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Disease Markers
Volume 2014, Article ID 594093, 8 pages
http://dx.doi.org/10.1155/2014/594093
Research Article

Identification of Human Tissue Kallikrein 6 as a Potential Marker of Laryngeal Cancer Based on the Relevant Secretory/Releasing Protein Database

1Department of Biochemistry and Molecular Biology, Molecular Medicine and Cancer Research Center, Chongqing Medical University, Chongqing 400016, China
2State Key Laboratory of Molecular Oncology, Beijing Key Laboratory for Carcinogenesis and Cancer Prevention, Cancer Institute (Hospital), Peking Union Medical College & Chinese Academy of Medical Sciences, P.O. Box 2258, Beijing 100021, China
3Department of Head and Neck Surgical Oncology, Cancer Institute (Hospital), Peking Union Medical College & Chinese Academy of Medical Sciences, Beijing 100021, China
4National Center of Biomedical Analysis, Beijing 100021, China

Received 14 November 2013; Revised 3 January 2014; Accepted 4 January 2014; Published 11 February 2014

Academic Editor: Olav Lapaire

Copyright © 2014 Ying Zhang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Objective. This study was aimed to create a large-scale laryngeal cancer relevant secretory/releasing protein database and further discover candidate biomarkers. Methods. Primary tissue cultures were established using tumor tissues and matched normal mucosal tissues collected from four laryngeal cancer patients. Serum-free conditioned medium (CM) samples were collected. These samples were then sequentially processed by SDS-PAGE separation, trypsin digestion, and LC-MS/MS analysis. The candidates in the database were validated by ELISA using plasma samples from laryngeal cancer patients, benign patients, and healthy individuals. Results. Combining MS data from the tumor tissues and normal tissues, 982 proteins were identified in total; extracellular proteins and cell surface proteins accounted for 15.0% and 4.3%, respectively. According to stringent criteria, 49 proteins were selected as candidates worthy of further validation. Of these, human tissue kallikrein 6 (KLK6) was verified. The level of KLK6 was significantly increased in the plasma samples from the cancer cohort compared to the benign and healthy cohorts and moreover showed a slight decrease in the postoperative plasma samples in comparison to the preoperative plasma samples. Conclusions. This laryngeal cancer-derived protein database provides a promising repository of candidate blood biomarkers for laryngeal cancer. The diagnostic potential of KLK6 deserves further investigation.