Biliverdin reductase: more than a namesake – the reductase, its peptide fragments, and biliverdin regulate activity of the three classes of protein kinase C
- 1 Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, NY, USA
- 2 Max Planck Institute for Immunobiology and Epigenetics, Freiburg, Germany
The expanse of human biliverdin reductase (hBVR) functions in the cells is arguably unmatched by any single protein. hBVR is a Ser/Thr/Tyr-kinase, a scaffold protein, a transcription factor, and an intracellular transporter of gene regulators. hBVR is an upstream activator of the insulin/IGF-1 signaling pathway and of protein kinase C (PKC) kinases in the two major arms of the pathway. In addition, it is the sole means for generating the antioxidant bilirubin-IXα. hBVR is essential for activation of ERK1/2 kinases by upstream MAPKK-MEK and by PKCδ, as well as the nuclear import and export of ERK1/2. Small fragments of hBVR are potent activators and inhibitors of the ERK kinases and PKCs: as such, they suggest the potential application of BVR-based technology in therapeutic settings. Presently, we have reviewed the function of hBVR in cell signaling with an emphasis on regulation of PKCδ activity.
Keywords: biliverdin reductase, protein kinase C, signaling pathways, peptides, biliverdin
Citation: Gibbs PEM, Tudor C and Maines MD (2012) Biliverdin reductase: more than a namesake – the reductase, its peptide fragments, and biliverdin regulate activity of the three classes of protein kinase C. Front. Pharmacol. 3:31. doi: 10.3389/fphar.2012.00031
Received: 05 February 2012; Accepted: 16 February 2012;
Published online: 13 March 2012.
Copyright: © 2012 Gibbs, Tudor and Maines. This is an open-access article distributed under the terms of the Creative Commons Attribution Non Commercial License, which permits non-commercial use, distribution, and reproduction in other forums, provided the original authors and source are credited.
*Correspondence: Mahin. D. Maines, Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Rochester, NY 14624, USA. e-mail: email@example.com