| First Author | Blair D | Year | 2012 |
| Journal | Biochem J | Volume | 448 |
| Issue | 1 | Pages | 165-9 |
| PubMed ID | 22994860 | Mgi Jnum | J:191267 |
| Mgi Id | MGI:5461390 | Doi | 10.1042/BJ20121225 |
| Citation | Blair D, et al. (2012) Protein kinase Cbeta is critical for the metabolic switch to glycolysis following B-cell antigen receptor engagement. Biochem J 448(1):165-9 |
| abstractText | Signals derived from the BCR (B-cell antigen receptor) control survival, development and antigenic responses. One mechanism by which BCR signals may mediate these responses is by regulating cell metabolism. Indeed, the bioenergetic demands of naive B-cells increase following BCR engagement and are characterized by a metabolic switch to aerobic glycolysis; however, the signalling pathways involved in this metabolic reprogramming are poorly defined. The PKC (protein kinase C) family plays an integral role in B-cell survival and antigenic responses. Using pharmacological inhibition and mice deficient in PKCbeta, we demonstrate an essential role of PKCbeta in BCR-induced glycolysis in B-cells. In contrast, mice deficient in PKCdelta exhibit glycolytic rates comparable with those of wild-type B-cells following BCR cross-linking. The induction of several glycolytic genes following BCR engagement is impaired in PKCbeta-deficient B-cells. Moreover, blocking glycolysis results in decreased survival of B-cells despite BCR engagement. The results establish a definitive role for PKCbeta in the metabolic switch to glycolysis following BCR engagement of naive B-cells. |
