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CA2 — CAPN7

Text-mined interactions from Literome

Penna et al., J Immunol 1999 : Two lines of evidence indicate that the Ca2+ dependent cysteine protease calpain plays a major role in initiating ZAP-70 degradation : 1 ) treatment of T cells with cell permeating inhibitors of calpain markedly reduces ZAP-70 degradation ; 2 ) ZAP-70 is cleaved in vitro by calpain
Ishihara et al., Neurosci Lett 2000 (Carcinoma, Embryonal) : Taken together, these results suggest that oxidative stress induces degradation of cytoskeletal proteins presumably resulting from increased intracellular Ca2+ concentration and subsequent activation of calpain
Gadea et al., J Neurochem 2002 (Second Messenger Systems) : Our results further suggest that Gly transport is under cytoskeletal control, as activation of calpain by major increases in [ Ca2+ ] i induced by ionophores, as well as actin destabilization clearly inhibit uptake
Thompson et al., Life Sci 2002 : Placenta mu-calpain requires 50-70 microM Ca2+ and placenta m-calpain requires 450-460 microM Ca2+ for half-maximal proteolytic activity
Goll et al., Bioessays 1992 : It seems likely that calpain activity is regulated by binding of Ca2+ to specific sites on the calpain molecule, with binding to each site eliciting a response ( proteolytic activity, calpastatin binding, etc. ) specific for that site
Schölzke et al., Eur J Neurosci 2003 : However, inhibition of the glutamate activated Ca2+ dependent protease calpain by calpeptin completely blocked IkappaBalpha degradation and reduced the nuclear translocation of p65 ... Our data indicate that the Ca2+ dependent protease calpain is involved in the NF-kappaB activation in neurons in response to N-methyl-d-aspartate receptor occupancy by glutamate
Wada et al., Frontiers in bioscience : a journal and virtual library 2004 (Calcium Signaling) : Long lasting ( but not short-term ) increase of cytoplasmic Ca2+ down-regulated Na+ channels ; a slowly developing moderate increase of Ca2+ activated PKC-alpha and calpain , promoting internalization of Na+ channels, whereas an immediate monophasic and salient plateau increase of Ca2+ lowered alpha- and beta1-subunit mRNA levels
Ariyoshi et al., Biochem Int 1992 : In a cell re-constituted system, the membrane binding of calpain-I was also Ca2+ dependent and was significantly inhibited by a substrate of calpain
Hosfield et al., J Mol Biol 2004 : Activation of calpain by Ca2+ : roles of the large subunit N-terminal and domain III-IV linker peptides
Bozóky et al., Biochem J 2005 (Calcium Signaling) : Multiple interactions of the ` transducer ' govern its function in calpain activation by Ca2+
Guyton et al., J Neurosci Res 2005 (Acute Disease...) : From these findings, we conclude that increases in Ca2+ induced calpain activity may play a crucial role in neurodegeneration in acute EAE
Tanaka et al., J Biol Chem 2005 : These results suggest that Ca2+ stimulated calpain activity and CHOP expression play important roles in celecoxib induced apoptosis in gastric mucosal cells
Murphy et al., Am J Physiol Cell Physiol 2006 (Autolysis) : Biochemical assays suggest that mu-calpain becomes proteolytically active in the presence of 2-200 microM Ca2+
Ishii et al., Nihon rinsho. Japanese journal of clinical medicine 1992 : [ Intracellular Ca2+ behavior and activation of calpain-I in activated platelets ] ... It was demonstrated that the localization of calpain-I was changed from the cytosol to the membrane and calpain-I was activated on the membrane by Ca2+ , elevated through the initial elevation after activation of platelets
Tyagi et al., J Cell Biochem 2005 (Hyperhomocysteinemia...) : In this process, Ca2+ dependent mitochondrial nitric oxide synthase ( mtNOS ) and calpain are induced which lead to cytoskeletal de-arrangement and cellular remodeling
Murphy et al., J Physiol 2006 : Ca2+ activation of diffusible and bound pools of mu-calpain in rat skeletal muscle
Montero et al., Chem Biodivers 2004 : Since the peptide-biphenyl hybrids reported in the present paper do not possess a reactive electrophilic functionality, we hypothesize that they interfere with the activation of calpain by Ca2+ , and present experimental and computational results on the binding of peptide-biphenyl hybrids to Ca2+
Yang et al., Chem Res Toxicol 2007 (Necrosis) : The increased Ca2+ subsequently mediated calpain activation and intracellular ROS production
Hayashi et al., Biochem Biophys Res Commun 1992 : A leupeptin analogue, Cbz-Leu-Leu-Leu-aldehyde ( ZLLLal ), inhibits both the autolytic activation of mu-calpain and fusion induced by A2C and Ca2+
Dewitt et al., J Leukoc Biol 2007 : The molecular pathway for the unwrinkling of the leukocyte plasma membrane may involve Ca2+ activation of mu-calpain and cleavage of cytoskeletal linkage molecules such as talin and ezrin
Brown et al., Platelets 2007 : Regulation of plasma membrane Ca2+-ATPase in human platelets by calpain
Savart et al., Biochimie 1991 : Leupeptin, calpain inhibitor II, and the more selective calpain inhibitors calpeptin and MDL 28170 did not block the activation of the purified PKC by Ca2+ and phosphatidylserine
Bellinger et al., Proc Natl Acad Sci U S A 2008 : A small molecule ( S107 ) that prevents depletion of calstabin1 from the RyR1 complex improved force generation and exercise capacity, reduced Ca2+ dependent neutral protease calpain activity and plasma creatine kinase levels
Das et al., Brain Res 2008 (Brain Neoplasms...) : Besides, apoptosis was associated with alterations in expression of pro-apoptotic Bax and anti-apoptotic Bcl-2 proteins resulting in an increase in Bax : Bcl-2 ratio, mitochondrial release of cytochrome c and Smac, downregulation of selective baculoviral inhibitor-of-apoptosis repeat containing ( BIRC ) molecules, an increase in intracellular free [Ca2+ ], and activation of calpain and caspase-3
Rasbach et al., Arch Biochem Biophys 2008 : Oxidants and Ca+2 induce PGC-1alpha degradation through calpain
Norberg et al., Cell Death Differ 2008 : An increase in intracellular Ca2+ is required for the activation of mitochondrial calpain to release AIF during cell death
Olorunsogo et al., Biosci Rep 1990 (Anemia, Sickle Cell...) : Identical electrophoretic mobility on SDS-polyacrylamide gradient gel, sensitivity to micromolar amounts of Ca2+, absolute requirement for a reducing environment and a high susceptibility to inhibition by leupeptin and thiol-group modifying reagents confirm that calpain preparations from these erythrocytes are equivalent to calpain I. Whereas the extent of calpain activation of erythrocyte membrane Ca2 ( + ) -pumping ATPase of normal subjects was almost equal to that due to calmodulin, calpain activation of the HTN and SCA pump was greater than activation by calmodulin
Murachi et al., Prog Clin Biol Res 1990 : Calpain I requires low ( or microM ) -Ca2+ for activation and calpain II requires high ( or mM ) -Ca2+
Jang et al., Biochem J 2012 (Alzheimer Disease...) : Interestingly, the citrullination of enolase effectively promoted its proteolytic degradation by Ca2+ dependent calpain-1 , and leupeptin ( calpain inhibitor I ) abrogated this degradation
Wang et al., Particle and fibre toxicology 2012 : PM also mediated intracellular calcium mobilization via the transient receptor potential cation channel M2 ( TRPM2 ), in a ROS dependent manner with subsequent activation of the Ca2+ dependent protease calpain
Francis et al., J Leukoc Biol 2013 (Necrosis) : Ca2+ activation of cytosolic calpain induces the transition from apoptosis to necrosis in neutrophils with externalized phosphatidylserine
Mellgren et al., Biochem Biophys Res Commun 1990 : In contrast, calpain II required at least 50 microM Ca2+ to produce detectable proteolysis of soluble or membrane associated substrates
Murachi et al., Biochem Int 1989 : Evidence for Ca2+ induced translocation of calpain to the cell membrane, followed by its autolytic activation, has been discussed
Kapprell et al., J Biol Chem 1989 : Unautolyzed mu-calpain , however, required slightly more Ca2+ for half-maximal binding to calpastatin than for half-maximal activity
Murachi et al., Adv Exp Med Biol 1989 : Calpain I requires low Ca2+ for activation and calpain II requires high Ca2+
Au et al., Biochim Biophys Acta 1987 : Activation of erythrocyte membrane Ca2+-ATPase by calpain
Wang et al., Arch Biochem Biophys 1988 : We now demonstrate a similar kind of activation of the human erythrocyte membrane Ca2+-ATPase by calpain ( calcium dependent neutral protease ) isolated from the human red cell cytosol
Poland et al., Arch Biochem Biophys 1988 : The Ca2+ dependent proteinase which hydrolyzes the 95-kDa peptide has the properties of calpain II : ( i ) an absolute requirement for Ca2+ , with maximal activity at 0.5 to 1.0 mM Ca2+ ; ( ii ) a pH optimum of 7.5 to 8.0 ; ( iii ) inhibition by EDTA, iodoacetamide, leupeptin and L-trans-epoxysuccinylleucylamido ( 4-guanidino ) butane, but not by soybean trypsin inhibitor, aprotinin, or phenylmethanesufonyl fluoride
Fukui et al., Biochemistry 1988 : The isolated 70-kDa calpain I, or monomeric artifact, requires only 1 microM Ca2+ for half-maximal activation, and it is less pH stable and much less heat stable than the parent heterodimeric calpain I
Pintér et al., Biochem J 1988 : These properties resemble those of the Ca2+ dependent thiol-proteinase calpain
Pant et al., Biochem J 1988 : The degradation of phosphorylated and dephosphorylated neurofilament proteins by the Ca2+ activated neutral proteinase calpain was studied
Sakihama et al., Proc Natl Acad Sci U S A 1985 : Our results suggest that the Ca2+ mediated proteolytic activity of calpain is controlled through the cooperative and/or sequential actions of multiple Ca2+ binding sites present in both two-subunit molecules, heavy and light subunits of calpain
De Flora et al., Biomed Biochim Acta 1987 (Favism...) : Cytosolic procalpain ( i.e., the proenzyme species of Ca2+ activated neutral proteinase, or calpain ) had considerably lower activity than in matched RBC from asymptomatic G6PD-deficient subjects
Glaser et al., Proc Natl Acad Sci U S A 1994 : Alkylation of erythrocyte thiols also promoted translocation of calpain to the membrane, especially in the presence of Ca2+
Kawabe et al., Biochem Genet 1993 (Body Weight) : Calpain activity was determined by western blot analysis of steady-state concentrations of m-calpain ( calpain requiring millimolar Ca2+ for activation ) and also by northern blot analysis of steady-state concentrations of mRNA encoding m-calpain in three lines of quail : a random bred control line ( RR ) and two lines selected for body weight, one for increased body weight ( LL ) and another for decreased body weight ( SS )
Edelstein et al., Ren Fail 1996 (Acute Kidney Injury) : This rise in [Ca2+ ] i activates calpain , a Ca2+ dependent cysteine protease, and constitutive nitric oxide synthase (NOS), the Ca2+ dependent form of NOS
Zhang et al., Oncogene 1997 : Purified mu-calpain required only 1 to 3 microM Ca2+ to proteolyze p53 in WI-38 cell lysates
Baouz et al., J Biol Chem 1997 : Accordingly, the GEF activity of CDC25 ( Mm ) was increased severalfold by the Ca2+ dependent protease calpain that cleaves around a PEST-like region ( residues 798-853 ), producing C-terminal fragments of 43-56 kDa
Takagaki et al., J Neurochem 1997 (Anoxia...) : The enhancement of fodrin breakdown was completely blocked by omission of extracellular Ca2+ and significantly inhibited by calpain inhibitors such as E-64 and calpain inhibitor-I, thereby suggesting that the fodrin breakdown induced by hypoxia/hypoglycemia is due to the activation of Ca2+ stimulated neutral protease calpain
Yamazaki et al., Biochem Biophys Res Commun 1997 : Furthermore, the Ca2+ induced activation of mu-calpain and the processing of profilaggrin were affected by the addition of the synthetic calpastatin inhibitor
Michetti et al., Biochem J 1997 : The results presented provide more information on the sequential mechanism that promotes the Ca2+ induced activation of human erythrocyte mu-calpain under physiological conditions
Audesirk et al., Toxicology 1998 : In the presence of 1 microM free Ca2+ , 10 pM free Pb2+ reduced calpain activity, but in the presence of 100 microM free Ca2+, 1 nM free Pb2+ failed to inhibit calpain