Expression and clinical value of peroxiredoxin-1 in patients with pancreatic cancer

Cai, Chong-Yang; Zhai, Limin; Wu, Yun; Tang, Zhichen

doi:10.1016/j.ejso.2014.11.037

Cited by 50 publications

(40 citation statements)

References 37 publications

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“…13 versus 1,730, 55 versus 2,490, and 110 versus 4,020 ppm, respectively). Some cancer cells might also take advantage of the Prx1-CAT activity as the expressions of CAT are deficient or highly down-regulated in many of cancer cells (47), whereas those of Prx1 are up-regulated in cancer cells, including breast, lung, and urinary cancers and hepatocellular carcinoma (48). The down-and up-regulation of CAT and Prx1 were also clearly supported by comparing the MOPED protein expression profiles between cancer and non-cancer cells (Fig.…”

Section: Gvlmentioning

confidence: 71%

Cysteine-independent Catalase-like Activity of Vertebrate Peroxiredoxin 1 (Prx1)

Sun

Dong

Zhao

et al. 2015

Journal of Biological Chemistry

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Background: Peroxiredoxin (Prx) was previously known only as a Cys-dependent thioredoxin. Results: Cys-independent catalase-like activity was observed in two vertebrate Prx1 proteins. Conclusion: Prx1 possesses dual antioxidant activities with varied affinities toward H 2 O 2 . Significance: This discovery extends our knowledge on Prx1 and provides new opportunities to further study the biological roles of this family of antioxidants.

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Section: Gvlmentioning

confidence: 71%

Cysteine-independent Catalase-like Activity of Vertebrate Peroxiredoxin 1 (Prx1)

Sun

Dong

Zhao

et al. 2015

Journal of Biological Chemistry

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“…13 vs. 1730, 55 vs. 2490, and 110 vs. 4020 ppm, respectively). Some cancer cells might also take advantage of the Prx1-CAT activity, since the expressions of CAT were deficient or highly down-regulated in many cancer cells [53], whereas those of Prx1 were up-regulated in cancer cells including breast, lung and urinary cancers and hepatocellular carcinoma [54]. The down- and up-regulation of CAT and Prx1 was also clearly supported by comparing the MOPED protein expression profiles between cancer and non-cancer cells (Supplementary Figure S2b).…”

Section: Discussionmentioning

confidence: 99%

Peroxiredoxin 1 (Prx1) is a dual-function enzyme by possessing Cys-independent catalase-like activity

Sun

Dong

Shao

et al. 2017

Biochemical Journal

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Peroxiredoxin (Prx) was previously known as a Cys-dependent thioredoxin. However, we unexpectedly observed that Prx1 from the green spotted puffer fish Tetraodon nigroviridis (TnPrx1) was able to reduce H2O2 in a manner independent of Cys peroxidation and reductants. This study aimed to validate a novel function for Prx1, delineate the biochemical features and explore its antioxidant role in cells. We have confirmed that Prx1 from the puffer fish and humans truly possesses a catalase (CAT)-like activity that is independent of Cys residues and reductants, but dependent on iron. We have identified that the GVL motif was essential to the CAT-like activity of Prx1, but not to the Cys-dependent thioredoxin peroxidase (POX) activity, and generated mutants lacking POX and/or CAT-like activities for individual functional validation. We discovered that the TnPrx1 POX and CAT-like activities possessed different kinetic features in the reduction of H2O2. The overexpression of wild-type TnPrx1 and mutants differentially regulated the intracellular levels of reactive oxygen species (ROS) and the phosphorylation of p38 in HEK-293T cells treated with H2O2. Prx1 is a dual-function enzyme by acting as POX and CAT with varied affinities towards ROS. This study extends our knowledge on Prx1 and provides new opportunities to further study the biological roles of this family of antioxidants.

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“…An increased level of PRDX1 has been described in lung cancer (60), in bladder cancer (61), in ovarian carcinoma (62), in aggressive esophageal squamous carcinomas (63), in hilar cholangiocarcinoma (64), in liver cancer (65), in pancreatic cancer (66), in mesothelioma (67) and in glioblastoma (68). In prostate cancer, PRDX1 overexpression induces tumor growth and tumor progression through the Toll-like receptor 4 (TLR4)-dependent regulation of tumor vasculature, increasing the expression of the vascular endothelial growth factor (VEGF) (69).…”

Section: Prdxs In Tumorigenesismentioning

confidence: 99%

The role of peroxiredoxins in cancer

Nicolussi

D’Inzeo

Capalbo

et al. 2017

Molecular and Clinical Oncology

154

126

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Peroxiredoxins (PRDXs) are a ubiquitously expressed family of small (22–27 kDa) non-seleno peroxidases that catalyze the peroxide reduction of H2O2, organic hydroperoxides and peroxynitrite. They are highly involved in the control of various physiological functions, including cell growth, differentiation, apoptosis, embryonic development, lipid metabolism, the immune response, as well as cellular homeostasis. Although the protective role of PRDXs in cardiovascular and neurological diseases is well established, their role in cancer remains controversial. Increasing evidence suggests the involvement of PRDXs in carcinogenesis and in the development of drug resistance. Numerous types of cancer cells, in fact, are characterized by an increase in reactive oxygen species (ROS) production, and often exhibit an altered redox environment compared with normal cells. The present review focuses on the complex association between oxidant balance and cancer, and it provides a brief account of the involvement of PRDXs in tumorigenesis and in the development of chemoresistance.

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Expression and clinical value of peroxiredoxin-1 in patients with pancreatic cancer

Cited by 50 publications

References 37 publications

Cysteine-independent Catalase-like Activity of Vertebrate Peroxiredoxin 1 (Prx1)

Cysteine-independent Catalase-like Activity of Vertebrate Peroxiredoxin 1 (Prx1)

Peroxiredoxin 1 (Prx1) is a dual-function enzyme by possessing Cys-independent catalase-like activity

The role of peroxiredoxins in cancer

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