Jeremy Craig, 404-413-1357
ATLANTA — Researchers at Georgia State University have discovered more about how enzymes work in cancer cells – work that expands our understanding of how scientists might be able to specifically target and kill cancer cells while avoiding the destruction of healthy tissues.
The team of scientists studied the mechanisms of a metabolism enzyme, pyruvate kinase 2 (PKM2), in the growth of cancer. Their new study shows that one type of structure of PKM2 proteins stimulates cancer growth.
One structure, the dimer of PKM2, was found by the researchers to promote cancer growth by acting as a regulator of gene expression. The two types of PKM2 structures differ.
The dimer structure consists of the two same proteins to form a complex of two proteins, which allow the complex to act as a protein kinase — an enzyme that modifies target proteins.
The other structure — the tetramer — consists of two dimers to form a complex of four proteins, which allows the complex act as the default enzyme in the metabolism of glucose. Glucose is the source of energy for cells.
Knowing which form helps to cause cancer growth allows scientists to better aim at destroying cancer cells.
The research was recently published in Molecular Cell. The team of scientists included Xueliang Gao, Haizhen Wang, Jenny Yang, Xiaowei Liu and Zhi-Ren Liu.
“This is a significant finding, because the protein kinase active dimer form is so unique to cancer, and it can be targeted,” said Zhi-Ren Liu, professor of cancer biology and a Georgia Cancer Coalition Distinguished Cancer Scholar. “These results are quite exciting, as this enzyme has been a ‘hot’ field of research for many years.”
The work was supported by the National Cancer Institute, the Georgia Cancer Coalition and a Molecular Basis of Disease fellowship from Georgia State.
The study is "Xueliang Gao, Haizhen Wang, Jenny J. Yang, Xiaowei Liu, Zhi-Ren Liu, Pyruvate Kinase M2 Regulates Gene Transcription by Acting as a Protein Kinase, Molecular Cell, ISSN 1097-2765, DOI: 10.1016/j.molcel.2012.01.001."
It is available online at http://www.sciencedirect.com/science/article/pii/S1097276512000032.
Feb. 10, 2012