Mice carrying the homologous human shelterin POT1-L259S mutation linked to pulmonary fibrosis show a telomerase deficiency-like phenotype with telomere shortening with increasing mouse generations

Pulmonary fibrosis is a lethal disease associated with damaging insults to the lung and with organismal aging. The presence of short and dysfunctional telomeres has been placed at the origin of this disease in a percentage of both familial and sporadic cases. Recently, a mutation in the telomere-bin...

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Detalles Bibliográficos
Autores: Sánchez-Vázquez, Raúl, Burgaz García-Oteyza, Sonia, Serrano, Rosa, Flores Landeira, Juana María, Martínez, Paula, Blasco, Maria A.
Tipo de recurso: artículo
Fecha de publicación:2025
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/129353
Acceso en línea:https://hdl.handle.net/20.500.14352/129353
Access Level:acceso abierto
Palabra clave:636.09
Aging
Pulmonary fibrosis
Shelterin
Telomeres
Veterinaria
3109 Ciencias Veterinarias
Descripción
Sumario:Pulmonary fibrosis is a lethal disease associated with damaging insults to the lung and with organismal aging. The presence of short and dysfunctional telomeres has been placed at the origin of this disease in a percentage of both familial and sporadic cases. Recently, a mutation in the telomere-binding protein protection of telomeres 1 in humans (hPOT1), the hPOT1-L259S mutation, was found in families with idiopathic pulmonary fibrosis. Here, we generated a Pot1a L261S knock-in mouse harboring the murine homologous hPOT1-L259S mutation. We found that the homozygous Pot1a L261S mice show shorter telomeres and degenerative pathologies in the intestine, testes, and lungs at old ages, a phenotype that is aggravated with increasing mouse generations, in striking analogy to the telomerase-deficient mouse models. Furthermore, we found that the POT1a-L261S mutant protein binds more strongly to TPP1 and to telomerase and impedes telomerase-dependent telomere lengthening in vivo. We show that telomerase activity at telomeres is reduced in the presence of POT1a-L261S, which behaves as a dominant negative mutant, thus providing a potential mechanism by which Pot1a L261S knock-in mice phenocopy the short telomere phenotype of the telomerase knockout model