2013, Número 4
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Biotecnol Apl 2013; 30 (4)
Identificación de la primera molécula peptídica que inhibe efectos biológicos de la interleucina-15
Santos A, Reyes O, Cabrales A, Rodríguez Y, Geronimo H, Garay HE, Arrieta CA, Ojeda M, Machado AC, Suarez J, Ancisar JA, Vázquez M, Guillén G, Chico A, Estévez M, Llopiz A, Noda J, Sánchez A, Silengo L, Altruda F, Perea S
Idioma: Ingles.
Referencias bibliográficas: 24
Paginas: 317-319
Archivo PDF: 197.62 Kb.
RESUMEN
La interleucina-15 (IL-15) es una citocina proinflamatoria que se expresa en varias enfermedades autoinmunes e inflamatorias. Se identificó la secuencia 36-45 KVTAMKCFLL de la IL-15 humana, reconocida por la proteína de fusión hIL-15Rα-Fc soluble. Esta secuencia, sintetizada como un péptido de 10 aminoácidos, se une a la IL-15Rα y
bloquea la actividad biológica de la IL-15 en dos líneas celulares dependientes de IL-15. Mediante la estrategia de
barrido de Ala, se detectó un péptido más activo por sustitución de la segunda lisina de la secuencia del péptido por el aminoácido polar, no cargado, treonina. Usando el péptido P8 en el paso de captura de un ensayo por inmunoabsorción ligado a enzimas (ELISA), recientemente desarrollado, se cuantificó IL-15Rα soluble en fluido sinovial de pacientes con artritis reumatoide (AR) u osteoartritis (OA). Este trabajo mereció el Premio Anual de la Academia de Ciencias de Cuba, en el año 2012.
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