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Nuclear translocation of haeme oxygenase-1 is associated to prostate cancer

Authors :
Roberto Meiss
Gabriel Casas
Elba Vazquez
Nora M. Navone
Juan Carlos Calvo
Paula Alejandra Sacca
Osvaldo Mazza
Source :
Br. J. Cancer 2007;97(12):1683-1689, Biblioteca Digital (UBA-FCEN), Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales, instacron:UBA-FCEN, CONICET Digital (CONICET), Consejo Nacional de Investigaciones Científicas y Técnicas, instacron:CONICET, British Journal of Cancer
Publication Year :
2007
Publisher :
Nature Publishing Group, 2007.

Abstract

The role of oxidative stress in prostate cancer has been increasingly recognised. Acute and chronic inflammations generate reactive oxygen species that result in damage to cellular structures. Haeme oxygenase-1 (HO-1) has cytoprotective effects against oxidative damage. We hypothesise that modulation of HO-1 expression may be involved in the process of prostate carcinogenesis and prostate cancer progression. We thus studied HO-1 expression and localisation in 85 samples of organ-confined primary prostate cancer obtained via radical prostatectomy (Gleason grades 4-9) and in 39 specimens of benign prostatic hyperplasia (BPH). We assessed HO-1 expression by immunohistochemical staining. No significant difference was observed in the cytoplasmic positive reactivity among tumours (84%), non-neoplastic surrounding parenchyma (89%), or BPH samples (87%) (P=0.53). Haeme oxygenase-1 immunostaining was detected in the nuclei of prostate cancer cells in 55 of 85 (65%) patients but less often in non-neoplastic surrounding parenchyma (30 of 85, 35%) or in BPH (9 of 39, 23%) (P

Details

Language :
English
Database :
OpenAIRE
Journal :
Br. J. Cancer 2007;97(12):1683-1689, Biblioteca Digital (UBA-FCEN), Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales, instacron:UBA-FCEN, CONICET Digital (CONICET), Consejo Nacional de Investigaciones Científicas y Técnicas, instacron:CONICET, British Journal of Cancer
Accession number :
edsair.doi.dedup.....8f19cc31b7f582ec41a5b15add416efd