Results 1 to 10 of about 28,592 (236)

Mitochondrial dysfunction and consequences in calpain-3-deficient muscle [PDF]

Skeletal Muscle, 2020
Background Nonsense or loss-of-function mutations in the non-lysosomal cysteine protease calpain-3 result in limb-girdle muscular dystrophy type 2A (LGMD2A).
Vanessa E. Jahnke, Jennifer M. Peterson, Jack H. Van Der Meulen, Jessica Boehler, Kitipong Uaesoontrachoon, Helen K. Johnston, Aurelia Defour, Aditi Phadke, Qing Yu, Jyoti K. Jaiswal, Kanneboyina Nagaraju   +10 more
doaj   +5 more sources

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

Cells
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.
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   +13 more
doaj   +2 more sources

Calpain 3 is important for muscle regeneration: Evidence from patients with limb girdle muscular dystrophies [PDF]

BMC Musculoskeletal Disorders, 2012
Background Limb girdle muscular dystrophy (LGMD) type 2A is caused by mutations in the CAPN3 gene and complete lack of functional calpain 3 leads to the most severe muscle wasting.
Hauerslev Simon, Sveen Marie-Louise, Duno Morten, Angelini Corrado, Vissing John, Krag Thomas O   +5 more
doaj   +2 more sources

Calpain activity is negatively regulated by a KCTD7–Cullin-3 complex via non-degradative ubiquitination

Cell Discovery, 2023
Calpains are a class of non-lysosomal cysteine proteases that exert their regulatory functions via limited proteolysis of their substrates. Similar to the lysosomal and proteasomal systems, calpain dysregulation is implicated in the pathogenesis of ...
Jaiprakash Sharma, Shalaka Mulherkar, Uan-I Chen, Yan Xiong, Lakshya Bajaj, Byoung-Kyu Cho, Young Ah Goo, Hon-Chiu Eastwood Leung, Kimberley F. Tolias, Marco Sardiello   +9 more
doaj   +2 more sources

Case report: A single novel calpain 3 gene variant associated with mild myopathy [PDF]

Frontiers in Genetics
Recessively inherited limb-girdle muscular dystrophy type 1, caused by mutations in the calpain 3 gene, is the most common limb-girdle muscular dystrophy worldwide. Recently, cases of autosomal dominant calpainopathy have been described.
Sara Massucco, Paola Fossa, Chiara Fiorillo, Elena Faedo, Chiara Gemelli, Rita Barresi, Michela Ripolone, Serena Patrone, Andrea Gaudio, Paola Mandich, Paola Mandich, Fabio Gotta, Serena Baratto, Monica Traverso, Livia Pisciotta, Livia Pisciotta, Federico Zaottini, Mattia Camera, Elena Scarsi, Marina Grandis, Marina Grandis   +20 more
doaj   +2 more sources

Human calpain-3 and its structural plasticity: Dissociation of a homohexamer into dimers on binding titin. [PDF]

J Biol Chem
Calpain-3 is an intracellular Ca2+-dependent cysteine protease abundant in skeletal muscle. Loss-of-function mutations in its single-copy gene cause a dystrophy of the limb-girdle muscles.
Ye Q, Henrickson A, Demeler B, Balasco Serrão VH, Davies PL.   +4 more
europepmc   +2 more sources

Titin splicing regulates cardiotoxicity associated with calpain 3 gene therapy for limb-girdle muscular dystrophy type 2A. [PDF]

Sci Transl Med, 2019
International audienceLimb-girdle muscular dystrophy type 2A (LGMD2A or LGMDR1) is a neuromuscular disorder caused by mutations in the calpain 3 gene (CAPN3). Previous experiments using adeno-associated viral (AAV) vector-mediated calpain 3 gene transfer
Lostal W, Roudaut C, Faivre M, Charton K, Suel L, Bourg N, Best H, Smith JE, Gohlke J, Corre G, Li X, Elbeck Z, Knöll R, Deschamps JY, Granzier H, Richard I.   +15 more
europepmc   +2 more sources

Modeling Patient-Specific Muscular Dystrophy Phenotypes and Therapeutic Responses in Reprogrammed Myotubes Engineered on Micromolded Gelatin Hydrogels

Frontiers in Cell and Developmental Biology, 2022
In vitro models of patient-derived muscle allow for more efficient development of genetic medicines for the muscular dystrophies, which often present mutation-specific pathologies.
Florian Barthélémy, Florian Barthélémy, Jeffrey W. Santoso, Laura Rabichow, Laura Rabichow, Rongcheng Jin, Isaiah Little, Isaiah Little, Stanley F. Nelson, Stanley F. Nelson, Stanley F. Nelson, Megan L. McCain, Megan L. McCain, M. Carrie Miceli, M. Carrie Miceli   +14 more
doaj   +1 more source

Calpastatin exon 1B-derived peptide, a selective inhibitor of calpain: Enhancing cell permeability by conjugation with penetratin [PDF]

, 2003
Gil-Parrado S, Assfalg-Machleidt I, Fiorino F, et al. Calpastatin exon 1B-derived peptide, a selective inhibitor of calpain: Enhancing cell permeability by conjugation with penetratin. BIOLOGICAL CHEMISTRY.
Dominga Deluca, Schaschke, N., Gil-Parrado, S, Werner M.a.c.h.l.e.i.d.t., Luis Moroder, Dietmar Pfeiler, Irmgard Assfalg Machleidt, Machleidt, Werner, Fiorino, F, Pfeiler, D., Pfeiler, D, Machleidt, W, Schaschke, Norbert, Assfalg-Machleidt, Irmgard, Moroder, L, Deluca, D, Gil-Parrado, S., Moroder, L., Machleidt, W., Fiorino, F., Assfalg-Machleidt, I, Norbert Schaschke, Deluca, D., Assfalg-Machleidt, I., FIORINO, FERDINANDO, Shirley Gil Parrado   +25 more
core   +1 more source

Proteolysis of insulin-like growth factor binding proteins (IGFBPs) by calpain [PDF]

, 2005
Calpains are non-lysosomal, Ca2+-dependent cysteine proteases, which are ubiquitously distributed across cell types and vertebrate species. The rules that govern calpain specificity have not yet been determined.
Mann, Karlheinz, Mann, K., Ghosh, M., Machleidt, W., Machleidt, Werner, Siwanowicz, I., Ghosh, Madhumita, Holak, Tad A., Holak, T. A., Holak, T., Siwanowicz, Igor, Shanker, Sreejesh, Shanker, S.   +12 more
core   +1 more source