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Biliverdin reductase: more than a namesake - the reductase, its Peptide fragments, and biliverdin regulate activity of the three classes of protein kinase C.

Authors :
Gibbs PE
Tudor C
Maines MD
Source :
Frontiers in pharmacology [Front Pharmacol] 2012 Mar 13; Vol. 3, pp. 31. Date of Electronic Publication: 2012 Mar 13 (Print Publication: 2012).
Publication Year :
2012

Abstract

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.

Details

Language :
English
ISSN :
1663-9812
Volume :
3
Database :
MEDLINE
Journal :
Frontiers in pharmacology
Publication Type :
Academic Journal
Accession number :
22419908
Full Text :
https://doi.org/10.3389/fphar.2012.00031