BCATs: Metabolic Regulators of Inflammation and Cancer Progression

Recombinant Human BCAT1 and BCAT2 are now available!

Branched-chain-amino-acid aminotransferases (BCATs) are enzymes that catalyze the first reaction in the catabolism of the essential branched-chain amino acids leucine, isoleucine, and valine to their respective keto-acids while producing glutamate.

Recombinant Human BCATs are measured by their ability to convert leucine and alpha-ketoglutarate to alpha-ketoisocaproate and glutamate through an enzymatically coupled assay. Using this assay system, Recombinant Human BCAT1 (Catalog # 9536-BA; blue, left) has approximately 2X higher turnover and specific activity than BCAT2 (Catalog # 9537-BA; blue, right) as described previously. Negative controls are shown in green and red.

There are two BCAT isozymes in humans, a mitochondrial form known as BCATm or BCAT2 and a cytosolic form known as BCATc or BCAT1. Both enzymes are regulated by redox and implicated as markers for oxidative stress linked to Alzheimer’s disease and dementia (1-3). More recently BCATc has been shown to cause cell proliferation in cancer (4-7) and was recently described as a diagnostic marker in cancers (8-10). In addition, two recent high-profile papers have linked BCAT activity to tumor metabolism and inflammatory disease (11,12). These studies suggest that BCATs may be novel drug targets for both cancer and inflammatory disorders.

References

1. Coles, S.J. et al (2012) Acta. Biochim. Biophys. Sin. 44:172.
2. El Hindy, M. et al (2014) Antioxid Redox Signal 20:2497.
3. Ashby, E.L. et al (2017) Neurochem. Res. 42:306.
4. Tonjes, M. et al (2013). Nature Medicine 19: 901.
5. Zhang, L. and J. Han (2017) Biochem. Biophys. Res. Commun. 486:224.
6. Zhu, W. et al (2017) Mol. Carcinog. 56:1570.
7. Zheng, Y.H. et al (2016) Liver Int. 36:1836.
8. Young, G.P. et al (2016) Cancer Med. 5:2763.
9. Pedersen, S.K. (2015) BMC Cancer. 15:654.
10. Diaz-Lagares, A. et al (2016) Clin Cancer Res. 22:3361.
11. Hattori, A. et al (2017) Nature 545:500.
12. Papathanassiu, A.E. et al (2017) Nature Commun. 8:16040. doi: 10.1038/ncomms16040.