Results 11 to 20 of about 28,592 (236)

Calpain 3: a key regulator of the sarcomere? [PDF]

The FEBS Journal, 2006
International audienceCalpain 3 is a 94-kDa calcium-dependent cysteine protease mainly expressed in skeletal muscle. In this tissue, it localizes at several regions of the sarcomere through binding to the giant protein, titin.
Richard, Isabelle, Marc Bartoli, Bartoli, Marc, Stéphanie Duguez, Duguez, Stéphanie, Isabelle Richard   +5 more
core   +3 more sources

Calpain 3 is expressed in astrocytes of rat and Microcebus brain.

Journal of Chemical Neuroanatomy, 2003
International audienceThe calcium-dependent protease calpain is involved in numerous functions, including the control of cell survival, plasticity and motility.
Raynaud, Fabrice, Raynaud, F., Benyamin, Yves, Durand, Micheline, Feane, Helen, Rossel, Mireille, Mestre-Francés, Nadine, Ouali, Ahmed, König, Norbert   +8 more
core   +5 more sources

Mutations in Calpain 3 Associated with Limb Girdle Muscular Dystrophy: Analysis by Molecular Modeling and by Mutation in m-Calpain [PDF]

Biophysical Journal, 2001
Limb-girdle muscular dystrophy type 2A (LGMD2A) is an autosomal recessive disorder characterized by selective atrophy of the proximal limb muscles. Its occurrence is correlated, in a large number of patients, with defects in the human CAPN3 gene, a gene ...
Zongchao Jia, Jacques S. Beckmann, Wong, A., Jia, Zongchao, Elce, John S., Davies, Peter L., Beckmann, Jacques S., Tudor Moldoveanu, Vitali Petrounevitch, Wong, Andrew, Moldoveanu, Tudor, Elce, J. S., Andrew Wong, John S. Elce, Jia, Z., Peter L. Davies, Petrounevitch, V., Moldoveanu, T., Petrounevitch, Vitali, Beckmann, J. S., Davies, P. L.   +20 more
core   +3 more sources

Calpain 3/p94 is not involved in postmortem proteolysis

Journal of animal science, 2005
International audienceStudies on the correlation between expression and/or autolysis of calpain and postmortem proteolysis in muscle have provided conflicting evidence regarding the possible role of calpain 3 in postmortem tenderization of meat.
Geesink, M., Taylor, Richard, Koohmaraie, M.   +2 more
core   +4 more sources

N-terminal cleavage of GSK-3 by calpain: A new form of GSK-3 regulation [PDF]

Journal of Biological Chemistry, 2007
Although GSK-3 activity can be regulated by phosphorylation and through interaction with GSK-3-binding proteins, here we describe N-terminal proteolysis as a novel way to regulate GSK-3.
Lucas, José Javier, Hernández, Félix, Goñi-Oliver, Paloma, Ávila, Jesús   +3 more
core   +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

Regulation of GSK-3beta by calpain in the 3-nitropropionic acid model.

Hippocampus, 2010
Glycogen synthase kinase-3 beta (GSK-3 beta) is a crucial component in the cascade of events that culminate in a range of neuro-degenerative diseases. It is controlled by several pathways, including calpain-mediated cleavage.
M. Pallas, D. Melchiorri, F. Nicoletti, NICOLETTI, Ferdinando, A.M. Canudas, J. Gutiérrez‐Cuesta, J. Gutierrez Cuesta, MELCHIORRI, Daniela, N. Crespo‐Biel, N. Crespo Biel, A. Camins, A. M. Canudas   +11 more
core   +3 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

Possible Regulation of the Conventional Calpain System by Skeletal Muscle-specific Calpain, p94/Calpain 3 [PDF]

Journal of Biological Chemistry, 2004
p94 (also called calpain 3) is the skeletal muscle-specific calpain and is considered to be a "modulator protease" in various cellular processes. Analysis of p94 at the protein level is an urgent issue because the loss of p94 protease activity causes limb-girdle muscular dystrophy type 2A. In this study, we enzymatically characterized one alternatively
Yasuko, Ono, Kazumi, Kakinuma, Fukuyo, Torii, Akihiro, Irie, Kazuhiro, Nakagawa, Siegfried, Labeit, Keiko, Abe, Koichi, Suzuki, Hiroyuki, Sorimachi   +8 more
openaire   +2 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   +7 more sources