Different immunohistochemical levels of Hsp60 and Hsp70 in a subset of brain tumors and putative role of Hsp60 in neuroepithelial tumorigenesis

被引:23
|
作者
Rappa, F. [1 ]
Unti, E. [2 ]
Baiamonte, P. [2 ]
Cappello, F. [1 ,3 ]
Scibetta, N.
机构
[1] Univ Palermo, Sez Anat Umana, Dipartimento Biomed Sperimentale & Neurosci Clin, I-90133 Palermo, Italy
[2] Osped Civ & Fatebenefratelli, Unita Operat Complessa Anat Patol, Palermo, Italy
[3] Ist Euromediterraneo Sci & Tecnol, Palermo, Italy
来源
EUROPEAN JOURNAL OF HISTOCHEMISTRY | 2013年 / 57卷 / 02期
关键词
Hsp60; Hsp70; astrocytoma; glioblastoma multiformae; medulloblastoma; meningioma; HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; EXPRESSION; CANCER; STRESS; CARCINOGENESIS; RELEASE; HSP10; P53;
D O I
10.4081/ejh.2013.e20
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
In this work we analysed, by immunohistochemistry, a series of brain tumors to detect the levels and cellular distribution of Hsp60 and Hsp70. We found that Hsp60 levels were significantly higher than those of Hsp70 in neuroepithelial tumors, while levels of both molecules were not significantly different from each other in meningeal neoplasms. In particular, Hsp60 immunopositivity was present mainly at the cytoplasmic level, while Hsp70 immunopositivity was found both in the cytoplasm and in the nucleus of tumor cells. The levels of these molecules in healthy control cells were always very low. Finally, Hsp60 and Hsp70 levels did not correlate with the different types (WHO grade) of neoplasm. Our results are partially in agreement with previous studies and suggest that Hsp60 is not increased by a passive phenomenon (e.g., due to the stress caused by the peritumor environment on cancer cells) but may be actively implicated in tumor progression, e.g. inhibiting tumor cell death or antitumor immune system response, as already postulated in vitro. We also briefly discuss the most recent publications on the extramitochondrial localization of Hsp60 in tumor cells and its role in tumor progression.
引用
收藏
页码:124 / 127
页数:4
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