Modulatory influence of tin-protoporphyrin on gossypol-induced alterations of heme oxygenase activity in male wistar rats

2003 ◽  
Vol 28 (3) ◽  
pp. 237-243 ◽  
Author(s):  
Ritu Aneja ◽  
Sujata K. Dass ◽  
Ramesh Chandra
Keyword(s):  
Heme Oxygenase ◽  
Wistar Rats ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity ◽  
Male Wistar Rats ◽  
Tin Protoporphyrin

scholarly journals Heme oxygenase-1-derived bilirubin ameliorates postischemic myocardial dysfunction

2000 ◽  
Vol 278 (2) ◽  
pp. H643-H651 ◽  
Author(s):  
James E. Clark ◽  
Roberta Foresti ◽  
Padmini Sarathchandra ◽  
Harparkash Kaur ◽  
Colin J. Green ◽  
...  
Keyword(s):  
Infarct Size ◽  
Heme Oxygenase ◽  
Myocardial Function ◽  
Myocardial Dysfunction ◽  
Protoporphyrin Ix ◽  
Heme Oxygenase 1 ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity ◽  
Tin Protoporphyrin

Bilirubin is a potent antioxidant generated intracellularly during the degradation of heme by the enzyme heme oxygenase. The purpose of this study was to determine the role of increased cardiac bilirubin in protection against postischemic myocardial dysfunction. Rat hearts were isolated and perfused according to the Langendorff technique to evaluate the recovery of myocardial function after 30 min of global ischemia and 60 min of reperfusion. We found that upregulation of the inducible isoform of heme oxygenase (HO-1) by treatment of animals with hemin 24 h before ischemia ameliorated myocardial function and reduced infarct size (tetrazolium staining) on reperfusion of isolated hearts. Tin protoporphyrin IX, an inhibitor of heme oxygenase activity, completely abolished the improved postischemic myocardial performance observed after hemin-mediated HO-1 induction. Likewise, cardiac tissue injury was exacerbated by treatment with tin protoporphyrin IX. Increased cardiac HO-1 expression and heme oxygenase activity were associated with enhanced tissue bilirubin content and an increased rate of bilirubin release into the perfusion buffer. Furthermore, exogenously administered bilirubin at concentrations as low as 100 nanomolar significantly restored myocardial function and minimized both infarct size and mitochondrial damage on reperfusion. Our data provide strong evidence for a primary role of HO-1-derived bilirubin in cardioprotection against reperfusion injury.

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

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.

Sign in / Sign up

Export Citation Format

Share Document