Pyruvate carboxylase 

Pyruvate carboxylase is a key mitochondrial anaplerotic enzyme that catalyzes the conversion of pyruvate to oxaloacetate. Pyruvate carboxylase not only maintains tricarboxylic acid cycle activity and redox homeostasis, but also drives hepatic gluconeogenesis and fatty acid synthesis. The activity of Pyruvate carboxylase is upregulated in insulin-resistant states, exacerbating hepatic glucose production. Pyruvate carboxylase also shows significantly enhanced expression in early-stage non-small cell lung cancer (NSCLC). Pyruvate carboxylase promotes tumor proliferation by supporting nucleotide and lipid synthesis, and its functional deficiency cannot be compensated by glutaminolysis. Pyruvate carboxylase can be used in the research of prediabetes type 2 and NSCLC^[1][2].

Endogenous pyruvate carboxylase is significantly increased in the livers of high-fat diet-fed insulin-resistant mice, and its activity correlates linearly with the in vivo ¹³C label exchange rate k_pyr->asp^[1].
Pyruvate carboxylase suppression via shRNA slows non-small-cell lung cancer xenograft growth in NSG mice by 2-fold, reduces endpoint tumor weight by 30%, and impairs key metabolic pathways supporting tumor proliferation^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9014-19-1

[Pyruvate carboxylase]

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• [1]. Lee P, et al. In vivo hyperpolarized carbon‐13 magnetic resonance spectroscopy reveals increased pyruvate carboxylase flux in an insulin‐resistant mouse model[J]. Hepatology, 2013, 57(2): 515-524.

  [2]. Sellers K, et al. Pyruvate carboxylase is critical for non-small-cell lung cancer proliferation. J Clin Invest. 2015;125(2):687-698.  [Content Brief]