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Originally published In Press as doi:10.1074/mcp.R600005-MCP200 on June 19, 2006.
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Molecular & Cellular Proteomics 5:1787-1798, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

Cancer

Mass Spectrometry-based Proteomic Studies of Human Anaplastic Large Cell Lymphoma*

Megan S. Lim{ddagger} and Kojo S. J. Elenitoba-Johnson

From the Department of Pathology and Associated Regional and University Pathologists Institute for Clinical and Experimental Pathology, University of Utah Health Sciences Center, Salt Lake City, Utah 84132

Malignant lymphomas are a diverse group of malignant neoplasms that arise as a result of a complex interplay of multiple factors including genetic aberrations, immunosuppression, and exposure to noxious agents such as ionizing radiation and chemical agents. Anaplastic large cell lymphoma (ALCL) is an aggressive T-lineage lymphoma harboring chromosomal translocations involving the anaplastic lymphoma kinase (ALK) tyrosine kinase. The most common translocation in ALCL is the t(2;5)(p23;q35). This results in the formation of a chimeric fusion kinase, nucleophosmin/ALK. Nucleophosmin/ALK activates numerous downstream signaling pathways resulting in enhanced survival and proliferation. Using a variety of mass spectrometry-driven proteomic strategies, we have studied several aspects of the ALCL proteome. In this review, we provide a summary of mass spectrometry-based proteomic studies that expands the current understanding of the molecular pathogenesis of ALCL and provides the basis for the identification of biomarkers and targets for novel therapeutic agents.

{ddagger} To whom correspondence should be addressed: Div. of Anatomic Pathology, University of Utah Health Sciences Center, 50 North Medical Dr., Salt Lake City, UT 84132. Tel.: 801-581-5854; Fax: 801-585-3831; E-mail: megan.lim{at}path.utah.edu


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