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Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán

2008, Número 4

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Rev Invest Clin 2008; 60 (4)


Significado funcional de las proteínas de choque térmico de 90 kDa

Cortés-González CC, Ramírez-González V, Ariza AC, Bobadilla NA

Idioma: Español
Referencias bibliográficas: 62
Paginas: 311-320
Archivo PDF: 171.72 Kb.


RESUMEN

La subfamilia de proteínas de choque térmico de 90 kDa (Hsp90) está compuesta por cinco isoformas, dentro de las cuales las dos isoformas citosólicas más abundantes se conocen como la Hsp90α y la Hsp90β. Estas proteínas son conocidas como chaperonas moleculares y regulan diferentes procesos celulares a través de interactuar con más de 100 proteínas conocidas como proteínas cliente de Hsp90. Dentro de las proteínas cliente destacan: factores de transcripción, prote-ínas cinasas y proteínas que participan en la regulación transcripcional y trasduccional de señales, tales como el receptor de hormonas esteroideas y las sintasas de óxido nítrico. Esta revisión ofrece una retrospectiva sobre el avance en el conocimiento de las funciones celulares y moleculares de Hsp90 en la fisiología vascular. También se describen los estudios que han intentado esclarecer la participación de Hsp90 en la fisiología y la fisiopatología renal. Al mismo tiempo, se revisan las herramientas moleculares alternativas que se han desarrollado con el fin de manipular la expresión de Hsp90 in vitro e in vivo, mediante su inhibición o su sobre-expresión, lo que ha permitido incrementar nuestro conocimiento sobre esta subfamilia de proteínas en condiciones normales y durante procesos fisiopatológicos.


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