In human T-cell acute lymphoblastic leukemia (T-ALL), β-hydroxybutyrate dehydrogenase 1, the metabolic enzyme responsible for cell-autonomous BHB synthesis shows elevated protein expression without a corresponding increase at the mRNA level. We reasoned that BDH1 is deregulated is dysregulated post-transcriptionally and sought to identify the regulatory factors that sustain its aberrant protein expression.

In human T-cell acute lymphoblastic leukemia (T-ALL), β-hydroxybutyrate dehydrogenase 1, the metabolic enzyme responsible for cell-autonomous BHB synthesis shows elevated protein expression without a corresponding increase at the mRNA level. We reasoned that BDH1 is deregulated is dysregulated post-transcriptionally and sought to identify the regulatory factors that sustain its aberrant protein expression.To identify BDH1 interacting proteins, total cellular proteins extracted from T-ALL cells overexpressing either the pHAGE vector or pHAGE-BDH1 were subjected to immunoprecipitation and were subjected to LC-MS.