Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.
Peptides composed of two amino acid units.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
A group of acylated oligopeptides produced by Actinomycetes that function as protease inhibitors. They have been known to inhibit to varying degrees trypsin, plasmin, KALLIKREINS, papain and the cathepsins.
A heterogenous group of inherited muscular dystrophy that can be autosomal dominant or autosomal recessive. There are many forms (called LGMDs) involving genes encoding muscle membrane proteins such as the sarcoglycan (SARCOGLYCANS) complex that interacts with DYSTROPHIN. The disease is characterized by progressing wasting and weakness of the proximal muscles of arms and legs around the HIPS and SHOULDERS (the pelvic and shoulder girdles).
A 235-kDa cytoplasmic protein that is also found in platelets. It has been localized to regions of cell-substrate adhesion. It binds to INTEGRINS; VINCULIN; and ACTINS and appears to participate in generating a transmembrane connection between the extracellular matrix and the cytoskeleton.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.

Cyclin D1 proteolysis: a retinoid chemoprevention signal in normal, immortalized, and transformed human bronchial epithelial cells. (1/2088)

BACKGROUND: Retinoids (derivatives of vitamin A) are reported to reduce the occurrence of some second primary cancers, including aerodigestive tract tumors. In contrast, beta-carotene does not reduce the occurrence of primary aerodigestive tract cancers. Mechanisms explaining these effective retinoid and ineffective carotenoid chemoprevention results are poorly defined. Recently, the all-trans-retinoic acid (RA)-induced proteolysis of cyclin D1 that leads to the arrest of cells in G1 phase of the cell cycle was described in human bronchial epithelial cells and is a promising candidate for such a mechanism. In this study, we have investigated this proteolysis as a common signal used by carotenoids or receptor-selective and receptor-nonselective retinoids. METHODS: We treated cultured normal human bronchial epithelial cells, immortalized human bronchial epithelial cells (BEAS-2B), and transformed human bronchial epithelial cells (BEAS-2BNNK) with receptor-selective or receptor-nonselective retinoids or with carotenoids and studied the effects on cell proliferation by means of tritiated thymidine incorporation and on cyclin D1 expression by means of immunoblot analysis. We also examined whether calpain inhibitor I, an inhibitor of the 26S proteasome degradation pathway, affected the decline (i.e., proteolysis) of cyclin D1. RESULTS: Receptor-nonselective retinoids were superior to the carotenoids studied in mediating the decline in cyclin D1 expression and in suppressing the growth of bronchial epithelial cells. Retinoids that activated retinoic acid receptor beta or retinoid X receptor pathways preferentially led to a decrease in the amount of cyclin D1 protein and a corresponding decline in growth. The retinoid-mediated degradation of cyclin D1 was blocked by cotreatment with calpain inhibitor I. CONCLUSIONS: Retinoid-dependent cyclin D1 proteolysis is a common chemoprevention signal in normal and neoplastic human bronchial epithelial cells. In contrast, carotenoids did not affect cyclin D1 expression. Thus, the degradation of cyclin D1 is a candidate intermediate marker for effective retinoid-mediated cancer chemoprevention in the aerodigestive tract.  (+info)

Modifications to rat lens major intrinsic protein in selenite-induced cataract. (2/2088)

PURPOSE: To identify modifications to rat lens major intrinsic protein (MIP) isolated from selenite-induced cataract and to determine whether m-calpain (EC 3.4.22.17) is responsible for cleavage of MIP during cataractogenesis. METHODS: Cataracts were induced in rats by a single injection of sodium selenite. Control and cataract lenses were harvested on day 16 and dissected into cortical and nuclear regions. Membranes were washed with urea buffer followed by NaOH. The protein was reduced/alkylated, delipidated, and cleaved with cyanogen bromide (CNBr). Cleavage products were fractionated by high-performance liquid chromatography (HPLC), and peptides were characterized by mass spectrometry and tandem mass spectrometry. MIP cleavage by m-calpain was carried out by incubation with purified enzyme, and peptides released from the membrane were analyzed by Edman sequencing. RESULTS: The intact C terminus, observed in the control nuclear and cataractous cortical membranes, was not observed in the cataractous nuclear membranes. Mass spectrometric analysis revealed heterogeneous cleavage of the C terminus of MIP in control and cataract nuclear regions. The major site of cleavage was between residues 238 and 239, corresponding to the major site of in vitro cleavage by m-calpain. However, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometric analysis indicated that in vivo proteolysis during cataract formation also included sites closer to the C terminus not produced by m-calpain in vitro. Evidence for heterogeneous N-terminal cleavage was also observed at low levels with no differences between control and cataractous lenses. The major site of phosphorylation was determined to be at serine 235. CONCLUSIONS: Specific sites of MIP N- and C-terminal cleavage in selenite-induced cataractous lenses were identified. The heterogeneous cleavage pattern observed suggests that m-calpain is not the sole enzyme involved in MIP C-terminal processing in rat lens nuclei.  (+info)

Caspase-dependent activation of calpain during drug-induced apoptosis. (3/2088)

We have previously demonstrated that calpain is responsible for the cleavage of Bax, a proapoptotic protein, during drug-induced apoptosis of HL-60 cells (Wood, D. E., Thomas, A., Devi, L. A., Berman, Y., Beavis, R. C., Reed, J. C., and Newcomb, E. W. (1998) Oncogene 17, 1069-1078). Here we show the sequential activation of caspases and calpain during drug-induced apoptosis of HL-60 cells. Time course experiments using the topoisomerase I inhibitor 9-amino-20(S)-camptothecin revealed that cleavage of caspase-3 substrates poly(ADP-ribose) polymerase (PARP) and the retinoblastoma protein as well as DNA fragmentation occurred several hours before calpain activation and Bax cleavage. Pretreatment with the calpain inhibitor calpeptin blocked calpain activation and Bax cleavage but did not inhibit PARP cleavage, DNA fragmentation, or 9-amino-20(S)-camptothecin-induced morphological changes and cell death. Pretreatment with the pan-caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD-fmk) inhibited PARP cleavage, DNA fragmentation, calpain activation, and Bax cleavage and increased cell survival by 40%. Interestingly, Z-VAD-fmk-treated cells died in a caspase- and calpain-independent manner that appeared morphologically distinct from apoptosis. Our results suggest that excessive or uncontrolled calpain activity may play a role downstream of and distinct from caspases in the degradation phase of apoptosis.  (+info)

Degradation of protein kinase Malpha by mu-calpain in a mu-calpain-protein kinase Calpha complex. (4/2088)

In previous studies, we isolated and identified a mu-calpain-PKCalpha complex from rabbit skeletal muscle. At the same time we pointed out that an association between mu-calpain and PKCalpha could occur at the level of the plasma membrane of muscle cells, and that PKCalpha could thus be considered as a potential mu-calpain substrate. In the present study, using the mu-calpain-PKCalpha complex as a model, we report that mu-calpain is activated in the combined presence of physiological calcium concentrations (less than 1 microM) and phosphatidylserine. Furthermore our data also show that: (1) there exists a correlation between the appearance of autolyzed mu-calpain forms and PKCalpha hydrolysis which leads to the formation of PKMalpha; (2) in certain experimental conditions, autolyzed mu-calpain forms are able to hydrolyze PKMalpha independently of the presence of diacylglycerol.  (+info)

Hydrostatic pressure and calcium-induced dissociation of calpains. (5/2088)

The dissociation of mu- and m-calpains was studied by fluorescence spectroscopy under high hydrostatic pressure (up to 650 MPa). Increasing pressure induced a red shift of the tryptophan fluorescence of the calcium-free enzyme. The concentration dependence of the spectral transition was consistent with a pressure-induced dissociation of the subunits. Rising temperature increased the stability of calpain heterodimers and confirmed the predominance of hydrophobic interactions between monomers. At saturating calcium, the spectral transition was not observed for native or iodoacetamide-inactivated calpains, indicating that they were already dissociated by calcium. The reaction volume was about -150 ml mol-1 for both isoforms, and the dissociation constants at atmospheric pressure are approximately 10-12 M and 10-15 M for mu- and m-calpains, respectively. This result indicates a tighter interaction in the isoform that requires higher calcium concentration for activity.  (+info)

Calpain inhibitor I increases beta-amyloid peptide production by inhibiting the degradation of the substrate of gamma-secretase. Evidence that substrate availability limits beta-amyloid peptide production. (6/2088)

The calpain inhibitor N-acetyl-leucyl-leucyl-norleucinal (ALLN) has been reported to have complex effects on the production of the beta-amyloid peptide (Abeta). In this study, the effects of ALLN on the processing of the amyloid precursor protein (APP) to Abeta were examined in 293 cells expressing APP or the C-terminal 100 amino acids of APP (C100). In cells expressing APP or low levels of C100, ALLN increased Abeta40 and Abeta42 secretion at low concentrations, decreased Abeta40 and Abeta42 secretion at high concentrations, and increased cellular levels of C100 in a concentration-dependent manner by inhibiting C100 degradation. Low concentrations of ALLN increased Abeta42 secretion more dramatically than Abeta40 secretion. ALLN treatment of cells expressing high levels of C100 did not alter cellular C100 levels and inhibited Abeta40 and Abeta42 secretion with similar IC50 values. These results suggest that C100 can be processed both by gamma-secretase and by a degradation pathway that is inhibited by low concentrations of ALLN. The data are consistent with inhibition of gamma-secretase by high concentrations of ALLN but do not support previous assertions that ALLN is a selective inhibitor of the gamma-secretase producing Abeta40. Rather, Abeta42 secretion may be more dependent on C100 substrate concentration than Abeta40 secretion.  (+info)

Posttranslational regulation of the retinoblastoma gene family member p107 by calpain protease. (7/2088)

The retinoblastoma protein plays a critical role in regulating the G1/S transition. Less is known about the function and regulation of the homologous pocket protein p107. Here we present evidence for the posttranslational regulation of p107 by the Ca2+-activated protease calpain. Three negative growth regulators, the HMG-CoA reductase inhibitor lovastatin, the antimetabolite 5-fluorouracil, and the cyclic nucleotide dibutyryl cAMP were found to induce cell type-specific loss of p107 protein which was reversible by the calpain inhibitor leucyl-leucyl-norleucinal but not by the serine protease inhibitor phenylmethylsulfonylfluoride, caspase inhibitors, or lactacystin, a specific inhibitor of the 26S proteasome. Purified calpain induced Ca2+-dependent p107 degradation in cell lysates. Transient expression of the specific calpain inhibitor calpastatin blocked the loss of p107 protein in lovastatin-treated cells, and the half-life of p107 was markedly lengthened in lovastatian-treated cells stably transfected with a calpastatin expression vector versus cells transfected with vector alone. The data presented here demonstrate down-regulation of p107 protein in response to various antiproliferative signals, and implicate calpain in p107 posttranslational regulation.  (+info)

Ubiquitination and degradation of ATF2 are dimerization dependent. (8/2088)

Ubiquitination and proteasome-dependent degradation are key determinants of the half-lives of many transcription factors. Homo- or heterodimerization of basic region-leucine zipper (bZIP) transcription factors is required for their transcriptional activities. Here we show that activating transcription factor 2 (ATF2) heterodimerization with specific bZIP proteins is an important determinant of the ubiquitination and proteasome-dependent degradation of ATF2. Depletion of c-Jun as one of the ATF2 heterodimer partners from the targeting proteins decreased the efficiency of ATF2 ubiquitination in vitro, whereas the addition of exogenously purified c-Jun restored it. Similarly, overexpression of c-Jun in 293T human embryo kidney cells increased ATF2 ubiquitination in vivo and reduced its half-life in a dose-dependent manner. Mutations of ATF2 that disrupt its dimerization inhibited ATF2 ubiquitination in vitro and in vivo. Conversely, removal of residues 150 to 248, as in a constitutively active ATF2 spliced form, enhanced ATF2 dimerization and transactivation, which coincided with increased ubiquitination and decreased stability. Our findings indicate the increased sensitivity of transcriptionally active dimers of ATF2 to ubiquitination and proteasome-dependent degradation. Based on these observations, we conclude that increased targeting of a transcriptionally active ATF2 form indicates the mechanism by which the magnitude and the duration of the cellular stress response are regulated.  (+info)

Calpain Substrate IV, Cell-Permeable, Fluorogenic - Calbiochem The non-permeant fluorogenic Calpain Substrate III is made cell-permeable by a c-terminal heptaarginine extension via a Glu linkage. - Find MSDS or SDS, a COA, data sheets and more information.
The small subunit of calpain, a calcium-dependent cysteine protease, was found to interact with the cytoplasmic domain of the common cytokine receptor γ chain (γ c) in a yeast two-hybrid interaction trap assay. This interaction was functional as demonstrated by the ability of calpain to cleave in vitro-translated wild-type γc, but not γc containing a mutation in the PEST (proline, glutamate, serine, and threonine) sequence in its cytoplasmic domain, as well as by the ability of endogenous calpain to mediate cleavage of γc in a calcium-dependent fashion. In T cell receptor-stimulated murine thymocytes, calpain inhibitors decreased cleavage of γ c. Moreover, in single positive CD4+ thymocytes, not only did a calpain inhibitor augment CD3-induced proliferation, but antibodies to γ c blocked this effect. Finally, treatment of cells with ionomycin could inhibit interleukin 2-induced STAT protein activation, but this inhibition could be reversed by calpain inhibitors. Together, these data ...
A calpain (/ˈkælpeɪn/; EC 3.4.22.52, EC 3.4.22.53) is a protein belonging to the family of calcium-dependent, non-lysosomal cysteine proteases (proteolytic enzymes) expressed ubiquitously in mammals and many other organisms. Calpains constitute the C2 family of protease clan CA in the MEROPS database. The calpain proteolytic system includes the calpain proteases, the small regulatory subunit CAPNS1, also known as CAPN4, and the endogenous calpain-specific inhibitor, calpastatin. The history of calpain originates in 1964, when calcium-dependent proteolytic activities caused by a calcium-activated neutral protease (CANP) were detected in brain, lens of the eye and other tissues. In the late 1960s the enzymes were isolated and characterised independently in both rat brain and skeletal muscle. These activities were caused by an intracellular cysteine protease not associated with the lysosome and having an optimum activity at neutral pH, which clearly distinguished it from the cathepsin family ...
Calpastatin (CAST) is a calpain inhibitor, a calcium-dependent cysteine protease that is widely distributed in higher order animals. There are different types of calpastatins; examples include the 68 kDa erythrocyte-derived calpastatin and the 107 kDa myocyte-derived calpastatin (as evidenced by SDS-PAGE). Through its inhibition of calpain, calpastatin is believed to play important roles in the regulation of cell proliferation, differentiation and aging. CAST is also involved in the proteolysis of amyloid precursor protein (APP). ...
Calpastatin (CAST) is a calpain inhibitor, a calcium-dependent cysteine protease that is widely distributed in higher order animals. There are different types of calpastatins; examples include the 68 kDa erythrocyte-derived calpastatin and the 107 kDa myocyte-derived calpastatin (as evidenced by SDS-PAGE). Through its inhibition of calpain, calpastatin is believed to play important roles in the regulation of cell proliferation, differentiation and aging. CAST is also involved in the proteolysis of amyloid precursor protein (APP). ...
Calpains are calcium-dependent cysteine proteases involved in signal transduction in a variety of cellular processes. A functional calpain protein consists of an invariant small subunit and 1 of a family of large subunits. CAPN5 is one of the large subunits. Unlike some of the calpains, CAPN5 and CAPN6 lack a calmodulin-like domain IV. Because of the significant similarity to Caenorhabditis elegans sex determination gene tra-3, CAPN5 is also called as HTRA3. [provided by RefSeq, Jul 2008 ...
Limb-girdle muscular dystrophy type 2A (LGMD2A) is a genetic disease that is caused by mutations in the calpain 3 gene (CAPN3), which encodes the skeletal muscle-specific calpain, calpain 3 (also known as p94). However, the precise mechanism by which p94 functions in the pathogenesis of this disease …
Calpain II was purified to apparent homogeneity from bovine neural retinas. It was found to be biochemically similar to brain calpain II, purified by the same procedure, with respect to: subunit mobility in SDS-polyacrylamide gel electrophoresis; Ca2+ sensitivity; inhibition by calpeptin and other cysteine protease inhibitors; and optimal pH. Semithin cryosections were immuno-labeled with antibodies specific for the catalytic subunit of calpain II. Calpain II was detected in most layers of the retina, with the most pronounced label present in the plexiform layers (synaptic regions) and the photoreceptor outer segments. In dark-adapted retinas, the label was distributed throughout the outer segments. In light-adapted retinas, outer segment labeling was concentrated in the connecting cilium, and the inner segments were labeled. A partially pure preparation of calpain II from isolated rod outer segments was found to have the same biochemical characteristics as calpain II prepared in the same way ...
Cell-attached and whole-cell patch-clamp recordings were done at 32°C from visually identified CA1 pyramidal neurons using an EPC 10 amplifier and Pulse software (HEKA). Patch pipettes were fabricated from borosilicate glass (Harvard Apparatus), and their resistance ranged from 4.5 to 6.5 MΩ. The pipette solution consisted of (in mm): 30 N-methyl-d-glucamine-HCl, 95 K-gluconate, 1 EGTA, 5 HEPES, 10 d-glucose, 2 Mg-ATP, 20 sucrose, 0.1 Alexa Fluor 488, 2 NaOH, and 5.4 KOH, pH 7.3. For recordings, slices were positioned in a submerged-type recording chamber and continuously perfused at a rate of 3.5 ml/min with extracellular solution containing (in mm): 124 NaCl, 3.5 KCl, 2 CaCl2, 25 NaHCO3, 1.1 NaH2PO4, 2 MgSO4, and 10 d-glucose, equilibrated with 95% O2 and 5% CO2, pH 7.4. Membrane potential values were corrected for calculated liquid junction potentials (Barry, 1994). Interictal-like activity was induced by omitting Mg2+ from the extracellular solution after recovery and during the recordings ...
The c-Fos and c-Jun transcription factors are rapidly turned over in vivo. One of the multiple pathways responsible for their breakdown is probably initiated by calpains, which are cytoplasmic calcium-dependent cysteine proteases. The c-fos gene has been transduced by two murine oncogenic retroviruses called Finkel-Biskis-Jenkins murine sarcoma virus (FBJ-MSV) and Finkel-Biskis-Reilly murine sarcoma virus (FBR-MSV); c-jun has been transduced by the chicken avian sarcoma virus 17 (ASV17) retrovirus. Using an in vitro degradation assay, we show that the mutated v-FosFBR, but not v-FosFBJ or v-JunASV17, is resistant to calpains. This property raises the interesting possibility that decreased sensitivity to calpains might contribute to the tumorigenic potential of FBR-MSV by allowing greater accumulation of the protein that it encodes in infected cells. It has also been demonstrated that resistance to cleavage by calpains does not result from mutations that have accumulated in the Fos moiety of the ...
Calpains are calcium-dependent cysteine proteases involved in sigl transduction in a variety of cellular processes. A functiol calpain protein…
Calpains make up a ubiquitously expressed, well-conserved family of calcium-dependent cysteine proteases. The calpain proteins are heterodimers…
TY - JOUR. T1 - Inhibitors of calpain activation (PD150606 and E-64) and renal ischemia-reperfusion injury. AU - Chatterjee, P.K.. AU - Todorovic, Z.. AU - Sivarajah, A.. AU - Mota-Filipe, H.. AU - Brown, P.A.J.. AU - Stewart, K.N.. AU - Mazzon, E.. AU - Cuzzocrea, S.. AU - Thiemermann, C.. PY - 2005/4. Y1 - 2005/4. N2 - Calpain activation has been implicated in the development of ischemia-reperfusion (I-R) injury. Here we investigate the effects of two inhibitors of calpain activity, PD150606 and E-64, on the renal dysfunction and injury caused by I-R of rat kidneys in vivo. Male Wistar rats were administered PD150606 or E-64 (3 mg/kg i.p.) or vehicle (10%, v/v, DMSO) 30 min prior to I-R. Rats were subjected to bilateral renal ischemia (45 min) followed by reperfusion (6 h). Serum and urinary biochemical indicators of renal dysfunction and injury were measured; serum creatinine (for glomerular dysfunction), fractional excretion of Na+ (FENa, for tubular dysfunction) and urinary ...
The major finding of the present study is that type 2 diabetes mellitus is associated with the cleavage of platelet PECAM-1 through a mechanism involving the tyrosine nitration of SERCA-2, an increase in [Ca2+]i, and the activation of the Ca2+-dependent protease μ-calpain. Moreover, treating subjects with type 2 diabetes mellitus with the PPAR-γ agonist rosiglitazone successfully reversed many of these changes and restored platelet [Ca2+]i, calpain activity, and PECAM-1 to levels comparable to those detected in nondiabetic subjects. From these results, it is clear that megakaryocytes/platelets are an additional cellular target for PPAR-γ agonists.. Intracellular Ca2+ homeostasis in platelets from patients with type 2 diabetes mellitus is reported to be altered, leading to an increased adhesiveness and spontaneous aggregation. One factor that contributes to the disturbed platelet [Ca2+]i in diabetic subjects is a marked reduction in Ca2+-ATPase activity.3,4 Although human platelets coexpress ...
Group B coxsackieviruses (CVB) are associated with viral-induced heart disease and are among the leading causes of aseptic meningitis worldwide. Here we show that CVB entry into polarized brain microvasculature and aortic endothelial cells triggers a depletion of intracellular calcium stores initiated through viral attachment to the apical attachment factor decayaccelerating factor. Calcium release was dependent upon a signaling cascade that required the activity of the Src family of tyrosine kinases, phospholipase C, and the inositol 1,4,5-trisphosphate receptor isoform 3. CVB-mediated calcium release was required for the activation of calpain-2, a calcium-dependent cysteine protease, which controlled the vesicular trafficking of internalized CVB particles. These data point to a specific role for calcium signaling in CVB entry into polarized endothelial monolayers and highlight the unique signaling mechanisms used by these viruses to cross endothelial barriers. © 2010 Bozym et al.. ...
A reciprocal relationship exists between agrin and acetylcholine (ACh) in controlling acetylcholine receptor (AChR) clustering at the neuromuscular junction: Agrin promotes clustering, and ACh disperses clusters. Chen et al. provide insight into how these opposing signals may allow stabilization of AChR at the neuromuscular junction by differential activity of the calcium-activated proteases calpains. Exposure of C2C12 myotubes in culture to the cholinergic agonist carbachol triggered a calcium transient, activation of calpain, and stimulation of cyclin-dependent kinase 5 (CDK5) through production of the activator p25 by cleavage of the CDK5 regulatory partner p35. (CDK5 has been previously implicated in AChR dispersal, and p35 is a known substrate for calpain.) Activation of CDK5 by carbachol was blocked by pharmacological inhibition of calpain with calpeptin, and the dispersal of AChR clusters induced by agrin was also prevented if calpain activity was blocked (pharmacologically or by RNAi). ...
TY - JOUR. T1 - Activation of m-Calpain Is Required for Chromosome Alignment on the Metaphase Plate during Mitosis. AU - Honda, Shinobu. AU - Marumoto, Tomotoshi. AU - Hirota, Toru. AU - Nitta, Masayuki. AU - Arima, Yoshimi. AU - Ogawa, Michio. AU - Saya, Hideyuki. PY - 2004/3/12. Y1 - 2004/3/12. N2 - Calpains form a superfamily of Ca2+-dependent intracellular cysteine proteases with various isoforms. Two isoforms, μ- and m-calpains, are ubiquitously expressed and known as conventional calpains. It has been previously shown that the mammalian calpains are activated during mitosis by transient increases in cytosolic Ca2+ concentration. However, it is still unknown whether the activation of calpains contributes to particular events in mitosis. With the use of RNA interference (RNAi), we investigated the roles of calpains in mitosis. Cells reduced the levels of m-calpain, but not μ-calpain, arrested at prometaphase and failed to align their chromosomes at the spindle equator. Specific peptidyl ...
The report generally describes calpain inhibitor i, examines its uses, production methods, patterns. CALPAIN INHIBITOR I market situation is overviewed;
Oxidized low-density lipoprotein (oxLDL) is known to induce apoptosis in endothelial cells, and this is believed to contribute to the progression of atherosclerosis. In the present study we made the novel observation that oxLDL-induced death of HMEC-1 cells is accompanied by activation of calpain. The μ-calpain inhibitor PD 151746 decreased oxLDL-induced cytotoxicity, whereas the general caspase inhibitor BAF (t-butoxycarbonyl-Asp-methoxyfluoromethylketone) had no effect. Also, oxLDL provoked calpain-dependent proteolysis of cytoskeletal α-fodrin in the HMEC-1 cells. Our observation of an autoproteolytic cleavage of the 80 kDa subunit of μ-calpain provided further evidence for an oxLDL-induced stimulation of calpain activity. The Bcl-2 protein Bid was also cleaved during oxLDL-elicited cell death, and this was prevented by calpain inhibitors, but not by inhibitors of cathepsin B and caspases. Treating the HMEC-1 cells with oxLDL did not result in detectable activation of procaspase 3 or ...
Comparative Studies on Metabolic Rate and Calpain/Calpastatin Activity between Hanwoo and Holstein Beef - Hanwoo Beef;Holstein Beef;Temperature Conditioning;Metabolic Rate;Calpain;Calpastatin;
To The Editor:. In the March 28, 2008 issue of Circulation Research, Letavernier et al assessed the effects of calpain inhibition on angiotensin (Ang) II-induced cardiovascular remodeling.1 These authors used transgenic mice expressing high levels of calpastatin to inhibit Ang II-dependent calpain activation. They show that prevention of Ang II-induced calpain activation is associated with impaired nuclear factor (NF)-κB activation in heart tissue, which eventually leads to decreased Ang II-induced cardiac hypertrophy. This finding adds substantial novel information to our understanding of how calpains might be involved in the complex regulation of cardiac hypertrophy. However, compelling evidence as to how calpains are activated by Ang II in the myocardium and how the calpain/calpastatin system is linked to NF-κB activation is not provided. In the May 23, 2008 issue of Circulation Research, we show that Ang II induces calcium release via the inositol 1,4,5-trisphosphate receptor (InsP3R) ...
Ionotropic glutamate receptors mediate most excitatory synaptic transmission in mammalian brain, and play important roles in neuronal development and synaptic plasticity. In particular, long-term potentiation (LTP) and long-term depression (LTD) are generally considered to represent cellular mechanisms involved in certain forms of learning and memory. Calpain is a calcium-dependent neutral protease that plays significant roles in synaptic plasticity, cell motility, as well as in various forms of neurodegeneration. We compared the rates of calpain-mediated truncation of GluR1 and GluR2 subunits with those of GluR1 phosphorylated at serine 831 or serine 845, and GluR2 phosphorylated at serine 880. Rat brain membranes were treated with calpain and calcium and levels of total and phosphorylated GluR1 and GluR2 subunits were analyzed by western blots. Rates of calpain-mediated truncation of phosphorylated GluR1 (either at serine 831 or 845) were much slower than for total GluR1. On the other hand, ...
Results Doxorubicin decreased calpain activities in cultured neonatal mouse cardiomyocytes and in vivomouse hearts, which correlated with down-regulation of calpain-1 and calpain-2 proteins. Over-expression of calpastatin or treatment with pharmacological calpain inhibitors aggravated apoptosis in neonatal and adult cardiomyocytes caused by doxorubicin. On the while, over-expression of calpain-2 but not calpain-1 decreased doxorubicin-induced apoptosis in cardiomyocytes. The pro-apoptotic effects of calpain inhibition were concerned with down-regulation of AKT protein and mRNA expression, and a concomitant reduction in GSK-3 beta phosphorylation (Ser9) in doxorubicin-treated cardiomyocytes. Inhibiting AKT further increased doxorubicin-induced cardiac injuries, suggesting the effects of calpain inhibition may be mediated through inactivating the AKT signalling. In an in vivomodel of doxorubicin-induced cardiotoxicity, overexpression of calpastatin aggravated myocardial dysfunction in transgenic ...
Abstract: : Purpose: Our previous study suggested that calpains played an important role in retinal cell death induced by ischemia-reperfusion in rat. However, the relationship between changes in signaling pathways caused by activation of calpain and retinal cell death is not clear. Recently, calpain-induced proteolysis of p35, a regulator of cdk5, to p25 was reported in Alzheimers disease. Thus, the purpose of present study to determine if p35 was similarly proteolyzed by m-calpain to p25 during retinal cell damage occurring in vitro. Methods: Rat retinas were incubated in RPMI medium with glucose under conditions supplying oxygen sufficient for retinal cell survival. To induce a hypoxia, retinas were incubated in RPMI medium without glucose under 95 % N2/5 % CO2 instead of 95 % O2/5 % CO2. Leakage of LDH into the medium assessed membrane damage and cell death. Casein zymography and immunoblotting assessed activation of calpain and proteolysis of α-spectrin and p35. Results: Results Leakage ...
TY - JOUR. T1 - CAPN5 mutation in hereditary uveitis. T2 - The R243L mutation increases calpain catalytic activity and triggers intraocular inflammation in a mouse model. AU - Wert, Katherine J.. AU - Bassuk, Alexander G.. AU - Wu, Wen Hsuan. AU - Gakhar, Lokesh. AU - Coglan, Diana. AU - Mahajan, Mary Ann. AU - Wu, Shu. AU - Yang, Jing. AU - Lin, Chyuan Sheng. AU - Tsang, Stephen H.. AU - Mahajan, Vinit B.. PY - 2015/4/28. Y1 - 2015/4/28. N2 - A single amino acid mutation near the active site of the CAPN5 protease was linked to the inherited blinding disorder, autosomal dominant neovascular inflammatory vitreoretinopathy (ADNIV, OMIM #193235). In homology modeling with other calpains, this R243L CAPN5 mutation was situated in a mobile loop that gates substrate access to the calcium-regulated active site. In in vitro activity assays, the mutation increased calpain protease activity and made it far more active at low concentrations of calcium. To test whether the disease allele could yield an ...
Calpain Inhibitor Set - Calbiochem The Calpain Inhibitor Set controls the biological activity of Calpain. This small molecule/inhibitor is primarily used for Protease Inhibitors applications. - Find MSDS or SDS, a COA, data sheets and more information.
The peptidyl-proline isomerase, Protein Never in Mitosis Gene A Interacting-1 (PIN1), regulates turnover of inducible nitric oxide synthase (iNOS) in murine aortic endothelial cells (MAEC) stimulated with E. coli endotoxin (LPS) and interferon-γ (IFN). Degradation of iNOS was reduced by a calpain inhibitor, suggesting that PIN1 may affect induction of other calpain-sensitive inflammatory proteins, such as cyclooxygenase (COX)-2, in MAEC. MAEC, transduced with lentivirus encoding an inactive control short hairpin (sh) RNA or one targeting PIN1 that reduced PIN1 by 85%, were used. Cells were treated with LPS/IFN, calpain inhibitors (carbobenzoxy-valinyl-phenylalaninal (zVF), PD150606), cycloheximide and COX inhibitors to determine the effect of PIN1 depletion on COX-2 and calpain. LPS or IFN alone did not induce COX-2. However, treatment with 10 μg LPS plus 20 ng IFN per ml induced COX-2 protein 10-fold in Control shRNA MAEC. Induction was significantly greater (47-fold) in PIN1 shRNA cells. COX-2
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Calpains are intracellular Ca(2+)-dependent Cys proteases that play important roles in a wide range of biological phenomena via the limited proteolysis of their substrates. Genetic defects in calpain genes cause lethality and/or functional deficits in many organisms, including humans. Despite their …
Two types of cell death can be distinguished by morphological features, although it is likely that these are two ends of a spectrum with possible intermediate forms. Apoptosis involves shrinkage, nuclear disassembly, and fragmentation of the cell into discrete bodies with intact plasma membranes. These are rapidly phagocytosed by neighbouring cells. An important feature of apoptosis is the requirement for adenosine triphosphate (ATP) to initiate the execution phase. In contrast, necrotic cell death is characterized by cell swelling and lysis. This is usually a consequence of profound loss of mitochondrial function and resultant ATP depletion, leading to loss of ion homeostasis, including volume regulation, and increased Ca2+. The latter activates a number of nonspecific hydrolases (i.e., proteases, nucleases, and phospholipases) as well as calcium dependent kinases. Activation of calpain I, the Ca2+-dependent cysteine protease cleaves the death-promoting Bcl-2 family members Bid and Bax which ...
Calpain-like mRNAs have been identified in other organisms including bacteria, but the molecules encoded by these mRNAs have not been isolated, so little is known about their properties. How calpain activity is regulated in these organisms cells is still unclear In metazoans, the activity of calpain is controlled by a single proteinase inhibitor, calpastatin (IPR001259). The calpastatin gene can produce eight or more calpastatin polypeptides ranging from 17 to 85 kDa by use of different promoters and alternative splicing events. The physiological significance of these different calpastatins is unclear, although all bind to three different places on the calpain molecule; binding to at least two of the sites is Ca2+ dependent. The calpains ostensibly participate in a variety of cellular processes including remodelling of cytoskeletal/membrane attachments, different signal transduction pathways, and apoptosis. Deregulated calpain activity following loss of Ca2+ homeostasis results in tissue damage ...
Fulvestrant (ICI 182 780, ICI) has been used in treating patients with hormone-sensitive breast cancer, yet initial or acquired resistance to endocrine therapies frequently arises and, in particular, cancer recurs as metastasis. We demonstrate here that both 17-beta-estradiol (E2) and ICI enhance cell adhesion to matrigel in MCF-7 breast cancer cells, with increased autolysis of calpain 1 (large subunit) and proteolysis of focal adhesion kinase (FAK), indicating calpain activation. Additionally, either E2 or ICI induced down-regulation of estrogen receptor α without affecting G protein coupled estrogen receptor 30 (GPR30) expression. Interestingly, GPR30 agonist G1 triggered calpain 1 autolysis but not calpain 2, whereas ER agonist diethylstilbestrol caused no apparent calpain autolysis. Furthermore, the actions of E2 and ICI on calpain and cell adhesion were tremendously suppressed by G15, or knockdown of GPR30. E2 and ICI also induced phosphorylation of extracellular regulated protein kinases ...
Hypoxia-specific upregulation of calpain activity and gene expression in pulmonary artery endothelial cells.: The effects of exposure to hypoxia on the catalyti
Methods Male wild type mice were randomly divided into control and PD150606 groups. Mice were subjected to myocardial ischemia by occlusion of the left anterior descending coronary artery for 45 min and reperfusion for 3 h (I/R). Terminal deoxynucleotidyl transferase d-UTP nick end labeling (TUNEL) staining was performed using an In Situ Cell Death Detection kit on paraffin heart sections (5 mm). Hoechst 33342 was used as a counter-stain. Adult mouse cardiomyocytes were isolated and cultured, then subjected to ischemia for 1 h, and reperfusion for 3 h. The survival of cardiomyocytes, activity of calpain and caspase-3, cytoplasmic DNA fragments and cytochrome c concentrations were determined. Results Compared to control, the numbers of TUNEL-positive nuclei were significantly increased in the peri-infarct area in I/R mice (p,0.05). Compared to normal cultured cardiomyocytes, the survival of the cells significantly decreased, however the activation of calpain and caspase-3, and cytoplasmic DNA ...
The pSUPER.retro (Oligoengine) RNA interference system was used to achieve stable expression of siRNAs. Oligonucleotides targeted to calpain 2 or PTP1B mRNA as well as a nonsilencing control were synthesized by Integrated DNA Technologies, annealed, and cloned into the pSUPER.retro.puro vector according to manufacturers instructions. Retroviral transfection was performed as described previously (Franco et al., 2004a). Wild-type MTLn3 cells were infected at 32°C for 6 h and allowed to recover in growth medium for 24 h before selection with 1 μg/ml puromycin for 4-5 d. Target sequences for calpain 2 in MTLn3 cells: control, 5′-TTCTCCGAACGTGTCACGT-3′; Capn2 si-A, 5′-AGGCCTATGCCAAGATCAA-3′; and Capn2 si-B, 5′-GAATGGCGATTTCTGCATC-3′. Target sequences for PTP1B in MTLn3 cells: PTP1B si-A, 5′-GCTGACACTGATCTCTGAA-3′; and PTP1Bsi-B, 5′-CAGGAGGAGCCTTGGTGTC-3′. Target sequences for human calpain 2 have been described previously (Su et al., 2006). Target sequences for cortactin: ...
The activity of calpain is controlled by the free intracellular calcium level and by the proteins intrinsically disordered endogenous inhibitor, calpastatin, mediated by short conserved segments: subdomains A-C. The exact binding mode of calpastatin to the enzyme has until now been unclear. Our NMR data of the 141 amino acid long inhibitor, with and without calcium and calpain, have revealed structural changes and a tripartite binding mode, in which the disordered inhibitor wraps around, and contacts, the enzyme at three points, facilitated by flexible linkers. This unprecedented binding mode permits a unique combination of specificity, speed and binding strength in regulation.. ...
Health, ...EDITORS PICK: Calpain inhibitors never forget: improving memory in Al...Overactivation of proteins known as calpains which are involved in me...It is thought that dysfunctional signaling between nerve cells contrib...TITLE: Inhibition of calpains improves memory and synaptic transmissio...,JCI,online,early,table,of,contents:,July,1,,2008,medicine,medical news today,latest medical news,medical newsletters,current medical news,latest medicine news
FUNCTION: The protein encoded by this gene is a member of the calpain family of proteins. Unlike many members of the calpain gene family, this gene lacks a calmodulin-like domain, required for calcium binding. Mouse models for Huntington's disease displayed increased levels of the protein encoded by this gene. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2014 ...
Calpains encompass a family of calcium-dependent, nonlysosomal proteases characterized by a cysteine-protease domain that includes a conserved catalytic sequence Cys-His-Arg combined with a calmodulin-like Ca2+-binding site (Sorimachi and Suzuki 2001). The configuration of the cysteine-protease domain determines the formation of an active catalytic pocket, which only occurs when calcium is present. Calpains are involved in a large variety of calcium-regulated processes, such as signal transduction, cell proliferation, and PCD (Goll et al. 2003).. The calpain family comprises a heterogeneous group of cysteine proteases with a large expression pattern. The proteases belonging to this family have been subdivided into three groups depending on their primary structure and the presence or absence of regulatory subunits. These three groups are defined as: typical (also called ubiquitous or conventional), atypical, and other EF-calpains (Goll et al. 2003; Saez et al. 2006). The most important and most ...
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Sigma-Aldrich offers Sigma-A6060, Calpain Inhibitor II for your research needs. Find product specific information including CAS, MSDS, protocols and references.
Calpains are a family of intracellular cysteine proteases activated by calcium. They participate in many processes including cell motility, cell cycle progression and cell death, in response to calcium signaling. Because ...
M2 Ethyl methanesulfonate (EMS) mutagenized Ler seeds were purchased from Lehle Seeds and examined under a dissecting microscope for the absence of giant cells in the sepal.. The dek1-4 mutation isolated contains a C to T change at base 6316 of the CDS, which causes a single amino acid substitution of a cysteine for conserved arginine 2106 in domain III of the calpain protease (supplementary material Fig. S2A) (Sorimachi and Suzuki, 2001). The dek1-4 allele fails to complement the reference dek1-3 (SAIL_384_G07) allele (data not shown), establishing that the absence of giant cells is due to the mutation in the DEK1 gene.. The dek1-4 mutation can be PCR genotyped by amplifying with oAR448 (5′-TGTTGGTGGAACAGACTATGTGAATTCA-3′) and oAR449 (5′-TGAAGACTGAAAGGACAAAAGGTGC-3′) with a 60°C annealing temperature followed by digesting the product with BsaAI to produce a 108 bp wild-type product or a 137 bp mutant product.. The atml1-2 allele isolated in this mutant screen contains a C to T change ...
The photoswitchable N-terminal diazo and triazene-dipeptide aldehydes 8a-d, 10a,b, and 17a,b present predominantly as the (E)-isomer, which purportedly binds deep in the S3 pocket of calpain. All compounds are potent inhibitors of m-calpain, with 8b being the most active (IC50 of 35 nM). The diazo-containing inhibitors 8a, 8c, and 10a were irradiated at 340 nm to give a photostationary state enriched in the (Z)-isomer, and in all cases, these were less active. The most water soluble triazene 17a (IC50 of 90 nM) retards calpain-induced cataract formation in lens culture ...
Fingerprint Dive into the research topics of Temporal response of rabbits to beta-adrenergic agonist feeding: tissue weight, calpains and calpastatin activities, and nucleic acid and protein concentrations.. Together they form a unique fingerprint. ...
The calpain family is named for the calcium dependence of the papain-like, thiol protease activity of the well-studied ubiquitous vertebrate enzymes calpain-1 (μ-calpain) and calpain-2 (m-calpain). Proteins showing sequence relatedness to the catalytic core domains of these enzymes are included in this ancient and diverse eukaryotic protein family. Calpains are examples of highly modular organization, with several varieties of amino-terminal or carboxy-terminal modules flanking a conserved core. Acquisition of the penta-EF-hand module involved in calcium binding (and the formation of heterodimers for some calpains) seems to be a relatively late event in calpain evolution. Several alternative mechanisms for binding calcium and associating with membranes/phospholipids are found throughout the family. The gene family is expanded in mammals, trypanosomes and ciliates, with up to 26 members in Tetrahymena, for example; in striking contrast to this, only a single calpain gene is present in many other
4PHK: The Structural Basis of Differential Inhibition of Human Calpain by Indole and Phenyl alpha-Mercaptoacrylic Acids. The complex with (Z)-3-(4-chlorophenyl)-2-mercaptoacrylic acid
Calpain兔多克隆抗体(ab124631)可与小鼠, 大鼠, 人, 曼氏血吸虫样本反应并经WB, IP, ELISA实验严格验证。所有产品均提供质保服务,中国75%以上现货。
From NCBI Gene:. Calpains represent a ubiquitous, well-conserved family of calcium-dependent cysteine proteases. The calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large catalytic subunit has four domains: domain I, the N-terminal regulatory domain that is processed upon calpain activation; domain II, the protease domain; domain III, a linker domain of unknown function; and domain IV, the calmodulin-like calcium-binding domain. This gene encodes a large subunit. It is an atypical calpain in that it lacks the calmodulin-like calcium-binding domain and instead has a divergent C-terminal domain. It is similar in organization to calpains 5 and 6. This gene is associated with type 2 or non-insulin-dependent diabetes mellitus (NIDDM), and is located within the NIDDM1 region. Multiple alternative transcript variants have been described for this gene. [provided by RefSeq, Sep 2010]. From UniProt: ...
Calpains form a family of Ca(2+)-dependent cysteine proteases involved in diverse cellular processes. However, the specific functions of each calpain isoform remain unknown. Recent reports have shown that calpain 2 (Capn2) is essential for cell viability. We have recently shown that Capn2 is a nuclear protease associated with chromosomes during mitosis in mammalian embryonic cells. We now report that Capn2 depletion impairs mitosis and induces apoptosis in murine cells. Low Capn2 levels induce chromosome alignment defects, the loss of histone H3 threonine 3 phosphorylation at centromeres, and premature sister chromatid separation. Thus, Capn2 may play a role in fundamental mitotic functions, such as the maintenance of sister chromatid cohesion.
context: it has been reported that the equilibrium between the erythrocyte protease calpain i and its physiological inhibitor calpastatin is disrupted in patients with essential hypertension. objective: to investigate the activity of non-purified calpain i...
TY - JOUR. T1 - Involvement of calpain in AMPA-induced toxicity to rat cerebellar Purkinje neurons. AU - Mansouri, Bobbak. AU - Henne, William M.. AU - Oomman, Sowmini K.. AU - Bliss, Richard. AU - Attridge, Jennifer. AU - Finckbone, VelvetLee. AU - Zeitouni, Tarek. AU - Hoffman, Trent. AU - Bahr, Ben A.. AU - Strahlendorf, Howard K.. AU - Strahlendorf, Jean C.. PY - 2007/2/28. Y1 - 2007/2/28. N2 - AMPA receptor-elicited excitotoxicity is manifested as both a type of programmed cell death termed dark cell degeneration and edematous necrosis, both of which are linked to increased intracellular Ca2+ concentration. The appearance of marked cytoskeletal changes in response to abusive AMPA receptor activation, coupled with increased intracellular Ca2+ concentration suggests activation of various destructive enzymes such as calpains, a family of Ca2+-dependent cysteine proteases. Since calpains and AMPA have been linked to both necrotic cell death and programmed cell death, we sought to determine the ...
Glioblastoma is an aggressive primary brain tumor with a 5-year survival rate of less than 5%. The ability of glioblastoma cells to invade surrounding brain tissue presents the primary challenge for the success of focal therapeutic approaches. We previously reported that the calcium-activated protease calpain 2 is critical for glioblastoma cell invasion in vitro. Here, we show that expression of calpain 2 is required for the dispersal of glioblastoma cells in a living brain microenvironment. Knockdown of calpain 2 resulted in a 2.9-fold decrease in the invasion of human glioblastoma cells in zebrafish brain. Control cells diffusely migrated up to 450 µm from the site of injection, whereas knockdown cells remained confined in clusters. The invasion study was repeated in organotypic mouse brain tissues, and calpain 2 knockdown cells demonstrated a 2.3-fold lower area of dispersal compared with control cells. In zebrafish brain, glioblastoma cells appeared to migrate in part along the blood ...
ABSTRACT Meat tenderness is one of the most important factors affecting consumers assessment of meat quality. Variation in meat tenderness among chickens is genetically controlled and it is also influenced by environmental factors. There has been an increased interest in genetic polymorphisms associated with the variation in meat tenderness among chicken breeds. Understanding and identifying the polymorphisms of candidate genes will facilitate selection programs for genetic improvement in tenderness. Calpain1 (CAPN1), a gene encoding the enzyme μ-calpain which degrades myofibrillar proteins post-mortem, is a physiological candidate gene for meat tenderness. In Malaysia there are two commercially available chicken lines, native and commercial broilers. Native breeds are known to have lower meat tenderness compared to the broilers. The aim of this study is to investigate the reported association between the single nucleotide polymorphisms (SNPs) G3535A, C7198A and G9950A markers in the CAPN1 ...
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.. The ability of macrophages to clear pathogens and elicit a sustained immune response is regulated by various cytokines, including interferon-gamma (IFN-gamma). To investigate the molecular mechanisms by which IFN-gamma modulates phagosome functions, we profiled the changes in composition, abundance, and phosphorylation of phagosome proteins in resting and activated macrophages by using quantitative proteomics and bioinformatics approaches. We identified 2415 phagosome proteins together with 2975 unique phosphorylation sites with a high level of sensitivity. Using network analyses, we determined that IFN-gamma delays phagosomal acquisition of lysosomal hydrolases and peptidases for the gain of antigen presentation. Furthermore, this gain in antigen presentation is dependent on phagosomal networks of the actin cytoskeleton and vesicle-trafficking proteins, as well as Src kinases and calpain proteases. Major ...
Overexpression of suprachiasmatic nucleus circadian oscillatory protein (SCOP), a negative ERK regulator, blocks long-term memory encoding. Inhibition of calpain-mediated SCOP degradation also prevents the formation of long-term memory, suggesting rapid SCOP breakdown is necessary for memory encoding. However, whether SCOP levels also control the magnitude of long-term synaptic plasticity is unknown. Here we show that following synaptic activity-induced SCOP degradation, SCOP is rapidly replaced via mTOR-mediated protein synthesis. We further show that early SCOP degradation is specifically catalysed by μ-calpain, whereas late SCOP resynthesis is mediated by m-calpain. We propose that μ-calpain promotes long-term potentiation induction by degrading SCOP and activating ERK, whereas m-calpain activation limits the magnitude of potentiation by terminating the ERK response via enhanced SCOP synthesis. This unique braking mechanism could account for the advantages of spaced versus massed training in the
Apoptosis is a highly conserved process which can be triggered by a broad range of physiological and pathological conditions. Recent evidence suggests that most proapoptotic stimuli induce the activation of a family of intracellular cysteine proteases called caspases ((1), (2)). These proteases are synthesized as inactive proenzymes which, upon proteolytic cleavage at aspartate residues, form an active complex composed of two heterodimeric subunits. Caspases lead to the proteolysis of a number of cellular substrates, a process which finally results in the apoptotic collapse of the cell.. One of the best-defined apoptotic pathways is mediated by the death receptor CD95 (APO-1/Fas; references (3)-(5)). Triggering of CD95 by its natural ligand CD95L or agonistic antibodies induces the formation of a death-inducing signaling complex (DISC) consisting of the adaptor protein Fas-associated death domain protein (FADD [MORT-1]) and procaspase-8 (FADD-like IL-1β-converting enzyme [FLICE, Mch5]) ...
Title: Pharmacological Modulation of Caspase Activation. VOLUME: 4 ISSUE: 4. Author(s):Ute Fischer and Klaus Schulze-Osthoff. Affiliation:Institute of Molecular Medicine, University of Dusseldorf, Building 23.12, Universitatsstr. 1, D-40225Dusseldorf, Germany.. Keywords:apoptosis, caspase, smac, inhibitor, therapy. Abstract: Deregulation of apoptosis resulting either in inappropriate loss or accumulation of cells is a major cause of many severe pathological conditions such as cancer, autoimmune diseases, microbial infections and degenerative disorders. Consequently, great interest has emerged in devising therapeutic strategies for intervening with cell death, either in a pro- or antiapoptotic direction. Among the different apoptosis-based drug targets, caspases, a family of intracellular cysteine proteases are most promising candidates, because they form the central core of the apoptotic machinery that coordinate cell death from various signals. Inappropriate cell death can be efficiently ...
Supplementary Materials Supplemental Materials supp_24_18_2966__index. Dorsal, a take flight NFB/Rel homologue. We display that proteolytic cleavage by CalpA generates Cactus fragments lacking an N-terminal region required for Toll responsiveness. These fragments are generated in vivo and display properties unique from those of full-length Cactus. We propose that CalpA focuses on free Cactus, which is definitely integrated into and modulates Toll-responsive complexes in the embryo and immune system. Intro Calpains are Ca2+-dependent modulatory proteases with several substrates and functions. They have been implicated in several diseases, such as limb-girdle muscular dystrophy, Huntington disease, Alzheimer disease, and malignancy (Bertipaglia and Carafoli, 2007 ). Unlike degrading enzymes, calpains cleave substrates in a limited manner, generating novel activities by substrate proteolysis (Friedrich and Bozoky, 2005 ; Sorimachi to investigate in more detail the mechanism of calpain action and ...
Calpain 3 (CAPN 3) is an intracellular muscle specific nonlysosomal cysteine protease with a variety of cytoskeletal and myofibrillar substrates. CAPN 3 is vital for cytoskeletal rearrangements, sarcomere function, remodeling, and apoptosis (Kramerova et al. 2005). Knockout Capn3 -/- mice do not demonstrate any clinical myopathic signs throughout their lifespan. However on histologic examination progressive myopathy is evident. There are central nuclei present as well as areas of inflammatory infiltrates that increase as the animal ages (Fougerousse et al. 2003). This model was used to elucidate the pathophysiology of LGMD2A.. ...
Background Chronic microglia-mediated inflammation and oxidative stress are well-characterized underlying factors in neurodegenerative disease, whereby reactive inflammatory microglia enhance ROS production and impact neuronal integrity. Recently, it has been shown that during chronic inflammation, neuronal integrity is compromised through targeted disruption of the axon initial segment (AIS), the axonal domain critical for action potential initiation. AIS disruption was associated with contact by reactive inflammatory microglia which wrap around the AIS, increasing association with disease progression. While it is clear that chronic microglial inflammation and enhanced ROS production impact neuronal integrity, little is known about how acute microglial inflammation influences AIS stability. Here, we demonstrate that acute neuroinflammation induces AIS structural plasticity in a ROS-mediated and calpain-dependent manner. Methods C57BL/6J and NOX2−/− mice were given a single injection of
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Reagents. All chemicals used were commercial products of the highest grade of purity available. The sources of these reagents are detailed in Supplemental Methods.. Mice. Mice were fed chow (CRF-1; Oriental Yeast Co.) or HFD (F2HFD1; CRF-1 supplemented with 16.5% fat, 1.25% cholesterol, and 0.5% sodium cholate; Oriental Yeast Co.) for 12 weeks from 8 weeks of age. Generation of Capn6- and Capn9-deficient mice was performed as described previously (20, 32). Capn6−/y mice express LacZ instead of CAPN6. Ldlr−/− mice (C57/BL6J) were obtained from The Jackson Laboratory (stock no. 2207). Capn6−/yLdlr−/− and Capn9−/−Ldlr−/− mice were generated by intercrossing Capn6−/y and Capn9−/− mice with Ldlr−/− mice, respectively. Capn6+/yLdlr−/−, Capn6−/yLdlr−/−, Capn9+/+Ldlr−/−, and Capn9−/−Ldlr−/− mice were maintained by homozygous breeding, as they have a common genetic background; the genotypes were determined by standard PCR-based genotyping with specific ...
Calpain-1 Substrate II, Fluorogenic - Calbiochem An internally quenched peptide substrate that is optimized for calpain-1 amino acid recognition motifs at the primed as well as the non-primed sides. - Find MSDS or SDS, a COA, data sheets and more information.
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Yorikawa C, Takaya E, Osako Y, Tanaka R, Terasawa Y, Hamakubo T, Mochizuki Y, Iwanari H, Kodama T, Maeda T et al. (2008) Human calpain 7/PalBH associates with a subset of ESCRT-III-related proteins in its N-terminal region and partly localizes to endocytic membrane compartments. J Biochem 143, 731-745 ...
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Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1 at His-410. Mediates, with UTP25, the proteasome-independent degradation of p53/TP53.
Complete information for CAPN10-AS1 gene (RNA Gene), CAPN10 Antisense RNA 1 (Head To Head), including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Reliable and easy to perform assays for studying the crucial role of alternative proteolytic enzymes during apoptosis. We offer various assays to detect and quantify cathepsin, calpain and granzyme B activity and screen for respective enzyme inhibitors.. ...
Order monoclonal and polyclonal Calpain 2 antibodies for many applications. Selected quality suppliers for anti-Calpain 2 antibodies.
Rabbit polyclonal Calpain 1 antibody validated for WB, IHC, ICC/IF and tested in Human, Mouse and Rat. Referenced in 14 publications. Immunogen corresponding…
Mouse polyclonal antibody raised against a full-length human CAPN12 protein. CAPN12 (AAI53094.1, 1 a.a. ~ 719 a.a) full-length human protein. (H00147968-B01P) - Products - Abnova
Characterizing Caplains Implications for production agriculture and human health Calpains and calpastatin may not be household words but their action is as clo
Calpain. "Kiki Memorial and Art Gathering". Equestria Daily. Retrieved February 15, 2015. Sporeman, Sean (May 6, 2015). "Follow ...
Calpain (2017-06-21). "(AU) MLP Season 7 Episode 13 - The Perfect Pear - Stream / Discussion". Equestria Daily. Retrieved 2017- ...
Calpain (October 5, 2016). "(It Aired!) UK - Season 6 Episode 25 - To Where and Back Again - Stream / Discussion (It Aired!)". ...
Calpain (October 5, 2016). "(It Aired!) UK - Season 6 Episode 25 - To Where and Back Again - Stream / Discussion (It Aired!)". ... Calpain (August 24, 2018). "(AUS) My Little Pony Season 8 Episode 21 - A Rockhoof and a Hard Place - Stream / Discussion". ... Calpain (August 10, 2018). "(AUS) My Little Pony Season 8 Episode 17 - The End in Friend - Stream / Discussion". Equestria ... Calpain (August 17, 2018). "(AUS) My Little Pony Season 8 Episode 19 - On the Road to Friendship - Stream / Discussion". ...
Calpain (2018-08-24). "(AUS) My Little Pony Season 8 Episode 21 - A Rockhoof and a Hard Place - Stream / Discussion". Equestria ... Calpain (2018-08-10). "(AUS) My Little Pony Season 8 Episode 17 - The End in Friend - Stream / Discussion". Equestria Daily. ... Calpain (2018-08-17). "(AUS) My Little Pony Season 8 Episode 19 - On the Road to Friendship - Stream / Discussion". Equestria ... Calpain (2018-08-03). "(AUS) My Little Pony Season 8 Episode 15 - The Hearth's Warming Club - Stream / Discussion". Equestria ...
Calpain (2015-02-16). "Season 5 Concept Art at PonyCon Appears! New Characters and More Revealed!". Equestria Daily. Retrieved ... Calpain (2015-01-19). "PonyCon 2015 To Premiere New Season 5 Trailer With MLP Directors!". Equestria Daily. Retrieved 2015-01- ...
Calpain (September 20, 2017). "America's Got Talent Special MLP Movie Sneak Peak". Equestria Daily. Retrieved September 27, ...
Calpain (September 29, 2015). "Ratings For The 'Friendship Games' Are In". Equestria Daily. Retrieved September 29, 2015. ...
Calpain 3 is unique from other calpain proteases in that it is relatively specific to muscle. Calpain 3 is both a protease and ... Research is being done to identify the proteins cleaved by calpain-3. Gene therapy is being studied to replace the function of ... Mutation in the gene CAPN3, which encodes the protein calpain-3 (CAPN3), is the cause of calpainopathy. As of 2019, more than ... The structural role of calpain 3 is stabilization of the triad protein complexes. A triad protein complex plays a role ...
"Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members". The Journal of Biological Chemistry ...
Löfvenberg L, Backman L (1999). "Calpain-induced proteolysis of beta-spectrins". FEBS Lett. 443 (2): 89-92. doi:10.1016/S0014- ...
1997). "Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells". J. Cell. ... 1989). "Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene". J. Biol. ... It consists of an N-terminal domain L and four repetitive calpain-inhibition domains (domains 1-4), and it is involved in the ... 1990). "Cloning and expression of the genes for calpains and calpastatins". Biochem. Soc. Symp. 55: 29-44. PMID 2559735. Asada ...
This protein is a substrate of calpain II. A second transcript from this gene has been described, but its full length nature ...
The protease calpain has also been shown to be involved in this type of cell destruction; just as the use of calpain inhibitors ... Wang KK (Jan 2000). "Calpain and caspase: can you tell the difference?". Trends in Neurosciences. 23 (1): 20-26. doi:10.1016/ ... Villa PG, Henzel WJ, Sensenbrenner M, Henderson CE, Pettmann B (Mar 1998). "Calpain inhibitors, but not caspase inhibitors, ...
These cysteine proteases include calpain, caspase, and cathepsin. These three proteins are examples of detectable signs of ...
This group includes the calpains. Basic proteases (or alkaline proteases) Proteases are involved in digesting long protein ...
Calpain-5 is a protein that in humans is encoded by the CAPN5 gene. Calpains are calcium-dependent cysteine proteases involved ... "Entrez Gene: CAPN5 calpain 5". Vanderklish PW, Bahr BA (2001). "The pathogenic activation of calpain: a marker and mediator of ... A functional calpain protein consists of an invariant small subunit and 1 of a family of large subunits. CAPN5 is one of the ... 2007). "Calpain-5 gene variants are associated with diastolic blood pressure and cholesterol levels". BMC Med. Genet. 8: 1. doi ...
... interacts with many sarcomeric proteins including: Z line region: telethonin and alpha-actinin I band region: calpain-3 ... July 1998). "Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular ... Kinbara K, Sorimachi H, Ishiura S, Suzuki K (August 1998). "Skeletal muscle-specific calpain, p49: structure and physiological ... Sorimachi H, Ono Y, Suzuki K (2000). "Skeletal muscle-specific calpain, p94, and connectin/titin: their physiological functions ...
Weber, Jonasz J.; Ortiz Rios, Midea M.; Riess, Olaf; Clemens, Laura E.; Nguyen, Huu P. (2016-01-01). "The calpain-suppressing ... "Olesoxime suppresses calpain activation and mutant huntingtin fragmentation in the BACHD rat". Brain. 138 (12): 3632-3653. doi: ... effects of olesoxime were attributed to modulating the activity of calcium-dependent proteases called calpains. A 2009-2011 ...
May 2002). "Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain". Molecular and Cellular Biology. 22 (10 ...
This includes a binding site for SA1 or SA2, recognition motifs for separase, caspase, and calpain to cleave, as well as a ... Panigrahi AK, Zhang N, Mao Q, Pati D (November 2011). "Calpain-1 cleaves Rad21 to promote sister chromatid separation". ... RAD21 is cleaved by several proteases including Separase and Calcium-dependent cysteine endopeptidase Calpain-1 during mitosis ...
Calpain-10 is a protein that in humans is encoded by the CAPN10 gene. Calpains are ubiquitous, well-conserved family of calcium ... "Entrez Gene: CAPN10 calpain 10". Sorimachi H, Ishiura S, Suzuki K (1998). "Structure and physiological function of calpains". ... 2001). "Characterization and expression of calpain 10. A novel ubiquitous calpain with nuclear localization". J. Biol. Chem. ... Horikawa Y (2007). "Calpain-10 (NIDDM1) as a Susceptibility Gene for Common Type 2 Diabetes". Endocr. J. 53 (5): 567-76. doi: ...
Baliova M, Betz H, Jursky F (2004). "Calpain-mediated proteolytic cleavage of the neuronal glycine transporter, GlyT2". J. ...
One possibility is that the calcium-dependent protease calpain is involved: it has been shown that the inhibition of calpain ... Focal adhesion components are amongst the known calpain substrates, and it is possible that calpain degrades these components ... "Regulation of cell migration by the calcium-dependent protease calpain". Journal of Biological Chemistry. 272 (52): 32719-22. ...
... undergoes N-terminal cleavage by Calpain-1 and Calpain-2. The cleaved ATG5 translocates from the cytosol to the ... Yousefi S, Perozzo R, Schmid I, Ziemiecki A, Schaffner T, Scapozza L, Brunner T, Simon HU (October 2006). "Calpain-mediated ...
Synuclein Inclusions via the Activation of Calpain". Journal of Biological Chemistry. 278 (43): 41890-9. doi:10.1074/jbc. ...
The p35 form of this protein is proteolytically cleaved by calpain, generating a p25 form. The cleavage of p35 into p25 results ... Patzke H, Tsai LH (2002). "Calpain-mediated cleavage of the cyclin-dependent kinase-5 activator p39 to p29". J. Biol. Chem. 277 ... 2000). "Neurotoxicity induces cleavage of p35 to p25 by calpain". Nature. 405 (6784): 360-4. Bibcode:2000Natur.405..360L. doi: ...
Calle, Y; Carragher, NO; Thrasher, AJ; Jones, GE (Jun 1, 2006). "Inhibition of calpain stabilises podosomes and impairs ...
In cardiac muscle under stress conditions, cardiac TnT is cleaved by calpain I, restrictively removing the entire N-terminal ... Geesink GH, Kuchay S, Chishti AH, Koohmaraie M (Oct 2006). "Micro-calpain is essential for postmortem proteolysis of muscle ... deletion of the NH2-terminal variable region of cardiac troponin T in ischemia reperfusion by myofibril-associated mu-calpain ...
Ca2+ activates calpain, a cysteine protease, which promotes lysosome rupture. The lysosome is further digested by ASP-1, which ...
As the first calpain whose three-dimensional structure was determined, m-calpain is the type-protease for the C2 (calpain) ... calpain and m-calpain (or calpain I and II), that differed primarily in their calcium requirements in vitro. Their names ... Calpain for Modulatory Proteolysis Database The Calpain Family of Proteases. (2001). University of Arizona. Calpain Info with ... Calpains constitute the C2 family of protease clan CA in the MEROPS database. The calpain proteolytic system includes the ...
Overactivation of calpain 1 and calpain 2 (and their small subunit) has long been tied to acute neurological disorders (e.g. ... The number of mammalian calpain protease family members has grown to 14 on last count. ... The number of mammalian calpain protease family members has grown to 14 on last count. Overactivation of calpain 1 and calpain ... Calpain 10 was recently identified as a susceptibility gene for type 2 diabetes, whereas calpain 9 appears to be a gastric ...
J:43496 Dear N, et al., A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain ...
... mu-CANP or calpain I; a form sensitive to calcium in the milli-molar range, known as m-calpain, m-CANP or calpain II; and a ... How calpain activity is regulated in these organisms cells is still unclear In metazoans, the activity of calpain is controlled ... This group of cysteine peptidases belong to the MEROPS peptidase family C2 (calpain family, clan CA). A type example is calpain ... Calpain-like mRNAs have been identified in other organisms including bacteria, but the molecules encoded by these mRNAs have ...
Host Cell Calpains Can Cleave Structural Proteins from the Enterovirus Polyprotein  Laajala, Mira; Hankaniemi, Minna M.; ... calpain CVB3 EV1 infection timetable picornavirus polyprotein virukset infektiot enterovirukset viruses infections ... The inhibition of calpains before 120 min post-infection inhibited both Echovirus 1 and Coxsackievirus B3 infection. The ... An array of experiments was performed in order to determine the time window when calpains are required for the infection and to ...
Calbiochem Calpain Inhibitor III, CAS 88191-84-8, is a potent, cell-permeable inhibitor of calpain I and II (Ki = 8 nM). - Find ... Calpain Inhibitor III, CAS 88191-84-8, is a potent, cell-permeable inhibitor of calpain I and II (Ki = 8 nM).. More,, Calpain ... Calpain Inhibitor III, CAS 88191-84-8, is a potent, cell-permeable inhibitor of calpain I and II (Ki = 8 nM).. ... A potent, cell-permeable inhibitor of calpain I and II (Ki = 8 nM) that also reduces capsaicin-mediated cell death in cultured ...
Molecular downregulation or RNA interference-mediated depletion of mu-calpain (calpain 1) but not M-calpain (calpain 2) blocked ... Moreover, treatment with the pan-calpain inhibitor ALLN and isoform-specific downregulation of m-calpain (CAPN2) using RNA ... Functional properties of recombinant calpain I and of mutants lacking domains III and IV of the catalytic subunit. Vilei, E.M ... Increased M-calpain expression in the mesencephalon of patients with Parkinsons disease but not in other neurodegenerative ...
Schön, Christian; Paquet-Durand, Francois; Michalakis, Stylianos (2016): Ca(v)1.4 L-Type Calcium Channels Contribute to Calpain ... Our results show that genetic deletion of the synaptic Ca-v 1.4 L-type VGCCs impairs calpain activation and leads to a short- ... Cacna1f x rd1 double mutant mice displayed a strong decrease in the activation of the Ca2+-dependent protease calpain during ...
Arabinda Das, Surajit Karmakar, Sunil J. Patel, Naren L. Banik, Swapan K. Ray; Activation of proteolytic activities of calpain ... Activation of proteolytic activities of calpain and caspase-3 in apoptosis of human malignant glioblastoma cell lines T98G and ... and overexpression and activation of calpain and caspase-3 leading to the cleavage of 270 kD α-spectrin at specific sites for ...
... we discovered calpain-5 (CAPN5) and the ubiquitin ligase Casitas B-lineage lymphoma proto-oncogene B (CBLB) to form a complex ... Hepatitis C virus enters liver cells using the CD81 receptor complex proteins calpain-5 and CBLB Janina Bruening 1 Lisa ... we discovered calpain-5 (CAPN5) and the ubiquitin ligase Casitas B-lineage lymphoma proto-oncogene B (CBLB) to form a complex ... Hepatitis C virus enters liver cells using the CD81 receptor complex proteins calpain-5 and CBLB. PLoS Pathogens, Public ...
LGMD type 2A (calpain 3 myopathy). The onset of this childhood form of LGMD is in the first decade of life (9.7 ±3 y). The ... Calpain 3 cleaves filamin C and regulates its ability to interact with gamma- and delta-sarcoglycans. Muscle Nerve. 2003 Oct. ... The locus of the culprit gene is on 15q15, and the protein product is calpain-3. [27, 28] ... Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell. 1995 Apr 7. 81(1):27-40. [ ...
Calpain-1 appeared to preferentially degrade JAK-phosphorylated-STAT6, which was blocked by calpastatin-mediated inhibition or ... Additionally, our results show that STAT6 is a bonafide substrate for chaperone-mediated autophagy in a selective and calpain- ... Poly(ADP-ribosyl)ation protected phosphorylated-STAT6 against calpain-1-mediated degradation. ... its integrity in the presence of calpains, and its connection to autophagy. This study was conducted using primary splenocytes ...
Calpain-like protease X-linked protein, Protein Calpain-like protease X-linked, Human Calpain-like protease X-linked Protein, ... Human Calpain-like protease X-linked, Human protein Calpain-like protease X-linked ... CAPNX, CalpM, CANPX, Calpamodulin, Calpain-like protease X-linked, CAPNX protein, Protein CAPNX, Human CAPNX Protein, Human ...
Rat CAPN1 (calpain 1) ELISA Kit, Cat#EKE62424. Write a Review Write a Review. × ... Rat CAPN1 (calpain 1) ELISA Kit, Cat#EKE62424. Rating Required Select Rating. 1 star (worst). 2 stars. 3 stars (average). 4 ...
Calpain inhibitors have already been used in the therapy of various other diseases. Analyzing the effects of calpain inhibitors ... Possible candidates as causes of AD are a particular type of proteins called calpains. These proteins have shown the ability to ... Battaglia is investigating how a treatment with calpain inhibitors may restore normal communication between synaptic ...
Calpain-10: from genome search to function. Diabetes Metab Res Rev 2005;21:505-14. ...
Order Calpain 2 Proteins from many different species. Find the right product on antibodies-online.com. ... Trouvez Calpain 2 Protéines pour une variété despèces telles que anti-Human Calpain 2, anti-Mouse Calpain 2, anti-Cow Calpain ... calpain 2 (CAPN2) Protéines. calpain 2 (Capn2) Protéines. calpain 2, gene2 (capn2.2) Protéines. calpain 2, (m/II) large subunit ... Calpain 2 Protéines par Grade. On trouve ici des Calpain 2 Protéines avec un Grade spécifique. Les Grade mentionnés ici sont ...
CAPN3: calpain 3. *CARD9: caspase recruitment domain family member 9. *CARD11: caspase recruitment domain family member 11 ...
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LGMD2A (calpainopathy; LGMDR1 Calpain-3; 15q15). *. LGMD2A is likely the most common autosomal recessive LGMD, accounting for ... The calpain-3 isoform is a homodimer that is abundant in skeletal muscle. More than 450 distinct pathological mutations have ... Impaired regeneration in calpain-3 null muscle is associated with perturbations in mTORC1 signaling and defective mitochondrial ... LGMD1I (LGMDD4 Calpain-3; 15q15) *. Similar syndrome to LGMD2A (calpainopathy), but milder. ...
Calpain test has been informative in a large group of patients and carriers tested so far. Since the calpain test is cost and ... which monitors the m-calpain (milli-calpain), a proteolytic enzyme in the platelets, using an ELISA technique. Four of the ... Deletion analysis & calpain status for carrier detection in a family with Duchenne muscular dystrophy. Indian Journal of ... Eight females with a family history of Duchenne muscular dystrophy (DMD) were analysed for their carrier status by m-calpain ...
To determine whether calpain-cleavage of α-Syn occurs in PD and DLB, we designed site-directed calpain-cleavage antibodies to α ... Moreover, calpain-cleaved α-Syn fragments identified within LBs colocalized with activated calpain in neurons of the PD and DLB ... Detection of calpain-cleaved α-Syn was evident in mouse models of cerebral ischemia and PD and in a Drosophila model of PD. In ... In the present study, we demonstrate that proteolytic processing of α-Syn by the protease calpain I leads to the formation of ...
Calpain-2 inhibitor therapy in Non-severe Hemophilia A Calpain-2 inhibitors ...
Calpain 1 antibody;Calpain 1 large subunit antibody;Calpain 1, (mu/I) large subunit antibody;Calpain mu type antibody;Calpain ... Calpain 2 and Calpain p94. Calpastatin regulates Calpain by inhibiting both the proteolytic activity of Calpain and its binding ... Calpain small subunit 1 antibody;Calpain, large polypeptide L1 antibody;Calpain-1 catalytic subunit antibody;Calpain-1 large ... Micromolar Calpain antibody;Micromolar-calpain antibody;Mu Calpain antibody;muCANP antibody;muCL antibody ...
PubMed] [Google Scholar](e) Mukherjee A, Sadler PJ. kinase Pim1 confirmed an ATP-competitive binding with the intended hydrogen bonding between the phthalimide moiety and the hinge region of the ATP-binding site. Introduction Metal complexes are highly versatile structural scaffolds for the molecular recognition of biomolecules such as nucleic acids and proteins.1C4 Over the last several years our laboratory contributed to this area of research with the design of substitutionally inert ruthenium(II),5 osmium(II),6 rhodium(III),7 iridium(III),8 and platinum(II)9 complexes as highly potent and selective ATP-competitive inhibitors of protein kinases and lipid kinases.10 Our previous design was mainly inspired by the natural product staurosporine with the maleimide moiety of pyridocarbazole metal complexes (Figure 1) undergoing hydrogen bonding with the hinge region of the ATP-binding site, while the pyridocarbazole heterocycle occupying the hydrophobic adenine binding cleft, and the Griseofulvin ...
Role of macrophage-specific calpain-2 in hypercholesterolemia induced atherosclerosis .. *Subramanian, Venkateswaran (PI) ...
The C-terminal portion of c-Jun is relatively resistant to calpain such that an 18kDa fragment, which includes the DNA binding ... The activity of c-Jun in cultured cells can be modified by changing the level of calpastatin, an endogenous calpain inhibitor, ... Calcium-dependent neutral protease (calpain), a candidate for the degradation of PEST-containing proteins, digests c-Jun and c- ... This is the first demonstration that transcription factors are substrates for calpain. ...
Investigating Calpain Expression on Tau Toxicity., 2013. Download whole document (PDF) (2.34 MB) ...
Ma, C.J., Jung, W.J., Lee, K.Y., Kim, Y.C. and Sung, S.H., "Calpain inhibitory flavonoids isolated from Orostachys japonicus," ...
  • The calpain proteolytic system includes the calpain proteases, the small regulatory subunit CAPNS1, also known as CAPN4, and the endogenous calpain-specific inhibitor, calpastatin. (wikipedia.org)
  • Structurally, these two heterodimeric isoforms share an identical small (28 kDa) subunit (CAPNS1 (formerly CAPN4)), but have distinct large (80 kDa) subunits, known as calpain 1 and calpain 2 (each encoded by the CAPN1 and CAPN2 genes, respectively). (wikipedia.org)
  • Overactivation of calpain 1 and calpain 2 (and their small subunit) has long been tied to acute neurological disorders (e.g. stroke and traumatic brain injury) and recently to Alzheimer's disease. (nih.gov)
  • Calpain 1 (large subunit), also designated µ-calpain, is an intracellular calcium-dependent protease that cleaves cyto-skeletal and submembranous proteins. (huabio.com)
  • Calpains are heterodimers of a small regulatory subunit and one of three large catalytic subunits, designated Calpain 1 (large subunit), Calpain 2 and Calpain p94. (huabio.com)
  • Both mu- and m-calpain are heterodimers containing an identical 28-kDa subunit and an 80-kDa subunit that shares 55-65% sequence homology between the two proteases. (scienceopen.com)
  • The crystallographic structure of m-calpain reveals six 'domains' in the 80-kDa subunit: 1). (scienceopen.com)
  • Since 1989, cDNA cloning has identified 12 additional mRNAs in mammals that encode polypeptides homologous to domains IIa and IIb of the 80-kDa subunit of mu- and m-calpain, and calpain-like mRNAs have been identified in other organisms. (scienceopen.com)
  • Subcellular localization and in vivo subunit interactions of ubiquitous μ-calpain. (mpg.de)
  • Calpain-1 appeared to preferentially degrade JAK-phosphorylated-STAT6, which was blocked by calpastatin-mediated inhibition or by genetic knockout in mouse fibroblasts. (biomedcentral.com)
  • Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms. (huabio.com)
  • Calpastatin regulates Calpain by inhibiting both the proteolytic activity of Calpain and its binding to membranes. (huabio.com)
  • The activity of c-Jun in cultured cells can be modified by changing the level of calpastatin, an endogenous calpain inhibitor, indicating that c-Jun is also a substrate for calpain in vivo. (pasteur.fr)
  • Spinal cord analysis of SMA mice treated with calpeptin, a calpain inhibitor, showed an increase of SMN, calpain, and its endogenous inhibitor calpastatin in MNs. (udl.cat)
  • Calpastatin exon 1B-derived peptide, a selective inhibitor of calpain: Enhancing cell permeability by conjugation with penetratin. (mpg.de)
  • The calpain system originally comprised three molecules: two Ca2+-dependent proteases, mu-calpain and m-calpain, and a third polypeptide, calpastatin, whose only known function is to inhibit the two calpains. (scienceopen.com)
  • A central question has been how calpastatin is so exquisitely specific in attaching to calpain and inhibiting it-essentially ignoring other highly similar enzymes in the cell. (anl.gov)
  • Previous studies on calpastatin had revealed how a few of the parts of the calpastatin molecule attach to calpain in the inhibition process," said Green. (anl.gov)
  • Tudor Moldoveanu, a postdoctoral fellow in Green's laboratory, performed x-ray structural analysis on such a protein crystal that consisted of a critical part of the calpastatin molecule attached to calpain. (anl.gov)
  • The structural picture obtained of the two proteins clutched together clearly revealed why calpastatin so specifically attaches to calpain. (anl.gov)
  • Calpain has multiple domains, and what we saw was that calpastatin wraps itself around pretty much every domain of calpain," said Moldoveanu. (anl.gov)
  • This broad embrace also guarantees that calpastatin will precisely recognize only calpains, rather than mistakenly attach to other similar enzymes in the cell. (anl.gov)
  • Furthermore, the researchers discovered how calpastatin evades being chewed up by calpain. (anl.gov)
  • The researchers' structural information also showed how calpain changes its shape once it is activated by calcium and how this transformation renders it a target of calpastatin attachment and thus inhibition. (anl.gov)
  • Four of these genes [IGFBP1, peroxiredoxin3, TNFR1, and calpastatin (endogenous inhibitor of calpain)] could be validated by real-time PCR. (cun.es)
  • 1991). Koohmaraie (1996) identified the protease μ-calpain ( CAPN1 ) and its inhibitor calpastatin ( CAST ) as major factors affecting post-mortem tenderization in meat. (unl.edu)
  • Previous studies have shown that the inhibition of calpains prevents the enterovirus infection after entry and RNA release into the cytoplasm. (jyu.fi)
  • However, previous studies have shown that the inhibition of the cellular calpains inhibits the enterovirus RNA-replication. (jyu.fi)
  • The inhibition of calpains before 120 min post-infection inhibited both Echovirus 1 and Coxsackievirus B3 infection. (jyu.fi)
  • The inhibition of calpains prevented the intracellular membrane modifications characteristic to enterovirus infection. (jyu.fi)
  • PARP-1 inhibition appears to destabilize STAT6 on IL-4 or allergen exposure potentially through a calpain-dependent mechanism as a partially specific calpain inhibitor (ALLN) reversed this process [ 5 ]. (biomedcentral.com)
  • Finally, in vitro calpeptin treatment prevented microtubule-associated protein 1A/1B-light chain 3 (LC3) increase in MNs neurites, indicating that calpain inhibition may reduce autophagosome accumulation in neuron prolongations, but not in soma. (udl.cat)
  • Thus, our results show that calpain activity is increased in SMA MNs and its inhibition may have a beneficial effect on SMA phenotype through the increase of SMN in spinal cord MNs. (udl.cat)
  • Calpain inhibition by 100 mM MDL partially prevented these changes and increased stimulus-dependent phosphorylation of PKC-specific protein substrates. (edu.pl)
  • Inhibition of calpain after the window of opportunity slows down the rate of lamellipodial extension but doesn't arrest it. (bgu.ac.il)
  • Soy isoflavones and calpain inhibition have been suggested to exert inhibitory effects on cancer development and progression. (biomedcentral.com)
  • Inhibition of calpain activity amplified the Haelan-induced growth inhibition of CAPAN-1 and BxPC-3 cells, but failed to amplify the growth inhibition of Haelan-treated AR42J cells. (biomedcentral.com)
  • In fibroblasts, calpain inhibition induced Haelan-independent growth inhibition. (biomedcentral.com)
  • Calpain inhibition also amplified the Haelan-induced apoptotic activity in all cancer cell lines, but exerted no further effect in fibroblasts. (biomedcentral.com)
  • Calpain inhibition strengthens integrin-cytoskeletal linkages and greatly reduces integrin-extraction during rear retraction. (mit.edu)
  • Calpain Inhibition Is Protective in Machado-Joseph Disease Zebrafish Due to Induction of Autophagy. (ataxin.com)
  • On the other hand, calpain inhibition upregulates TRPM7, decreases intracellular magnesium and enhances the sensitivity to doxorubicin of resistant LoVo cells. (unicatt.it)
  • Dr. Battaglia is investigating how a treatment with calpain inhibitors may restore normal communication between synaptic transmission and thereby slow the progression of the disease. (brightfocus.org)
  • Calpain inhibitors have already been used in the therapy of various other diseases. (brightfocus.org)
  • Analyzing the effects of calpain inhibitors in animal models of Alzheimer's might help to identify a new treatment for AD. (brightfocus.org)
  • Recent advances in SMA research postulate the role of calpain protease regulating survival motor neuron (SMN) protein and the positive effect on SMA phenotype of treatment with calpain inhibitors. (udl.cat)
  • The results show for the first time that Haelan may be a promising candidate in the treatment of human pancreatic cancer, and its anticancer activity may be potentiated when administered with calpain inhibitors. (biomedcentral.com)
  • This study provides new insight into the role of this protein family in influenza A viruses pathogenesis and shows that targeting calpains-dependent signaling pathways with calpain inhibitors has a protective effect in influenza A viruses infection, reduces viral replication, leukocyte infiltration and expression of pro-inflammatory mediators in bronchial epithelial cells. (hku.hk)
  • When the sequence of this enzyme became known, it was given the name "calpain", to recognize its common properties with two well-known proteins at the time, the calcium-regulated signalling protein, calmodulin, and the cysteine protease of papaya, papain. (wikipedia.org)
  • Under these physiological conditions, a transient and localized influx of calcium into the cell activates a small local population of calpains (for example, those close to Ca2+ channels), which then advance the signal transduction pathway by catalyzing the controlled proteolysis of its target proteins. (wikipedia.org)
  • Possible candidates as causes of AD are a particular type of proteins called calpains. (brightfocus.org)
  • Calcium-dependent neutral protease (calpain), a candidate for the degradation of PEST-containing proteins, digests c-Jun and c-Fos efficiently in vitro. (pasteur.fr)
  • Cell morphogenesis of Trypanosoma brucei requires the paralogous, differentially expressed calpain-related proteins CAP5.5 and CAP5.5V. (ox.ac.uk)
  • Proteins from the calpain super-family are involved in developmentally- and environmentally-regulated re-modelling of the eukaryotic cytoskeleton and the dynamic organisation of signal transduction cascades. (ox.ac.uk)
  • It is said that an accumulation of Calcium in the intact lens induces formation of high molecular weight proteins, which may be associated with the loss of lens transparency [ 4 ], Caused by prolonged increase in intracellular calcium would be expected to activate proteases such as calpain so any interference within the lens is also likely to have a cataract. (alliedacademies.org)
  • Although the physiological role of calpains is still poorly understood, they have been shown to be active participants in processes such as cell mobility and cell cycle progression, as well as cell-type specific functions such as long-term potentiation in neurons and cell fusion in myoblasts. (wikipedia.org)
  • Aim of this study is to investigate the role of calpains in Echovirus 1 and Coxsackievirus B3 infections. (jyu.fi)
  • These results suggest that the role of calpains in the enterovirus infection is after entry but before membrane rearrangements and RNA replication, most likely in the polyprotein processing. (jyu.fi)
  • Arguably, the best currently available fluorogenic calpain substrate is (EDANS)-Glu-Pro-Leu-Phe=Ala-Glu-Arg-Lys-(DABCYL), with cleavage occurring at the Phe=Ala bond. (wikipedia.org)
  • Additionally, our results show that STAT6 is a bonafide substrate for chaperone-mediated autophagy in a selective and calpain-dependent manner in the human Jurkat cell-line. (biomedcentral.com)
  • The proteolysis of spectrin, a calpain substrate and a major component of the membrane skeleton, occurs within this window of opportunity, in agreement with the hypothesis that spectrin proteolysis is an early step in the formation of the GC. (bgu.ac.il)
  • TUG is a calpain-10 substrate involved in the translocation of GLUT4 in adipocytes. (nih.gov)
  • αII-Spectrin, a structural protein of the cell cytoskeleton with a molecular weight of 250 kDa, is a major substrate of cytosolic cysteine proteases, such as calpains and caspases [ 5 ]. (biomedcentral.com)
  • Utilizing this model, bovine semitendinosus muscles were processed to generate long and short sarcomere lengths to study their effect on the degradation of Troponin-T. Myofibrils were isolated and western blot analysis of Troponin-T was conducted to analyze the effect of calpain digestion on isolated myofibrils. (usda.gov)
  • Effect of calpain 3 defficiency on calcium homeostasis. (deusto.es)
  • In contrast, cells with targeted knockout of either calpain-1 (CAPN1∼/∼) or -2 (CAPN2∼/∼) show near-normal repair of mechanical injuries, inferring that both calpain-1 and calpain-2 are equally capable of conducting the cascade of proteolytic cleavage events to reseal a membrane injury, including that of the known membrane repair agent dysferlin. (edu.au)
  • With CAPN1 variants associated with spastic paraplegia, a severe dystrophy observed with muscle-specific loss of calpain-1 and -2 activity identifies CAPN2 and CAPNS1 as plausible candidate neuromuscular disease genes. (edu.au)
  • Calpain Inhibitor III, CAS 88191-84-8, is a potent, cell-permeable inhibitor of calpain I and II (Ki = 8 nM). (emdmillipore.com)
  • A potent, cell-permeable inhibitor of calpain I and II (K i = 8 nM). (emdmillipore.com)
  • A new cell-permeable calpain inhibitor. (mpg.de)
  • Irreversible, non-toxic, cell-permeable inhibitor of cysteine proteases calpain, cathepsins B and L, and Trypanosome trypanopain . (enzolifesciences.com)
  • Calpeptin is a cell-permeable inhibitor of a group of proteases, including calpain I, calpain II, cathepsin L, and cathepsin K. (news-medical.net)
  • The calpains ostensibly participate in a variety of cellular processes including remodelling of cytoskeletal/membrane attachments, different signal transduction pathways, and apoptosis. (embl-heidelberg.de)
  • Lonomycin-activated calpain triggers apoptosis - A probable role for Bcl-2 family members. (mpg.de)
  • How calpain activity is regulated in cells is still unclear, but the calpains ostensibly participate in a variety of cellular processes including remodeling of cytoskeletal/membrane attachments, different signal transduction pathways, and apoptosis. (scienceopen.com)
  • We investigated the effects of the isoflavone containing beverage Haelan 951 and the calpain inhibitor PD150606 on the viability, growth and apoptosis of the human pancreatic cancer cell lines CAPAN-1 and BxPC-3, on the rat pancreatic cancer cell line AR42J, and on human fibroblasts as the control cell line. (biomedcentral.com)
  • CT-1-/- mice are highly sensitive to Fas-mediated apoptosis due in part to deficient STAT-3 activation and inadequate control of calpain activity during the apoptotic process. (cun.es)
  • This is the first demonstration that transcription factors are substrates for calpain. (pasteur.fr)
  • rather, caspase-8 interacts with a multiprotein complex that can include focal adhesion kinase and calpain 2 (CPN2), enhancing cleavage of focal adhesion substrates and cell migration. (elsevier.com)
  • In a cleavage experiment calpains were found capable of processing the Coxsackievirus B1 polyprotein. (jyu.fi)
  • Calpain-Cleavage of α-Synuclein: Connecting Proteolytic Processing to " by Brian M. Dufty, Lisa R. Warner et al. (boisestate.edu)
  • To determine whether calpain-cleavage of α-Syn occurs in PD and DLB, we designed site-directed calpain-cleavage antibodies to α-Syn and tested their utility in several animal model systems. (boisestate.edu)
  • Proteolytic cleavage of alpha-actinin by calpain in T cells stimulated with anti-CD3 monoclonal antibody. (jimmunol.org)
  • Our study suggests that calpain-dependent cleavage and dephosphorylation of KCC2 decreased the seizure threshold of rats under prenatal stress. (en-journal.org)
  • 1) GPS-CCD 1.0: A novel computational program for the prediction of calpain cleavage sites with GPS 2.1 algorithm. (biocuckoo.org)
  • We wished to decipher the PARP-1/STAT6 relationship in the context of intracellular trafficking and promoter occupancy of the transcription factor on target genes, its integrity in the presence of calpains, and its connection to autophagy. (biomedcentral.com)
  • Calpains are nonlysosomal, calcium-activated intracellular cysteine proteases. (huabio.com)
  • Our laboratory has established that local activation of calpain by a transient elevation of the free intracellular calcium concentration is crucial for the induction of growth cone (GC) formation in cultured Aplysia neurons. (bgu.ac.il)
  • High intracellular Ca(2 + ) causes activation of the enzyme calpain II, which leads to the denaturation of crystalline, the soluble lens protein required for maintaining the transparency of the lens. (alliedacademies.org)
  • It is concluded that the PKC phosphorylation system is severely affected by non-specific activation and a subsequent, calpain-dependent proteolysis in the acutely prepared hippocampal slices. (edu.pl)
  • The neutral proteases activated by calcium ions, called calpains, are partially responsible for postmortem proteolysis, leading to a progressive increase in meat tenderness. (usp.br)
  • The role of calpain-mediated proteolysis of ataxin-3 in Machado-Joseph disease: a molecular therapy approach with viral vectors. (fct.pt)
  • A severe muscular dystrophy in a murine model with skeletal muscle knockout of Capns1 highlights vital roles for calpain-1 and/or -2 for health and viability of skeletal muscles not compensated for by calpain-3 (CAPN3). (edu.au)
  • Poly(ADP-ribosyl)ation protected phosphorylated-STAT6 against calpain-1-mediated degradation. (biomedcentral.com)
  • Calpain contributes to silica-induced IkB-a degradation and nuclear factor-kB activation. (cdc.gov)
  • Exogenous '-calpain was added to myofibrils and the extent of Troponin-T degradation was monitored at 0, 2, 15, 60, 120 min, 1 d and 2d. (usda.gov)
  • Ischemia induced either by embolic middle cerebral artery occlusion (MCAO) in vivo or by oxygen and glucose deprivation in brain slices caused calpain-dependent conversion of the Cdk5-activating cofactor p35 to p25. (cdc.gov)
  • Recombinant protein within human calpain 1 aa 1-714 / 714. (huabio.com)
  • We identified calpain, a calcium-dependent protease, as a regulator of rear retraction and cell speed at high adhesiveness. (mit.edu)
  • Such molecules could include the calpains, ubiquitous calcium-dependent proteases. (hku.hk)
  • Furthermore, the expression levels of voltage-gated calcium channel Cav2.1, protein kinase C gamma and calcium-dependent protease, calpain-2, were increased after CDR antibody internalization. (uib.no)
  • Loss-of-function mutations of the calpain 3 gene have now been identified as the cause of limb-girdle muscular dystrophy 2A. (nih.gov)
  • These findings suggest that calpain I may participate in the disease-linked aggregation of α-Syn in various α-synucleinopathies. (boisestate.edu)
  • We suggest that calpain participates in two different processes: it is critical for the triggering of GC formation and plays a modulatory role during the extension of the GC's lamellipodia. (bgu.ac.il)
  • Eight females with a family history of Duchenne muscular dystrophy (DMD) were analysed for their carrier status by m-calpain test, which monitors the m-calpain (milli-calpain), a proteolytic enzyme in the platelets, using an ELISA technique. (who.int)
  • Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding. (cathdb.info)
  • But when a defective or overactive variation of that same enzyme, called calpain, is linked to a startling array of illnesses, then finding out how to regulate calpains becomes an important research objective. (anl.gov)
  • This attachment not only blocks the portion of the enzyme called the active site, where calpain performs its snipping function, but also covers regions away from that site. (anl.gov)
  • IL-1β-converting enzyme cleaves the inactive IL-1β Precursor and ProIL-1α is processed by calpain (4). (biolegend.com)
  • The potency of ANAVEX 2-73, inhibiting enzyme activities was also studied on enzyme assays including calpain, nitric oxide synthase (constitutive and inducible form), protein kinase (PKCα and PKCβ), EGF receptor kinase and calcineurin. (anavex.com)
  • The ubiquitous calpains, calpain-1 and -2, play important roles in Ca2+-dependent membrane repair. (edu.au)
  • Calpain 10 was recently identified as a susceptibility gene for type 2 diabetes, whereas calpain 9 appears to be a gastric cancer suppressor. (nih.gov)
  • In trypanosomatid parasites, calpain-related gene families are unusually large, but we have little insight into the functional roles played by these molecules during trypanosomatid lifecycles. (ox.ac.uk)
  • Using CRISPR gene-edited human embryonic kidney 293 (HEK293) cell lines, we established that loss of both calpains-1 and -2 (CAPNS1∼/∼) virtually ablates Ca2+-dependent repair of mechanical scrape injuries but does not affect injury or recovery from perforation by streptoly-sin-O or saponin. (edu.au)
  • Calpain 10 gene and laryngeal cancer: a survival analysis. (cdc.gov)
  • Trouvez Calpain 2 Protéines pour une variété d'espèces telles que anti-Human Calpain 2, anti-Mouse Calpain 2, anti-Cow Calpain 2. (anticorps-enligne.fr)
  • New evidence for calcium mishandling in human Calpain 3 deficient myotubes. (deusto.es)
  • Remarkably, Cacna1f x rd1 double mutant mice displayed a strong decrease in the activation of the Ca2+-dependent protease calpain during photoreceptor loss. (uni-muenchen.de)
  • In the present study, we demonstrate that proteolytic processing of α-Syn by the protease calpain I leads to the formation of aggregated high-molecular weight species and adoption of a β-sheet structure. (boisestate.edu)
  • Notably, we discovered calpain-5 (CAPN5) and the ubiquitin ligase Casitas B-lineage lymphoma proto-oncogene B (CBLB) to form a complex with CD81 and support HCV entry. (inserm.fr)
  • Calpains have been implicated in apoptotic cell death, and appear to be an essential component of necrosis. (wikipedia.org)
  • These results in the order animals, contrary to those in the other age groups, could be credited to a sarcopenic phenotype observed as increased muscle wasting due to altered calcium homeostasis, depleted muscle ATP content and activation of the calpain system and other apoptotic pathways (Bartoli et al. (uprm.edu)
  • Calpain is also involved in skeletal muscle protein breakdown due to exercise and altered nutritional states. (wikipedia.org)
  • Here we report that CAP5.5, a cytoskeletal calpain-related protein subject to strict stage-specific expression in the sleeping sickness parasite Trypanosoma brucei, is essential and required for correct cell morphogenesis of procyclic (tsetse mid-gut stage) T. brucei. (ox.ac.uk)
  • We propose that the dystrophic phenotype relates to loss of maintenance of plasma membrane/cytoskeletal networks by calpains-1 and -2 in response to directed and dysfunctional Ca2+-signaling, pathways hyperstimulated in the context of membrane injury. (edu.au)
  • Indeed, the calpain inhibitor calpeptin markedly increases the levels of TRPM7 in resistant cells. (unicatt.it)
  • Detergent fractionation revealed the cytosolic localization of calpain. (wikipedia.org)
  • Rapid detachment rate is regulated by integrin-ligand affinity and concentrations while slow detachment is regulated by integrin-cytoskeleton binding and calpain activity. (mit.edu)
  • 2013, Graduate Research, Investigating Calpain Expression on Tau Toxicity. (cmich.edu)
  • Expression of capn8.3, a novel calpain, was located in cells immediately flanking the AER . (xenbase.org)
  • Immunohistochemical analysis of paraffin-embedded rat testis tissue using anti-Calpain 1 antibody. (huabio.com)
  • Shortly thereafter, the activity was found to be attributable to two main isoforms, dubbed μ ("mu")-calpain and m-calpain (or calpain I and II), that differed primarily in their calcium requirements in vitro. (wikipedia.org)
  • Additionally, phosphorylation by protein kinase A and dephosphorylation by alkaline phosphatase have been found to positively regulate the activity of μ-calpains by increasing random coils and decreasing β-sheets in its structure. (wikipedia.org)
  • Phosphorylation improves proteolytic activity and stimulates auto-activation of μ-calpains. (wikipedia.org)
  • However, increased calcium concentration overruns the effects of phosphorylation and dephosphorylation on calpain activity, and thus calpain activity ultimately depends on the presence of calcium. (wikipedia.org)
  • Enhanced calpain activity, regulated by CAPNS1, significantly contributes to platelet hyperreactivity under hypoxic environment. (wikipedia.org)
  • Results indicate an increase of calpain activity in SMN-reduced MNs. (udl.cat)
  • In contrast, only the slices where calpain activity was inhibited responded to further NMDA or phorbol dibutyrate stimulation by a substantial increase of PKC-dependent protein phosphorylation. (edu.pl)
  • We began to study these questions by determining the nature of calpain's action and the stages in which calpain activity affects the cascade of events that leads to the formation of the GC and its extension. (bgu.ac.il)
  • No evidence of calpain, cathepsin B or H activity was found. (oregonstate.edu)
  • In this animal model, first, we evaluated baseline calpain activity. (en-journal.org)
  • Chronic inflammation induced extrasynaptic utrophin upregulation in muscle fibers of mdx mice is correlated with reduced calpain activity. (saba.edu)
  • We reported that PARP-1 regulates genes whose products are crucial for asthma, in part, by controlling STAT6 integrity speculatively through a calpain-dependent mechanism. (biomedcentral.com)
  • Calpains constitute the C2 family of protease clan CA in the MEROPS database. (wikipedia.org)
  • As the first calpain whose three-dimensional structure was determined, m-calpain is the type-protease for the C2 (calpain) family in the MEROPS database. (wikipedia.org)
  • We demonstrate that calpain-1 and -2 are master effectors of Ca2+-dependent repair of mechanical plasma membrane scrape injuries, although they are dispensable for repair/removal of small wounds caused by pore-forming agents. (edu.au)
  • No specific amino acid sequence is uniquely recognized by calpains. (wikipedia.org)
  • In our second body of work, we demonstrate that neuronal MDMX is reduced in AD and in AD models due to amyloid-induced caspase activation, and that loss of MDMX function contributes to pathological processes observed in AD, including mitochondrial damage, calpain activation, and Cdk5 hyperactivity. (upenn.edu)
  • We conclude that the oncoprotein MDMX promotes neuronal survival through regulation of mitochondria, calpains, and Cdk5. (upenn.edu)
  • In the brain, while μ-calpain is mainly located in the cell body and dendrites of neurons and to a lesser extent in axons and glial cells, m-calpain is found in glia and a small number in axons. (wikipedia.org)
  • As molecular overachievers, calpains play a role in many cellular processes, including the movement of cells in tissues, the death of damaged cells, insulin secretion, and brain cell and muscle function. (anl.gov)
  • Our results show that genetic deletion of the synaptic Ca-v 1.4 L-type VGCCs impairs calpain activation and leads to a short-term preservation of photoreceptors in the rd1 mouse. (uni-muenchen.de)
  • In addition to preventing caspase-3 activation, resveratrol also reduced calpain activation. (greenmedinfo.com)
  • Our investigation of E2F1 has resulted in the discovery of a role for this protein in activation of a calpain-dependent death pathway which has not been previously described. (upenn.edu)
  • One of our immediate lines of investigation is testing the hypothesis that E2F1 induces neuronal death in HIV encephalitis via calpain activation, a novel pathway. (upenn.edu)
  • In the human PD and DLB brain, calpain-cleaved α-Syn antibodies immunolabeled LBs and neurites in the substantia nigra. (boisestate.edu)