Interaction between calpain-1 and HSP90: new insights into the regulation of localization and activity of the protease. [PDF]
PLoS ONE, 2015 Here we demonstrate that heat shock protein 90 (HSP90) interacts with calpain-1, but not with calpain-2, and forms a discrete complex in which the protease maintains its catalytic activity, although with a lower affinity for Ca2+.
Monica Averna +7 more
doaj +1 more source
Calpain-1 and Calpain-2 in the Brain: Dr. Jekill and Mr Hyde? [PDF]
Current Neuropharmacology, 2019 Michel Baudry
exaly +2 more sources
N Terminus of Calpain 1 Is a Mitochondrial Targeting Sequence [PDF]
Journal of Biological Chemistry, 2008 The ubiquitous m- and mu-calpains are thought to be localized in the cytosolic compartment, as is their endogenous inhibitor calpastatin. Previously, mu-calpain was found to be enriched in mitochondrial fractions isolated from rat cerebral cortex and SH-SY5Y neuroblastoma cells, but the submitochondrial localization of mu-calpain was not determined. In
RamaKrishna, Badugu +4 more
openaire +2 more sources
Spatio-temporal regulation of calpain activity after experimental myocardial infarction in vivo
Biochemistry and Biophysics Reports, 2021 Background: Calpains are calcium activated cysteine proteases that play a pivotal role in the pathophysiology of cardiac remodeling. Methods: Here, we performed left anterior descending coronary artery ligation in rats as a model for ischemic systolic ...
Kun Zhang +13 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]
, 2001 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
The calpastatin-derived calpain inhibitor CP1B reduces mRNA expression of matrix metalloproteinase-2 and-9 and invasion by leukemic THP-1 cells [PDF]
, 2003 The ubiquitous proteases μ- and m-calpain are Ca2+-dependent cysteine endopeptidases. Besides involvement in a variety of physio(patho)logical processes, recent studies suggest a pivotal role of calpains in differentiation of hematopoietic cells and ...
Ries, C. +5 more
core +1 more source
Frontiers in Oncology, 2022 The low-density lipoprotein receptor-related protein 1 (LRP1) is a multifunctional endocytic receptor mediating the clearance of various molecules from the extracellular matrix.
Benoit Langlois +17 more
doaj +1 more source
Identification of calpain cleavage sites in the G1 cyclin-dependent kinase inhibitor p19(INK4d) [PDF]
, 2006 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
Inhibition of human mu-calpain by conformationally constrained calpastatin peptides [PDF]
, 2008 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
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 +12 more
core +1 more source