PKD prevents H2O2-induced apoptosis via NF-κB and p38 MAPK in RIE-1 cells

Jun Song; Jing Li; Jingbo Qiao; Sunil Jain; B. Mark Evers; Dai H. Chung

doi:10.1016/j.bbrc.2008.11.106

PKD prevents H₂O₂-induced apoptosis via NF-κB and p38 MAPK in RIE-1 cells

Jun Song, Jing Li, Jingbo Qiao, Sunil Jain, B. Mark Evers, Dai H. Chung

Research output: Contribution to journal › Article › peer-review

45 Scopus citations

Abstract

Previously, we demonstrated that protein kinase D (PKD) plays a protective role during H₂O₂-induced intestinal cell death. Here, we sought to determine whether this effect is mediated by nuclear factor-κB (NF-κB) and mitogen-activated protein kinases (MAPKs). Treatment with H₂O₂ activated NF-κB in RIE-1 cells; H₂O₂ also induced the translocation of NF-κB p65 as well as phosphorylation of IκB-α. PKD1 siRNA inhibited H₂O₂-induced activation, translocation of NF-κB, and phosphorylation of IκB-α. We also found that overexpression of wild type PKD1 attenuated H₂O₂-induced phosphorylation of p38 MAPK and its upstream activator, MAPK kinase (MKK) 3/6, whereas the phosphorylation was increased by PKD1 siRNA or kinase-dead PKD1. Phosphorylation of neither extracellular signal-regulated kinases (ERK) 1/2 nor c-Jun N-terminal kinases (JNK) was altered by PKD1 plasmids or siRNA. Our findings suggest that PKD protects intestinal cells through up-regulation of NF-κB and down-regulation of p38 MAPK.

Original language	English
Pages (from-to)	610-614
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	378
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2008.11.106
State	Published - Jan 16 2009

Bibliographical note

Funding Information:
The authors thank Karen Martin for manuscript preparation and Tatsuo Uchida for assistance with statistical analyses. This work was supported by the Grants RO1 DK61470, RO1 DK48498, RO1 CA104748, PO1 DK 35608 from the National Institutes of Health and a Grant #8580 from the Shriners Hospital for Children.

Funding

The authors thank Karen Martin for manuscript preparation and Tatsuo Uchida for assistance with statistical analyses. This work was supported by the Grants RO1 DK61470, RO1 DK48498, RO1 CA104748, PO1 DK 35608 from the National Institutes of Health and a Grant #8580 from the Shriners Hospital for Children.

Funders	Funder number
National Institutes of Health (NIH)	8580
National Institute of Diabetes and Digestive and Kidney Diseases	R01DK061470
Shriners Hospitals for Children Cincinnati

Keywords

NF-κB
Oxidative stress
Protein kinase D
p38 MAPK

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2008.11.106

Cite this

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title = "PKD prevents H2O2-induced apoptosis via NF-κB and p38 MAPK in RIE-1 cells",

abstract = "Previously, we demonstrated that protein kinase D (PKD) plays a protective role during H2O2-induced intestinal cell death. Here, we sought to determine whether this effect is mediated by nuclear factor-κB (NF-κB) and mitogen-activated protein kinases (MAPKs). Treatment with H2O2 activated NF-κB in RIE-1 cells; H2O2 also induced the translocation of NF-κB p65 as well as phosphorylation of IκB-α. PKD1 siRNA inhibited H2O2-induced activation, translocation of NF-κB, and phosphorylation of IκB-α. We also found that overexpression of wild type PKD1 attenuated H2O2-induced phosphorylation of p38 MAPK and its upstream activator, MAPK kinase (MKK) 3/6, whereas the phosphorylation was increased by PKD1 siRNA or kinase-dead PKD1. Phosphorylation of neither extracellular signal-regulated kinases (ERK) 1/2 nor c-Jun N-terminal kinases (JNK) was altered by PKD1 plasmids or siRNA. Our findings suggest that PKD protects intestinal cells through up-regulation of NF-κB and down-regulation of p38 MAPK.",

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author = "Jun Song and Jing Li and Jingbo Qiao and Sunil Jain and {Mark Evers}, B. and Chung, {Dai H.}",

note = "Funding Information: The authors thank Karen Martin for manuscript preparation and Tatsuo Uchida for assistance with statistical analyses. This work was supported by the Grants RO1 DK61470, RO1 DK48498, RO1 CA104748, PO1 DK 35608 from the National Institutes of Health and a Grant #8580 from the Shriners Hospital for Children.",

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AU - Jain, Sunil

AU - Mark Evers, B.

AU - Chung, Dai H.

N1 - Funding Information: The authors thank Karen Martin for manuscript preparation and Tatsuo Uchida for assistance with statistical analyses. This work was supported by the Grants RO1 DK61470, RO1 DK48498, RO1 CA104748, PO1 DK 35608 from the National Institutes of Health and a Grant #8580 from the Shriners Hospital for Children.

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N2 - Previously, we demonstrated that protein kinase D (PKD) plays a protective role during H2O2-induced intestinal cell death. Here, we sought to determine whether this effect is mediated by nuclear factor-κB (NF-κB) and mitogen-activated protein kinases (MAPKs). Treatment with H2O2 activated NF-κB in RIE-1 cells; H2O2 also induced the translocation of NF-κB p65 as well as phosphorylation of IκB-α. PKD1 siRNA inhibited H2O2-induced activation, translocation of NF-κB, and phosphorylation of IκB-α. We also found that overexpression of wild type PKD1 attenuated H2O2-induced phosphorylation of p38 MAPK and its upstream activator, MAPK kinase (MKK) 3/6, whereas the phosphorylation was increased by PKD1 siRNA or kinase-dead PKD1. Phosphorylation of neither extracellular signal-regulated kinases (ERK) 1/2 nor c-Jun N-terminal kinases (JNK) was altered by PKD1 plasmids or siRNA. Our findings suggest that PKD protects intestinal cells through up-regulation of NF-κB and down-regulation of p38 MAPK.

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