Linkage of cytosolic peroxiredoxin 2 to erythrocyte membrane imposed by hydrogen peroxide-induced oxidative stress

• Type: Article in International Scientific Journal
• Date: 2009

Authors

Susana Rocha (Author) FFUP; Elisio Costa (Author) FFUP; Susana Coimbra (Author) Other; Henrique Nascimento (Author) Other; Cristina Catarino (Author) FFUP; Petronila Rocha Pereira (Author) Other; Alexandre Quintanilha (Author) ICBAS; Luis Belo (Author) FFUP; Alice Santos Silva (Author) FFUP

Journal

Title: Blood Cells, Molecules, and Diseases

Vol. 43 No. 1

Pages: 68-73

ISSN: 1079-9796

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 30 Citations

ISI Web of Science

Scopus - 30 Citations

Scientific classification

FOS: Medical and Health sciences > Clinical medicine

CORDIS: Health sciences

Other information

Authenticus ID: P-003-HNA

DOI: 10.1016/j.bcmd.2009.03.002

Resumo (PT): Human erythrocyte peroxiredoxin 2 (Prx2) is a typical 2-cys cytosolic peroxiredoxin with thiol-dependent hydrogen peroxide scavenger activity. In a previous work, we reported Prx2 erythrocyte membrane linkage in some Hereditary Spherocytosis patients and that it seemed to be related to oxidative stress. The aim of the present work was to determine if Prx2 linkage to erythrocyte membrane could be induced by oxidative stress mediated by H2O2 and to further understand how and why this process occurs. We performed in vitro assays in which catalase or both Hb autoxidation and catalase were inhibited, under H2O2-induced oxidative stress conditions. Erythrocyte membrane linked Prx2 was detected by immunoblotting and quantified by densitometry. As oxidative stress markers, we determined membrane bound hemoglobin and lipid peroxidation, and we found that their values increased with H2O2 concentration. Prx2 linkage to the membrane also rose with increasing H2O2 concentration, and was only observed when the oxidized form of the enzyme was present in the cytosol. Oxidized Hb and Prx2 membrane linkages appear to be independent processes, although, both result from oxidative stress and may be useful as oxidative stress and/or erythrocyte damage/senescence markers. <br> <br> Keywords: Peroxiredoxin 2; Erythrocyte membrane; Oxidative stress; Hemoglobin autoxidation <br> <a target="_blank" href="http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WBV-4W329H8-2&_user=2460038&_coverDate=08%2F31%2F2009&_rdoc=14&_fmt=high&_orig=browse&_srch=doc-info(%23toc%236720%232009%23999569998%231178063%23FLA%23display%23Volume)&_cdi=6720&_sort=d&_docanchor=&_ct=24&_acct=C000057398&_version=1&_urlVersion=0&_userid=2460038&md5=290b14804204f242cd29b5cbb54cde0a "> Texto integral </a> <br> <br>

Abstract (EN): Human erythrocyte peroxiredoxin 2 (Prx2) is a typical 2-cys cytosolic peroxiredoxin with thiol-dependent hydrogen peroxide scavenger activity. In a previous work, we reported Prx2 erythrocyte membrane linkage in some Hereditary Spherocytosis patients and that it seemed to be related to oxidative stress. The aim of the present work was to determine if Prx2 linkage to erythrocyte membrane could be induced by oxidative stress mediated by H(2)O(2) and to further understand how and why this process occurs. We performed in vitro assays in which catalase or both Hb autoxidation and catalase were inhibited, under H(2)O(2)-induced oxidative stress conditions. Erythrocyte membrane linked Prx2 was detected by immunoblotting and quantified by densitometry. As oxidative stress markers, we determined membrane bound hemoglobin and lipid peroxidation, and we found that their values increased with H(2)O(2) concentration. Prx2 linkage to the membrane also rose with increasing H(2)O(2) concentration, and was only observed when the oxidized form of the enzyme was present in the cytosol. Oxidized Hb and Prx2 membrane linkages appear to be independent processes, although, both result from oxidative stress and may be useful as oxidative stress and/or erythrocyte damage/senescence markers.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6