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 <i>CAPN3</i> gene. Little is known about CAPN3’s function in muscle, but its loss results in aberrant sarcomere formation. Human muscle structure was analyzed in th...

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Main Authors: Andrea Valls, Cristina Ruiz-Roldán, Jenita Immanuel, Sonia Alonso-Martín, Eduard Gallardo, Roberto Fernández-Torrón, Mario Bonilla, Ana Lersundi, Aurelio Hernández-Laín, Cristina Domínguez-González, Juan Jesús Vílchez, Pablo Iruzubieta, Adolfo López de Munain, Amets Sáenz
Format: Article
Language:English
Published: MDPI AG 2025-03-01
Series:Cells
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Online Access:https://www.mdpi.com/2073-4409/14/6/446
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author Andrea Valls
Cristina Ruiz-Roldán
Jenita Immanuel
Sonia Alonso-Martín
Eduard Gallardo
Roberto Fernández-Torrón
Mario Bonilla
Ana Lersundi
Aurelio Hernández-Laín
Cristina Domínguez-González
Juan Jesús Vílchez
Pablo Iruzubieta
Adolfo López de Munain
Amets Sáenz
author_facet Andrea Valls
Cristina Ruiz-Roldán
Jenita Immanuel
Sonia Alonso-Martín
Eduard Gallardo
Roberto Fernández-Torrón
Mario Bonilla
Ana Lersundi
Aurelio Hernández-Laín
Cristina Domínguez-González
Juan Jesús Vílchez
Pablo Iruzubieta
Adolfo López de Munain
Amets Sáenz
author_sort Andrea Valls
collection DOAJ
description Limb–girdle muscular dystrophy R1 (LGMDR1) is characterized by progressive proximal muscle weakness due to mutations in the <i>CAPN3</i> 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.
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institution Kabale University
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publisher MDPI AG
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series Cells
spelling doaj-art-1f4625f897944989b6af4af368ca43cd2025-08-20T03:43:15ZengMDPI AGCells2073-44092025-03-0114644610.3390/cells14060446The Role of Integrin β1D Mislocalization in the Pathophysiology of Calpain 3-Related Limb–Girdle Muscular DystrophyAndrea Valls0Cristina Ruiz-Roldán1Jenita Immanuel2Sonia Alonso-Martín3Eduard Gallardo4Roberto Fernández-Torrón5Mario Bonilla6Ana Lersundi7Aurelio Hernández-Laín8Cristina Domínguez-González9Juan Jesús Vílchez10Pablo Iruzubieta11Adolfo López de Munain12Amets Sáenz13Neuromuscular Diseases Group, Neurosciences Area, Biogipuzkoa Health Research Institute, 20014 San Sebastian, SpainNeuromuscular Diseases Group, Neurosciences Area, Biogipuzkoa Health Research Institute, 20014 San Sebastian, SpainNeuromuscular Diseases Group, Neurosciences Area, Biogipuzkoa Health Research Institute, 20014 San Sebastian, SpainCenter for Biomedical Network Research on Neurodegenerative Diseases (CIBERNED), Spanish Ministry of Science & Innovation, Carlos III Health Institute, 28029 Madrid, SpainNeuromuscular Diseases Unit, Department of Neurology, Hospital de la Santa Creu i Sant Pau, 08041 Barcelona, SpainNeuromuscular Diseases Group, Neurosciences Area, Biogipuzkoa Health Research Institute, 20014 San Sebastian, SpainStem Cells and Aging Group, Bioengineering Area, Biogipuzkoa Health Research Institute, 20014 San Sebastian, SpainDepartment of Traumatology, Donostialdea Integrated Health Organisation, Osakidetza, 20014 San Sebastian, SpainDepartment of Neuropathology, Hospital Universitario 12 de Octubre, 28041 Madrid, SpainCenter for Biomedical Network Research on Rare Diseases (CIBERER), Spanish Ministry of Science & Innovation, Carlos III Health Institute, 28029 Madrid, SpainCenter for Biomedical Network Research on Rare Diseases (CIBERER), Spanish Ministry of Science & Innovation, Carlos III Health Institute, 28029 Madrid, SpainCenter for Biomedical Network Research on Neurodegenerative Diseases (CIBERNED), Spanish Ministry of Science & Innovation, Carlos III Health Institute, 28029 Madrid, SpainNeuromuscular Diseases Group, Neurosciences Area, Biogipuzkoa Health Research Institute, 20014 San Sebastian, SpainNeuromuscular Diseases Group, Neurosciences Area, Biogipuzkoa Health Research Institute, 20014 San Sebastian, SpainLimb–girdle muscular dystrophy R1 (LGMDR1) is characterized by progressive proximal muscle weakness due to mutations in the <i>CAPN3</i> 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.https://www.mdpi.com/2073-4409/14/6/446limb-girdle muscular dystrophyLGMDR1calpain 3integrin β1costamere
spellingShingle Andrea Valls
Cristina Ruiz-Roldán
Jenita Immanuel
Sonia Alonso-Martín
Eduard Gallardo
Roberto Fernández-Torrón
Mario Bonilla
Ana Lersundi
Aurelio Hernández-Laín
Cristina Domínguez-González
Juan Jesús Vílchez
Pablo Iruzubieta
Adolfo López de Munain
Amets Sáenz
The Role of Integrin β1D Mislocalization in the Pathophysiology of Calpain 3-Related Limb–Girdle Muscular Dystrophy
Cells
limb-girdle muscular dystrophy
LGMDR1
calpain 3
integrin β1
costamere
title The Role of Integrin β1D Mislocalization in the Pathophysiology of Calpain 3-Related Limb–Girdle Muscular Dystrophy
title_full The Role of Integrin β1D Mislocalization in the Pathophysiology of Calpain 3-Related Limb–Girdle Muscular Dystrophy
title_fullStr The Role of Integrin β1D Mislocalization in the Pathophysiology of Calpain 3-Related Limb–Girdle Muscular Dystrophy
title_full_unstemmed The Role of Integrin β1D Mislocalization in the Pathophysiology of Calpain 3-Related Limb–Girdle Muscular Dystrophy
title_short The Role of Integrin β1D Mislocalization in the Pathophysiology of Calpain 3-Related Limb–Girdle Muscular Dystrophy
title_sort role of integrin β1d mislocalization in the pathophysiology of calpain 3 related limb girdle muscular dystrophy
topic limb-girdle muscular dystrophy
LGMDR1
calpain 3
integrin β1
costamere
url https://www.mdpi.com/2073-4409/14/6/446
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