Presence of cytosolic peroxiredoxin 2 in the erythrocyte membrane of patients with hereditary spherocytosis

• Type: Article in International Scientific Journal
• Date: 2008

Authors

Susana Rocha (Author) FFUP; Rui M P Vitorino (Author) Other; Francisco M Lemos Amado (Author) Other; Elisabeth Bayer Castro (Author) Other; Petronila Rocha Pereira (Author) Other; Jose Barbot (Author) Other; Esmeralda Cleto (Author) Other; Fatima Ferreira (Author) Other; Alexandre Quintanilha (Author) ICBAS; Luis Belo (Author) FFUP; Alice Santos Silva (Author) FFUP

Journal

Title: Blood Cells, Molecules, and Diseases

Vol. 41 No. 1

Pages: 5-9

ISSN: 1079-9796

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 36 Citations

ISI Web of Science

Scopus - 39 Citations

Scientific classification

FOS: Medical and Health sciences > Clinical medicine

CORDIS: Health sciences

Other information

Authenticus ID: P-003-XWV

DOI: 10.1016/j.bcmd.2008.02.008

Resumo (PT): performed standardized diagnosis tests, including electrophoretic membrane protein analysis to identify and quantify protein deficiencies underlying HS. Membrane bound hemoglobin (MBH) and band 3 profiles were determined as oxidative stress and aging markers. A protein of about 22 kDa, present in 21 of 57 HS patients, but not in controls, was identified as peroxiredoxin 2 (Prx2), by mass-spectroscopy and by immunoblotting. Human erythrocyte Prx2 is a peroxiredoxin with thiol-specific antioxidant activity. The presence of Prx2 in erythrocyte membranes was linked to higher levels of oxidative stress, as reflected by significantly increased MBH in those HS patients. No relation with HS clinical severity was observed and Prx2 was detected in all types of membrane protein abnormalities. Prx2 membrane linkage is associated with a higher oxidative stress susceptibility of HS erythrocytes. <br> <br> Keywords: Hereditary spherocytosis Peroxiredoxin 2 Oxidative stress Erythrocyte membrane proteins Mass-spectroscopy <br> <a target="_blank" href="http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WBV-4S62CR3-4&_user=2460038&_coverDate=08%2F31%2F2008&_rdoc=3&_fmt=high&_orig=browse&_srch=doc-info(%23toc%236720%232008%23999589998%23691336%23FLA%23display%23Volume)&_cdi=6720&_sort=d&_docanchor=&_ct=25&_acct=C000057398&_version=1&_urlVersion=0&_userid=2460038&md5=97a84495b882e47f682727eae999109b"> Texto integral</a>

Abstract (EN): We studied 82 Portuguese individuals, 57 with hereditary spherocytosis (HS) and 25 unaffected controls. We performed standardized diagnosis tests, including electrophoretic membrane protein analysis to identify and quantify protein deficiencies underlying HS. Membrane bound hemoglobin (MBH) and band 3 profiles were determined as oxidative stress and aging markers. A protein of about 22 kDa, present in 21 of 57 HS patients, but not in controls, was identified as peroxiredoxin 2 (Prx2), by mass-spectroscopy and by immunoblotting. Human erythrocyte Prx2 is a peroxiredoxin with thiol-specific antioxidant activity. The presence of Prx2 in erythrocyte membranes was linked to higher levels of oxidative stress, as reflected by significantly increased MBH in those HS patients. No relation with HS clinical severity was observed and Prx2 was detected in all types of membrane protein abnormalities. Prx2 membrane linkage is associated with a higher oxidative stress susceptibility of HS erythrocytes.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 5