Online citations, reference lists, and bibliographies.
← Back to Search

The Autoxidation Of αα Cross-Linked Hemoglobin: A Possible Role In The Oxidative Stress To Endothelium

R. Motterlini, R. Foresti, K. Vandegriff, R. Winslow
Published 1995 · Chemistry

Save to my Library
Download PDF
Analyze on Scholarcy
Share
The aim of the present study was to investigate the role of hemoglobin autoxidation in the induction of endothelial heme oxygenase (HO), an inducible “stress” protein which is responsible for heme catabolism. Porcine aortic endothelial cells were incubated for six hours in the presence of 60 μM unmodified hemoglobin (HbA0), hemoglobin cross-linked between the a chains with bis-(3,5-dibromosalicyl) fumarate (ααHb) or cyanomet-αα-hemoglobin (CNmetααHb). Microsomal HO content increased 4.1-fold in the presence of ααHb, 2.7-fold with HbA0 and 1.8-fold with CNmetααHb over the control value. The rates of methemoglobin formation exhibited a linear relationship over the time of incubation (r = 0.94) and the apparent rate constant was 1.8-fold higher for ααHb (0.023 h-1) than HbA0 (0.013 h-1). In addition, a linear relationship was obtained by plotting the rates of autoxidation of hemoglobins versus the HO activity (r = 0.99). When cells were incubated with 100% methemoglobin, HO activity increased 5.0-fold and 4....
This paper references
10.1016/0006-2952(93)90621-3
Differential susceptibilities of the prosthetic heme of hemoglobin-based red cell substitutes. Implications in the design of safer agents.
Y. Osawa (1993)
10.3109/10731199009117306
Coronary vasoconstrictor activity of purified and modified human hemoglobin.
V. Macdonald (1990)
Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species.
G. Balla (1991)
10.1073/PNAS.90.20.9285
Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage.
J. Balla (1993)
10.1016/0020-711X(88)90093-6
The physiological significance of heme oxygenase.
N. Abraham (1988)
10.1152/JAPPL.1993.74.4.1769
Systemic and pulmonary hypertension after resuscitation with cell-free hemoglobin.
J. Hess (1993)
10.1016/s0021-9258(18)73873-8
MICRODETERMINATION OF OXYHEMOGLOBIN, METHEMOGLOBIN, AND SULFHEMOGLOBIN IN A SINGLE SAMPLE OF BLOOD
K. A. Evelyn (1938)
10.3109/10731199009117305
Liver and kidney injury after administration of hemoglobin cross-linked with bis(3,5-dibromosalicyl) fumarate.
C. Smith (1990)
10.1016/s0021-9258(18)93628-8
Exchange of heme among hemoglobins and between hemoglobin and albumin.
H. Bunn (1968)
The enzymatic catabolism of hemoglobin: stimulation of microsomal heme oxygenase by hemin.
R. Tenhunen (1970)
10.1016/0006-291X(89)92284-5
The effect of crosslinking by bis(3,5-dibromosalicyl) fumarate on the autoxidation of hemoglobin.
T. Yang (1989)
10.1152/JAPPL.1993.75.5.2224
Cell-free hemoglobin potentiates acetylcholine-induced coronary vasoconstriction in rabbit hearts.
R. Motterlini (1993)
10.1016/s0021-9258(17)42604-4
Hemoglobin. A biologic fenton reagent.
S. M. Sadrzadeh (1984)
10.3109/10731199009117301
Generation of free oxygen radicals and the toxicity of hemoglobin solutions.
J. Simoni (1990)
10.1016/0076-6879(94)31003-3
Pilot-scale preparation of hemoglobin solutions.
R. Winslow (1994)
10.1016/0003-9861(92)90101-2
Consequences of chemical modifications on the free radical reactions of human hemoglobin.
A. Alayash (1992)
10.1016/s0021-9258(18)77197-4
The stability of the heme-globin linkage in some normal, mutant, and chemically modified hemoglobins.
R. Benesch (1990)
10.1016/s0021-9258(19)37165-0
Ferritin: a cytoprotective antioxidant strategem of endothelium.
G. Balla (1992)



This paper is referenced by
Semantic Scholar Logo Some data provided by SemanticScholar