Heat shock protein 27 overexpression in breast cancer lymph node metastasis

Fk, Storm; Dm, Mahvi; Kw, Gilchrist

doi:10.1007/bf02306091

Cited by 32 publications

(25 citation statements)

References 8 publications

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“…radiotherapy and chemotherapeutic drugs (Ciocca and Calderwood 2005), and high Hsp-27 often correlates with shorter disease-free survival/recurrence following treatment in patients with advanced breast cancer (Ciocca et al 1993;Vargas-Roig et al 1998) and is therefore a poor prognostic indicator. Hsp-27 is also increased in >70% of patients with lymph node metastasis even when primary tumours are negative for Hsp-27 (Storm et al 1996). Hsp-27 enhances anchorage-independent growth (Rust et al 1999) and increases resistance to drugs (Ciocca et al 1992;Oesterreich et al 1993;Yamamoto et al 2001) and metastatic potential (Lemieux et al 1997) by acting in different capacities in cells.…”

Section: Introductionmentioning

confidence: 99%

Hsp-27 induction requires POU4F2/Brn-3b TF in doxorubicin-treated breast cancer cells, whereas phosphorylation alters its cellular localisation following drug treatment

Fujita

Ounzain

Wang

et al. 2011

Cell Stress and Chaperones

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POU4F2/Brn-3b transcription factor (referred to as Brn-3b) is elevated in >60% of breast cancers and profoundly alters growth and behaviour of cancer cells by regulating distinct subsets of target genes. Previous studies showed that Brn-3b was required to maximally transactivate small heat shock protein, HSPB1/Hsp-27 (referred to as , and consequently, Brn-3b expression correlated well with Hsp27 levels in human breast biopsies. In these studies, we showed that Brn-3b is increased in MCF7 breast cancer cells that survive following treatment with chemotherapeutic drug doxorubicin (Dox) with concomitant increases in Hsp-27 expression. Targeting of Brn3b using short interfering RNA reduced Hsp-27 in Doxtreated cells, suggesting that Brn-3b regulates Hsp-27 expression under these conditions. Wound healing assays showed increased Brn-3b in Dox-treated migratory cells that also express Hsp-27. Interestingly, Hsp-27 phosphorylation and cellular localisation are also significantly altered at different times following Dox treatment. Thus, phosphoHsp-27 (p-Hsp27) protein displayed widespread distribution after 24 hrs of Dox treatment but was restricted to the nucleus after 5 days. However, in drug-resistant cells (grown in Dox for >1 month), p-Hsp-27 was excluded from nuclei and most of the cytoplasm and appeared to be associated with the cell membrane. Studies to determine how this protein promotes survival and migration in breast cancer cells showed that the protective effects were conferred by unphosphorylated Hsp-27 protein.

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Section: Introductionmentioning

confidence: 99%

Hsp-27 induction requires POU4F2/Brn-3b TF in doxorubicin-treated breast cancer cells, whereas phosphorylation alters its cellular localisation following drug treatment

Fujita

Ounzain

Wang

et al. 2011

Cell Stress and Chaperones

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“…In addition to its putative involvement in drug resistance and radioresistance, HSP27 has also been shown to be related to cell growth and motility (24,25). High HSP27 levels may be associated with aggressive growth and infiltration and with poor prognosis (26)(27)(28).…”

Section: Introductionmentioning

confidence: 99%

Inhibition of Heat Shock Protein 27–Mediated Resistance to DNA Damaging Agents by a Novel PKCδ-V5 Heptapeptide

Kim¹,

Lee

Lee³

et al. 2007

Cancer Research

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Heat shock protein 27 (HSP27), which is highly expressed in human lung and breast cancer tissues, induced resistance to cell death against various stimuli. Treatment of NCI-H1299 cells, which express a high level of HSP27, with small interference RNA specifically targeting HSP27 resulted in inhibition of their resistance to radiation or cisplatin, suggesting that HSP27 contributed to cellular resistance in these lung cancer cells. Furthermore, because HSP27 interacts directly with the COOH terminus of the protein kinase CD (PKCD)-V5 region with ensuing inhibition of PKCD activity and PKCD-mediated cell death, we wished to determine amino acid residues in the V5 region that mediate its interaction with HSP27. Investigation with various deletion mutants of the region revealed that amino acid residues 668 to 674 of the V5 region mediate its interaction with HSP27.

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“…As such, high hsp27 levels might be associated with aggressive growth and infiltration and hence with poor prognosis. Indeed, high hsp27 expression has been associated with poor prognosis in different types of malignancy (Thor et al, 1991;Storm et al, 1996;Seymour et al, 1990). With respect to ovarian carcinomas, hsp27 levels were significantly higher in malignant than in benign or borderline tumours (Langdon et al, 1995).…”

mentioning

confidence: 99%

Heat-shock-protein-27(HSP27) expression in ovarian carcinoma: Relation in response to chemotherapy and prognosis

Arts¹,

et al. 1999

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Heat shock protein 27 overexpression in breast cancer lymph node metastasis

Abstract: hsp-27 appears to confer cytoprotection for metastatic cells, which may help explain why hsp-27 overexpression is associated with reduced disease-free survival in breast carcinomas.

Cited by 32 publications

References 8 publications

Hsp-27 induction requires POU4F2/Brn-3b TF in doxorubicin-treated breast cancer cells, whereas phosphorylation alters its cellular localisation following drug treatment

Hsp-27 induction requires POU4F2/Brn-3b TF in doxorubicin-treated breast cancer cells, whereas phosphorylation alters its cellular localisation following drug treatment

Inhibition of Heat Shock Protein 27–Mediated Resistance to DNA Damaging Agents by a Novel PKCδ-V5 Heptapeptide

Heat-shock-protein-27(HSP27) expression in ovarian carcinoma: Relation in response to chemotherapy and prognosis

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