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A Peptide Selected by Biopanning Identifies the Integrin _vß₆ as a Prognostic Biomarker for Nonsmall Cell Lung Cancer

¹ Division of Translational Research, Department of Internal Medicine, ² Department of Clinical Sciences, ³ Simmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, Dallas, Texas and ⁴ Department of Pathology, ⁵ Department of Thoracic/Head and Neck Medical Oncology, ⁶ Section of Thoracic Molecular Oncology, Department of Thoracic and Cardiovascular Surgery, University of Texas M. D. Anderson Cancer Center, Houston, Texas

Requests for reprints: Kathlynn C. Brown, 5323 Harry Hines Boulevard, Dallas, TX 75390-9185. Phone: 214-645-6348; Fax: 214-648-4156; E-mail: Kathlynn.Brown{at}UTSouthwestern.edu.

The development of new modes of diagnosis and targeted therapy for lung cancer is dependent on the identification of unique cell surface features on cancer cells and isolation of reagents that bind with high affinity and specificity to these biomarkers. We recently isolated a 20-mer peptide which binds to the lung adenocarcinoma cell line, H2009, from a phage-displayed peptide library. We show here that the cellular receptor for this peptide, TP H2009.1, is the uniquely expressed integrin, _vß₆, and the peptide binding to lung cancer cell lines correlates to integrin expression. The peptide is able to mediate cell-specific uptake of a fluorescent nanoparticle via this receptor. Expression of _vß₆ was assessed on 311 human lung cancer samples. The expression of this integrin is widespread in early-stage nonsmall cell lung carcinoma (NSCLC). Log-rank test and Cox regression analyses show that expression of this integrin is significantly associated with poor patient outcome. Preferential expression is observed in the tumors compared with the surrounding normal lung tissue. Our data indicate that _vß₆ is a prognostic biomarker for NSCLC and may serve as a receptor for targeted therapies. Thus, cell-specific peptides isolated from phage biopanning can be used for the discovery of cell surface biomarkers, emphasizing the utility of peptide libraries to probe the surface of a cell. [Cancer Res 2007;67(12):5889–95]

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