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Expression of heat shock protein 27 and alpha-crystallins in human retinoblastoma after chemoreduction
  1. Satoru Kase (skase{at}usc.edu),
  2. Jignesh G Parikh,
  3. Narsing Rao (nrao{at}usc.edu)
  1. Doheny Eye Institute, United States
  2. Doheny Eye Institute, United States
  3. Doheny Eye Institute, United States

    Abstract

    Purpose: Small heat shock proteins (sHSP) play an important role in the resistance to anticancer drugs. We examined the expression of the sHSP family, HSP27 and α-crystallins, in human retinoblastoma with and without preoperative chemotherapy.

    Methods: Eighteen enucleated eyes from patients with retinoblastoma were used. Six patients had undergone chemotherapy before enucleation. Formalin fixed, paraffin embedded tissue sections were processed for hematoxylin-eosin staining and examined by immunohistochemistry using anti-HSP27 and α-crystallins antibodies.

    Results: Eleven of 12 cases with no history of preoperative chemotherapy showed weakly positive or negative staining for HSP27, whereas six and five cases were strongly positive for αA and αB-crystallin, respectively. In the six cases with a history of chemotherapy, several viable retinoblastoma cells remained. Immunoreactivity for HSP27 and αB-crystallin was strongly detected in the cytoplasm of viable retinoblastoma cells, while αA-crystallin immunoreactivity was less marked. Immunoreactivity for HSP27 was significantly higher in retinoblastoma cases with preoperative chemotherapy than in those without chemotherapy (P<0.0001). In contrast, immunoreactivity for αA-crystallin was significantly lower in cases with chemotherapy than in cases without chemotherapy (P<0.01).

    Conclusions: HSP27 and αB-crystallin, but not αA-crystallin, were highly expressed in viable tumour cells after chemotherapy, suggesting that HSP27 and αB-crystallin may protect tumour cells from apoptotic signals produced by anticancer drugs in retinoblastoma.

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