, Annapoorna Sreedhar, Lindsey G Andres-Beck, Kiran Kurmi, Yuan-Ping Pang, Larry M Karnitz, Wilson I Gonsalves and Taro Hitosugi.
What is the abstract?
The PKM2 paradox in the Warburg effect is a phenomena whereby lactate generation is lowered following pharmacological stimulation of the glycolytic enzyme PKM2 or expression of the constitutively active PKM1 isoform in cancer cells. Here, we demonstrate that oxaloacetate (OAA) inhibits human lactate dehydrogenase A competitively, and that increased PKM2 activity boosts the de novo production of OAA by glutaminolysis, inhibiting LDHA in cancer cells. Furthermore, we demonstrate how the contradictory relationship between increased PKM2 activity and lower lactate concentration in cancer cells treated with a PKM2 activator was abolished by substituting human LDHA with rabbit LDHA, which is highly resistant to OAA inhibition. In addition, rabbit LDHA-expressing tumors were more resistant to the PKM2 activator than human LDHA-expressing tumors in mice.
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