Sn-protoporphyrin lowers serum bilirubin levels, decreases biliary bilirubin output, enhances biliary heme excretion and potently inhibits hepatic heme oxygenase activity in normal human subjects

Hepatology ◽  
1988 ◽  
Vol 8 (3) ◽  
pp. 625-631 ◽  
Author(s):  
Lars Berglund ◽  
Bo Angelin ◽  
Rolf Blomstrand ◽  
George Drummond ◽  
Attallah Kappas
Keyword(s):  
Heme Oxygenase ◽  
Serum Bilirubin ◽  
Human Subjects ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity ◽  
Normal Human

scholarly journals Suppression of hyperbilirubinemia in the rat neonate by chromium-protoporphyrin. Interactions of metalloporphyrins with microsomal heme oxygenase of human spleen.

1982 ◽  
Vol 156 (6) ◽  
pp. 1878-1883 ◽  
Author(s):  
G S Drummond ◽  
A Kappas
Keyword(s):  
Single Dose ◽  
Heme Oxygenase ◽  
Competitive Inhibitor ◽  
Bile Pigment ◽  
Human Spleen ◽  
Oxidation Activity ◽  
Heme Oxygenase Activity ◽  
Heme Degradation ◽  
Oxygenase Activity ◽  
Liver And Kidney

The synthetic metalloporphyrin, Cr-protoporphyrin, as a potent competitive inhibitor of heme oxygenase activity in rat spleen, liver, and kidney. When administered to neonatal animals in a single dose immediately after birth, Cr-protoporphyrin suppresses postnatal hyperbilirubinemia and produces a marked and sustained lowering of heme oxidation activity in liver, spleen, and kidney. The metalloporphyrin also potently inhibited the rate of heme degradation to bile pigment in human spleen.

Heme oxygenase activity causes transient hypersensitivity to oxidative ultraviolet a radiation that depends on release of iron from heme

2000 ◽  
Vol 28 (8) ◽  
pp. 1191-1196 ◽  
Author(s):  
Egil Kvam ◽  
Vidya Hejmadi ◽  
Stefan Ryter ◽  
Charareh Pourzand ◽  
Rex M Tyrrell
Keyword(s):  
Heme Oxygenase ◽  
Ultraviolet A ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity

The protective properties of synthetic porphyrin tin complexes in toxic hyperbilirubinemia

2000 ◽  
Vol 04 (03) ◽  
pp. 243-247 ◽  
Author(s):  
T. O. PHILIPPOVA ◽  
B. N. GALKIN ◽  
N. YA. GOLOVENKO ◽  
Z. I. ZHILINA ◽  
S. V. VODZINSKII
Keyword(s):  
Heme Oxygenase ◽  
Serum Bilirubin ◽  
Protoporphyrin Ix ◽  
Serum Bilirubin Level ◽  
Oxygenase Activity ◽  
Tetraphenyl Porphyrin ◽  
Tin Complexes ◽  
Cytochrome P 450

Tin complexes of meso-substituted synthetic porphyrins, namely Sn 4+-meso-tetraphenyl- porphyrin ( Sn - TPP ) and Sn 4+-meso-tetrakis(N-methyl-3-pyridyl)porphyrin tetratosylate ( Sn - TMe -3- PyP ), efficiently decrease the serum bilirubin level when injected subcutaneously at a dose of 100 μM kg−1 body weight into mice. These compounds are active during hyperbilirubinemia, induced by phenylhydrazine, hemin and tetrachloromethane, and also during autoimmune hemolytic anemia. In the latter case a decrease in serum bilirubin content was observed, as well as a decrease in the amount of blood reticulocytes which reflects a milder course of the disease. The Sn complexes under study induce, in vivo, cytochrome P-450, inhibit microsomal heme oxygenase and decrease the intensity of lipid peroxidation. At the same time, in vitro the hepatic and splenic heme oxygenase activity is blocked only when a 0.1 μM concentration of Sn - TMe -3- PyP or Sn -protoporphyrin IX is added to the incubation mixture. Sn - TPP does not affect the activity of this enzyme in vitro.

scholarly journals Heme oxygenase activity and hemoglobin neurotoxicity are attenuated by inhibitors of the MEK/ERK pathway

2009 ◽  
Vol 56 (5) ◽  
pp. 922-928 ◽  
Author(s):  
Jing Chen-Roetling ◽  
Zhi Li ◽  
Mai Chen ◽  
Olatilewa O. Awe ◽  
Raymond F. Regan
Keyword(s):  
Heme Oxygenase ◽  
Erk Pathway ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity

281 HEME OXYGENASE ACTIVITY IN THE MOUSE PLACENTA DURING FETAL DEVELOPMENT.:

2006 ◽  
Vol 54 (1) ◽  
pp. S128.3-S128
Author(s):  
H. Zhao ◽  
R. J. Wong ◽  
I. Morioka ◽  
F. A. Kalish ◽  
D. K. Stevenson
Keyword(s):  
Heme Oxygenase ◽  
Fetal Development ◽  
Heme Oxygenase Activity ◽  
Mouse Placenta ◽  
Oxygenase Activity

Gas-chromatographic assay for heme oxygenase activity.

1982 ◽  
Vol 28 (10) ◽  
pp. 2026-2032 ◽  
Author(s):  
F W Sunderman ◽  
J R Downs ◽  
M C Reid ◽  
L M Bibeau
Keyword(s):  
Gas Chromatography ◽  
Detection Limit ◽  
Heme Oxygenase ◽  
Liver Microsomes ◽  
Microsomal Protein ◽  
Spectrophotometric Assay ◽  
Rat Tissues ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity ◽  
Kidney Microsomes

Abstract We have developed an improved assay for microsomal heme oxygenase activity, based on the enzymic release of CO from the alpha-methene bridge of hemin and the quantitation of CO by gas chromatography. The within-run coefficient of variation (CV) of heme oxygenase assays in microsomes from rat tissues (liver, kidney) averaged 8%; the between-run CV averaged 15%. The detection limit for heme oxygenase activity was approximately 1 nmol/h per milligram of microsomal protein. Gas-chromatographic assays of heme oxygenase activities in rat tissues correlated well (r = 0.94) with results by a spectrophotometric assay based on bilirubin production. In untreated rats, heme oxygenase activity averaged 7 +/- 3 nmol/h per milligram of protein (n = 36) in kidney microsomes and 14 +/- 5 nmol/h per milligram of protein (n = 17) in liver microsomes. Heme oxygenase activity was increased 10-fold in kidney microsomes and threefold in liver microsomes from rats killed 17 h after subcutaneous injection of NiCl2 (0.5 mmol/kg body wt). These findings illustrate the efficacy of the gas-chromatographic assay for measuring xenobiotic effects on heme oxygenase activity.

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