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El estrés del retículo endoplasmático y la base inflamatoria de las enfermedades metabólicas
1Department of Genetics and Complex Diseases, Broad Institute of Harvard and MIT, Harvard School of Public Health, Boston, MA 02115, USA. ghotamis@hsph.harvard.edu
Cell
|March 23, 2010
Resumen
El retículo endoplasmático (ER) es vital para el plegamiento de las proteínas. Su disfunción desencadena la respuesta proteica desplegada (UPR), que vincula el estrés celular con enfermedades inflamatorias y metabólicas como la obesidad y la diabetes.
Área de la Ciencia:
- Biología celular Biología celular.
- Biología Molecular Biología Molecular
- Investigación de Enfermedades Metabólicas.
Sus antecedentes:
- El retículo endoplasmático (ER) es un orgánulo crucial para la síntesis, el plegamiento y el transporte de proteínas.
- El estrés celular puede abrumar la capacidad del ER, lo que lleva a la respuesta proteica desplegada (UPR).
Objetivo del estudio:
- Explorar el papel del estrés ER y el UPR en el contexto de las enfermedades metabólicas crónicas.
- Para investigar la intersección de la señalización de ER, la inflamación y la disfunción metabólica.
Principales métodos:
- El estudio integra el conocimiento de la biología celular y las vías de señalización molecular.
- Análisis de la literatura existente sobre el estrés de ER, UPR, inflamación y enfermedad metabólica.
Principales resultados:
- El estrés ER y la activación de la UPR están vinculados a las vías de señalización inflamatorias y de estrés.
- Estas vías están implicadas en la patogénesis de la obesidad, la resistencia a la insulina y la diabetes tipo 2.
Conclusiones:
- El ER y sus redes de señalización asociadas representan un nexo clave para la inflamación y las enfermedades metabólicas.
- Dirigirse a la función ER puede ofrecer nuevas estrategias terapéuticas para los trastornos metabólicos.
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01:31Regulation of the Unfolded Protein Response
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01:37The Unfolded Protein Response
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01:24Type II Diabetes II: Pathophysiology
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01:27Post-translational Translocation of Proteins to the RER
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
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Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...