PFKFB4, also known as6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4, is used in the synthesis of fructose 2,6-diphosphate and is widely present in various biological cells. PFKFB4 is highly expressed in brain, heart, liver, muscle, placenta, adipose tissue, ovary, fallopian tubes, and testis, and is overexpressed in human tumors, suggesting a potential role in the development and/or progression of cancer. PFKFB4 may be an effective molecular target for the development of antitumor drugs.
The team of Professor Bert O’Malley at Baylor College of Medicine cracked the mystery of the glycolysis energy supply in the cancerous aerobic environment. They discovered that the key fructokinase PFKFB4 in the process of glycolysis could even modify the protein! The enzyme can act on the transcriptional activator protein SRC-3, increase its transcriptional activity, and then become the accomplice of breast cancer cell proliferation and metastasis. The researchers found that ablation of PFKFB4 or SRC-3 in tumor tissue can almost completely eliminate the possibility of breast cancer recurrence and metastasis. The same effect was achieved by modifying SRC-3 so that it could not be modified by PFKFB4. Further studies have shown that PFKFB4 can add a phosphate group to serine at position 857 of SRC-3 protein, thereby increasing the transcriptional activity of SRC-3 and promoting the proliferation and metastasis of breast cancer. In the mouse model, the researchers found that if the PFKFB4 or SRC-3 in the tumor were removed, the recurrence and metastasis of the breast cancer could be almost completely eliminated. In addition, inhibition of phosphorylation of SRC-3 also has the same effect. These studies suggest that PFKFB4-mediated phosphorylation of SRC-3 is indeed the key to cancer induction, and it also provides two potential targets for the development of future cancer therapies.
Biobool has developed the ELISA kit for PFKFB4. Welcome to consult.
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