Your browser doesn't support javascript.
loading
Functional and Structural Characterization of ClC-1 and Nav1.4 Channels Resulting from CLCN1 and SCN4A Mutations Identified Alone and Coexisting in Myotonic Patients.
Brenes, Oscar; Barbieri, Raffaella; Vásquez, Melissa; Vindas-Smith, Rebeca; Roig, Jeffrey; Romero, Adarli; Valle, Gerardo Del; Bermúdez-Guzmán, Luis; Bertelli, Sara; Pusch, Michael; Morales, Fernando.
Afiliación
  • Brenes O; Departamento de Fisiología, Escuela de Medicina, Universidad de Costa Rica, 11501 San José, Costa Rica.
  • Barbieri R; Centro de Investigación en Neurociencias (CIN), Universidad de Costa Rica, 11501 San José, Costa Rica.
  • Vásquez M; Istituto di Biofisica, CNR, 16149 Genova, Italy.
  • Vindas-Smith R; Instituto de Investigaciones en Salud (INISA), Universidad de Costa Rica, 11501 San José, Costa Rica.
  • Roig J; Instituto de Investigaciones en Salud (INISA), Universidad de Costa Rica, 11501 San José, Costa Rica.
  • Romero A; Instituto de Investigaciones en Salud (INISA), Universidad de Costa Rica, 11501 San José, Costa Rica.
  • Valle GD; Escuela de Biología, Universidad de Costa Rica, 11501 San José, Costa Rica.
  • Bermúdez-Guzmán L; Laboratorio de Neurofisiología (Neurolab), 11801 San José, Costa Rica.
  • Bertelli S; Sección de Genética y Biotecnología, Escuela de Biología, Universidad de Costa Rica, 11501 San José, Costa Rica.
  • Pusch M; Istituto di Biofisica, CNR, 16149 Genova, Italy.
  • Morales F; Scuola Internazionale Superiore di Studi Avanzati (SISSA), 34136 Trieste, Italy.
Cells ; 10(2)2021 02 11.
Article en En | MEDLINE | ID: mdl-33670307
Non-dystrophic myotonias have been linked to loss-of-function mutations in the ClC-1 chloride channel or gain-of-function mutations in the Nav1.4 sodium channel. Here, we describe a family with members diagnosed with Thomsen's disease. One novel mutation (p.W322*) in CLCN1 and one undescribed mutation (p.R1463H) in SCN4A are segregating in this family. The CLCN1-p.W322* was also found in an unrelated family, in compound heterozygosity with the known CLCN1-p.G355R mutation. One reported mutation, SCN4A-p.T1313M, was found in a third family. Both CLCN1 mutations exhibited loss-of-function: CLCN1-p.W322* probably leads to a non-viable truncated protein; for CLCN1-p.G355R, we predict structural damage, triggering important steric clashes. The SCN4A-p.R1463H produced a positive shift in the steady-state inactivation increasing window currents and a faster recovery from inactivation. These gain-of-function effects are probably due to a disruption of interaction R1463-D1356, which destabilizes the voltage sensor domain (VSD) IV and increases the flexibility of the S4-S5 linker. Finally, modelling suggested that the p.T1313M induces a strong decrease in protein flexibility on the III-IV linker. This study demonstrates that CLCN1-p.W322* and SCN4A-p.R1463H mutations can act alone or in combination as inducers of myotonia. Their co-segregation highlights the necessity for carrying out deep genetic analysis to provide accurate genetic counseling and management of patients.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Canales de Cloruro / Canal de Sodio Activado por Voltaje NAV1.4 / Mutación / Miotonía / Miotonía Congénita Tipo de estudio: Prognostic_studies Límite: Female / Humans / Male / Middle aged Idioma: En Revista: Cells Año: 2021 Tipo del documento: Article País de afiliación: Costa Rica Pais de publicación: Suiza

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Canales de Cloruro / Canal de Sodio Activado por Voltaje NAV1.4 / Mutación / Miotonía / Miotonía Congénita Tipo de estudio: Prognostic_studies Límite: Female / Humans / Male / Middle aged Idioma: En Revista: Cells Año: 2021 Tipo del documento: Article País de afiliación: Costa Rica Pais de publicación: Suiza