On the role of Hsp27 in regulating apoptosis

Concannon, C. G.; Gorman, A. M.; Samali, A.

doi:10.1023/a:1021601103096

Cited by 516Heat shock proteins researchCell death mechanisms and regulationClusterin in disease pathology

On the role of Hsp27 in regulating apoptosis

Concannon, C. G., Gorman, A. M., Samali, A.·2003·Apoptosis

DOI 10.1023/a:1021601103096

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Abstract

Heat shock proteins (Hsps) comprise several different families of proteins that are induced in response to a wide variety of physiological and environmental insults. One such protein which is highly induced during the stress response is a 27-kDa protein, termed Hsp27 whose expression is seen to correlate with increased survival in response to cytotoxic stimuli. It has been shown to prevent cell death by a wide variety of agents that cause apoptosis. Hsp27 is a molecular chaperone with an ability to interact with a large number of proteins. Recent evidence has shown that Hsp27 regulates apoptosis through an ability to interact with key components of the apoptotic signalling pathway, in particular, those involved in caspase activation and apoptosis. This article will review recent advances in the field and will address some of the potential mechanisms by which Hsp27 functions as an anti-apoptotic molecule.

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Three genes overlapped between the microglial and astrocyte factors that were not part of consensus mouse gene lists (UBC, DDIT4 and HSPB1), and these are part of cellular stress and damage response machinery.
“Finally, there were three genes that overlapped between the microglial and astrocyte factors that were not a part of consensus mouse gene lists (UBC, DDIT4 and HSPB1), but which unsurprisingly are also part of cellular stress and damage response machinery52–55.”
From Dissection of artifactual and confounding glial signatures by single-cell sequencing of mouse and human brain (2022) · cites this paper as [52]

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Identification and Characterization of cvHsp
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Characterization of two novel human small heat shock proteins: protein kinase-related HspB8 and testis-specific HspB9
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Small Heat Shock Protein 27 (HSP27) Associates with Tubulin/Microtubules in HeLa Cells
Hino, M., Kurogi, K., Okubo, M., Murata‐Hori, M., & Hosoya, H. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2553 · Cited by 98 · see citing works
Identification and Characterization of the Gene Encoding a New Member of the α-Crystallin/Small hsp Family, Closely Linked to the αB-Crystallin Gene in a Head-to-Head Manner
Iwaki, A., Nagano, T., Nakagawa, M., Iwaki, T., & Fukumaki, Y. (1997) · Genomics · doi:10.1006/geno.1997.4956 · Cited by 92 · see citing works
SV40 DNA in human osteosarcomas shows sequence variation among T-antigen genes
Lednicky, J. A., Stewart, A. R., Jenkins, J. J., Finegold, M. J., & Butel, J. S. (1997) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(19970904)72:5 · Cited by 91 · see citing works
Human αB-Crystallin
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Defined sequence segments of the small heat shock proteins HSP25 and αB‐crystallin inhibit actin polymerization
Wieske, M., Benndorf, R., Behlke, J., Dölling, R., Grelle, G., BIELKA, H., & Lutsch, G. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02082.x · Cited by 83 · see citing works
A 27 kDa heat shock protein that has anomalous prognostic powers in early and advanced breast cancer
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Apoptosis-the story so far...
Samali, A., Gorman, A. M., & Cotter, T. G. (1996) · Cellular and Molecular Life Sciences · doi:10.1007/bf01920101 · Cited by 79 · see citing works
Self-citation
Abundance of heat shock proteins (hsp89, hsp60, and hsp27) in malignant cells of Hodgkin's disease.
Hsu, P., & Hsu, S. M. (1998) · PubMed · Cited by 65 · see citing works
Apoptosis of Ewing's sarcoma cells is accompanied by accumulation of ubiquitinated proteins.
Солдатенков, В. А., & Dritschilo, A. (1997) · PubMed · Cited by 65 · see citing works
Enhancement of expression of stress proteins by agents that lower the levels of glutathione in cells
Ito, H., Okamoto, K., & Kato, K. (1998) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(98)00010-4 · Cited by 56 · see citing works
HspB3, the most deviating of the six known human small heat shock proteins
Boelens, W. C., van Boekel, M. A. M., & JONG, W. W. D. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(98)00215-5 · Cited by 53 · see citing works
Evidence for a Novel Set of Small Heat-Shock Proteins That Associates with the Mitochondria of Murine PC12 Cells and Protects NADH:Ubiquinone Oxidoreductase from Heat and Oxidative Stress
Downs, C. A., Jones, L. R., & Heckathorn, S. A. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1177 · Cited by 53 · see citing works
Protein kinase inhibitors can suppress stress-induced dissociation of Hsp27
Kato, K., Ito, H., Iwamoto, I., Iida, K., & Inaguma, Y. (2001) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2001)006 · Cited by 51 · see citing works
Heat shock proteins are differentially expressed in human gastrointestinal cancers
Ehrenfried, J. A., Herron, B. E., Townsend, C. M., & Evers, B. M. (1995) · Surgical Oncology · doi:10.1016/s0960-7404(10)80036-2 · Cited by 48 · see citing works
The small heat shock protein HSP27 is not an independent prognostic marker in axillary lymph node-negative breast cancer patients.
Oesterreich, S., Hilsenbeck, S. G., Ciocca, D. R., Allred, D. C., Clark, G. M., Chamness, G. C., Osborne, C. K., & Fuqua, S. A. W. (1996) · PubMed · Cited by 47 · see citing works
Heat shock protein 27 stimulates recovery of RNA and protein synthesis following a heat shock
Carper, S. W., Rocheleau, T. A., Cimino, D. F., & Storm, F. K. (1997) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19970801)66:2 · Cited by 35 · see citing works
Heat shock proteins: protective effect and potential therapeutic use (review).
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Expression of the small heat shock genes during Drosophila development: comparison of the accumulation of hsp23 and hsp27 mRNAs and polypeptides
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Heat shock protein expression in human tumours grown in severe combined immunodeficient mice
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Hsp90-containing multiprotein complexes in the eukaryotic microbe Achlya
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Cellular Stress Responses: Cell Survival and Cell Death
Fulda, S., Gorman, A. M., Hori, O., & Samali, A. (2010) · International Journal of Cell Biology · doi:10.1155/2010/214074 · Cited by 1,508 · see citing works
Self-citation
Molecular basis for chemoprevention by sulforaphane: a comprehensive review
Juge, N., Mithen, R. F., & Τράκα, Μ. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-6484-5 · Cited by 696 · see citing works
Heat shock genes — integrating cell survival and death
Arya, R., Mallik, M., & Lakhotia, S. C. (2007) · Journal of Biosciences · doi:10.1007/s12038-007-0059-3 · Cited by 503 · see citing works
Dissection of artifactual and confounding glial signatures by single-cell sequencing of mouse and human brain
Marsh, S. E., Walker, A. J., Kamath, T., Dissing-Olesen, L., Hammond, T. R., de Soysa, T. Y., Young, A. M. H., Murphy, S., Abdulraouf, A., Nadaf, N., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01022-8 · Cited by 432 · see citing works
Oxidative stress and its effects during dehydration
França, M. B., Panek, A. D., & Eleutherio, E. C. A. (2007) · Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2006.02.030 · Cited by 422 · see citing works
Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy
Irobi, J., Impe, K. V., Seeman, P., Jordanova, A., Dierick, I., Verpoorten, N., Michalik, A., Vriendt, E. D., Jacobs, A., Gerwen, V. V., et al. (2004) · Nature Genetics · doi:10.1038/ng1328 · Cited by 417 · see citing works
Stress management at the ER: Regulators of ER stress-induced apoptosis
Gorman, A. M., Healy, S., Jäger, R., & Afshin Samali, A. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.02.003 · Cited by 404 · see citing works
Self-citation
Antisense therapy for cancer
Gleave, M. E., & Monia, B. P. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1631 · Cited by 380 · see citing works
Incomplete response to Anti-VEGF therapy in neovascular AMD: Exploring disease mechanisms and therapeutic opportunities
Mettu, P. S., Allingham, M. J., & Cousins, S. W. (2021) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100906 · Cited by 370 · see citing works
Neuronal cell death in neurodegenerative diseases: recurring themes around protein handling
Gorman, A. M. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00402.x · Cited by 362 · see citing works
Self-citation
Heat Shock Protein 27 Increases after Androgen Ablation and Plays a Cytoprotective Role in Hormone-Refractory Prostate Cancer
Rocchi, P., So, A., Kojima, S., Signaevsky, M., Beraldi, E., Fazli, L., Hurtado‐Coll, A., Yamanaka, K., & Gleave, M. E. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3998 · Cited by 318 · see citing works
Trehalose As a “Chemical Chaperone”
Crowe, J. H. (2007) · Springer eBooks · doi:10.1007/978-0-387-39975-1_13 · Cited by 316 · see citing works
Proteomic Study Reveals That Proteins Involved in Metabolic and Detoxification Pathways Are Highly Expressed in HER-2/neu-positive Breast Cancer
Zhang, D.-H., Tai, L. K., Wong, L. L., Chiu, L.-L., Sethi, S. K., & Koay, E. S. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400221-mcp200 · Cited by 312 · see citing works
The facial nerve axotomy model
Moran, L. B., & Graeber, M. B. (2004) · Brain Research Reviews · doi:10.1016/j.brainresrev.2003.11.004 · Cited by 309 · see citing works
Hsp27 (HspB1) and αB‐crystallin (HspB5) as therapeutic targets
Arrigo, A., Simon, S., Gibert, B., Kretz‐Remy, C., Nivon, M., Czekalla, A., Guillet, D., Moulin, M., Diaz‐Latoud, C., & Vicart, P. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.04.033 · Cited by 305 · see citing works
The proteomic response of the mussel congeners Mytilus galloprovincialis and M. trossulus to acute heat stress: implications for thermal tolerance limits and metabolic costs of thermal stress
Tomanek, L., & Zuzow, M. J. (2010) · Journal of Experimental Biology · doi:10.1242/jeb.041228 · Cited by 291 · see citing works
Temporal expression of heat shock genes during cold stress and recovery from chill coma in adult Drosophila melanogaster
Colinet, H., Lee, S. F., & Hoffmann, A. A. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07470.x · Cited by 270 · see citing works
Patterns of Gene Expression That Characterize Long-term Survival in Advanced Stage Serous Ovarian Cancers
Berchuck, A., Iversen, E. S., Lancaster, J. M., Pittman, J., Luo, J. R., Lee, P., Murphy, S. K., Dressman, H. K., Febbo, P. G., West, M., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-2398 · Cited by 266 · see citing works
New Indicators of Beef Sensory Quality Revealed by Expression of Specific Genes
Bernard, C., Cassar‐Malek, I., Cunff, M. L., Dubroeucq, H., Renand, G., & Hocquette, J.-F. J.-F. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf063372l · Cited by 263 · see citing works
Heat Shock Response and Heat Shock Proteins: Current Understanding and Future Opportunities in Human Diseases
Singh, M. K., Shin, Y., Ju, S., Han, S., Choe, W., Yoon, K., Kim, S. S., & Kang, I. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084209 · Cited by 231 · see citing works
Blockade of Hsp27 overcomes Bortezomib/proteasome inhibitor PS-341 resistance in lymphoma cells.
Chauhan, D., Li, G., Shringarpure, R., Podar, K., Ohtake, Y., Hideshima, T., & Anderson, K. C. (2003) · PubMed · Cited by 228 · see citing works
Increased Hsp27 after Androgen Ablation Facilitates Androgen-Independent Progression in Prostate Cancer via Signal Transducers and Activators of Transcription 3–Mediated Suppression of Apoptosis
Rocchi, P., Beraldi, E., Ettinger, S., Fazli, L., Vessella, R. L., Nelson, C. C., & Gleave, M. E. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1840 · Cited by 225 · see citing works
The Cellular “Networking” of Mammalian Hsp27 and Its Functions in the Control of Protein Folding, Redox State and Apoptosis
Arrigo, A. (2007) · Springer eBooks · doi:10.1007/978-0-387-39975-1_2 · Cited by 207 · see citing works
Binding of Tau to Heat Shock Protein 27 Leads to Decreased Concentration of Hyperphosphorylated Tau and Enhanced Cell Survival
Shimura, H., Miura-Shimura, Y., & Kosik, K. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400351200 · Cited by 194 · see citing works
Small Heat‐shock Proteins and Clusterin: Intra‐ and Extracellular Molecular Chaperones with a Common Mechanism of Action and Function?
Carver, J. A., Rekas, A., Thorn, D. C., & Wilson, M. R. (2003) · IUBMB Life · doi:10.1080/15216540310001640498 · Cited by 189 · see citing works
Regulation of clusterin/apolipoprotein J, a functional homologue to the small heat shock proteins, by oxidative stress in ageing and age-related diseases
Trougakos, I. P., & Gonos, E. S. (2006) · Free Radical Research · doi:10.1080/10715760600902310 · Cited by 184 · see citing works
Cigarette Smoke–Related Oxidants and the Development of Sub-RPE Deposits in an Experimental Animal Model of Dry AMD
Espinosa‐Heidmann, D. G., Suñer, I. J., Catanuto, P., Hernandez, E. P., Marin‐Castaño, M. E., & Cousins, S. W. (2006) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.05-0719 · Cited by 183 · see citing works
Proteomic profiling of hepatocellular carcinoma in Chinese cohort reveals heat‐shock proteins (Hsp27, Hsp70, GRP78) up‐regulation and their associated prognostic values
Luk, J. M., Lam, C.-T., Siu, F., Lam, B., Ng, I. O., Hu, M., Che, C., & Fan, S. (2006) · PROTEOMICS · doi:10.1002/pmic.200500306 · Cited by 182 · see citing works
Stabilization of Dry Mammalian Cells: Lessons from Nature
Crowe, J. H. (2005) · Integrative and Comparative Biology · doi:10.1093/icb/45.5.810 · Cited by 178 · see citing works
Blocking Tumor Cell Migration and Invasion with Biphenyl Isoxazole Derivative KRIBB3, a Synthetic Molecule That Inhibits Hsp27 Phosphorylation
Shin, K. D., Lee, M. Y., Shin, D., Lee, S., Son, K., Koh, S., Paik, Y., Kwon, B., & Han, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507209200 · Cited by 172 · see citing works
Binding of Caspase-3 Prodomain to Heat Shock Protein 27 Regulates Monocyte Apoptosis by Inhibiting Caspase-3 Proteolytic Activation
Voss, O. H., Batra, S., Kolattukudy, S. J., González-Mejía, M. E., Smith, J. B., & Doseff, A. I. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701740200 · Cited by 169 · see citing works
Heat shock proteins and Drosophila aging
Tower, J. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.09.002 · Cited by 167 · see citing works
Hsp27 inhibits release of mitochondrial protein Smac in multiple myeloma cells and confers dexamethasone resistance
Chauhan, D., Li, G., Hideshima, T., Podar, K., Mitsiades, C. S., Mitsiades, N., Catley, L. P., Tai, Y. T., Hayashi, T., Shringarpure, R., et al. (2003) · Blood · doi:10.1182/blood-2003-05-1417 · Cited by 158 · see citing works
Chemoresistance of lung cancer stemlike cells depends on activation of Hsp27
Hsu, H., Lin, J.-H., Huang, W., Hsu, T., Su, K., Chiou, S., Tsai, Y.-T., & Hung, S. (2010) · Cancer · doi:10.1002/cncr.25599 · Cited by 145 · see citing works
HSP27: Mechanisms of Cellular Protection Against Neuronal Injury
Stetler, R. A., Gao, Y., Signore, A. P., Cao, G., & Chen, J. (2009) · Current Molecular Medicine · doi:10.2174/156652409789105561 · Cited by 142 · see citing works
PROTEASOME INHIBITION IN MULTIPLE MYELOMA: Therapeutic Implication
Chauhan, D., Hideshima, T., & Anderson, K. C. (2005) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.100037 · Cited by 135 · see citing works
Effects of heat stress on antioxidant defense system, inflammatory injury, and heat shock proteins of Muscovy and Pekin ducks: evidence for differential thermal sensitivities
Zeng, T., Li, J., Wang, D., Li, G., Wang, G., & Lu, L. (2014) · Cell Stress and Chaperones · doi:10.1007/s12192-014-0514-7 · Cited by 136 · see citing works
Hsp27 Protects against Ischemic Brain Injury via Attenuation of a Novel Stress-Response Cascade Upstream of Mitochondrial Cell Death Signaling
Stetler, R. A., Cao, G., Gao, Y., Zhang, F., Wang, S., Weng, Z., Vosler, P. S., Zhang, L., Signore, A. P., Graham, S. H., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.4407-08.2008 · Cited by 135 · see citing works
Hsp27 Modulates p53 Signaling and Suppresses Cellular Senescence
O’Callaghan-Sunol, C., Gabai, V. L., & Sherman, M. Y. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-2441 · Cited by 134 · see citing works
Heat-Shock Proteins in Neuroinflammation
Dukay, B., Csoboz, B., & Tóth, M. E. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00920 · Cited by 132 · see citing works
Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?
Choi, S.-K., Kam, H., Kim, K.-Y., Park, S. I., & Lee, Y. (2019) · Cancers · doi:10.3390/cancers11081195 · Cited by 130 · see citing works
HSP27 but not HSP70 has a potent protective effect against α‐synuclein‐induced cell death in mammalian neuronal cells
Zourlidou, A., Smith, M. D. P., & Latchman, D. S. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02273.x · Cited by 129 · see citing works
Extracellular Release of the Atheroprotective Heat Shock Protein 27 Is Mediated by Estrogen and Competitively Inhibits acLDL Binding to Scavenger Receptor-A
Rayner, K. J., Chen, Y.-X., McNulty, M. S., Simard, T., Zhao, X., Wells, D. J., de Belleroche, J., & O’Brien, E. R. (2008) · Circulation Research · doi:10.1161/circresaha.108.172155 · Cited by 128 · see citing works
Transcriptome Analysis of Human Colon Caco-2 Cells Exposed to Sulforaphane
Τράκα, Μ., Gasper, A. V., Smith, J. A., Hawkey, C. J., Bao, Y., & Mithen, R. F. (2005) · Journal of Nutrition · doi:10.1093/jn/135.8.1865 · Cited by 126 · see citing works
Heat Shock Protein 27 Functions in Inflammatory Gene Expression and Transforming Growth Factor-β-activated Kinase-1 (TAK1)-mediated Signaling
Alford, K. A., Glennie, S. J., Turrell, B. R., Rawlinson, L. M., Saklatvala, J., & Dean, J. L. E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610987200 · Cited by 123 · see citing works
Phosphorylated tau and the neurodegenerative foldopathies
Kosik, K. S., & Shimura, H. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.10.011 · Cited by 123 · see citing works
Molecular chaperones, stress resistance and development in Artemia franciscana
MacRae, T. H. (2003) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2003.09.019 · Cited by 119 · see citing works
Small heat shock proteins in smooth muscle
Salinthone, S., Tyagi, M., & Gerthoffer, W. T. (2008) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2008.04.005 · Cited by 117 · see citing works
Overexpression of LASP-1 mediates migration and proliferation of human ovarian cancer cells and influences zyxin localisation
Grünewald, T. G. P., Kämmerer, U., Winkler, C., Schindler, D., Sickmann, A., Hönig, A., & Butt, E. (2007) · British Journal of Cancer · doi:10.1038/sj.bjc.6603545 · Cited by 116 · see citing works
A small stress protein acts synergistically with trehalose to confer desiccation tolerance on mammalian cells
Ma, X., Jamil, K., MacRae, T. H., Clegg, J. S., Russell, J. M., Villeneuve, T. S., Euloth, M., Sun, Y., Crowe, J. H., Tablin, F., et al. (2005) · Cryobiology · doi:10.1016/j.cryobiol.2005.04.007 · Cited by 116 · see citing works
Mammalian HspB1 (Hsp27) is a molecular sensor linked to the physiology and environment of the cell
Arrigo, A. (2017) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0765-1 · Cited by 114 · see citing works
Changes in the Cellular Proteins of Pulmonary Alveolar Macrophage Infected with Porcine Reproductive and Respiratory Syndrome Virus by Proteomics Analysis
Zhang, H., Guo, X., Ge, X., Chen, Y., Sun, Q., & Yang, H. (2009) · Journal of Proteome Research · doi:10.1021/pr900002f · Cited by 112 · see citing works
Roles for αB-crystallin and HSPB2 in protecting the myocardium from ischemia-reperfusion-induced damage in a KO mouse model
Morrison, L. E., Whittaker, R., Klepper, R. E., Wawrousek, E. F., & Glembotski, C. C. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00715.2003 · Cited by 112 · see citing works
Enhancement of Chaperone Function of α-Crystallin by Methylglyoxal Modification
Nagaraj, R. H., Oya‐Ito, T., Padayatti, P. S., Kumar, R., Mehta, S., West, K. A., Levison, B. S., Sun, J., Crabb, J. W., & Padival, A. K. (2003) · Biochemistry · doi:10.1021/bi034541n · Cited by 111 · see citing works
Novel Triazole Ribonucleoside Down-Regulates Heat Shock Protein 27 and Induces Potent Anticancer Activity on Drug-Resistant Pancreatic Cancer
Xia, Y., Liu, Y., Wan, J., Wang, M., Rocchi, P., Qu, F., Iovanna, J., & Peng, L. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900960v · Cited by 100 · see citing works
Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks
Csermely, P., & VÃgh, L. (2007) · Springer eBooks · doi:10.1007/978-0-387-39975-1 · Cited by 99 · see citing works
Differences in the chaperone-like activities of the four main small heat shock proteins of Drosophila melanogaster
Morrow, G., Heikkila, J. J., & Tanguay, R. M. (2006) · Cell Stress and Chaperones · doi:10.1379/csc-166.1 · Cited by 97 · see citing works
Effect of dietary supplemental ascorbic acid and folic acid on the growth performance, redox status, and immune status of broiler chickens under heat stress
Gouda, A., Amer, S. A., Gabr, S., & Tolba, S. A. (2020) · Tropical Animal Health and Production · doi:10.1007/s11250-020-02316-4 · Cited by 96 · see citing works
Insights into function and regulation of small heat shock protein 25 (HSPB1) in a mouse model with targeted gene disruption
Huang, L., Min, J., Masters, S. C., Mivechi, N. F., & Moskophidis, D. (2007) · genesis · doi:10.1002/dvg.20319 · Cited by 94 · see citing works
Retinal pigment epithelium response to oxidant injury in the pathogenesis of early age-related macular degeneration
Mettu, P. S., Wielgus, A. R., Ong, S. S. Y., & Cousins, S. W. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.04.006 · Cited by 90 · see citing works
The small heat shock protein Hsp27: Present understanding and future prospects
Singh, M. K., Sharma, B., & Tiwari, P. K. (2017) · Journal of Thermal Biology · doi:10.1016/j.jtherbio.2017.06.004 · Cited by 90 · see citing works
Hsp27 and Hsp70 administered in combination have a potent protective effect against FALS-associated SOD1-mutant-induced cell death in mammalian neuronal cells
Patel, Y. J. K., Smith, M. D. P., de Belleroche, J., & Latchman, D. S. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.10.028 · Cited by 89 · see citing works
Proteomic and metabolomic analysis of atrial profibrillatory remodelling in congestive heart failure
Souza, A. I. D., Cardin, S., Wait, R., Chung, Y., Vijayakumar, M., Maguy, A., Camm, A. J., & Nattel, S. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.07.008 · Cited by 89 · see citing works
Biological Significance of Decreased HSP27 in Human Atherosclerosis
Martı́n-Ventura, J. L., Nicolas, V., Houard, X., Blanco‐Colio, L. M., Leclercq, A., Egido, J., Vranckx, R., Michel, J., & Meilhac, O. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000220108.97208.67 · Cited by 89 · see citing works
Over-Expression of Heat Shock Protein 27 Attenuates Doxorubicin-Induced Cardiac Dysfunction in Mice
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Authors: Concannon, C. G., Gorman, A. M., & Samali, A.
Affiliations: Ollscoil na Gaillimhe – University of Galway (IE)
ORCID: Gorman, A. M.
Venue: Apoptosis
Publisher: Springer Science and Business Media LLC
Published: 2003-01
Volume: 8
Issue: 1
Pages: 61-70
ISSN: 1360-8185 (ISSN-L)
1573-675X
DOI: 10.1023/a:1021601103096
OpenAlex: W2144228610
Cited by: 513
References: 109
Citations by year: 2026: 8 · 2025: 11 · 2024: 5 · 2023: 21 · 2022: 11 · 2021: 18 · 2020: 24 · 2019: 19 · 2018: 10 · 2017: 13 · 2016: 13 · 2015: 16 · 2014: 28 · 2013: 26 · 2012: 31
FWCI: 11.83
Type: journal article
Language: en
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: APOPTOSIS (publishedVersion)
PubMed (publishedVersion)
Funders: European Commission
Higher Education Authority
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Health Sciences › Medicine › Oncology › Clusterin in disease pathology
Keywords: HSP27, heat shock proteins, anti-apoptotic proteins, caspase activation, molecular chaperones, cell survival
MeSH terms: Animals, Cytoskeleton, Enzyme Activation, Heat-Shock Proteins, Humans, Models, Biological, Neoplasm Proteins, Neoplasms, Oxidation-Reduction, Protein Binding, Signal Transduction, Apoptosis, Reactive Oxygen Species, Molecular Chaperones, Caspases, HSP27 Heat-Shock Proteins, Caspase Inhibitors

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