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Mutation type classification and pathogenicity assignment of sixteen missense variants located in the EGF-precursor homology domain of the LDLR.
Galicia-Garcia, Unai; Benito-Vicente, Asier; Uribe, Kepa B; Jebari, Shifa; Larrea-Sebal, Asier; Alonso-Estrada, Rocio; Aguilo-Arce, Joseba; Ostolaza, Helena; Palacios, Lourdes; Martin, Cesar.
Afiliación
  • Galicia-Garcia U; Instituto Biofisika (UPV/EHU, CSIC), 48080, Bilbao, Spain.
  • Benito-Vicente A; Instituto Biofisika (UPV/EHU, CSIC) and Departamento de Bioquímica, Universidad del País Vasco, Apdo. 644, 48080, Bilbao, Spain.
  • Uribe KB; Instituto Biofisika (UPV/EHU, CSIC) and Departamento de Bioquímica, Universidad del País Vasco, Apdo. 644, 48080, Bilbao, Spain.
  • Jebari S; Instituto Biofisika (UPV/EHU, CSIC) and Departamento de Bioquímica, Universidad del País Vasco, Apdo. 644, 48080, Bilbao, Spain.
  • Larrea-Sebal A; Instituto Biofisika (UPV/EHU, CSIC) and Departamento de Bioquímica, Universidad del País Vasco, Apdo. 644, 48080, Bilbao, Spain.
  • Alonso-Estrada R; Instituto Biofisika (UPV/EHU, CSIC), 48080, Bilbao, Spain.
  • Aguilo-Arce J; Instituto Biofisika (UPV/EHU, CSIC) and Departamento de Bioquímica, Universidad del País Vasco, Apdo. 644, 48080, Bilbao, Spain.
  • Ostolaza H; Instituto Biofisika (UPV/EHU, CSIC) and Departamento de Bioquímica, Universidad del País Vasco, Apdo. 644, 48080, Bilbao, Spain.
  • Palacios L; Progenika Biopharma, a Grifols Company, Derio, Spain.
  • Martin C; Instituto Biofisika (UPV/EHU, CSIC) and Departamento de Bioquímica, Universidad del País Vasco, Apdo. 644, 48080, Bilbao, Spain. cesar.martin@ehu.eus.
Sci Rep ; 10(1): 1727, 2020 02 03.
Article en En | MEDLINE | ID: mdl-32015373
The primary genetic cause of familial hypercholesterolemia (FH) is related to mutations in the LDLR gene encoding the Low-density Lipoprotein Receptor. LDLR structure is organized in 5 different domains, including an EGF-precursor homology domain that plays a pivotal role in lipoprotein release and receptor recycling. Mutations in this domain constitute 51.7% of the total missense variants described in LDLR. The aim of the present work was to analyse how clinically significant variants in the EGF-precursor homology domain impact LDLR. The activity of sixteen LDLR variants was functionally characterized by determining LDLR expression by Western blot and LDLR expression, LDL binding capacity and uptake, and LDLR recycling activity by flow cytometry in transfected CHO-ldlA7 cells. Of the analysed variants, we found six non-pathogenic LDLR variants and ten pathogenic variants distributed as follow: three class 3 variants; four class 2 variants; and three class 5 variants. These results can be incorporated into clinical management of patients by helping guide the appropriate level of treatment intensity depending on the extent of loss of LDLR activity. This data can also contribute to cascade-screening for pathogenic FH variants.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores de LDL / Mutación Missense / Hiperlipoproteinemia Tipo II Límite: Animals / Humans Idioma: En Revista: Sci Rep Año: 2020 Tipo del documento: Article País de afiliación: España Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores de LDL / Mutación Missense / Hiperlipoproteinemia Tipo II Límite: Animals / Humans Idioma: En Revista: Sci Rep Año: 2020 Tipo del documento: Article País de afiliación: España Pais de publicación: Reino Unido