Heat shock proteins and survivin: Relationship and effects on proliferation index of retinoblastoma cells

• Autores: L.-B. Jiang, X.-Q. Liu, B. Li, X.-J. He, Y.-L. Jin, L.-Q. Li, F. Gao, Ning-Li Wang
• Localización: Histology and histopathology: cellular and molecular biology, ISSN-e 1699-5848, ISSN 0213-3911, Vol. 23, Nº. 7, 2008, págs. 826-831
• Idioma: inglés
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• Resumen

  • Survivin and HSPs (heat shock proteins) are important anti-apoptotic proteins. However, limited research has been done regarding the collective effects of HSPs and survivin on the proliferative activities of RB cells. The purpose of this study was to narrow this gap by focusing on the expression of HSP70 and HSP90 and the interaction of these proteins with survivin. The proliferative activities of RB cells were analyzed by assessing the Ki-67 labeling index. Ki-67 recognizes a nuclear antigen expressed in all phases of the cell cycle except G(0) and early G(1), which makes it an excellent marker of cells in the proliferative phase. Immunohistochemical procedures were performed on retinal tissues from 43 RB patients who had undergone enucleation. Expression of HSP70, HSP90 and survivin was found in 65.12%, 86.05% and 62.79% of the cases respectively. No expression of any of these markers was found in normal retinal tissues. Expression of survivin was more frequent when HSP90 was detected than when HSP90 was not detected (P<0.05). The Ki-67 labeling index was higher in cases in which HSP90 or survivin was found than in cases in which neither protein was found (P<0.05). The Ki-67 labeling index was higher in cases positive for both HSP90 and survivin than in cases in which neither protein or only one protein was found (P<0.05). Expression of HSP70 neither correlated with that of survivin, nor had any significant effect on the Ki-67 labeling index (P>0.05). Although expression of HSPs and survivin and the Ki-67 labeling index did not correlate with histopathologic typing of RB (P>0.05), our findings demonstrate that expression of HSP90 correlates with that of survivin in RB and the co-existence of survivin and HSP90 probably plays an important role in cellular proliferation in RB. Further work is indicated to clarify the role of these processes in progression of RB.