ArticleCancer science2009
Heat shock protein 70-binding protein 1 is highly expressed in high-grade gliomas, interacts with multiple heat shock protein 70 family members, and specifically binds brain tumor cell surfaces.
Article in Cancer science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 39 citations in OpenAlex.
- Identification of 5' upstream sequence involved in HSPBP1 gene transcription and its downregulation during HIV-1 infection.Virus research · 2023Article
- HspBP1 is a dual function regulatory protein that controls both DNA repair and apoptosis in breast cancer cells.Cell death & disease · 2022Article
- P2X7 receptor: the regulator of glioma tumor development and survival.Purinergic signalling · 2022Article
- Unconventional Protein Secretion in Brain Tumors Biology: Enlightening the Mechanisms for Tumor Survival and Progression.Frontiers in cell and developmental biology · 2022Review
- The Co-Chaperone HspBP1 Is a Novel Component of Stress Granules that Regulates Their Formation.Cells · 2020Article
- Exosomal Chaperones and miRNAs in Gliomagenesis: State-of-Art and Theranostics Perspectives.International journal of molecular sciences · 2018Review
- The unfolded protein response in glioblastomas: targetable or trouble?Future science OA · 2015Review
- Article
- Investigation into the potential for hypoxic interior of neoplasms to enhance HSPA expression in glioma.Molecular and cellular biochemistry · 2014Article
- Reliability of HSP70 (HSPA) expression as a prognostic marker in glioma.Molecular and cellular biochemistry · 2014Article
- Endoplasmic reticulum chaperones and their roles in the immunogenicity of cancer vaccines.Frontiers in oncology · 2014Review
- Glioblastoma extracellular vesicles: reservoirs of potential biomarkers.Pharmacogenomics and personalized medicine · 2014Review
- Article
- The unfolded protein response in glioblastomas: passing the stress test.CNS oncology · 2013Article
- Characterization of tumor differentiation factor (TDF) and its receptor (TDF-R).Cellular and molecular life sciences : CMLS · 2013Review
- Induction of the unfolded protein response drives enhanced metabolism and chemoresistance in glioma cells.PloS one · 2013Article
- Identification of potential tumor differentiation factor (TDF) receptor from steroid-responsive and steroid-resistant breast cancer cells.The Journal of biological chemistry · 2012Article
- Medulloblastoma exosome proteomics yield functional roles for extracellular vesicles.PloS one · 2012Article
- Radioresistance of human glioma spheroids and expression of HSP70, p53 and EGFr.Radiation oncology (London, England) · 2011Article
- The heat shock-binding protein (HspBP1) protects cells against the cytotoxic action of the Tag7-Hsp70 complex.The Journal of biological chemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Chaperone proteins and heat shock proteins (HSP) are essential components of cellular protein folding systems under normal conditions; their expression and activities are upregulated during stress. Chronically stressed tumors frequently exhibit high chaperone protein levels, exploiting their anti-apoptotic mechanisms and general proteome homeostasis amidst a background of genetic instability. Co-chaperones interact with chaperones as malleable regulatory components of protein folding activity and may represent a conduit for modification of chaperone activity to the detriment of the tumor. We have initially characterized one such co-chaperone, heat shock protein 70-binding protein (HspBP) 1 from human brain tumors, their xenografts grown in immune-compromised mice, and in syngeneic murine models in immune-competent mice. Immunohistochemical analyses show HspBP1 overexpression (with unusual subcellular localizations) in patient brain tumors relative to normal brain tissue. This holds true for the xenograft and syngeneic murine tumor models. In biochemical affinity chromatography assays, HspBP1 interacts with members of the HSP70 family from brain tumor lysates and from surface-derived samples, including HSP70, glucose regulated protein (GRP)75, GRP78, and HSP110. From normal brain lysates, only heat shock cognate (HSC)70, GRP75, and HSP110 bind to HspBP1. FACS analyses indicate that HspBP1 binds to brain tumor cell surfaces, possibly via HSP70 family members, and internalizes into cells. This has implications for HspBP1 biology as well as its utility as a tumor-targeting agent. Our results suggest that HspBP1 may play a role in tumor (dys)regulation of chaperone proteins, and that HspBP1 may have extracellular roles with therapeutic implications.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.