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Mutational analysis is especially important in GIST because most GISTs are defined by activating mutations in the KIT or PDGFRA genes. Moreover, the response of GISTs to certain drug treatments varies according to the mutation status of the tumors.
Application of agents that inhibit NNMT binding to FGFR1 in tumor prevention and treatment
This invention provides the application of agents that inhibit NNMT binding to FGFR1 in the prevention and treatment of tumors. Through mutation analysis and interactomics analysis, it reveals a previously unknown, non-enzyme-dependent role of NNMT in promoting aerobic glycolysis in breast cancer. It discovers that NNMT binds to FGFR1 and acts as a scaffold protein, promoting phosphorylation of PKM2 and LDHA at Y105 and Y10 sites, respectively. By positioning the FGFR1 binding interface to the 140-154 amino acid region of NNMT, this invention designs a competitive cell-penetrating peptide, NNMT-15, which can disrupt the NNMT-FGFR1 interaction, reduce the phosphorylation levels of PKM2 and LDHA, inhibit glycolysis, and suppress proliferation in NNMT-high-expressing cancer cells and cancer-associated fibroblasts. These findings reveal NNMT as a dual-function metabolic regulator and establish the NNMT-FGFR1 scaffolding effect as a targeted therapeutic axis in glycolysis-dependent tumors.
Owner:THE AFFILIATED SIR RUN RUN SHAW HOSPITAL OF SCHOOL OF MEDICINE ZHEJIANG UNIV