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
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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
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Is the expression of [-G93A(+)] human SOD1 a model to study neurodegenerations?
Journal of Biological Research, 2011 To relate the alterations occurring in neurodegenerations with Ca2+ homeostasis dysregulation, we analyzed the functional properties of the Ca2+-dependent calpain/calpastatin system in neuronal cells of transgenic mice overexpressing human mutated -G93A(+
R. Stifanese +6 more
doaj +1 more source
Calpastatin Subdomains A and C Are Activators of Calpain [PDF]
Journal of Biological Chemistry, 2002 The inhibitory domains of calpastatin contain three highly conserved regions, A, B, and C, of which A and C bind calpain in a strictly Ca(2+)-dependent manner but have no inhibitory activity whereas region B inhibits calpain on its own. We synthesized the 19-mer oligopeptides corresponding to regions A and C of human calpastatin domain I and tested ...
Tompa, P +3 more
openaire +3 more sources
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
Meat quality, post-mortem proteolytic enzymes, and myosin heavy chain isoforms of different Thai native cattle muscles [PDF]
Animal Bioscience, 2021 Objective This study investigated the meat quality characteristics, endogenous proteolytic enzymes, collagen content, and myosin heavy chain (MyHC) isoforms of different muscles of Thai native cattle (TNC).
Chanporn Chaosap +7 more
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Media Peternakan, 2013 Thin tail sheep has good adaptation in tropics condition, but they have low meat quality. Quality of thin tail hogget can be improved by selection. Calpastatin (CAST) gene is an indigenous inhibitor of calpain that involved in regulation of protein turn ...
B. W. Putra, C. Sumantri, Nurhidayat
doaj +1 more source
Frontiers in Genetics, 2018 Autogenous proteolytic enzymes of the calpain family are implicated in myofibrillar protein degradation. As a result, the μ-calpain gene and its specific inhibitor, calpastatin, have been repeatedly investigated for their association with meat quality ...
Joel D. Leal-Gutiérrez +5 more
doaj +1 more source
Journal of Experimental Neuroscience, 2017 Excessive intracellular calcium levels induce calpain activation, thereby triggering the cell death cascade. Several lines of evidence have demonstrated the neuroprotective role of the overexpression of calpain inhibitor, calpastatin.
Jirapa Chetsawang +4 more
doaj +1 more source
The role of proteinase enzymes in the process of conversion of muscle to meat [PDF]
Veterinarski Glasnik, 2006 Post mortem meat tenderization is a complex mechanism and unfortunately it has not been fully identified scientifically. It is known that endogenous proteinases have an important role in this mechanism.
Dümen Emek
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