Proteomic profiling reveals upregulated protein expression of Hsp70 in keloids

JuHee Lee, Jung U. Shin, Inhee Jung, Hemin Lee, Dong Kyun Rah, Jin Young Jung, Won Jai Lee

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Background. The biochemical characteristics of keloid-derived fibroblasts differ from those of adjacent normal fibroblasts, and these differences are thought to be the cause of abnormal fibrosis. Therefore, we investigated the characteristic proteins that are differentially expressed in keloid-derived fibroblasts using proteomics tools. Objective. We attempted to investigate the novel proteins that play important roles in the pathophysiology of keloids. Methods. Proteomics analysis was performed to identify differentially expressed proteins in keloid-derived fibroblasts. Keloid-derived fibroblasts and adjacent normal fibroblasts were analyzed with 2-DAGE. We validated these proteins with immunoblot analysis, real-time RT-PCR, and immunohistochemistry. Results. Sixteen differentially expressed protein spots were identified in keloid-derived fibroblasts. Among them, heat shock protein 70 (Hsp70) was specifically upregulated in keloid-derived fibroblasts. Also, immunohistochemistry and western blot analysis revealed increased Hsp70, TGF-β, and PCNA expressions in keloids compared to normal tissue. Conclusion. Hsp70 is overexpressed in keloid fibroblasts and tissue. The overexpression of Hsp70 may be involved in the pathogenesis of keloids, and the inhibition of Hsp70 could be a new therapeutic tool for the treatment of keloids.

Original languageEnglish
Article number621538
JournalBioMed Research International
Volume2013
DOIs
Publication statusPublished - 2013 Nov 18

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Keloid
HSP70 Heat-Shock Proteins
Fibroblasts
Proteomics
Proteins
Tissue
Immunohistochemistry
Proliferating Cell Nuclear Antigen
Real-Time Polymerase Chain Reaction
Fibrosis
Western Blotting

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Cite this

Lee, J., Shin, J. U., Jung, I., Lee, H., Rah, D. K., Jung, J. Y., & Lee, W. J. (2013). Proteomic profiling reveals upregulated protein expression of Hsp70 in keloids. BioMed Research International, 2013, [621538]. https://doi.org/10.1155/2013/621538
Lee, JuHee ; Shin, Jung U. ; Jung, Inhee ; Lee, Hemin ; Rah, Dong Kyun ; Jung, Jin Young ; Lee, Won Jai. / Proteomic profiling reveals upregulated protein expression of Hsp70 in keloids. In: BioMed Research International. 2013 ; Vol. 2013.
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Proteomic profiling reveals upregulated protein expression of Hsp70 in keloids. / Lee, JuHee; Shin, Jung U.; Jung, Inhee; Lee, Hemin; Rah, Dong Kyun; Jung, Jin Young; Lee, Won Jai.

In: BioMed Research International, Vol. 2013, 621538, 18.11.2013.

Research output: Contribution to journalArticle

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N2 - Background. The biochemical characteristics of keloid-derived fibroblasts differ from those of adjacent normal fibroblasts, and these differences are thought to be the cause of abnormal fibrosis. Therefore, we investigated the characteristic proteins that are differentially expressed in keloid-derived fibroblasts using proteomics tools. Objective. We attempted to investigate the novel proteins that play important roles in the pathophysiology of keloids. Methods. Proteomics analysis was performed to identify differentially expressed proteins in keloid-derived fibroblasts. Keloid-derived fibroblasts and adjacent normal fibroblasts were analyzed with 2-DAGE. We validated these proteins with immunoblot analysis, real-time RT-PCR, and immunohistochemistry. Results. Sixteen differentially expressed protein spots were identified in keloid-derived fibroblasts. Among them, heat shock protein 70 (Hsp70) was specifically upregulated in keloid-derived fibroblasts. Also, immunohistochemistry and western blot analysis revealed increased Hsp70, TGF-β, and PCNA expressions in keloids compared to normal tissue. Conclusion. Hsp70 is overexpressed in keloid fibroblasts and tissue. The overexpression of Hsp70 may be involved in the pathogenesis of keloids, and the inhibition of Hsp70 could be a new therapeutic tool for the treatment of keloids.

AB - Background. The biochemical characteristics of keloid-derived fibroblasts differ from those of adjacent normal fibroblasts, and these differences are thought to be the cause of abnormal fibrosis. Therefore, we investigated the characteristic proteins that are differentially expressed in keloid-derived fibroblasts using proteomics tools. Objective. We attempted to investigate the novel proteins that play important roles in the pathophysiology of keloids. Methods. Proteomics analysis was performed to identify differentially expressed proteins in keloid-derived fibroblasts. Keloid-derived fibroblasts and adjacent normal fibroblasts were analyzed with 2-DAGE. We validated these proteins with immunoblot analysis, real-time RT-PCR, and immunohistochemistry. Results. Sixteen differentially expressed protein spots were identified in keloid-derived fibroblasts. Among them, heat shock protein 70 (Hsp70) was specifically upregulated in keloid-derived fibroblasts. Also, immunohistochemistry and western blot analysis revealed increased Hsp70, TGF-β, and PCNA expressions in keloids compared to normal tissue. Conclusion. Hsp70 is overexpressed in keloid fibroblasts and tissue. The overexpression of Hsp70 may be involved in the pathogenesis of keloids, and the inhibition of Hsp70 could be a new therapeutic tool for the treatment of keloids.

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