Oxidative interactions between haemoglobin and membrane lipid. A liposome model

J. Szebeni, C. C. Winterbourn, R. W. Carrell

Research output: Contribution to journalArticle

106 Citations (Scopus)

Abstract

The relationship between haemoglobin and membrane oxidation was studied using liposomes containing haemoglobin (haemosomes) as a red cell model. Rapid oxidation occurred in haemosomes formed from purified haemoglobin and unsaturated lipid (egg phosphatidylcholines). After 3 h at 37°C most of the haemoglobin was oxidized, predominantly to methaemoglobin with some haemichrome formation. The oxidation of haemoglobin was paralleled by membrane lipid peroxidation as measured by thiobarbituric acid rectivity. These changes were largely abolished by using freshly prepared haemolysate instead of purified haemoglobin, or when haemosomes were prepared with saturated phosphatidylcholines. In haemosomes consisting of fresh haemolysate and saturated phosphatidylcholine, the rate of haemoglobin oxidation at 37°C corresponded to that of non-encapsulated haemolysate, and after 4 months storage at 4°C 45% of oxyhaemoglobin was oxidized. In haemosomes prepared from purified haemoglobin and egg lecithin, α-tocopherol, catalase and ascorbate each protected against both haemoglobin oxidation and lipid peroxidation. Superoxide dismutase or reduced glutathione had no effect. In unsaturated-lipid haemosomes containing haemolysate, the rate of haemoglobin oxidation increased when catalase was inhibited or reduced glutathione was depeleted, but after long term incubation only concurrent catalase-inhibition and glutathione depletion could increase thiobarbituric acid reactivity. These results demonstrate a close interdependence between haemoglobin oxidation and lipid peroxidation, and show that constituents of haemolysate strongly protect against both processes. H2O2 appears to be an important mediator, with its removal by either catalase or the glutathione/glutathione peroxidase system protecting against both oxidative changes

Original languageEnglish
Pages (from-to)685-692
Number of pages8
JournalBiochemical Journal
Volume220
Issue number3
Publication statusPublished - 1984

Fingerprint

Membrane Lipids
Liposomes
Hemoglobins
Oxidation
Catalase
Glutathione
Phosphatidylcholines
Lipid Peroxidation
Lipids
Ovum
Methemoglobin
Oxyhemoglobins
Tocopherols
Lecithins
Glutathione Peroxidase
Superoxide Dismutase
Cells
Membranes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Oxidative interactions between haemoglobin and membrane lipid. A liposome model. / Szebeni, J.; Winterbourn, C. C.; Carrell, R. W.

In: Biochemical Journal, Vol. 220, No. 3, 1984, p. 685-692.

Research output: Contribution to journalArticle

Szebeni, J, Winterbourn, CC & Carrell, RW 1984, 'Oxidative interactions between haemoglobin and membrane lipid. A liposome model', Biochemical Journal, vol. 220, no. 3, pp. 685-692.
Szebeni, J. ; Winterbourn, C. C. ; Carrell, R. W. / Oxidative interactions between haemoglobin and membrane lipid. A liposome model. In: Biochemical Journal. 1984 ; Vol. 220, No. 3. pp. 685-692.
@article{6acb8d9d55294ed089961907d74c61be,
title = "Oxidative interactions between haemoglobin and membrane lipid. A liposome model",
abstract = "The relationship between haemoglobin and membrane oxidation was studied using liposomes containing haemoglobin (haemosomes) as a red cell model. Rapid oxidation occurred in haemosomes formed from purified haemoglobin and unsaturated lipid (egg phosphatidylcholines). After 3 h at 37°C most of the haemoglobin was oxidized, predominantly to methaemoglobin with some haemichrome formation. The oxidation of haemoglobin was paralleled by membrane lipid peroxidation as measured by thiobarbituric acid rectivity. These changes were largely abolished by using freshly prepared haemolysate instead of purified haemoglobin, or when haemosomes were prepared with saturated phosphatidylcholines. In haemosomes consisting of fresh haemolysate and saturated phosphatidylcholine, the rate of haemoglobin oxidation at 37°C corresponded to that of non-encapsulated haemolysate, and after 4 months storage at 4°C 45{\%} of oxyhaemoglobin was oxidized. In haemosomes prepared from purified haemoglobin and egg lecithin, α-tocopherol, catalase and ascorbate each protected against both haemoglobin oxidation and lipid peroxidation. Superoxide dismutase or reduced glutathione had no effect. In unsaturated-lipid haemosomes containing haemolysate, the rate of haemoglobin oxidation increased when catalase was inhibited or reduced glutathione was depeleted, but after long term incubation only concurrent catalase-inhibition and glutathione depletion could increase thiobarbituric acid reactivity. These results demonstrate a close interdependence between haemoglobin oxidation and lipid peroxidation, and show that constituents of haemolysate strongly protect against both processes. H2O2 appears to be an important mediator, with its removal by either catalase or the glutathione/glutathione peroxidase system protecting against both oxidative changes",
author = "J. Szebeni and Winterbourn, {C. C.} and Carrell, {R. W.}",
year = "1984",
language = "English",
volume = "220",
pages = "685--692",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "3",

}

TY - JOUR

T1 - Oxidative interactions between haemoglobin and membrane lipid. A liposome model

AU - Szebeni, J.

AU - Winterbourn, C. C.

AU - Carrell, R. W.

PY - 1984

Y1 - 1984

N2 - The relationship between haemoglobin and membrane oxidation was studied using liposomes containing haemoglobin (haemosomes) as a red cell model. Rapid oxidation occurred in haemosomes formed from purified haemoglobin and unsaturated lipid (egg phosphatidylcholines). After 3 h at 37°C most of the haemoglobin was oxidized, predominantly to methaemoglobin with some haemichrome formation. The oxidation of haemoglobin was paralleled by membrane lipid peroxidation as measured by thiobarbituric acid rectivity. These changes were largely abolished by using freshly prepared haemolysate instead of purified haemoglobin, or when haemosomes were prepared with saturated phosphatidylcholines. In haemosomes consisting of fresh haemolysate and saturated phosphatidylcholine, the rate of haemoglobin oxidation at 37°C corresponded to that of non-encapsulated haemolysate, and after 4 months storage at 4°C 45% of oxyhaemoglobin was oxidized. In haemosomes prepared from purified haemoglobin and egg lecithin, α-tocopherol, catalase and ascorbate each protected against both haemoglobin oxidation and lipid peroxidation. Superoxide dismutase or reduced glutathione had no effect. In unsaturated-lipid haemosomes containing haemolysate, the rate of haemoglobin oxidation increased when catalase was inhibited or reduced glutathione was depeleted, but after long term incubation only concurrent catalase-inhibition and glutathione depletion could increase thiobarbituric acid reactivity. These results demonstrate a close interdependence between haemoglobin oxidation and lipid peroxidation, and show that constituents of haemolysate strongly protect against both processes. H2O2 appears to be an important mediator, with its removal by either catalase or the glutathione/glutathione peroxidase system protecting against both oxidative changes

AB - The relationship between haemoglobin and membrane oxidation was studied using liposomes containing haemoglobin (haemosomes) as a red cell model. Rapid oxidation occurred in haemosomes formed from purified haemoglobin and unsaturated lipid (egg phosphatidylcholines). After 3 h at 37°C most of the haemoglobin was oxidized, predominantly to methaemoglobin with some haemichrome formation. The oxidation of haemoglobin was paralleled by membrane lipid peroxidation as measured by thiobarbituric acid rectivity. These changes were largely abolished by using freshly prepared haemolysate instead of purified haemoglobin, or when haemosomes were prepared with saturated phosphatidylcholines. In haemosomes consisting of fresh haemolysate and saturated phosphatidylcholine, the rate of haemoglobin oxidation at 37°C corresponded to that of non-encapsulated haemolysate, and after 4 months storage at 4°C 45% of oxyhaemoglobin was oxidized. In haemosomes prepared from purified haemoglobin and egg lecithin, α-tocopherol, catalase and ascorbate each protected against both haemoglobin oxidation and lipid peroxidation. Superoxide dismutase or reduced glutathione had no effect. In unsaturated-lipid haemosomes containing haemolysate, the rate of haemoglobin oxidation increased when catalase was inhibited or reduced glutathione was depeleted, but after long term incubation only concurrent catalase-inhibition and glutathione depletion could increase thiobarbituric acid reactivity. These results demonstrate a close interdependence between haemoglobin oxidation and lipid peroxidation, and show that constituents of haemolysate strongly protect against both processes. H2O2 appears to be an important mediator, with its removal by either catalase or the glutathione/glutathione peroxidase system protecting against both oxidative changes

UR - http://www.scopus.com/inward/record.url?scp=0021259483&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021259483&partnerID=8YFLogxK

M3 - Article

C2 - 6466294

AN - SCOPUS:0021259483

VL - 220

SP - 685

EP - 692

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 3

ER -