Parkin induces upregulation of 40s ribosomal protein SA and posttranslational modification of cytokeratins 8 and 18 in human cervical cancer Cells

Dae Geun Song, Yoon Suk Kim, Byung Chul Jung, Ki Jong Rhee, Cheol Ho Pan

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Parkin was originally identified as a protein associated with Parkinson's disease. Recently, numerous research studies have suggested that parkin acts as a tumor suppressor. In accordance with these studies, we previously reported that overexpression of parkin in HeLa cells induced growth inhibition. To elucidate possible mechanisms by which parkin may inhibit cell growth, HeLa cells were infected with adenoviruses expressing either the parkin gene or adenovirus alone for 72 h and a total proteomic analysis was performed using 2-D gel electrophoresis followed by LC-MS/MS. We identified three proteins whose expression changed between the two groups: the 40S ribosomal protein SA (RPSA) was downregulated in parkin virus-infected cells, and cytokeratins 8 and 18 exhibited an acid shift in pI value without a change in molecular weight, suggesting that these proteins became phosphorylated in parkin virus-infected cells. The changes in these three proteins were first observed at 60 h postinfection and were most dramatic at 72 h postinfection. Because upregulation of RPSA and dephosphorylation of cytokeratins 8/18 have been linked with tumor progression, these data suggest that parkin may inhibit cell growth, at least in part, by decreasing RPSA expression and inducing phosphorylation of cytokeratin 8/18.

Original languageEnglish
Pages (from-to)1630-1638
Number of pages9
JournalApplied Biochemistry and Biotechnology
Volume171
Issue number7
DOIs
Publication statusPublished - 2013 Dec 1

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Keratin-8
Keratin-18
Ribosomal Proteins
Post Translational Protein Processing
Uterine Cervical Neoplasms
Up-Regulation
Cells
Proteins
Cell growth
Viruses
HeLa Cells
Adenoviridae
Tumors
Growth
Phosphorylation
Electrophoresis, Gel, Two-Dimensional
Electrophoresis
Proteomics
Neoplasms
Down-Regulation

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology

Cite this

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abstract = "Parkin was originally identified as a protein associated with Parkinson's disease. Recently, numerous research studies have suggested that parkin acts as a tumor suppressor. In accordance with these studies, we previously reported that overexpression of parkin in HeLa cells induced growth inhibition. To elucidate possible mechanisms by which parkin may inhibit cell growth, HeLa cells were infected with adenoviruses expressing either the parkin gene or adenovirus alone for 72 h and a total proteomic analysis was performed using 2-D gel electrophoresis followed by LC-MS/MS. We identified three proteins whose expression changed between the two groups: the 40S ribosomal protein SA (RPSA) was downregulated in parkin virus-infected cells, and cytokeratins 8 and 18 exhibited an acid shift in pI value without a change in molecular weight, suggesting that these proteins became phosphorylated in parkin virus-infected cells. The changes in these three proteins were first observed at 60 h postinfection and were most dramatic at 72 h postinfection. Because upregulation of RPSA and dephosphorylation of cytokeratins 8/18 have been linked with tumor progression, these data suggest that parkin may inhibit cell growth, at least in part, by decreasing RPSA expression and inducing phosphorylation of cytokeratin 8/18.",
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Parkin induces upregulation of 40s ribosomal protein SA and posttranslational modification of cytokeratins 8 and 18 in human cervical cancer Cells. / Song, Dae Geun; Kim, Yoon Suk; Jung, Byung Chul; Rhee, Ki Jong; Pan, Cheol Ho.

In: Applied Biochemistry and Biotechnology, Vol. 171, No. 7, 01.12.2013, p. 1630-1638.

Research output: Contribution to journalArticle

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