Abstract

BackgroundPeroxiredoxins (Prxs) are a novel group of peroxidases containing high antioxidant efficiency. The mammalian Prx family has six distinct members (Prx I-VI) in various subcellular locations, including peroxisomes and mitochondria, places where oxidative stress is most evident. The function of Prx I in particular has been implicated in regulating cell proliferation, differentiation, and apoptosis. Since thioredoxin1 (Trx1) as an electron donor is functionally associated with Prx I, we investigated levels of expression of both Prx I and Trx1.MethodsWe investigated levels of expression of both Prx I and Trx1 in breast cancer by real-time polymerase chain reaction (RT-PCR) and Western blot.ResultsLevels of messenger RNA (mRNA) for both Prx I and Trx1 in normal human breast tissue were very low compared to other major human tissues, whereas their levels in breast cancer exceeded that in other solid cancers (colon, kidney, liver, lung, ovary, prostate, and thyroid). Among members of the Prx family (Prx I-VI) and Trx family (Trx1, Trx2), Prx I and Trx1 were preferentially induced in breast cancer. Moreover, the expression of each was associated with progress of breast cancer and correlated with each other. Western blot analysis of different and paired breast tissues revealed consistent and preferential expression of Prx I and Trx1 protein in breast cancer tissue.ConclusionPrx I and Trx1 are overexpressed in human breast carcinoma and the expression levels are associated with tumor grade. The striking induction of Prx I and Trx1 in breast cancer may enable their use as breast cancer markers.

Highlights

  • Peroxiredoxins (Prxs) are a novel group of peroxidases containing high antioxidant efficiency

  • Organisms living under aerobic conditions are exposed to reactive oxygen species (ROS) such as superoxide anion (O2-), hydrogen peroxide (H2O2), and nitric oxide (NO), which are generated by redox metabolism, mainly in mitochondria

  • Thioredoxin 1, as cytoplasmic electron donor to Prx I, was expressed at the lowest level (0.24 × 10-4 pg) among 48 major human tissues (Figure 1B). To address whether this low expression was specific to Prx I, we investigated messenger RNA (mRNA) levels of all members of the Prx family (Prx I-VI) using the same 96well Human Major Tissues real-time (HMRT) array

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Summary

Introduction

Peroxiredoxins (Prxs) are a novel group of peroxidases containing high antioxidant efficiency. The function of Prx I in particular has been implicated in regulating cell proliferation, differentiation, and apoptosis. It has been demonstrated in vitro that ROS in small amounts participate in many physiological processes such as signal transduction, cell differentiation, apoptosis, and modulation of transcription factors [1,2,3]. From prokaryotes to primates, are equipped with different defensive systems to combat the toxic processes of ROS. These defensive systems include antioxidant enzymes such as superoxide dismutases, catalases, glutathione peroxidases, and a new type of peroxidase, the rapidly growing family of peroxiredoxins (Prxs) [3,4]. Journal of Experimental & Clinical Cancer Research 2009, 28:93 http://www.jeccr.com/content/28/1/93. Clinical Diagnosis BRN0 Brain Normal 26/M Normal BRC0

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