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Could small heat shock protein (HSP27) be a first line approach for preventing protein aggregation in Parkinson’s disease?

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dc.contributor.authorNavarro Zaragoza, Javier
dc.contributor.authorCuenca Bermejo, Lorena
dc.contributor.authorAlmela Rojo, Pilar
dc.contributor.authorLaorden Carrasco, María Luisa
dc.contributor.authorHerrero Ezquerro, María Trinidad
dc.contributor.departmentFarmacología
dc.date.accessioned2026-04-13T07:49:57Z
dc.date.available2026-04-13T07:49:57Z
dc.date.copyright© 2021 by the authors
dc.date.issued2021-03-16
dc.description.abstractSmall heat shock proteins (HSPs), such as HSP27, are ubiquitously expressed molecular chaperones and are essential for cellular homeostasis. The major functions of HSP27 include chaperoning misfolded or unfolded polypeptides and protecting cells from toxic stress. Dysregulation of stress proteins is associated with many human diseases including neurodegenerative diseases, such as Parkinson’s disease (PD). PD is characterized by the presence of aggregates of alpha-synuclein in the central and peripheral nervous system, which induces the degeneration of dopaminergic neurons in the substantia nigra pars compacta (SNpc) and in the autonomic nervous system. Autonomic dysfunction is an important non-motor phenotype of PD, which includes cardiovascular dysregulation, among others. Nowadays, the therapies for PD focus on dopamine (DA) replacement. However, certain non-motor symptoms with a great impact on quality of life do not respond to dopaminergic drugs; therefore, the development and testing of new treatments for non-motor symptoms of PD remain a priority. Since small HSP27 was shown to prevent -synuclein aggregation and cytotoxicity, this protein might constitute a suitable target to prevent or delay the motor and non-motor symptoms of PD. In the first part of our review, we focus on the cardiovascular dysregulation observed in PD patients. In the second part, we present data on the possible role of HSP27 in preventing the accumulation of amyloid fibrils and aggregated forms of alpha-synuclein. We also include our own studies, highlighting the possible protective cardiac effects induced by L-DOPA treatment through the enhancement of HSP27 levels and activity.
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dc.identifier.citationNavarro-Zaragoza, J.; Cuenca-Bermejo, L.; Almela, P.; Laorden, M.-L.; Herrero, M.-T. Could Small Heat Shock Protein HSP27 Be a First-Line Target for Preventing Protein Aggregation in Parkinson’s Disease?. Int. J. Mol. Sci. 2021, 22, 3038. https://doi.org/10.3390/ijms22063038
dc.identifier.doihttps://doi.org/10.3390/ijms22063038
dc.identifier.eissn1422-0067
dc.identifier.urihttp://hdl.handle.net/10201/225162
dc.languageeng
dc.relationSpanish Ministry of Science (SAF/FEDER2013-49076-P, FIS PI10 02827) and Fundación Séneca (20847/PI/18).
dc.relation.publisherversionhttps://www.mdpi.com/1422-0067/22/6/3038
dc.rightsAttribution 4.0 International*
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectAlpha-synuclein
dc.subjectCardiac dysfunction
dc.subjectL-DOPA
dc.subjectNon-motor symptoms
dc.subjectSmall heat shock protein 27
dc.subjectParkinson's Disease
dc.subject.odsObjetivo 3: Salud
dc.titleCould small heat shock protein (HSP27) be a first line approach for preventing protein aggregation in Parkinson’s disease?
dc.typeinfo:eu-repo/semantics/article
dc.type.versioninfo:eu-repo/semantics/publishedVersion
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