Heat shock proteins hsp27 and hsp70: Lack of correlation with response to tamoxifen and clinical course of disease in estrogen receptor-positive metastatic breast cancer (a Southwest Oncology Group study)

Daniel R. Ciocca, Stephanie Green, Richard M Elledge, Gary M. Clark, Reginald Pugh, Peter Ravdin, Danika Lew, Silvana Martino, C. Kent Osborne

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

In this study, we tested the hypothesis that heat shock proteins (hsps) 27 and 70 are associated with clinical resistance to tamoxifen. hsp27 is, like progesterone receptor, an estrogen-regulated protein. hsp70 is also of interest because of its interaction with estrogen receptors and because hsp70 is a component of the molecular chaperone machinery functioning in the assembly and trafficking of steroid receptors. In addition, hsps in general help protect cells against noxious stimuli and stress, and their expression has been linked to drug resistance. The study involved 205 tumors from estrogen receptor-positive tamoxifen-treated breast cancer patients with metastatic disease. All patients received daily tamoxifen as initial therapy for metastatic disease. The study began in 1982, and follow-up is now 9 years. hsp27 and hsp70 were detected by immunohistochemistry and scored according to the nuclear and/or cytoplasmic content. Expression of hsp27 or hsp70 was unrelated to estrogen receptor content, progesterone receptor content, menopausal status, age, and presence of visceral disease. Cytoplasmic and nuclear hsp27 positivities were weakly and inversely related to each other (P = 0.05). There was a significant association between cytoplasmic hsp27 and cytoplasmic hsp70 content (P < 0.001), as well as between nuclear hsp70 and nuclear hsp27 content (P = 0.001). Cytoplasmic and nuclear hsp70 were also associated (P = 0.02). However, increased hsp27 and hsp70 expression (nuclear or cytoplasmic) was not significantly associated with response to tamoxifen, time to treatment failure, or survival. Thus, this study clarifies the lack of clinical utility of hsp27 and hsp70 in predicting the response to tamoxifen in an estrogen receptor-positive breast cancer population.

Original languageEnglish (US)
Pages (from-to)1263-1266
Number of pages4
JournalClinical Cancer Research
Volume4
Issue number5
StatePublished - May 1998

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Tamoxifen
Heat-Shock Proteins
Estrogen Receptors
Breast Neoplasms
Progesterone Receptors
HSP27 Heat-Shock Proteins
Molecular Chaperones
HSP70 Heat-Shock Proteins
Steroid Receptors
Treatment Failure
Drug Resistance
Immunohistochemistry
Survival
Population
Neoplasms

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

Cite this

Heat shock proteins hsp27 and hsp70 : Lack of correlation with response to tamoxifen and clinical course of disease in estrogen receptor-positive metastatic breast cancer (a Southwest Oncology Group study). / Ciocca, Daniel R.; Green, Stephanie; Elledge, Richard M; Clark, Gary M.; Pugh, Reginald; Ravdin, Peter; Lew, Danika; Martino, Silvana; Osborne, C. Kent.

In: Clinical Cancer Research, Vol. 4, No. 5, 05.1998, p. 1263-1266.

Research output: Contribution to journalArticle

Ciocca, Daniel R. ; Green, Stephanie ; Elledge, Richard M ; Clark, Gary M. ; Pugh, Reginald ; Ravdin, Peter ; Lew, Danika ; Martino, Silvana ; Osborne, C. Kent. / Heat shock proteins hsp27 and hsp70 : Lack of correlation with response to tamoxifen and clinical course of disease in estrogen receptor-positive metastatic breast cancer (a Southwest Oncology Group study). In: Clinical Cancer Research. 1998 ; Vol. 4, No. 5. pp. 1263-1266.
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