The lipocalin alpha1-microglobulin protects erythroid K562 cells against oxidative damage induced by heme and reactive oxygen species.
Gram, Magnus LU
; Olofsson, Tor
LU
; Tapper, Hans
LU
and Åkerström, Bo
LU
(2008)
In Free Radical Research
42(8).
p.725-736
- Abstract
- Alpha(1)-microglobulin is a 26 kDa plasma and tissue glycoprotein that belongs to the lipocalin protein superfamily. Recent reports show that it is a reductase and radical scavenger and that it binds heme and has heme-degrading properties. This study has investigated the protective effects of alpha(1)-microglobulin against oxidation by heme and reactive oxygen species in the human erythroid cell line, K562. The results show that alpha(1)-microglobulin prevents intracellular oxidation and up-regulation of heme oxygenase-1 induced by heme, hydrogen peroxide and Fenton reaction-generated hydroxyl radicals in the culture medium. It also reduces the cytosol of non-oxidized cells. Endogeneous expression of alpha(1)-microglobulin was up-regulated... (More)
- Alpha(1)-microglobulin is a 26 kDa plasma and tissue glycoprotein that belongs to the lipocalin protein superfamily. Recent reports show that it is a reductase and radical scavenger and that it binds heme and has heme-degrading properties. This study has investigated the protective effects of alpha(1)-microglobulin against oxidation by heme and reactive oxygen species in the human erythroid cell line, K562. The results show that alpha(1)-microglobulin prevents intracellular oxidation and up-regulation of heme oxygenase-1 induced by heme, hydrogen peroxide and Fenton reaction-generated hydroxyl radicals in the culture medium. It also reduces the cytosol of non-oxidized cells. Endogeneous expression of alpha(1)-microglobulin was up-regulated by these oxidants and silencing of the alpha(1)-microglobulin expression increased the cytosol oxidation. alpha(1)-microglobulin also inhibited cell death caused by heme and cleared cells from bound heme. Binding of heme to alpha(1)-microglobulin increased the radical reductase activity of the protein as compared to the apo-protein. Finally, alpha(1)-microglobulin was localized mainly at the cell surface both when administered exogeneously and in non-treated cells. The results suggest that alpha(1)-microglobulin is involved in the defence against oxidative cellular injury caused by haemoglobin and heme and that the protein may employ both heme-scavenging and one-electron reduction of radicals to achieve this. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1223063
- author
- Gram, Magnus
LU
; Olofsson, Tor
LU
; Tapper, Hans
LU
and Åkerström, Bo
LU
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Free Radical Research
- volume
- 42
- issue
- 8
- pages
- 725 - 736
- publisher
- Harwood Academic
- external identifiers
-
- wos:000258624800004
- pmid:18712632
- scopus:50949096034
- pmid:18712632
- ISSN
- 1029-2470
- DOI
- 10.1080/10715760802337265
- language
- English
- LU publication?
- yes
- id
- 4c2ae30f-4f6c-4172-951b-d8ba6ecf4a21 (old id 1223063)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/18712632?dopt=Abstract
- date added to LUP
- 2016-04-01 14:44:22
- date last changed
- 2024-10-10 21:05:41
@article{4c2ae30f-4f6c-4172-951b-d8ba6ecf4a21,
abstract = {{Alpha(1)-microglobulin is a 26 kDa plasma and tissue glycoprotein that belongs to the lipocalin protein superfamily. Recent reports show that it is a reductase and radical scavenger and that it binds heme and has heme-degrading properties. This study has investigated the protective effects of alpha(1)-microglobulin against oxidation by heme and reactive oxygen species in the human erythroid cell line, K562. The results show that alpha(1)-microglobulin prevents intracellular oxidation and up-regulation of heme oxygenase-1 induced by heme, hydrogen peroxide and Fenton reaction-generated hydroxyl radicals in the culture medium. It also reduces the cytosol of non-oxidized cells. Endogeneous expression of alpha(1)-microglobulin was up-regulated by these oxidants and silencing of the alpha(1)-microglobulin expression increased the cytosol oxidation. alpha(1)-microglobulin also inhibited cell death caused by heme and cleared cells from bound heme. Binding of heme to alpha(1)-microglobulin increased the radical reductase activity of the protein as compared to the apo-protein. Finally, alpha(1)-microglobulin was localized mainly at the cell surface both when administered exogeneously and in non-treated cells. The results suggest that alpha(1)-microglobulin is involved in the defence against oxidative cellular injury caused by haemoglobin and heme and that the protein may employ both heme-scavenging and one-electron reduction of radicals to achieve this.}},
author = {{Gram, Magnus and Olofsson, Tor and Tapper, Hans and Åkerström, Bo}},
issn = {{1029-2470}},
language = {{eng}},
number = {{8}},
pages = {{725--736}},
publisher = {{Harwood Academic}},
series = {{Free Radical Research}},
title = {{The lipocalin alpha1-microglobulin protects erythroid K562 cells against oxidative damage induced by heme and reactive oxygen species.}},
url = {{http://dx.doi.org/10.1080/10715760802337265}},
doi = {{10.1080/10715760802337265}},
volume = {{42}},
year = {{2008}},
}