The Role of Integrin β1D Mislocalization in the Pathophysiology of Calpain 3-Related Limb-Girdle Muscular Dystrophy

Limb-girdle muscular dystrophy R1 (LGMDR1) is characterized by progressive proximal muscle weakness due to mutations in the CAPN3 gene. Little is known about CAPN3's function in muscle, but its loss results in aberrant sarcomere formation. Human muscle structure was analyzed in this study, with...

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Detalhes bibliográficos
Autores: Valls-Mateu, Aida|||0000-0003-3616-7809, Ruiz-Roldán, C., Immanuel, J., Alonso-Martín, S., Gallardo, Eduard|||0000-0002-3942-3436, Fernandez-Torron, Roberto|||0000-0002-2202-8165, Bonilla, M., Lersundi, A., Hernández-Laín, A., Domínguez-González, Cristina|||0000-0001-5151-988X, Vílchez, J.J., Iruzubieta, P., López de Munain, A., Sáenz, A.
Formato: artículo
Fecha de publicación:2025
País:España
Recursos:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:321771
Acesso em linha:https://ddd.uab.cat/record/321771
https://dx.doi.org/urn:doi:10.3390/cells14060446
Access Level:acceso abierto
Palavra-chave:LGMDR1
Calpain 3
Costamere
Integrin β1
Limb-girdle muscular dystrophy
Descrição
Resumo:Limb-girdle muscular dystrophy R1 (LGMDR1) is characterized by progressive proximal muscle weakness due to mutations in the CAPN3 gene. Little is known about CAPN3's function in muscle, but its loss results in aberrant sarcomere formation. Human muscle structure was analyzed in this study, with observations including integrin β1D isoform (ITGβ1D) mislocalization, a lack of Talin-1 (TLN1) in the sarcolemma and the irregular expression of focal adhesion kinase (FAK) in LGMDR1 muscles, suggesting a lack of integrin activation with an altered sarcolemma, extracellular matrix (ECM) assembly and signaling pathway deregulation, which may cause frailty in LGMDR1 muscle fibers. Additionally, altered nuclear morphology, centrosome distribution and microtubule organization have been found in muscle cells derived from LGMDR1 patients.