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Expression of tropomyosin alpha 4 chain is increased in esophageal squamous cell carcinoma as evidenced by proteomic profiling by two‐dimensional electrophoresis and liquid chromatography‐mass spectrometry/mass spectrometry
Author(s) -
Harada Toshio,
Kuramitsu Yasuhiro,
Makino Akira,
Fujimoto Masanori,
Iizuka Norio,
Hoshii Yoshinobu,
Takashima Motonari,
Tamesa Michiko,
Nishimura Taku,
Takeda Shigeru,
Abe Toshihiro,
Yoshino Shigefumi,
Oka Masaaki,
Nakamura Kazuyuki
Publication year - 2007
Publication title -
proteomics – clinical applications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.948
H-Index - 54
eISSN - 1862-8354
pISSN - 1862-8346
DOI - 10.1002/prca.200600609
Subject(s) - tropomyosin , microbiology and biotechnology , chemistry , gene isoform , proteomics , gel electrophoresis , mass spectrometry , two dimensional gel electrophoresis , alpha chain , immunohistochemistry , biology , biochemistry , actin , receptor , chromatography , gene , immunology
To identify proteins associated with esophageal carcinogenesis, we performed protein profiling of 16 esophageal squamous cell carcinomas (ESCCs) and paired noncancerous tissues by 2‐DE and MS/MS. In cancerous tissues, three spots showed significant up‐regulation in the amount of protein, while eight spots were significantly down‐regulated. The identities of the spots were determined by PMF with LC‐MS/MS and were confirmed by immunoblotting. The up‐regulated proteins were tropomyosin alpha 4 chain, transgelin, and pyruvate kinase. The down‐regulated proteins were serum albumin precursor, isoforms of annexin A1, tropomyosin beta chain, 14‐3‐3 protein sigma, and isoforms of serotransferrin precursor. In all 16 cases, up‐regulation of the tropomyosin alpha 4 chain was confirmed by immunoblotting. Localization of the tropomyosin alpha 4 chain in ESCC cells and adjacent fibroblasts was confirmed by immunohistochemistry.