The biliverdin reductase (BVR) isozymes BVRA and BVRB are cell surface membrane receptors with pleiotropic functions. This review compares, for the first time, the structural and functional differences between the isozymes. They reduce biliverdin, a byproduct of heme catabolism, to bilirubin, display kinase activity, and BVRA, but not BVRB, can act as a transcription factor. The binding motifs present in the BVR isozymes allow a wide range of interactions with components of metabolically important signaling pathways such as the insulin receptor kinase cascades, protein kinases (PKs), and inflammatory mediators. In addition, serum bilirubin levels have been negatively associated with abdominal obesity and hypertriglyceridemia. We discuss the roles of the BVR isozymes in metabolism and their potential as therapeutic targets.
|Number of pages||9|
|Journal||Trends in Endocrinology and Metabolism|
|State||Published - 2015|
Bibliographical noteFunding Information:
This work was supported by the National Institutes of Health (NIH) PRIDE grant (HL106365) (T.D.H.), grants from the National Heart, Lung, and Blood Institute [K01HL-125445 (T.D.H.), PO1HL-051971, HL088421 (D.E.S.), and 1T32HL105324 (P.A.H)], and the National Institute of General Medical Sciences (P20GM-104357).
© 2015 Elsevier Ltd.
- Biliverdin reductase
- Heme oxygenase
ASJC Scopus subject areas
- Endocrinology, Diabetes and Metabolism