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JNCI Journal of the National Cancer Institute 2004 96(22):1718-1721; doi:10.1093/jnci/djh292
© 2004 by Oxford University Press
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© 2004 Oxford University Press

BRIEF COMMUNICATION

Expression of Pirh2, a Newly Identified Ubiquitin Protein Ligase, in Lung Cancer

Wenrui Duan, Li Gao, Lawrence J. Druhan, Wei-Guo Zhu, Carl Morrison, Gregory A. Otterson, Miguel A. Villalona-Calero

Affiliations of authors: Comprehensive Cancer Center and Department of Internal Medicine (WD, LG, LJD, W-GZ, GAO, MAV-C) and Department of Pathology (CM), The Ohio State University College of Medicine and Public Health, Columbus

Correspondence to: Miguel A. Villalona-Calero, MD, Arthur G. James Cancer Hospital and Richard J. Solove Research Institute, The Ohio State University, B406 Starling-Loving Hall, 320 W. 10th Ave., Columbus, OH 43210-1240 (e-mail: villalona-1{at}medctr.osu.edu)

Maintenance of p53 function is important for normal cell growth and development, and loss of p53 function contributes directly to malignant tumor development. The recently discovered Pirh2 protein is an ubiquitin–protein ligase that negatively regulates p53 through activity by targeting it for degradation. To determine how Pirh2 may mediate lung tumorigenesis, we evaluated Pirh2 expression in human and mouse lung tumor samples and paired normal lung tissues using immunoblot analysis and immunohistochemistry. Pirh2 protein expression was higher in 27 (84%) of 32 human lung neoplasms than in matched normal lung tissue and in 14 of 15 mouse lung tumors evaluated. In addition, p53 protein was more ubiquitinated in the mouse lung tumors than in normal tissue, and overall p53 expression was lower than that in normal tissue. These results are consistent with the hypothesis that increased Pirh2 expression affects lung tumorigenesis by reducing p53 activity. To our knowledge, this is the first description of altered Pirh2 expression in human and mouse tumors.


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