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Elexacaftor Mediates the Rescue of F508del CFTR Functional Expression Interacting with MSD2.
Bongiorno, Roberta; Ludovico, Alessandra; Moran, Oscar; Baroni, Debora.
Afiliación
  • Bongiorno R; Istituto di Biofisica, CNR, Via De Marini, 6, 16149 Genova, Italy.
  • Ludovico A; Istituto di Biofisica, CNR, Via De Marini, 6, 16149 Genova, Italy.
  • Moran O; Istituto di Biofisica, CNR, Via De Marini, 6, 16149 Genova, Italy.
  • Baroni D; Istituto di Biofisica, CNR, Via De Marini, 6, 16149 Genova, Italy.
Int J Mol Sci ; 24(16)2023 Aug 16.
Article en En | MEDLINE | ID: mdl-37629017
Cystic fibrosis (CF) is one of the most frequent lethal autosomal recessive diseases affecting the Caucasian population. It is caused by loss of function variants of the cystic fibrosis transmembrane conductance regulator (CFTR), a membrane protein located on the apical side of epithelial cells. The most prevalent CF-causing mutation, the deletion of phenylalanine at position 508 (F508del), is characterized by folding and trafficking defects, resulting in the decreased functional expression of the protein on the plasma membrane. Two classes of small-molecule modulators, termed potentiators and correctors, respectively, have been developed to rescue either the gating or the cellular processing of defective F508del CFTR. Kaftrio, a next-generation triple-combination drug, consisting of the potentiator ivacaftor (VX770) and the two correctors tezacaftor (VX661) and elexacaftor (VX445), has been demonstrated to be a life-changing therapeutic modality for the majority of people with CF worldwide. While the mechanism of action of VX770 and VX661 is almost known, the precise mechanism of action and binding site of VX445 have not been conclusively determined. We investigated the activity of VX445 on mutant F508del to identify the protein domains whose expression is mostly affected by this corrector and to disclose its mechanisms of action. Our biochemical analyses revealed that VX445 specifically improves the expression and the maturation of MSD2, heterologously expressed in HEK 293 cells, and confirmed that its effect on the functional expression of defective F508del CFTR is additive either with type I or type II CFTR correctors. We are confident that our study will help to make a step forward in the comprehension of the etiopathology of the CF disease, as well as to give new information for the development and testing of combinations of even more effective correctors able to target mutation-specific defects of the CFTR protein.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Regulador de Conductancia de Transmembrana de Fibrosis Quística / Fibrosis Quística Límite: Humans Idioma: En Revista: Int J Mol Sci Año: 2023 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Regulador de Conductancia de Transmembrana de Fibrosis Quística / Fibrosis Quística Límite: Humans Idioma: En Revista: Int J Mol Sci Año: 2023 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza