Mostrar el registro sencillo del ítem

dc.contributor.author
Mazaira, Gisela Ileana  
dc.contributor.author
Erlejman, Alejandra Giselle  
dc.contributor.author
Galigniana, Mario Daniel  
dc.contributor.other
Watanabe, Hiroto S.  
dc.date.available
2021-12-20T17:07:12Z  
dc.date.issued
2017  
dc.identifier.citation
Mazaira, Gisela Ileana; Erlejman, Alejandra Giselle; Galigniana, Mario Daniel; The role of heat-shock proteins and chaperonins in the pathogenesis and progression of cancer; Nova Science Publishers; 64; 2017; 34-84  
dc.identifier.isbn
978-1-53610-512-4  
dc.identifier.uri
http://hdl.handle.net/11336/149031  
dc.description.abstract
The superfamily of molecular chaperones plays a cardinal role in the maintenance of protein stability and function through a complex system of cooperative mechanisms able to balance proteostasis at different levels, from the synthesis of peptides to their proper folding, oligomerization, subcellular localization, and biological depuration. While most chaperones are also heat-shock proteins and show the ability to bind and release client-proteins of different sizes in a dynamic equilibrium, there is a subset of molecular chaperones that show the property to seize single peptide chains rather than bulky molecules, such that the protein is sequestered within a molecular cage arrangement. These are the so called chaperonins. There is considerable evidence to relate both types of molecular chaperones in the development and/or progression of cancer. The expression of several molecular chaperones is induced in many types of tumor, to the point that they are currently considered novel prognostic biomarkers. These findings have led to the development of synthetic organic ligands with therapeutic purposes. Comparatively, the contribution of chaperonins to cancer has not received as much attention to date compared to conventional heat-shock proteins. In several pathologies, both types of molecular chaperones are induced and are released from the cell by a still poorly understood mechanism. Extracellular molecular chaperones stimulate anti-inflammatory responses, thereby inducing a negative feedback to control of inflammation, such that immunization with defined peptides of some chaperones prevents the development of certain diseases. In this chapter, it is summarized the state of the art for heat-shock proteins in tumor development and progression, and is analyzed the evidence for the emerging role of chaperonins complexes in oncology.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Nova Science Publishers  
dc.rights
info:eu-repo/semantics/restrictedAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
cancer  
dc.subject
HSP90  
dc.subject
HSP70  
dc.subject
Chaperoninas  
dc.subject.classification
Bioquímica y Biología Molecular  
dc.subject.classification
Medicina Básica  
dc.subject.classification
CIENCIAS MÉDICAS Y DE LA SALUD  
dc.title
The role of heat-shock proteins and chaperonins in the pathogenesis and progression of cancer  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.type
info:eu-repo/semantics/bookPart  
dc.type
info:ar-repo/semantics/parte de libro  
dc.date.updated
2021-06-07T16:56:43Z  
dc.journal.volume
64  
dc.journal.pagination
34-84  
dc.journal.pais
Estados Unidos  
dc.journal.ciudad
Nueva York  
dc.description.fil
Fil: Mazaira, Gisela Ileana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina  
dc.description.fil
Fil: Erlejman, Alejandra Giselle. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina  
dc.description.fil
Fil: Galigniana, Mario Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://novapublishers.com/shop/horizons-in-cancer-research-volume-64/  
dc.conicet.paginas
231  
dc.source.titulo
Horizons in Cancer Research