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ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
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Research Article

Proteomic Profile of Epithelioid Sarcoma

Kenta Mukaihara1,2, Daisuke Kubota3, Akihiko Yoshida4, Naofumi Asano1, Yoshiyuki Suehara2, Kazuo Kaneko2, Akira Kawai3 and Tadashi Kondo1*

1Division of Pharmacoproteomics, National Cancer Center Research Institute, Tokyo, Japan

2Department of Orthopedic Surgery, Juntendo University School of Medicine, Tokyo, Japan

3Division of Musculoskeletal Oncology, National Cancer Center Hospital, Tokyo, Japan

4Pathology and Clinical Laboratory Division, National Cancer Center Hospital, Tokyo, Japan

*Corresponding Author:
Tadashi Kondo, MD, PhD
Division of Pharmacoproteomics
National Cancer Center Research Institute
5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045, Japan
Tel: +81-3-3542-2511
Fax: +81-3-3547-5298
E-mail: [email protected]

Received Date: May 20, 2014; Accepted Date: June 19, 2014; Published Date: June 24, 2014

Citation: Mukaihara K, Kubota D, Yoshida A, Asano N, Suehara Y, et al. (2014) Proteomic Profile of Epithelioid Sarcoma. J Proteomics Bioinform 7: 158-165. doi: 10.4172/jpb.1000316

Copyright: © 2014 Mukaihara K, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Epithelioid sarcoma (ES) is a rare soft tissue sarcoma affecting young adults. It is a slow-growing tumor with a high rate of recurrence and metastasis to lymph nodes. Although deletion of the tumor suppressor gene, SMARCB1/ INI1, has been identified in ES, the molecular background factors are largely unknown. To clarify the molecular aberrations contributing to the malignant features of ES, we investigated the proteins present in ES tumor tissues. Two-dimensional difference gel electrophoresis of homogenized tissue samples revealed 3363 protein spots, of which 91 showed differences in intensity between tumor and adjacent non-tumor tissues in eight ES cases. Using mass spectrometry, we characterized 69 unique proteins corresponding to these protein spots. We found that the complex histology of ES was obstacle for the investigation of molecular backgrounds of ES. For instance, although the higher expression of CAPZB in tumor tissues was confirmed by Western blotting, the immunohistochemistry did not determine the specific localize CAPZB in tumor cells. Our study demonstrated the possible utility of proteomic study, and at the same time the difficult aspect of proteomics using homogenized tissue samples.

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