Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation. [PDF]
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
Galectin-3 secretion and tyrosine phosphorylation is dependent on the calpain small subunit, Calpain 4 [PDF]
Cell adhesion and migration are important events that occur during embryonic development, immune surveillance, wound healing and in tumor metastasis. It is a multi-step process that involves both mechanical and biochemical signaling that results in cell protrusion, adhesion, contraction and retraction.
Shalini, Menon +2 more
openaire +2 more sources
A single c.1715G>C calpain 3 gene variant causes dominant calpainopathy with loss of calpain 3 expression and activity [PDF]
AbstractRecessively inherited limb girdle muscular dystrophy (LGMD) type 2A is the most common LGMD worldwide. Here, we report the first single missense variant in CAPN3 causing dominantly inherited calpainopathy. A 43‐year‐old proband, his father and two sons were heterozygous for a c.1715G>C p.(Arg572Pro) variant in CAPN3.
John Vissing +6 more
openaire +4 more sources
An eccentric calpain, CAPN3/p94/calpain-3
Calpains are Ca(2+)-regulated proteolytic enzymes that are involved in a variety of biological phenomena. Calpains process substrates by limited proteolysis to modulate various protein functions in the cell, and are thus called "modulator proteases." CAPN3, previously called p94 or calpain-3, has unique features that are not found in any of the other ...
Ono, Yasuko +4 more
openaire +2 more sources
Astragaloside IV Alleviates Brain Injury Induced by Hypoxia via the Calpain-1 Signaling Pathway
Long-term hypoxia can induce oxidative stress and apoptosis in hippocampal neurons that can lead to brain injury diseases. Astragaloside IV (AS-IV) is widely used in the antiapoptotic therapy of brain injury diseases.
Yan Meng +8 more
doaj +1 more source
Homodimerization of calpain 3 penta-EF-hand domain [PDF]
Calpains 1 and 2 are heterodimeric proteases in which large (relative molecular mass Mr 80000) and small (Mr 28000) subunits are linked through their respective PEF (penta-EF-hand) domains. The skeletal muscle-specific calpain 3 is believed not to form a heterodimer with the small subunit but might homodimerize through its PEF domain.
Ravikiran, Ravulapalli +3 more
openaire +2 more sources
Renal ischemia/reperfusion injury is a major contributor of acute kidney injury (AKI), leading to renal cell necrosis, apoptosis, and inflammation. Calpains, a family of Ca2+-dependent cysteine proteases, play a pivotal role in the pathogenesis of renal ...
Yong Wu +6 more
doaj +1 more source
Cystatins as calpain inhibitors: Engineered chicken cystatin- and stefin B-kininogen domain 2 hybrids support a cystatin-like mode of interaction with the catalytic subunit of μ-calpain [PDF]
Within the cystatin superfamily, only kininogen domain 2 (KD2) is able to inhibit μ- and m-calpain. In an attempt to elucidate the structural requirements of cystatins for calpain inhibition, we constructed recombinant hybrids of human stefin B (an ...
Gross, Stefan +9 more
core +1 more source
Inhibition of human mu-calpain by conformationally constrained calpastatin peptides [PDF]
Pfizer J, Assfalg-Machleidt I, Machleidt W, Schaschke N. Inhibition of human mu-calpain by conformationally constrained calpastatin peptides. BIOLOGICAL CHEMISTRY.
Machleidt, Werner +3 more
core +1 more source
Identification of calpain cleavage sites in the G1 cyclin-dependent kinase inhibitor p19(INK4d) [PDF]
Calpains are a large family of Ca2+-dependent cysteine proteases that are ubiquitously distributed across most cell types and vertebrate species. Calpains play a role in cell differentiation, apoptosis, cytoskeletal remodeling, signal transduction and ...
Popp, Oliver +15 more
core +1 more source

