Biliverdin reductase: A major physiologic cytoprotectant

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Biliverdin reductase: a major physiologic cytoprotectant.

Bilirubin, an abundant pigment that causes jaundice, has long lacked any clear physiologic role. It arises from enzymatic reduction by biliverdin reductase of biliverdin, a product of heme oxygenase activity. Bilirubin is a potent antioxidant that we show can protect cells from a 10,000-fold excess of H2O2. We report that bilirubin is a major physiologic antioxidant cytoprotectant. Thus, cellul...

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From the Cover: Biliverdin reductase: A major physiologic cytoprotectant

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Biliverdin-IXa Reductase and Biliverdin-IXP Reductase from Human Liver

This report describes for the first time the identification of four forms of biliverdin reductase including two biliverdin-MP reductases and two biliverdin-Ma reductases, designated isozymes I and I1 and isozymes I11 and IV, respectively, in human liver cytosolic fractions. The four forms of biliverdin reductase were purified to homogeneity. There was a 7,80&15,000-fold increase in specific act...

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Crystal Structure of Biliverdin Reductase

A heme (Fe-porphyrin complex) is a prosthetic group of hemoproteins such as hemoglobin, myoglobin, cytochromes and so on. In biological systems, the heme is decomposed by two enzymes (hemeoxygenase and biliverdin reductase) and excreted (Fig. 1). Biliverdin reductase (BVR) catalyzes the last step of the heme catabolism, in which the biliverdin is reduced into bilirubin with two electrons from N...

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Biliverdin reductase: a target for cancer therapy?

Biliverdin reductase (BVR) is a multifunctional protein that is the primary source of the potent antioxidant, bilirubin. BVR regulates activities/functions in the insulin/IGF-1/IRK/PI3K/MAPK pathways. Activation of certain kinases in these pathways is/are hallmark(s) of cancerous cells. The protein is a scaffold/bridge and intracellular transporter of kinases that regulate growth and proliferat...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2002

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.252626999