Results 1 to 10 of about 26,568 (204)

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

Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide. [PDF]

J Biol Chem, 2018
Calpains are intracellular, calcium-activated cysteine proteases. Calpain-3 is abundant in skeletal muscle, where its mutation-induced loss of function causes limb-girdle muscular dystrophy type 2A. Unlike the small subunit-containing calpain-1 and -2, the calpain-3 isoform homodimerizes through pairing of its C-terminal penta-EF-hand domain.
McCartney CE, Ye Q, Campbell RL, Davies PL.   +3 more
europepmc   +4 more sources

Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation. [PDF]

J Biol Chem, 2018
Limb-girdle muscular dystrophy type 2a arises from mutations in the Ca2+-activated intracellular cysteine protease calpain-3. This calpain isoform is abundant in skeletal muscle and differs from the main isoforms, calpain-1 and -2, in being a homodimer and having two short insertion sequences.
Ye Q, Campbell RL, Davies PL.
europepmc   +4 more sources

Calpain-3-mediated regulation of the Na⁺-Ca²⁺ exchanger isoform 3. [PDF]

Pflugers Arch, 2016
Ca(2+) disturbances are observed when Ca(2+)-dependent cysteine proteases malfunction, causing muscle weakness and wasting. For example, loss of calpain-3 (CAPN3) activity leads to limb-girdle muscular dystrophy 2A (LGMD2A). In neuronal excitotoxicity, the cleavage of the Na(+)-Ca(2+) exchanger isoform 3 (NCX3) has been associated with an increase in ...
Michel LY, Hoenderop JG, Bindels RJ.
europepmc   +5 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

Autolytic activation of calpain 3 proteinase is facilitated by calmodulin protein. [PDF]

J Biol Chem, 2015
Calpains are broadly distributed, calcium-dependent enzymes that induce limited proteolysis in a wide range of substrates. Mutations in the gene encoding the muscle-specific family member calpain 3 (CAPN3) underlie limb-girdle muscular dystrophy 2A.
Ermolova N, Kramerova I, Spencer MJ.
europepmc   +6 more sources

Calpain-3 not only proteolyzes calpain-1 and -2 but also is a substrate for calpain-1 and -2

The Journal of Biochemistry, 2023
Abstract Calpain is an intracellular cysteine protease that cleaves its specific substrates in a limited region to modulate cellular function. Calpain-1 (C1) and calpain-2 (C2) are ubiquitously expressed in mammalian cells, but calpain-3 (C3) is a skeletal muscle-specific type.
Koichi Ojima, Shoji Hata, Fumiko Shinkai-Ouchi, Yasuko Ono, Susumu Muroya   +4 more
openaire   +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

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   +1 more source