Proteomic interrogation of androgen action in prostate cancer cells reveals roles of aminoacyl tRNA synthetases

Adaikkalam Vellaichamy*, Arun Sreekumar, John R. Strahler, Theckelnaycke Rajendiran, Jindan Yu, Sooryanarayana Varambally, Yong Li, Gilbert S. Omenn, Arul M. Chinnaiyan, Alexey I. Nesvizhskii

*Corresponding author for this work

Research output: Contribution to journalArticle

38 Scopus citations

Abstract

Prostate cancer remains the most common malignancy among men in United States, and there is no remedy currently available for the advanced stage hormone-refractory cancer. This is partly due to the incomplete understanding of androgen-regulated proteins and their encoded functions. Whole-cell proteomes of androgen-starved and androgen-treated LNCaP cells were analyzed by semi-quantitative MudPIT ESI- ion trap MS/ MS and quantitative iTRAQ MALDI- TOF MS/MS platforms, with identification of more than 1300 high-confidence proteins. An enrichment-based pathway mapping of the androgen-regulated proteomic data sets revealed a significant dysregulation of aminoacyl tRNA synthetases, indicating an increase in protein biosynthesis- a hallmark during prostate cancer progression. This observation is supported by immunoblot and transcript data from LNCaP cells, and prostate cancer tissue. Thus, data derived from multiple proteomics platforms and transcript data coupled with informatics analysis provides a deeper insight into the functional consequences of androgen action in prostate cancer.

Original languageEnglish (US)
Article numbere7075
JournalPloS one
Volume4
Issue number9
DOIs
StatePublished - Sep 18 2009

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

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    Vellaichamy, A., Sreekumar, A., Strahler, J. R., Rajendiran, T., Yu, J., Varambally, S., Li, Y., Omenn, G. S., Chinnaiyan, A. M., & Nesvizhskii, A. I. (2009). Proteomic interrogation of androgen action in prostate cancer cells reveals roles of aminoacyl tRNA synthetases. PloS one, 4(9), [e7075]. https://doi.org/10.1371/journal.pone.0007075