ArticleBreast cancer research and treatment2010
The small heat shock protein HspB2 is a novel anti-apoptotic protein that inhibits apical caspase activation in the extrinsic apoptotic pathway.
Article in Breast cancer research and treatment, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Identification of cancer-associated fibroblast subpopulation and construction of an immunotherapy signature for gastric cancer.Translational cancer research · 2025Article
- Transcriptional profiling revealsFrontiers in immunology · 2025Article
- G-quadruplex formation within the promoter region ofHeliyon · 2024Article
- Review
- Evaluation of the Small Heat Shock Protein Family MembersInternational journal of molecular sciences · 2023Article
- Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities.MedComm · 2022Review
- High mRNA Expression Levels of Heat Shock Protein Family B Member 2 (International journal of molecular sciences · 2022Article
- miR-17-5p promotes the invasion and migration of colorectal cancer by regulating HSPB2.Journal of Cancer · 2022Article
- Competing endogenous RNA network analysis reveals pivotal ceRNAs in bladder urothelial carcinoma.Translational andrology and urology · 2021Article
- Integrated Transcriptomic and Proteomic Analysis Reveals Up-Regulation of Apoptosis and Small Heat Shock Proteins in Lens of Rats Under Low Temperature.Frontiers in physiology · 2021Article
- Small Heat Shock Proteins in Cancers: Functions and Therapeutic Potential for Cancer Therapy.International journal of molecular sciences · 2020Review
- Therapeutic Effect of Mongolian Medicine RuXian-I on Hyperplasia of Mammary Gland Induced by Estrogen/Progesterone through CRYAB-Promoted Apoptosis.Evidence-based complementary and alternative medicine : eCAM · 2020Article
- Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease.Frontiers in pharmacology · 2019Review
- Upregulation and phosphorylation of HspB1/Hsp25 and HspB5/αB-crystallin after transient middle cerebral artery occlusion in rats.Cell stress & chaperones · 2017Article
- An interaction study in mammalian cells demonstrates weak binding of HSPB2 to BAG3, which is regulated by HSPB3 and abrogated by HSPB8.Cell stress & chaperones · 2017Article
- Small heat shock proteins in ageing and age-related diseases.Cell stress & chaperones · 2017Review
- αB-crystallin and HspB2 deficiency is protective from diet-induced glucose intolerance.Genomics data · 2016Article
- Analysis of acquired resistance to metronomic oral topotecan chemotherapy plus pazopanib after prolonged preclinical potent responsiveness in advanced ovarian cancer.Angiogenesis · 2014Article
- alphaB-crystallin is a marker of aggressive breast cancer behavior but does not independently predict for patient outcome: a combined analysis of two randomized studies.BMC clinical pathology · 2014Article
- Myotonic dystrophy protein kinase (DMPK) prevents ROS-induced cell death by assembling a hexokinase II-Src complex on the mitochondrial surface.Cell death & disease · 2013Article
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5 authors.
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Abstract
Members of the conserved small heat shock protein (sHSP) family, such as αB-crystallin and Hsp27, are constitutively expressed in diverse malignancies and have been linked to several hallmark features of cancer including apoptosis resistance. In contrast, the sHSP HspB2/MKBP, which shares an intergenic promoter with αB-crystallin, was discovered as a chaperone of the myotonic dystrophy protein kinase and has not been previously implicated in apoptosis regulation. Here we describe a new function for HspB2 as a novel inhibitor of apical caspase activation in the extrinsic apoptotic pathway. Specifically, we demonstrate that HspB2 is expressed in a subset of human breast cancer cell lines and that ectopic expression of HspB2 in breast cancer cells confers resistance to apoptosis induced by both TRAIL and TNF-α. We also show that HspB2 inhibits the extrinsic apoptotic pathway by suppressing apical caspases-8 and 10 activation, thereby blocking downstream apoptotic events, such as Bid cleavage and caspase-3 activation. Consistent with these in vitro effects, HspB2 attenuates the anti-tumor activity of TRAIL in an orthotopic xenograft model of breast cancer. Collectively, our results reveal a novel function of HspB2 as an anti-apoptotic protein that negatively regulates apical caspase activation in the extrinsic apoptotic pathway.
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