Research program member: Cancer Molecular Genetics
1101 E. Marshall St.
Richmond, VA 23298
Assistant Professor, Obstetrics and Gynecology, School of Medicine
PhD, University of Cincinnati (2002)
The cancer cells fate depends on the amounts of tumorigenic peptides presented on the cell surface for immune cells to recognize as foreign and eliminate. To successfully survive the host immune surveillance, the cancer cells have mastered in inhibiting pathways that could send the warning signals. One of the ways to revert this pathway is to introduce a hyper peptide processing enzyme called endoplasmic reticulum aminopeptidase 2 (ERAP2). The goal of our cancer research is to determine a novel mechanism to unveil the cancer cells to be recognized by the immune cells via ERAP2. This has a tremendous translation potential for targeting solid tumors that had unsuccessful treatment by immunotherapy alone. We can improve the immune recognition of tumors by complementing immunotherapy by increasing tumorigenic peptides by ERAP2. Using our existing knowledge of ERAP2, an enzyme that processes peptide to be presented on human leukocyte antigen (HLA) that alters immune response, to address the question how the cancer cells escape from immune surveillance or in reverse promote immune clearance by overexpressing or reactivating this enzyme.
ERAP2, peptide processing, HLA, choriocarcinoma, melanoma