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Mol. Cells 2009; 28(6): 583-588

Published online December 31, 2009

https://doi.org/10.1007/s10059-009-0152-6

© The Korean Society for Molecular and Cellular Biology

Peroxiredoxin 6 Promotes Lung Cancer Cell
Invasion by Inducing Urokinase-Type Plasmi-nogen
Activator via p38 Kinase, Phosphoinositide
3-Kinase, and Akt

Seung Bum Lee, Jin-Nyoung Ho, Sung Hwan Yoon, Ga Young Kang, Sang-Gu Hwang, and
Hong-Duck Um

Received: September 9, 2009; Accepted: September 17, 2009

Abstract

The peroxiredoxin family of peroxidase has six mammalian members (Prx 1-6). Considering their frequent up-regulation in cancer cells, Prxs may contribute to cancer cells’ survival in face of oxidative stress. Here, we show that Prx 6 promotes the invasiveness of lung cancer cells, accompanied by an increase in the activity of phosphoinositide 3-kinase (PI3K), the phosphorylation of p38 kinase and Akt, and the protein levels of uPA. Functional studies reveal that these components support Prx 6-induced invasion in the sequence p38 kinase/PI3K, Akt, and uPA. The findings provide a new understanding of the action of Prx 6 in cancer.

Keywords cancer, cell signaling, invasion, peroxiredoxin 6

Article

Research Article

Mol. Cells 2009; 28(6): 583-588

Published online December 31, 2009 https://doi.org/10.1007/s10059-009-0152-6

Copyright © The Korean Society for Molecular and Cellular Biology.

Peroxiredoxin 6 Promotes Lung Cancer Cell
Invasion by Inducing Urokinase-Type Plasmi-nogen
Activator via p38 Kinase, Phosphoinositide
3-Kinase, and Akt

Seung Bum Lee, Jin-Nyoung Ho, Sung Hwan Yoon, Ga Young Kang, Sang-Gu Hwang, and
Hong-Duck Um

Received: September 9, 2009; Accepted: September 17, 2009

Abstract

The peroxiredoxin family of peroxidase has six mammalian members (Prx 1-6). Considering their frequent up-regulation in cancer cells, Prxs may contribute to cancer cells’ survival in face of oxidative stress. Here, we show that Prx 6 promotes the invasiveness of lung cancer cells, accompanied by an increase in the activity of phosphoinositide 3-kinase (PI3K), the phosphorylation of p38 kinase and Akt, and the protein levels of uPA. Functional studies reveal that these components support Prx 6-induced invasion in the sequence p38 kinase/PI3K, Akt, and uPA. The findings provide a new understanding of the action of Prx 6 in cancer.

Keywords: cancer, cell signaling, invasion, peroxiredoxin 6

Mol. Cells
Aug 31, 2022 Vol.45 No.8, pp. 513~602
COVER PICTURE
Cryo-EM structure of human porphyrin transporter ABCB6 (main figure) shows that binding of hemin (inset, magenta) in concert with two glutathione molecules (cyan) primes ABCB6 for high ATP turnover (Kim et al., pp. 575-587).

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