Increased expression of cytosolic chaperonin CCT in human hepatocellular and colonic carcinoma

The chaperonin-containing t-complex polypeptide 1 (CCT) is a hetero-oligomeric molecular chaperone that assists in the folding of actin, tubulin, and other cytosolic proteins. We recently reported that the expression level of CCT is closely correlated with growth rates of mammalian cultured cells. H...

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Published inCell stress & chaperones Vol. 6; no. 4; pp. 345 - 350
Main Authors Yokota, Shin-ichi, Yamamoto, Yuzo, Shimizu, Kenji, Momoi, Hirohito, Kamikawa, Tatsuhiko, Yamaoka, Yoshio, Yanagi, Hideki, Yura, Takashi, Kubota, Hiroshi
Format Journal Article
LanguageEnglish
Published Netherlands Cell Stress Society International 01.10.2001
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Summary:The chaperonin-containing t-complex polypeptide 1 (CCT) is a hetero-oligomeric molecular chaperone that assists in the folding of actin, tubulin, and other cytosolic proteins. We recently reported that the expression level of CCT is closely correlated with growth rates of mammalian cultured cells. Here we examine the levels of CCT subunits and other molecular chaperones in tumor tissues of patients with hepatocelluar and colonic carcinoma, and compare them with nontumor tissues in the same patients. Expression levels of CCTβ in tumor tissues was significantly higher than in nontumor tissues in all patients with hepatocellular carcinoma (n = 15) and 83% of patients with colonic carcinoma (n = 17). The increased level of CCT expression in colonic cancer cells was confirmed by immunohistochemistry with anti-CCTβ antibody. The levels of CCTβ were highly correlated (r = 0.606) with those of the proliferating cell nuclear antigen (PCNA), which was used as an indicator of cell growth. CCTα gave similar results, although the correlation with PCNA levels was weaker. Other cytosolic and endoplasmic reticulum chaperones also showed higher expression in significant numbers of tumor tissues but less frequently than that observed with CCT. These results suggest that CCT is up-regulated in rapidly proliferating tumor cells in vivo to effectively produce proteins required for growth, and may serve as a useful tumor marker because it is widely distributed in the cytosol.
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Correspondence to: Hiroshi Kubota, Tel: 81 75 751-4606; Fax: 81 75 751-4646; hkubota@frontier. kyoto-u.ac.jp.
Present address: Department of Microbiology, Sapporo Medical University School of Medicine, Chuo-ku, Sapporo 060-8556, Japan.
Sumitomo Pharmaceuticals Research Center, Konohana-ku, Osaka 554-0022, Japan.
ISSN:1355-8145
1466-1268
DOI:10.1379/1466-1268(2001)006<0345:IEOCCC>2.0.CO;2