RB in glutamine metabolism.

Brian Clem

doi:10.18632/oncoscience.39

Abstract

RB in glutamine metabolism.

Highlights

In a majority of cancer cells, inactivation of the retinoblastoma protein through hyperphosphorylation, deletion, or mutation leads to dissociation from E2F effector proteins and aberrant activation of downstream target genes
Tumor cells predominantly exhibit a metabolic switch towards aerobic glycolysis, which is characterized by an increase in glucose catabolism to lactate at the expense of mitochondrial oxidation
This may be of increased significance in neoplastic cells harboring a dysfunctional RB pathway since pRB suppression has been reported to cause an E2F-1-mediated increase in mitochondrial oxidative capacity via activation of a myriad of genes including those responsible for mitochondrial respiration [2]

Summary

Introduction

In a majority of cancer cells, inactivation of the retinoblastoma protein (pRB) through hyperphosphorylation, deletion, or mutation leads to dissociation from E2F effector proteins and aberrant activation of downstream target genes. Tumor cells predominantly exhibit a metabolic switch towards aerobic glycolysis (the Warburg effect), which is characterized by an increase in glucose catabolism to lactate at the expense of mitochondrial oxidation. While several oncogenes, such as MYC and KRAS, have been reported to mediate glycolytic flux to lactate, Hsieh et al recently demonstrated that loss of pRB function resulted in inhibition of glucose oxidation within the tricarboxylic acid (TCA) cycle.

Results

Conclusion