Lung tumor growth-promoting function of peroxiredoxin 6

Jo, Miran; Yun, Hyung-Mun; Park, Kyung-Ran; Park, Mi Hee; Kim, Tae Myoung; Pak, Jhang Ho; Lee, Soo Jae; Moon, Dong Cheul; Park, Chun‐Woong; Song, Sukgil; Lee, Chong-Kil; Han, Sang Bae; Hong, Jin Tae

doi:10.1016/j.freeradbiomed.2013.04.032

Cited by 37 publications

(44 citation statements)

References 44 publications

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“…iPLA2 also contributes to lung metastasis by stimulating plateletactivating factor production [43]. Recently, we also reported that GPx and iPLA2 activities were increased by PRDX6 in lung tumor tissues [19,32]. Thus, our data suggest that GPx and iPLA2 activities are important for lung tumor development in PRDX6-Tg mice.…”

Section: Discussionsupporting

confidence: 57%

“…We previously found that lung tumor growth was significantly increased by PRDX6 in in vivo xenograft and allograft mouse models [19,32]. These results indicate that PRDX6 may be an important factor in lung cancer cell growth.…”

Section: Discussionmentioning

confidence: 85%

“…2C). We previously found that GPx and iPLA2 activities of PRDX6 are important for lung tumor growth [19,32]. To examine the relative glutathione peroxidase and iPLA2 activities in the tumor lung tissues of PRDX6-Tg mice and non-Tg mice, we performed GPx and iPLA2 activity assays.…”

Section: Activation Of the Jak2/stat3 Pathway In The Lung Tumor Tissumentioning

confidence: 99%

“…It was shown that there was an almost threefold higher expression of PRDX6 and PRDX6 peroxidase activity in the normal lung tissue of the PRDX6-transgenic (Tg) mouse compared with the wild-type mouse [18]. Recently, we reported that PRDX6 promotes lung tumor in in vivo allograft and xenograft mouse models [19,20]. Thus, a growing number of studies are being Contents lists available at ScienceDirect journal homepage: www.elsevier.com/locate/freeradbiomed performed to address unanswered questions about the functional roles of PRDX6 as a tumorigenic protein and its potential value as a therapeutic target to fight cancer.…”

Section: Introuctionmentioning

confidence: 99%

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PRDX6 promotes tumor development via the JAK2/STAT3 pathway in a urethane-induced lung tumor model

Yun

Park

et al. 2015

Free Radical Biology and Medicine

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Section: Discussionsupporting

confidence: 57%

Section: Discussionmentioning

confidence: 85%

Section: Activation Of the Jak2/stat3 Pathway In The Lung Tumor Tissumentioning

confidence: 99%

Section: Introuctionmentioning

confidence: 99%

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PRDX6 promotes tumor development via the JAK2/STAT3 pathway in a urethane-induced lung tumor model

Yun

Park

et al. 2015

Free Radical Biology and Medicine

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“…Elevated expression levels for Prdx6 have been demonstrated in association with a broad variety of human cancers including lymphoma and cancer of the breast, esophagus, lung, liver, ovaries, pancreas, bladder, thyroid, gingiva, tongue, skin, and mesothelium among others (121)(122)(123)(124)(125)(126)(127)(128)(129)(130)(131)(132)(133).…”

Section: Cancer and Carcinogenesismentioning

confidence: 99%

The phospholipase A2 activity of peroxiredoxin 6 [S]

Fisher

2018

Journal of Lipid Research

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Peroxiredoxin 6 (Prdx6) is a Ca 2+ -independent intracellular phospholipase A 2 (called aiPLA 2 )that is localized to cytosol, lysosomes, and lysosomal-related organelles. Activity is minimal at cytosolic pH but is increased significantly with enzyme phosphorylation, at acidic pH, and in the presence of oxidized phospholipid substrate; maximal activity with phosphorylated aiPLA 2 is ~2 µmol/min/mg protein. Prdx6 is a "moonlighting" protein that also expresses glutathione peroxidase and lysophosphatidylcholine acyl transferase activities.The catalytic site for aiPLA 2 activity is an S32-H26-D140 triad; S32-H26 is also the phospholipid binding site. Activity is inhibited by a serine "protease" inhibitor (diethyl p-nitrophenyl phosphate),an analogue of the PLA 2 transition state (1-hexadecyl-3-(trifluoroethyl)-sn-glycero-2-phosphomethanol, MJ33), and by two naturally occurring proteins (surfactant protein A and p67 phox ), but not by bromoenol lactone. aiPLA 2 activity has important physiological roles in the turnover (synthesis and degradation) of lung surfactant phospholipids, in the repair of peroxidized cell membranes, and in the activation of NADPH oxidase (NOX2). The enzyme has been implicated in acute lung injury, carcinogenesis, neurodegenerative diseases, diabetes, male infertility, and sundry other conditions although its specific roles have not been well defined. Protein mutations and animal models are now available to further investigate the roles of Prdx6-aiPLA 2 activity in normal and pathological physiology.

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PRDX6 knockout restrains the malignant progression of intrahepatic cholangiocarcinoma

Zhong

et al. 2022

Med Oncol

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Intrahepatic cholangiocarcinoma (ICC) has a poor prognosis. The bifunctional protein peroxiredoxin 6 (PRDX6), which has both calcium-independent phospholipase A2 (iPLA2) and glutathione peroxidase (GPx) activity, participates in the development of multiple tumors. However, the function and clinical significance of PRDX6 in ICC remain unclear. In this study, we characterized PRDX6 in both human ICC and thioacetamide (TAA)-induced rat ICC. We found PRDX6 was significantly increased in ICC tissues, compared with the peritumoral tissues, and PRDX6 expression level was positively correlated with the malignant phenotype in ICC patients. Furthermore, PRDX6 genetic knockout significantly inhibited the tumor progression in rats. By using RNA sequencing analysis, we found 127 upregulated genes and 321 downregulated genes after PRDX6 knockout. In addition, we noticed a significant repression in the Wnt7a/b cascade, which has been shown to play an important role in the occurrence of ICC. We confirmed that gene expressions in the Wnt7a/b cascade were inhibited in ICC tissues after PRDX6 knockout by using qRT-PCR and immunohistochemistry analysis. Collectively, our findings suggest that PRDX6 may promote ICC by regulating the Wnt7a/b pathway, which could be a novel therapeutic target for ICC.

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Lung tumor growth-promoting function of peroxiredoxin 6

Cited by 37 publications

References 44 publications

PRDX6 promotes tumor development via the JAK2/STAT3 pathway in a urethane-induced lung tumor model

PRDX6 promotes tumor development via the JAK2/STAT3 pathway in a urethane-induced lung tumor model

The phospholipase A2 activity of peroxiredoxin 6 [S]

PRDX6 knockout restrains the malignant progression of intrahepatic cholangiocarcinoma

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