Biliverdin Reductase-A Deficiency Brighten and Sensitize Biliverdin-binding Chromoproteins
Tissue absorbance, light scattering, and autofluorescence are significantly lower in the near-infrared (NIR) range than in the visible range. Because of these advantages, NIR fluorescent proteins (FPs) are in high demand for in vivo imaging. Nevertheless, application of NIR FPs such as iRFP is still limited due to their dimness in mammalian cells.
Sumiyama, Kenta +5 more
openaire +5 more sources
Reduction of biliverdin and placental transfer of bilirubin and biliverdin in the pregnant guinea pig [PDF]
Biliverdin was reduced to bilirubin in pregnant and foetal guinea pigs, and the 100000 g supernatant from homogenates of foetal liver, placenta and maternal liver showed high biliverdin reductase activity. The placental transport of unconjugated bilirubin and biliverdin was compared by injecting unlabelled and radiolabelled pigments into the foetal or ...
A F, McDonagh, L A, Palma, R, Schmid
openaire +2 more sources
Study of fluorescent labelled bilirubine preparation [PDF]
Heme is a prosthetic group containing iron atom at the center of the tetrapyrrole cycle, which is the part of hemoglobin. Heme is metabolized by heme oxygenase to linear tetrapyrrolic pigment - biliverdine.
Dejmková, Veronika
core +1 more source
High-level expression of Myrothecium verrucaria bilirubin oxidase in Pichia pastoris, and its facile purification and characterization [PDF]
Bilirubin oxidase (BO) from Myrothecium verrucaria (authentic BO) catalyzing the oxidation of bilirubin to biliverdine was overexpressed in the methylotrophic yeast, Pichia pastoris. The cDNA encoding BO was cloned into the P.
15131 +10 more
core +1 more source
Biliverdine-Based Metalloradicals: Sterically Enhanced Noninnocence
This is a first density functional theory survey of transition-metal biliverdines (Blv), where we have chosen to focus on key Mn, Fe, Co, and Cu complexes.
Ingar Wasbotten (2538061) +1 more
core +1 more source
Biliverdin reductase isozymes in metabolism [PDF]
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 ...
Luke, O'Brien +4 more
openaire +2 more sources
Cycling the Wagons for Biliverdin Reductase [PDF]
This letter was prompted by our reading of the article by Maghzal et al. (1). Bilirubin (BR) is a major physiologic antioxidant cytoprotectant. Tissue levels are only in nanomolar concentrations, because high levels are neurotoxic, yet BR protects against micromolar levels of oxidants because of a cycle wherein biliverdin (BV) generated by BR ...
Thomas W, Sedlak, Solomon H, Snyder
openaire +2 more sources
Heme oxygenase substrates acutely lower blood pressure in hypertensive rats
Heme oxygenase catalyzes the metabolism of heme to biliverdine, free iron, and carbon monoxide. The current study was designed to determine if treatment with the heme oxygenase substrates heme-L-arginate or heme-L-lysinate, to stimulate formation of ...
M. Lavesa +4 more
core +1 more source
Biliverdin inhibits activation of NF‐κB: Reversal of inhibition by human biliverdin reductase [PDF]
AbstracthBVR functions in the cell as a reductase and as a kinase. In the first capacity, it reduces biliverdin, the product of HO activity, to the effective intracellular antioxidant, bilirubin; as a dual‐specificity kinase (S/T/Y) it activates the MAPK and IGF/IRK receptor signal transduction pathways. NF‐κB and the MAPK pathway are activated by ROS,
Peter E M, Gibbs, Mahin D, Maines
openaire +2 more sources
Typical change trends based on differential metabolite classes.
A. elevated change trend of arachidonic acid (free fatty acid). B. elevated change trend of hexanoylcarnitine (acylcarnitine). C. elevated change trend of glucosylceramide (sphingolipid). D. elevated change trend of cortisol (steroid hormone).
Steven R. Tannenbaum (116488) +7 more
core +1 more source

