ArticleCell stress & chaperones2009
HspBP1 levels are elevated in breast tumor tissue and inversely related to tumor aggressiveness.
Article in Cell stress & chaperones, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Comprehensive Molecular and Genomic Analysis of NCI-MATCH Subprotocol Y: Capivasertib in Patients With anJCO precision oncology · 2025Article
- The Antitumor Effect of the DNA Polymerase Alpha Inhibitor ST1926 in Glioblastoma: A Proteomics Approach.International journal of molecular sciences · 2023Article
- Identification of 5' upstream sequence involved in HSPBP1 gene transcription and its downregulation during HIV-1 infection.Virus research · 2023Article
- Construction of a breast cancer prognosis model based on alternative splicing and immune infiltration.Discover oncology · 2022Article
- HspBP1 is a dual function regulatory protein that controls both DNA repair and apoptosis in breast cancer cells.Cell death & disease · 2022Article
- HSP70 binding protein 1 (HspBP1) suppresses HIV-1 replication by inhibiting NF-κB mediated activation of viral gene expression.Nucleic acids research · 2016Article
- Article
- Gene expression profiles of NO- and HNO-donor treated breast cancer cells: insights into tumor response and resistance pathways.Nitric oxide : biology and chemistry · 2014Review
- Prognostic implication of HSPA (HSP70) in breast cancer patients treated with neoadjuvant anthracycline-based chemotherapy.Cell stress & chaperones · 2014Article
- Hsp70 protein complexes as drug targets.Current pharmaceutical design · 2013Review
- Molecular cochaperones: tumor growth and cancer treatment.Scientifica · 2013Review
- Impact of obesity and leptin on protein expression profiles in mouse colon.Digestive diseases and sciences · 2011Article
- Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
HspBP1 is a co-chaperone that binds to and regulates the chaperone Hsp70 (Hsp70 is used to refer to HSPA1A and HSPA1B). Hsp70 is known to be elevated in breast tumor tissue, therefore the purpose of these studies was to quantify the expression of HspBP1 in primary breast tumors and in serum of these patients with a follow-up analysis after 6 to 7 years. Levels of HspBP1, Hsp70, and anti-HspBP1 antibodies in sera of breast cancer patients and healthy individuals were measured by enzyme-linked immunosorbent assay. Expression of HspBP1 was quantified from biopsies of tumor and normal breast tissue by Western blot analysis. The data obtained were analyzed for association with tumor aggressiveness markers and with patient outcome. The levels of HspBP1 and Hsp70 were significantly higher in sera of patients compared to sera of healthy individuals. HspBP1 antibodies did not differ significantly between groups. HspBP1 levels were significantly higher in tumor (14.46 ng/microg protein, n = 51) compared to normal adjacent tissue (3.17 ng/microg protein, n = 41, p < 0.001). Expression of HspBP1 was significantly lower in patients with lymph node metastasis and positive for estrogen receptors. HspBP1 levels were also significantly lower in patients with a higher incidence of metastasis and death following a 6 to 7-year follow-up. The HspBP1/Hsp70 molar ratio was not associated with the prognostic markers analyzed. Our results indicate that low HspBP1 expression could be a candidate tumor aggressiveness marker.
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