Phosphorylation of PKM2 at Y105 has been shown to inhibit its enzymatic activity, and a reduction in PK activity is widely believed to promote anabolic processes by shunting glucose metabolites toward the creation of biomass.17 Furthermore, PKM2, which is capable of undergoing allosteric regulation, is often expressed in normal proliferating cells and most cancer cells.47–51 In this study, we found that proliferating osteoclast progenitors (BMMs) expressed PKM2, and mature osteoclasts maintained PKM2 expression levels. The gene discussed is PKM; the disease is cancer.