The distinctive role of small heat shock proteins in oncogenesis

被引：9
作者：
Laudanski, K
Wyczechowska, D
机构：
[1] Griffin Hosp, Dept Med, Derby, CT 06418 USA
[2] Med Univ Lodz, Dept Med Chem, Lodz, Poland
来源：
ARCHIVUM IMMUNOLOGIAE ET THERAPIAE EXPERIMENTALIS | 2006年 / 54卷 / 02期
关键词：
small heat shock proteins; alpha A-crystallin; alpha B-crystallin; HSP-27; carcinogenesis; neoplasm; immune system;
D O I：
10.1007/s00005-006-0013-3
中图分类号：
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号：
100102 ;
摘要：
Recently, the role of small heat shock proteins (HSPs) has been widely recognized in cancer research. Small HSPs are tumor-protective via numerous, independent mechanisms such as: oxidative stress, protection preventing protein denaturation, anti-apoptotic activity, and likely direct suppression of the immune system. However, it is unclear whether they play any role in the initial steps in carcinogenesis. This article seeks to familiarize the reader with general characteristics of small HSPs (especially HSP-27, alpha A/B-crystallins), their tissue distribution with special regard on expression in malignant specimens, and biological properties of intracellular HSP-27 and alpha A/B-crystallins promoting tumor genesis and growth. A separate chapter describes immunomodulatory characteristics of extracellular HSP-27 with special emphasis on their plausible effect on the neoplasm development.
引用
收藏
页码：103 / 111
页数：9
相关论文
共 117 条
[11]   HspB3, the most deviating of the six known human small heat shock proteins [J].
Boelens, WC ;
Van Boekel, MAM ;
De Jong, WW .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1998, 1388 (02) :513-516
[12]   Hsp27 negatively regulates cell death by interacting with cytochrome c [J].
Bruey, JM ;
Ducasse, C ;
Bonniaud, P ;
Ravagnan, L ;
Susin, SA ;
Diaz-Latoud, C ;
Gurbuxani, S ;
Arrigo, AP ;
Kroemer, G ;
Solary, E ;
Garrido, C .
NATURE CELL BIOLOGY, 2000, 2 (09) :645-652
[13]   Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo [J].
Bruey, JM ;
Paul, C ;
Fromentin, A ;
Hilpert, S ;
Arrigo, AP ;
Solary, E ;
Garrido, C .
ONCOGENE, 2000, 19 (42) :4855-4863
[14]   Small heat-shock proteins and clusterin: Intra- and extracellular molecular chaperones with a common mechanism of action and function? [J].
Carver, JA ;
Rekas, A ;
Thorn, DC ;
Wilson, MR .
IUBMB LIFE, 2003, 55 (12) :661-668
[15]   Ceramide formation during heat shock: A potential mediator of alpha B-crystallin transcription [J].
Chang, Y ;
Abe, A ;
Shayman, JA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (26) :12275-12279
[16]   Inhibition of Daxx-mediated apoptosis by heat shock protein 27 [J].
Charette, SJ ;
Lavoie, JN ;
Lambert, H ;
Landry, J .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (20) :7602-7612
[17]  
Charpentier AH, 2000, CANCER RES, V60, P5977
[18]   Heat shock factor 1 and heat shock proteins: Critical partners in protection against acute cell injury [J].
Christians, ES ;
Yan, LJ ;
Benjamin, IJ .
CRITICAL CARE MEDICINE, 2002, 30 (01) :S43-S50
[19]   Identification of metastasis-associated proteins through protein analysis of metastatic MDA-MB-435 and metastasis-suppressed BRMS1 transfected-MDA-MB-435 cells [J].
Cicek, M ;
Samant, RS ;
Kinter, M ;
Welch, DR ;
Casey, G .
CLINICAL & EXPERIMENTAL METASTASIS, 2004, 21 (02) :149-157
[20]   BIOLOGICAL AND CLINICAL IMPLICATIONS OF HEAT-SHOCK PROTEIN 27000 (HSP27) - A REVIEW [J].
CIOCCA, DR ;
OESTERREICH, S ;
CHAMNESS, GC ;
MCGUIRE, WL ;
FUQUA, SAW .
JNCI-JOURNAL OF THE NATIONAL CANCER INSTITUTE, 1993, 85 (19) :1558-1570
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