Researchers Discover Sequence in HER2 Protein Responsible For Cancer Cell Proliferation

Researchers Discover Sequence in HER2 Protein Responsible For Cancer Cell Proliferation
In a new study entitled “Blockade of a Key Region in the Extracellular Domain Inhibits HER2 Dimerization and Signaling,” researchers discover a key sequence in HER2 protein that, once disrupted, shuts down HER2-mediated cancer signaling pathways. The study was published in the Journal of the National Cancer Institute. Breast cancer patients who express higher levels of human epidermal growth factor receptor 2 (HER2) exhibit poorer survival rates. As such, therapeutic strategies have focused on inhibiting HER2 activity, mostly via antibody targeting of HER2 protein extracellular domain, the place where signal transduction is initiated through dimerization with other receptors, over stimulating cells proliferation and growth. Trastuzumab (commercial name Herceptin) and pertuzumab, both HER2 monoclonal antibodies, and cetuximab, an inhibitor, are currently used as treatments for women with HER2-positive breast cancer. However, despite their demonstrated clinical benefits, the results are only partially effective and there is a need for novel therapeutic strategies. In this study, a team of researchers at Mayo Clinic led by Ruth Lupu, Ph.D. hypothesized that blocking HER2's capacity to bind and thus form dimers with other receptors could block tumor growth. This is a new approach, since the team hypothesized that HER2 carries a "functional site," i.e., a specific sequence through which HER2 binds
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