Protein modification discovery opens cancer therapy possibilities
Why it matters: This discovery offers a new pathway for cancer therapies, potentially improving treatments for common and rare cancers.
- W. Andy Tao's team discovered a new protein modification caused by mutations in the isocitrate dehydrogenase (IDH) enzyme, which is prevalent in cancers like glioma and acute myeloid leukemia.
- IDH mutation leads to the accumulation of D-2-hydroxyglutarate (D2HG), a metabolite that modifies proteins involved in tumor progression, suggesting a regulatory role in cancer development.
- The chirality of D2HG is a key factor in this modification, with the study also noting the accumulation of its mirror image, L2HG, in hypoxic tumor conditions, highlighting a previously overlooked aspect of metabolic reprogramming.
Purdue University researchers, led by W. Andy Tao, have uncovered a novel protein modification linked to cellular mutations that hinder a crucial enzyme's energy-driving capabilities. Published in Nature Chemistry, this discovery, stemming from IDH enzyme mutations common in various cancers, opens a promising new avenue for therapeutic cancer intervention.
