The Antioxidative Effect of Heat-Shock Protein 70 in Dendritic Cells

J. H. Je, D. Y. Kim, H. J. Roh, C. Pak, D. H. Kim, D. Byamba, H. Jee, T. G. Kim, J. M. Park, S. K. Lee, M. G. Lee

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Reactive oxygen species (ROS) are produced by dendritic cells (DCs) during antigen presentation in contact hypersensitivity (CHS). ROS cause a number of non-enzymatic protein modifications, such as carbonylation. Carbonylated proteins in DCs in response to hapten have not been fully identified yet. To identify the proteins carbonylated by ROS, murine epidermis-derived DC line XS106 was challenged with a hapten, 2,4,6-trinitrobenzene sulphonic acid (TNBS). MALDI-TOF analysis revealed that heat-shock protein 70 (HSP70) was one of the carbonylated proteins induced by TNBS. To verify the role of HSP70 in TNBS-treated XS106 cell, we fused protein transduction domain (PTD) with HSP70 to facilitate protein delivery into the cell. The transfected fusion protein HSP70 within the cell caused transient increase of the cellular level of HSP70. Transient increase of HSP70 level in XS-106 DCs resulted in inhibition of ROS production, carbonylation of HSP70, p38 MAPK activation and subsequently IL-12 secretion. To investigate the effects of PTD-HSP70 in vivo, ear-swelling experiments with 2,4,6-trinitro-1-chlorobenzene (TNCB) were performed in BALB/c mice. Pretreatment of PTD-HSP70 reduced the CHS response to TNCB in vivo. We report here that carbonylation of HSP70 by ROS is associated with the pathogenesis of CHS, suggesting possibility of HSP70-targeting therapy in CHS.

Original languageEnglish
Pages (from-to)238-247
Number of pages10
JournalScandinavian Journal of Immunology
Volume78
Issue number3
DOIs
Publication statusPublished - 2013 Sep 1

Fingerprint

HSP70 Heat-Shock Proteins
Dendritic Cells
Contact Dermatitis
Reactive Oxygen Species
Sulfonic Acids
Picryl Chloride
Proteins
Haptens
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Antigen Presentation
p38 Mitogen-Activated Protein Kinases
Protein Transport
Interleukin-12
Epidermis
Ear

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

Je, J. H. ; Kim, D. Y. ; Roh, H. J. ; Pak, C. ; Kim, D. H. ; Byamba, D. ; Jee, H. ; Kim, T. G. ; Park, J. M. ; Lee, S. K. ; Lee, M. G. / The Antioxidative Effect of Heat-Shock Protein 70 in Dendritic Cells. In: Scandinavian Journal of Immunology. 2013 ; Vol. 78, No. 3. pp. 238-247.
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Je, JH, Kim, DY, Roh, HJ, Pak, C, Kim, DH, Byamba, D, Jee, H, Kim, TG, Park, JM, Lee, SK & Lee, MG 2013, 'The Antioxidative Effect of Heat-Shock Protein 70 in Dendritic Cells', Scandinavian Journal of Immunology, vol. 78, no. 3, pp. 238-247. https://doi.org/10.1111/sji.12078

The Antioxidative Effect of Heat-Shock Protein 70 in Dendritic Cells. / Je, J. H.; Kim, D. Y.; Roh, H. J.; Pak, C.; Kim, D. H.; Byamba, D.; Jee, H.; Kim, T. G.; Park, J. M.; Lee, S. K.; Lee, M. G.

In: Scandinavian Journal of Immunology, Vol. 78, No. 3, 01.09.2013, p. 238-247.

Research output: Contribution to journalArticle

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AU - Je, J. H.

AU - Kim, D. Y.

AU - Roh, H. J.

AU - Pak, C.

AU - Kim, D. H.

AU - Byamba, D.

AU - Jee, H.

AU - Kim, T. G.

AU - Park, J. M.

AU - Lee, S. K.

AU - Lee, M. G.

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N2 - Reactive oxygen species (ROS) are produced by dendritic cells (DCs) during antigen presentation in contact hypersensitivity (CHS). ROS cause a number of non-enzymatic protein modifications, such as carbonylation. Carbonylated proteins in DCs in response to hapten have not been fully identified yet. To identify the proteins carbonylated by ROS, murine epidermis-derived DC line XS106 was challenged with a hapten, 2,4,6-trinitrobenzene sulphonic acid (TNBS). MALDI-TOF analysis revealed that heat-shock protein 70 (HSP70) was one of the carbonylated proteins induced by TNBS. To verify the role of HSP70 in TNBS-treated XS106 cell, we fused protein transduction domain (PTD) with HSP70 to facilitate protein delivery into the cell. The transfected fusion protein HSP70 within the cell caused transient increase of the cellular level of HSP70. Transient increase of HSP70 level in XS-106 DCs resulted in inhibition of ROS production, carbonylation of HSP70, p38 MAPK activation and subsequently IL-12 secretion. To investigate the effects of PTD-HSP70 in vivo, ear-swelling experiments with 2,4,6-trinitro-1-chlorobenzene (TNCB) were performed in BALB/c mice. Pretreatment of PTD-HSP70 reduced the CHS response to TNCB in vivo. We report here that carbonylation of HSP70 by ROS is associated with the pathogenesis of CHS, suggesting possibility of HSP70-targeting therapy in CHS.

AB - Reactive oxygen species (ROS) are produced by dendritic cells (DCs) during antigen presentation in contact hypersensitivity (CHS). ROS cause a number of non-enzymatic protein modifications, such as carbonylation. Carbonylated proteins in DCs in response to hapten have not been fully identified yet. To identify the proteins carbonylated by ROS, murine epidermis-derived DC line XS106 was challenged with a hapten, 2,4,6-trinitrobenzene sulphonic acid (TNBS). MALDI-TOF analysis revealed that heat-shock protein 70 (HSP70) was one of the carbonylated proteins induced by TNBS. To verify the role of HSP70 in TNBS-treated XS106 cell, we fused protein transduction domain (PTD) with HSP70 to facilitate protein delivery into the cell. The transfected fusion protein HSP70 within the cell caused transient increase of the cellular level of HSP70. Transient increase of HSP70 level in XS-106 DCs resulted in inhibition of ROS production, carbonylation of HSP70, p38 MAPK activation and subsequently IL-12 secretion. To investigate the effects of PTD-HSP70 in vivo, ear-swelling experiments with 2,4,6-trinitro-1-chlorobenzene (TNCB) were performed in BALB/c mice. Pretreatment of PTD-HSP70 reduced the CHS response to TNCB in vivo. We report here that carbonylation of HSP70 by ROS is associated with the pathogenesis of CHS, suggesting possibility of HSP70-targeting therapy in CHS.

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