Erythrocytes decrease myocardial hydrogen peroxide levels and reperfusion injury

1989 ◽  
Vol 256 (2) ◽  
pp. H584-H588 ◽  
Author(s):  
J. M. Brown ◽  
M. A. Grosso ◽  
L. S. Terada ◽  
C. J. Beehler ◽  
K. M. Toth ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Carbon Monoxide ◽  
Superoxide Dismutase ◽  
Reperfusion Injury ◽  
Ventricular Function ◽  
Anion Channel ◽  
Human Erythrocytes ◽  
Rat Hearts ◽  
Perfused Hearts ◽  
Isolated Rat

Reperfusion with untreated, carbon monoxide-treated, or glutaraldehyde-fixed human erythrocytes (RBC) increased ventricular function and decreased myocardial hydrogen peroxide (H2O2) levels [assessed by H2O2-dependent aminotriazole (AMT) inactivation of myocardial catalase activities] of ischemic, isolated rat hearts. In contrast, reperfusion with RBC that lacked catalase (AMT treated) and/or glutathione (N-ethylmaleimide treated) did not increase ventricular function or decrease myocardial H2O2 levels as much as reperfusion with untreated RBC. By comparison, reperfusion with superoxide dismutase-depleted (diethyldithiocarbamate-treated) or anion channel-inhibited (diisothiocyanodisulfonic acid stilbene-treated) RBC increased ventricular function and decreased myocardial H2O2 levels the same as untreated RBC. The results suggest that catalase and/or glutathione in intact RBC can decrease endogenously generated H2O2 and related reperfusion injury in ischemic, isolated perfused hearts.

Albumin decreases hydrogen peroxide and reperfusion injury in isolated rat hearts

Inflammation ◽  
1989 ◽  
Vol 13 (5) ◽  
pp. 583-589 ◽  
Author(s):  
James M. Brown ◽  
Connie J. Beehler ◽  
Elaine M. Berger ◽  
Michael A. Grosso ◽  
Glenn J. Whitman ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Reperfusion Injury ◽  
Rat Hearts ◽  
Isolated Rat

scholarly journals Oxidation of glycine by Phaseolus leghaemoglobin with associated catabolic reactions at the haem

1978 ◽  
Vol 176 (2) ◽  
pp. 351-358 ◽  
Author(s):  
P Lehtovaara
Keyword(s):  
Hydrogen Peroxide ◽  
Carbon Monoxide ◽  
Superoxide Dismutase ◽  
Phaseolus Vulgaris ◽  
Initial Velocity ◽  
Root Nodules ◽  
Green Product ◽  
Oxygen Complex ◽  
Optimum Ph ◽  
Glycine Oxidase

Leghaemoglobin from the root nodules of kidney bean (Phaseolus vulgaris) reacts in alkaline glycine solutions as a glycine oxidase in a reaction that may also be regarded as a coupled oxidation. Leghaemoglobin is reduced to the ferrous form by glycinate, the oxygen complex is formed, and finally the haem is attacked to yield a green reaction product. Glycine is simultaneously oxidized to glyoxylate, and hydrogen peroxide is generated. The initial velocity of the formation of the green product is proportional to the concentrations of leghaemoglobin and glycine, and the optimum pH for the reaction is 10.2. The green product is not formed if carbon monoxide, azide of imidazole is bound to the haem, whereas oxidation of glycine to glyoxylate is not inhibited by azide and not essentially by carbon monoxide. Haem breakdown is activated by digestion of leghaemoglobin by carboxypeptidase, and partly inhibited by catalase and superoxide dismutase.

Melatonin scavenges hydroxyl radical and protects isolated rat hearts from ischemic reperfusion injury

Life Sciences ◽  
2000 ◽  
Vol 67 (2) ◽  
pp. 101-112 ◽  
Author(s):  
Shinji Kaneko ◽  
Kenji Okumura ◽  
Yasushi Numaguchi ◽  
Hideo Matsui ◽  
Kichiro Murase ◽  
...  
Keyword(s):  
Hydroxyl Radical ◽  
Reperfusion Injury ◽  
Ischemic Reperfusion Injury ◽  
Ischemic Reperfusion ◽  
Rat Hearts ◽  
Isolated Rat
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