Relevant bibliographies by topics / Calpain system

Academic literature on the topic 'Calpain system'

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Published: 11 March 2023

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Journal articles on the topic "Calpain system"

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GOLL, DARREL E., VALERY F. THOMPSON, HONGQI LI, WEI WEI, and JINYANG CONG. "The Calpain System." Physiological Reviews 83, no. 3 (July 2003): 731–801. http://dx.doi.org/10.1152/physrev.00029.2002.

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Goll, Darrel E., Valery F. Thompson, Hongqi Li, Wei Wei, and Jinyang Cong. The Calpain System. Physiol Rev 83: 731–801, 2003; 10.1152/physrev.00029.2002.—The calpain system originally comprised three molecules: two Ca2+-dependent proteases, μ-calpain and m-calpain, and a third polypeptide, calpastatin, whose only known function is to inhibit the two calpains. Both μ- 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. The crystallographic structure of m-calpain reveals six “domains” in the 80-kDa subunit: 1) a 19-amino acid NH2-terminal sequence; 2) and 3) two domains that constitute the active site, IIa and IIb; 4) domain III; 5) an 18-amino acid extended sequence linking domain III to domain IV; and 6) domain IV, which resembles the penta EF-hand family of polypeptides. The single 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. 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 μ- and m-calpain, and calpain-like mRNAs have been identified in other organisms. The molecules encoded by these mRNAs have not been isolated, so little is known about their properties. 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. Deregulated calpain activity following loss of Ca2+homeostasis results in tissue damage in response to events such as myocardial infarcts, stroke, and brain trauma.
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Theopold, U., M. Pintér, S. Daffre, Y. Tryselius, P. Friedrich, D. R. Nässel, and D. Hultmark. "CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells." Molecular and Cellular Biology 15, no. 2 (February 1995): 824–34. http://dx.doi.org/10.1128/mcb.15.2.824.

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Calpains are calcium-dependent proteases believed to participate in calcium-regulated signal pathways in cells. Ubiquitous calpains as well as tissue-specific calpains have been found in vertebrates. We isolated cDNA clones for a highly tissue-specific calpain gene from Drosophila melanogaster, CalpA, at 56C-D on the second chromosome. The expression of the CalpA gene product was monitored by using a specific antiserum directed against the product expressed by one cDNA clone. The encoded protein is found in a few neurons in the central nervous system, in scattered endocrine cells in the midgut, and in blood cells. In the blood cell line mbn-2, calpain is associated with a granular component in the cytoplasm. The expression of this protein is more restricted than that of the corresponding transcripts, which are widely distributed in the central nervous system, digestive tract, and other tissues. The sequence of CalpA is closely related to that of vertebrate calpains, but an additional segment is inserted in the calmodulin-like carboxy-terminal domain. This insert contains a hydrophobic region that may be involved in membrane attachment of the enzyme. Differential splicing also gives rise to a minor transcript that lacks the calmodulin-like domain.
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Fontenele, Marcio, Bomyi Lim, Danielle Oliveira, Márcio Buffolo, David H. Perlman, Trudi Schupbach, and Helena Araujo. "Calpain A modulates Toll responses by limited Cactus/IκB proteolysis." Molecular Biology of the Cell 24, no. 18 (September 15, 2013): 2966–80. http://dx.doi.org/10.1091/mbc.e13-02-0113.

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Calcium-dependent cysteine proteases of the calpain family are modulatory proteases that cleave their substrates in a limited manner. Among their substrates, calpains target vertebrate and invertebrate IκB proteins. Because proteolysis by calpains potentially generates novel protein functions, it is important to understand how this affects NFκB activity. We investigate the action of Calpain A (CalpA) on the Drosophila melanogaster IκB homologue Cactus in vivo. CalpA alters the absolute amounts of Cactus protein. Our data indicate, however, that CalpA uses additional mechanisms to regulate NFκB function. We provide evidence that CalpA interacts physically with Cactus, recognizing a Cactus pool that is not bound to Dorsal, a fly NFκB/Rel homologue. We show 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 distinct from those of full-length Cactus. We propose that CalpA targets free Cactus, which is incorporated into and modulates Toll-responsive complexes in the embryo and immune system.
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Goll, Darrel E., Valery F. Thompson, Richard G. Taylor, and Ahmed Ouali. "The calpain system and skeletal muscle growth." Canadian Journal of Animal Science 78, no. 4 (December 1, 1998): 503–12. http://dx.doi.org/10.4141/a98-081.

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The first protein of a group of proteins now identified as belonging to the calpain system was purified in 1976. The calpain system presently is known to be constituted of three well-characterized proteins; several lesser studied proteins that have been isolated from invertebrates; and 10 mRNAs, two each in Drosophila and C. elegans and six in vertebrates, that encode proteins, which, based on sequence homology, belong to the calpain family. The three well-characterized proteins in the calpain family include two Ca2+-dependent proteolytic enzymes, µ-calpain and m-calpain, and a protein, calpastatin, that has no known activity other than to inhibit the two calpains. A substantial amount of experimental evidence accumulated during the past 25 yr has shown that the calpain system has an important role both in rate of skeletal muscle growth and in rate and extent of postmortem tenderization. Calpastatin seems to be the variable component of the calpain system, and skeletal muscle calpastatin activity is highly related to rate of muscle protein turnover and rate of postmortem tenderization. The current paradigm is that high calpastatin activity: 1) decreases rate of muscle protein turnover and hence is associated with an increased rate of skeletal muscle growth; and 2) decreases calpain activity in postmortem muscle and hence is associated with a lower rate of postmortem tenderization. This article summarizes some of the known properties of the calpain system and discusses the potential importance of the calpain system to animal science. Key words: Calpain, calpastatin, postmortem tenderization, skeletal muscle growth
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Ilian, M. A., and N. E. Forsberg. "Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits." Biochemical Journal 287, no. 1 (October 1, 1992): 163–71. http://dx.doi.org/10.1042/bj2870163.

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To investigate the role of calpains in myofibrillar protein degradation in skeletal muscle and the regulation of their activity in vivo, we studied the effects of fasting on gene expression of calpains and calpastatin in the skeletal muscle of rabbits. In response to fasting, myofibrillar protein degradation increased 2-fold and mRNA levels of calpain I, calpain II and calpastatin were also increased. However, calpain and calpastatin activities remained unchanged. To investigate this discrepancy, we analysed polysomal calpain mRNA. Results indicated that fasting caused a 2-fold increase in the loading of calpain I and II mRNAs on ribosomes. Thus transcription of genes encoding calpain may be increased during fasting to ensure adequate synthesis of the proteinases needed to mobilize muscle protein reserves. The effect of fasting on calpain and calpastatin mRNA expression is shared by cathepsin D and proteasome C2 but not by beta-actin, implying that fasting invokes control of several proteolytic systems in skeletal muscle and underscores the possibility that each proteolytic system plays a role in the adaptation of skeletal muscle to the fasted state.
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Pánico, Pablo, Marcia Hiriart, Patricia Ostrosky-Wegman, and Ana María Salazar. "TUG is a calpain-10 substrate involved in the translocation of GLUT4 in adipocytes." Journal of Molecular Endocrinology 65, no. 3 (October 2020): 45–57. http://dx.doi.org/10.1530/jme-19-0253.

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The calpain-10 (CAPN10) protease is implicated in the translocation of the glucose transporter 4 (GLUT4), which is retained in the Golgi matrix via the Tether containing a UBX domain for GLUT4 (TUG) protein. Insulin stimulation induces the proteolytic processing of TUG, which leads to the translocation of GLUT4 to the cell membrane. We tested whether TUG is a CAPN10 substrate. Proteolysis of TUG by calpains was assessed using a cell-free system containing calpain-1 and TUG. In situ proteolysis of TUG by calpains was demonstrated in 3T3-L1 adipocytes in the presence of insulin or calpain inhibitors to modulate calpain activity. Proteolysis of TUG by CAPN10 was confirmed using transient or stable silencing of CAPN10 in 3T3-L1 adipocytes. Calpains proteolyzed the C-terminus of TUG in vitro. In adipocytes, insulin-induced cleavage of TUG was correlated with the activation of calpains. Treatment with calpain inhibitors reduced TUG cleavage, resulting in impaired GLUT4 translocation without altering Akt phosphorylation. Furthermore, CAPN10 but not calpain-1 or calpain-2 colocalized with GLUT4 in the absence of insulin, and their colocalization was reduced after stimulation with insulin. Finally, we demonstrated that CAPN10 knockdown reduced the proteolysis of TUG without altering the phosphorylation of Akt or the expression of the Usp25m protease. Thus, our results provide evidence that the TUG protein is cleaved by CAPN10 to regulate GLUT4 translocation.
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Miller, John A., Domenica E. Drouet, Leonid M. Yermakov, Mahmoud S. Elbasiouny, Fatima Z. Bensabeur, Michael Bottomley, and Keiichiro Susuki. "Distinct Changes in Calpain and Calpastatin during PNS Myelination and Demyelination in Rodent Models." International Journal of Molecular Sciences 23, no. 23 (December 6, 2022): 15443. http://dx.doi.org/10.3390/ijms232315443.

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Myelin forming around axons provides electrical insulation and ensures rapid and efficient transmission of electrical impulses. Disruptions to myelinated nerves often result in nerve conduction failure along with neurological symptoms and long-term disability. In the central nervous system, calpains, a family of calcium dependent cysteine proteases, have been shown to have a role in developmental myelination and in demyelinating diseases. The roles of calpains in myelination and demyelination in the peripheral nervous system remain unclear. Here, we show a transient increase of activated CAPN1, a major calpain isoform, in postnatal rat sciatic nerves when myelin is actively formed. Expression of the endogenous calpain inhibitor, calpastatin, showed a steady decrease throughout the period of peripheral nerve development. In the sciatic nerves of Trembler-J mice characterized by dysmyelination, expression levels of CAPN1 and calpastatin and calpain activity were significantly increased. In lysolecithin-induced acute demyelination in adult rat sciatic nerves, we show an increase of CAPN1 and decrease of calpastatin expression. These changes in the calpain-calpastatin system are distinct from those during central nervous system development or in acute axonal degeneration in peripheral nerves. Our results suggest that the calpain-calpastatin system has putative roles in myelination and demyelinating diseases of peripheral nerves.
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Weber, Jonasz J., Eva Haas, Yacine Maringer, Stefan Hauser, Nicolas L. P. Casadei, Athar H. Chishti, Olaf Riess, and Jeannette Hübener-Schmid. "Calpain-1 ablation partially rescues disease-associated hallmarks in models of Machado-Joseph disease." Human Molecular Genetics 29, no. 6 (January 21, 2020): 892–906. http://dx.doi.org/10.1093/hmg/ddaa010.

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Abstract Proteolytic fragmentation of polyglutamine-expanded ataxin-3 is a concomitant and modifier of the molecular pathogenesis of Machado–Joseph disease (MJD), the most common autosomal dominant cerebellar ataxia. Calpains, a group of calcium-dependent cysteine proteases, are important mediators of ataxin-3 cleavage and implicated in multiple neurodegenerative conditions. Pharmacologic and genetic approaches lowering calpain activity showed beneficial effects on molecular and behavioural disease characteristics in MJD model organisms. However, specifically targeting one of the calpain isoforms by genetic means has not yet been evaluated as a potential therapeutic strategy. In our study, we tested whether calpains are overactivated in the MJD context and if reduction or ablation of calpain-1 expression ameliorates the disease-associated phenotype in MJD cells and mice. In all analysed MJD models, we detected an elevated calpain activity at baseline. Lowering or removal of calpain-1 in cells or mice counteracted calpain system overactivation and led to reduced cleavage of ataxin-3 without affecting its aggregation. Moreover, calpain-1 knockout in YAC84Q mice alleviated excessive fragmentation of important synaptic proteins. Despite worsening some motor characteristics, YAC84Q mice showed a rescue of body weight loss and extended survival upon calpain-1 knockout. Together, our findings emphasize the general potential of calpains as a therapeutic target in MJD and other neurodegenerative diseases.
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Mellgren, Ronald L., and Xinhua Huang. "Fetuin A Stabilizes m-Calpain and Facilitates Plasma Membrane Repair." Journal of Biological Chemistry 282, no. 49 (October 17, 2007): 35868–77. http://dx.doi.org/10.1074/jbc.m706929200.

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Yeast two-hybrid experiments identified α2-Heremans-Schmid glycoprotein (human fetuin A) as a binding partner for calpain domain III (DIII). The tandem DIIIs of calpain-10 interacted under the most selective culture conditions, but DIIIs of m-calpain, calpain-3, and calpain-5 also interacted under less stringent selection. DIIIs of μ-calpain, calpain-6, and the tandem DIII-like domains of the Dictyostelium Cpl protein did not interact with α2-Heremans-Schmid glycoprotein in the yeast two-hybrid system. Bovine fetuin A stabilized proteolytic activity of purified m-calpain incubated in the presence of mm calcium chloride and prevented calcium-dependent m-calpain aggregation. Consistent with the yeast two-hybrid studies, fetuin A neither stabilized μ-calpain nor prevented its aggregation. Confocal immunofluorescence microscopy of scratch-damaged L6 myotubes demonstrated accumulation of m-calpain at the wound site in association with the membrane repair protein, dysferlin. m-Calpain also co-localized with fluorescein-labeled fetuin A at the wound site. The effect of fetuin A on calpain-mediated plasma membrane resealing was investigated using fibroblasts from Capns1-/- and Capns1+/+ mouse embryos. Capns1 encodes the small noncatalytic subunit that is required for the proteolytic function of m- and μ-calpains. Thus, Capns1-/- fibroblasts do not express these calpains in active form. Fetuin A increased resealing of scrape-damaged wild-type fibroblasts but not Capns1-/- fibroblasts. These studies identify fetuin A as a potential extracellular regulator of m-calpain at nascent sites of plasma membrane wounding.
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Bevers, Matthew B., and Robert W. Neumar. "Mechanistic Role of Calpains in Postischemic Neurodegeneration." Journal of Cerebral Blood Flow & Metabolism 28, no. 4 (December 12, 2007): 655–73. http://dx.doi.org/10.1038/sj.jcbfm.9600595.

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The calpain family of proteases is causally linked to postischemic neurodegeneration. However, the precise mechanisms by which calpains contribute to postischemic neuronal death have not been fully elucidated. This review outlines the key features of the calpain system, and the evidence for its causal role in postischemic neuronal pathology. Furthermore, the consequences of specific calpain substrate cleavage at various subcellular locations are explored. Calpain substrates within synapses, plasma membrane, endoplasmic reticulum, lysosomes, mitochondria, and the nucleus, as well as the overall effect of postischemic calpain activity on calcium regulation and cell death signaling are considered. Finally, potential pathways for calpain-mediated neurodegeneration are outlined in an effort to guide future studies aimed at understanding the downstream pathology of postischemic calpain activity and identifying optimal therapeutic strategies.
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Dissertations / Theses on the topic "Calpain system"

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Janardhanan, Anitha C. "Gene expression of components of the calpain system m-calpain, [mu]-calpain and calpastatin in male and female broiler skeletal muscle /." Morgantown, W. Va. : [West Virginia University Libraries], 1999. http://etd.wvu.edu/templates/showETD.cfm?recnum=895.

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Thesis (M.S.)--West Virginia University, 1999.
Title from document title page. Document formatted into pages; contains vii, 93 p. : ill. (some col.) Includes abstract. Includes bibliographical references (p. 72-80).
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Drouet, Saltos Domenica Elizabeth. "Calpain-Calpastatin System in Peripheral Nerve Myelination and Demyelination." Wright State University / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=wright1559220437439116.

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Jones, Simon W. "Fibre-type specific expression of the calpain proteolytic system in skeletal muscle." Thesis, University of Nottingham, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.312237.

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Delgado, Eduardo Francisquine. "The calpain system and postmortem tenderization in ovine meat from callipyge and normal phenotypes." Diss., The University of Arizona, 1998. http://hdl.handle.net/10150/288910.

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In an attempt to further our understanding of the relationship between the calpain system and postmortem tenderization, three muscles [biceps femoris (BF), infraspinatus (IS), and longissimus (LD)] from normal (N = 6) and callipyge (N = 6) sheep were studied. Callipyge is a genetic phenomenon where carriers of the callipyge gene present a hypertrophy of pelvic and torso muscles, such that BF and LD are affected while IS is not. It has been observed characteristically that calpastatin and m-calpain activities are increased in muscles of animals affected by the callipyge phenotype. Soluble calpain and calpastatin, and myofibril-bound μ-calpain activities, and myofibrillar fragmentation index (MFI) were determined at death, 1d, 3d and 10d postmortem. Sarcomere length was determined at 1d and 10d postmortem. Shear force of the longissimus muscle was determined at 1d, 3d and 10d postmortem. Western blots for calpastatin, μ-calpain, desmin, nebulin, titin, troponin-T and α-actinin were performed to follow the degradation pattern of those proteins. The calpastatin and m-calpain activities were more than two-fold greater in BF and LD muscles from callipyge than in the same muscles from normal animals. Calpastatin activities in infraspinatus muscle from normal animals were higher than in the other two muscles of this phenotype. Soluble μ-calpain activities were higher at death for normal phenotype in BF and IS muscles and it decreased rapidly during postmortem storage. However, the rate of this decrease in that activity was faster in normal than in callipyge phenotype. Myofibrils contained calcium dependent protease activity and this activity was inhibited by cysteine proteases inhibitors and by calpastatin to some degree. There was no difference in the myofibril-calcium dependent protease activity between phenotypes at any time postmortem, presenting lower activity at death. The magnitude of protein degradation and tenderization were assessed by MFI and shear force, respectively. Neither the MFI nor shear force changed appreciably during storage of the callipyge affected muscles. Calpastatin level seems to determine the rate of postmortem tenderization.
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Cataldo, Francesca. "Role of calpain in USP1 stability regulation and genome integrity maintenance." Doctoral thesis, Università degli studi di Trieste, 2012. http://hdl.handle.net/10077/7860.

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2010/2011
The calpains are a family of intracellular cysteine proteases, among which the best studied isoforms, micro- (CAPN1) and milli-calpain (CAPN2), are heterodimers consisting of a catalytic subunit and a common regulatory subunit, CAPNS1, required for function. Calpain is involved in many processes important for cancer biology, such as autophagy, indeed in calpain-depleted cells autophagy is impaired, with a subsequent increase in apoptosis sensitivity. Calpain is also important in all the stages of the stress response. A proteomic approach was employed for the identification of novel CAPNS1 interacting proteins. Proteins immunoprecipitating with endogenous CAPNS1 in HT1080 cell lysates were analyzed by Mass Spectrometry. We identified novel partners among which the deubiquitinating enzyme USP1, a key regulator of the DNA damage response and genome integrity maintenance via its specific action on FANCD2, involved in DNA repair and protection from chromosome instability, and PCNA, involved in the regulation of translesion DNA synthesis (TLS), that bypasses DNA lesions with low stringency basepairing requirements. We performed co-IP assays in lysates of 293T cells and confirmed that the interaction was specific. Furhermore, we observed that calpain is able to bind a USP1 C-terminal deleted mutant, suggesting that USP1 first 523 aminoacids were sufficient for the binding. To understand what is the effect exerted by calpain upon USP1, we depleted calpain activity in a series of cell lines, and followed the fate of endogenous USP1. We transfected CAPNS1 specific siRNAs, or treated cells with a specific inhibitor of calpain, and we observed a strong decrease in USP1 protein levels. This effect should be at a post-transcriptional level, since any significant change in USP1 mRNA levels is detected. We also obtained the same result by transfecting a siRNA specific for CAPN1, the gene encoding for the catalytic subunit micro-calpain. Moreover, we studied the role of calpain in the PCNA-mediated switch between high fidelity replication and TLS upon UV irradiation. In mouse embryonic fibroblasts knockout for CAPNS1, USP1 downregulation is coupled to an increase in PCNA monoubiquitination. Moreover, CAPNS1-depleted U2OS cells showed an increase in the percentage of nuclei containing PCNA-induced foci upon UV irradiation. Since we demonstrated that calpain can modulate an important regulator of DNA damage response such as USP1, we investigated if calpain could have a role in genome integrity maintenance. CAPNS1 depleted cells showed a reduced rescue in DNA repair compared to control cells, suggesting that increased levels in PCNA monoubiquitination could lead to an increased amount of errore-prone TLS. Calpain plays an important role in autophagy, so we asked if USP1 degradation in absence of calpain activity could involve autophagic pathways. We first blocked macroautophagy by silencing ATG5, and we observed that USP1 was downregulated, suggesting that the depletion of ATG5 could lead to an increased activity of other degradation pathways. To impaire chaperone-mediated autophagy (CMA), we silenced a protein important for autophagosome formation, LAMP-2A. Also in this case we observed a decrease in USP1 protein levels, thus suggesting that USP1 is alternatively degraded by different pathways. However, we observed that USP1 is stabilized upon inhibition of lysosomal enzymes, suggesting that USP1 may be degraded in the lysosome. To better understand the mechanism by which calpain affect USP1 stability we search for an effect of calpain upon USP1 co-factor and activator UAF1/WDR48. CAPNS1-depleted cells showed WDR48 downregulation, but WDR48 overexpression only partially rescue USP1 protein levels in this cells. Furthermore, we provided evidences that calpain regulation of p35/p25 activator of Cdk5 can affect Cdh1 phosphorylation and thus APC/Cdh1 activity, leading to a regulation of USP1 stabilization. In conclusion, we identified USP1 as a novel interactor of calpain, and we found that calpain is important for USP1 stability, since in its absence USP1 is downregulated. The importance of this novel regulation is strengthened by the recent findings that unveiled a role of USP1 in maintenance of a mesenchymal stem cell program in osteosarcoma, and thus placing calpain in a crucial regulatory position for cancer development.
XXIV Ciclo
1983
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Li, Liang. "The role of calpain-calpastatin system in in the SOD1G93A mouse model of amyotrophic lateral sclerosis." Thesis, University of Brighton, 2009. https://research.brighton.ac.uk/en/studentTheses/e0f03b52-5ddc-42cc-b769-ccde3e69e709.

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Amini, Mandana. "Analysis of Conditional Knock-out of Calpain Small Subunit, capns1, in Central Nervous System Development and Function." Thesis, Université d'Ottawa / University of Ottawa, 2014. http://hdl.handle.net/10393/31360.

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Calpains, a highly conserved family of calcium-dependent cysteine proteases, are divided in two groups; classical and non-conventional calpains. Calpain-1 and calpain-2, the classical ones, are ubiquitously expressed and abundant in the CNS. Findings through different experimental approaches, predominantly pharmacological calpain inhibitors, proposed the necessity of the proteases for the modulation of various biological events particularly in the CNS, or a functional link between calpain and neurodegeneration. Significant functions associated with calpain activity are neuronal proliferation/differentiation, signal transduction, apoptosis, and synaptic plasticity; or neuronal death in Alzheimer’s disease, Huntington’s disease, Parkinson’s disease, and ischemic stroke. However, due to limited insights of the approaches taken, such as non-specificity of the inhibitors, the exact roles of calpains in the CNS and the key mechanisms underlying them remain controversial. Calpain-1/calpain-2 germline knock-out are embryonic lethal at a very early stage hindering the use of these lines as mouse models for CNS studies. Accordingly, this thesis research introduced a unique brain-specific calpain-1/calpain-2 knock-out and explored the role of the proteases in brain development/function and in neuronal death. The first set of analyses examined how the elimination of calpain-1/calpain-2 activities in mouse brain impacts CNS development in general and synaptic plasticity in CA1 neurons of hippocampus. CNS-specific elimination of CAPNS1, the common small subunit, abolished calpain-1/calpain-2 activities in mouse brain. In contrast to Calpain-1/calpain-2 germ line knock-outs, the brain-specific knock-outs are viable and the general development of mouse brain is normal. However, morphology of dendrites in pyramidal neurons of the hippocampal CA1 region showed significantly decreased dendritic branching complexity and spine density. Consistent with dendrite morphological abnormalities, electrophysiological analyses revealed a significant decrease in field excitatory postsynaptic potentials, long term potentiation, and learning and memory in the hippocampal CA1 neurons of the mutants. In the second part of this research we investigated the direct role of the calpains in neuronal death and their potential downstream targets in in vitro models of PD and ischemic stroke. Our findings indicated that ablation of calpains activity improves survival of different types of neurons against mitochondrial toxin 1-methyl-4-phenylpyridinium (MPP+), glutamate, and hypoxia. Importantly, we demonstrated an increase in p35-cleavage to p25, a cyclin dependent kinase 5 (Cdk5) activator, and that restoration of p25 significantly suppresses the neuronal survival associated with calpain deficiency. Taken together, this work unequivocally establishes two central roles of calpain-1/calpain-2 in CNS function in plasticity and neuronal death.
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Kloock, Simon Johannes [Verfasser]. "Einfluss von VDAC1 auf das Calpain-System als mögliche therapeutische Option für Morbus Huntington / Simon Johannes Kloock." Tübingen : Universitätsbibliothek Tübingen, 2020. http://d-nb.info/1224882385/34.

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Howard, Benjamin. "Effects of Implanting Strategy and Zilpaterol Hydrochloride on the Calpain Proteolytic System in Sectioned Beef Steaks for Two Time Periods." Thesis, North Dakota State University, 2016. https://hdl.handle.net/10365/28128.

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The objective of this study was to evaluate the impact of an anabolic implant and its use with the beta-adrenergic agonist zilpaterol hydrochloride (ZH) the calpain proteolytic system activity across specific areas of the beef strip steak over two aging days. Crossbred heifers were blocked by weight and randomly assigned to one of three treatments: 1) no implant or ZH (CON), 2) implant, no ZH (IMP), and 3) implant and ZH (IMP+ZH). At slaughter, strip steaks were collected and aged for 3 and 14 d. Samples were evaluated for Minolta objective color scores, pH, bioelectrical impedance analysis, and were then cut into lateral, lateral/medial, and medial sections. Protein was extracted from each section, and the calpain proteolytic system was evaluated. A day of aging effect was seen in protein degradation, along with a treatment by section interaction proteolytic activity. No differences were found in pH or color by treatment.
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Lee, Hannah Yun Young. "Calcium homeostasis in lens transparency and the involmement of calpains in cataract." Lincoln University, 2006. http://hdl.handle.net/10182/1897.

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The absolute clarity of the lens of the eye is vital in the visual system. The unique structural and physiological properties of the lens are tightly integrated with highly ordered protein content to allow the lens to remain transparent. Consequently, any alteration or disturbance of these highly ordered proteins can affect the optical properties of the lens. In humans, cataracts are the major cause of blindness, yet the exact aetiology of cataract formation (cataractogenesis) is not fully understood. The purpose of the current research was to investigate whether deregulation of the Ca²⁺-dependent enzyme, calpains, following changes in lens Ca²⁺ homeostasis, is a key mechanism leading to undesired cleavage of a number of proteins that are linked with maintaining lens transparency and contributing to cataractogenesis. An ovine lens culture (in vitro) system and the heritable ovine cataract (in vivo) model were used to test the research hypothesis. The Ca²⁺ ionophore, ionomycin, was used to induce a Ca²⁺ overload and in vitro opacification during lens culture. Opacity in the lens was graded by a computer image analysis program. Protein profile (SDS-PAGE, 2-DE and Western detection), calpain activity (casein zymography), lens structure (microscopic view) and cytotoxicity level (LDH leakage assay) were analysed in Ca²⁺-induced opaque lenses. The involvement of calpain during opacification was further examined by applying synthetic exogenous calpain inhibitors to the in vitro system. Two novel exogenous calpain inhibitors were also assessed for their therapeutic potential in preventing the progression of cataracts in the in vivo cataract model by topical administration of the inhibitor direct to the sheep's eye over a 11 week period. HPLC was used to detect the penetration of these compounds into ocular tissues. Sustained Ca²⁺ influx into cultured lenses caused dense opacification. The opacity was characterised by formation of a turbid fraction and cell death in the outer cortex of the ovine lens. There was increased calpain autolysis associated with the progress of opacification, indicating increased calpain activity. Major degradation of the cytoskeletal proteins, spectrin and vimentin, was observed whilst there was limited degradation of the lens structural soluble proteins, crystallins, in response to a Ca²⁺ flux. Lens proteins were protected from degradation by adding synthetic calpain inhibitors to the culture medium. Topical administration of novel anti-calpain molecules failed to retard the progression of cataractogenesis in the ovine inherited cataract model. Further investigation of drug penetration showed that efficacy of inhibitory compounds was limited by permeability of these molecules across the cornea and the ability of the molecules to reach and penetrate into the lens. The ovine lens Ca²⁺-induced opacification (OLCO) model in this thesis has provided a model to understand the role of Ca²⁺ homeostasis in lens transparency. With sustained intracellular Ca²⁺ level, the degradation of cytoskeletal elements is highly correlated with calpain activity. Cataractogenesis is the pathological response to the loss of lens Ca²⁺ homeostasis in this model. The current results support the hypothesis that the deregulation of calpain activity is a trigger for a series of cascading events, leading to death of the cells in the lens.
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Books on the topic "Calpain system"

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Purintrapiban, Juntipa. Coordination of protease systems on muscle protein degradation and identification of calpain substrates using the yeast two-hybrid system. 1999.

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Book chapters on the topic "Calpain system"

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Samanta, Krishna, Pulak Kar, Tapati Chakraborti, and Sajal Chakraborti. "An Overview of Endoplasmic Reticulum Calpain System." In Proteases in Health and Disease, 3–19. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-9233-7_1.

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Murachi, Takashi, Toshio Murakami, Michiko Ueda, Ichiro Fukui, Takao Hamakubo, Yoshifumi Adachi, and Masakazu Hatanaka. "The Calpain-Calpastatin System in Hematopoietic Cells." In Calcium Protein Signaling, 445–54. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5679-0_47.

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Witkowski, Jacek M., Anna Mikosik, Ewa Bryl, and Tamas Fulop. "Calpain-Calpastatin System in Lymphoid Neoplasm of the Aged." In Geriatric Oncology, 1–12. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-44870-1_70-1.

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Witkowski, Jacek M., Anna Mikosik, Ewa Bryl, and Tamas Fulop. "Calpain-Calpastatin System in Lymphoid Neoplasm of the Aged." In Geriatric Oncology, 129–40. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-319-57415-8_70.

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Ashraf, Javaria, Jamil Ahmad, and Zaheer Ul-Haq. "Deciphering the Role of PKC in Calpain-CAST System Through Formal Modeling Approach." In Bioinformatics and Biomedical Engineering, 60–71. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-17938-0_6.

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Ray, S. K., M. K. Guyton, E. A. Sribnick, and N. L. Banik. "Calpain as a Target for Prevention of Neuronal Death in Injuries and Diseases of the Central Nervous System." In Handbook of Neurochemistry and Molecular Neurobiology, 445–67. Boston, MA: Springer US, 2007. http://dx.doi.org/10.1007/978-0-387-30379-6_15.

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Liang, Zhe, and Hilde-Gunn Opsahl-Sorteberg. "Use of the β-Glucuronidase (GUS) Reporter System to Localize Promoter Activities of the Endogenous Plant Calpain DEFECTIVE KERNEL1 (DEK1)." In Methods in Molecular Biology, 103–8. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8988-1_9.

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Parameswaran, Sreejit, Sujeet Kumar, and Rajendra K. Sharma. "Role of Calpains in Calmodulin Regulated Systems." In Proteases in Health and Disease, 33–48. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-9233-7_3.

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Luo, Y., D. F. Sellitti, and K. Suzuki. "The Calpain Proteolytic System." In Encyclopedia of Cell Biology, 670–80. Elsevier, 2016. http://dx.doi.org/10.1016/b978-0-12-394447-4.10075-6.

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Baudry, Michel, Wenyue Su, and Xiaoning Bi. "The Calpain Proteolytic System." In Reference Module in Life Sciences. Elsevier, 2022. http://dx.doi.org/10.1016/b978-0-12-821618-7.00223-6.

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Conference papers on the topic "Calpain system"

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Kajiwara, Y., M. Sakon, T. Tsujinaka, J. Kambayashi, T. Mori, and T. Murachi. "STUDIES ON ROLE OF CALPAIN IN PLATELET REACTION, UTILIZING NEWLY SYNTHETIZED PEPTIDE ANTAGONISTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642823.

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The system of calpain (Ca2+-activated protease) and its inhibitor calpastatin in platelets have been well characterized in our laboratory but the role of the system has not been fully elucidated yet, though various endogenous substrates have been identified. Employing SH inhibitors as calpain antagonists, We have proposed a possible role of platelet calpain in myosin light chain (20K) phosphorylation (Biochem.Int. 6,767,1986) but more specific calpain antagonists were required to draw conclusion. Recentry, series of peptide calpain antagonists(PCAs) were syn-thetized such as Ac-Leu-Leu-Nle.al(PCA-I), Ac-Leu-Leu-Met.al(PCA-II) and Leu-Leu-Phe.CH2Cl(PCA-III)(J.Biochem.99,173,1986) and attempts were made to apply them to platelet reaction. ID50 of PCAs against platelet calpain I was as follows; PCA-I:0.04uM,PCA-II:0.luM and PCA-III:0.4uM. Thus, these antagonists were 1000 times more potent than N-ethylmaleimide(NEM), and they did not inhibit Mg2+-ATPase activity of platelet myosin B in contrast to NEM. When PCAs were applied to intact platelets, no effect was obtained against stimulus-linked proteolysis of ABP(aotin binding protein) and P235, indicating poor permeability of the antagonists across the plasma membrane. Thereby PCA was applied to lysed platelets or to permeabilized platelets. Lysed platelets suspension with 2mM EGTA, 2mM EDTA was incubated at 37 C with 32P -ATP,2mM MgCl2, 3mM CaCl2 in the presence or absence of PCA-II and proteolysis of. ABP,P235 and phosphorylation of 20K,47K were studied. The proteolysis and phosphorylation were inhibited by PCA-II in a dose-related manner. Then, PCA-II was applied to permeabilized platelet prepared by a high voltage electric charge to which acriflavine was loaded. PCA-II inhibited Ca2+ stimulated proteolysis and phosphsrylation of the permeabilized platelets likewise but no effect was obtained on Ca2+ stimulated acriflavine secretion from dense granules. These observations indicated that the proteolysis and protein phosphorylation are mediated by calpain but that these phenomena may not be related to secretory process.
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verhallen, P. F. J., E. M. Bevers, P. Comfurius, W. M. A. Linkskens, and R. F. A. Zwaal. "CALPAIN-MEDIATED CYTOSKELETAL DEGRADATION CORRELATES WITH STIMULATION OF PLATELET PROCOAGULANT ACTIVITY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642821.

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We have shown earlier that the negatively charged phospholipid phosphatidylserine (PS), which becomes translocated from the inner surface to the outer surface of the plasma membrane upon platelet activation, is responsible for platelet procoagulant activity. Studies with erythrocytes have suggested a role for cytoskeletal proteins in the regulation of transmembrane asymmetry of PS. The possibility that platelet cytoskeletal proteins are involved in the loss of transmembrane asymmetry of PS, was explored by correlative investigations of both platelet prooagulant activity and activity of calpain, an endogenous Ca 2+ -dependent thiol-protease, known to hydrolyze major cytoskeletal proteins (e.g.: filamin, talin, myosin). Platelet procoagulant activity was assayed by determination of the prothrombinase activity under conditions at which the catalytic PS-surface was rate-limiting. Calpain-activity was monitored by the appearance of known degradation products of major cytoskeletal proteins. The following results were obtained: (1) The ability of thrombin, collagen, collagen & thrombin, or the Ca -ionophore A23187 to stimulate platelet procoagulant activity closely correlated with their ability to stimulate platelet calpain-activity (2). Generation of platelet procoagulant activity upon platelet stimulation by collagen & thrombin or by A23187 exhibited a time course identical to the development of calpain-activity. In addition, the local anesthetics dibucaine and tetracaine, shown to gradually stimulate calpain activity, were able to generate platelet procoagulant activity with a similar time course. (3) Using a Ca2+ buffering system and A23187 to equilibrate intracellular- and extracellular free Ca2+ , it was found that the Ca2+ -response relationship of both platelet calpain- and pro-coagulant-activity was identical. From these findings we conclude that the degradation of cytoskeletal proteins destroys their putative interactions with PS, enabling this lipid to participate in transbilayer movement, leading to the formation of a procoagulant outer surface of the platelet.
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duVERLE, DAVID, ICHIGAKU TAKIGAWA, YASUKO ONO, HIROYUKI SORIMACHI, and HIROSHI MAMITSUKA. "CaMPDB: A RESOURCE FOR CALPAIN AND MODULATORY PROTEOLYSIS." In Proceedings of the 9th Annual International Workshop on Bioinformatics and Systems Biology (IBSB 2009). IMPERIAL COLLEGE PRESS, 2010. http://dx.doi.org/10.1142/9781848165786_0017.

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Verhaagen, Don, Katie Hausman, and Emily Saopraseuth. "Calpine Improves Accuracy of Steam Flow Measurement With Top-Mounted Annubar Flowmeter." In ASME 2013 Power Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/power2013-98176.

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Getting steam out of the ground is the first crucial step in the conversion of geothermal steam into electricity. Getting it to the turbine and making the steam flow measurement is likewise important. It is at the turbine or, more precisely, just before the turbine, that many measurements are made. Performance Acceptance Tests (PAT’s) are conducted here to ensure that the equipment provided by the turbine manufacturer is performing as specified. The need for accurate steam flow measurement is critical on the main steam line (MSL). Historically, orifice plates, venturies and averaging pitot tubes have been used with greater or lesser success and with associated challenges. Orifice plates typically have high permanent pressure losses and averaging pitot tubes have small holes on their leading edge which can plug. A different solution is needed — one that provides an accurate and repeatable measurement with low maintenance requirements. In recent testing spanning over a year of operation, it was found that an Annubar™ flowmeter, installed in the top mounted position, provided the low permanent pressure loss, and met the accuracy, repeatability and maintenance requirements of the end user. Typically, in steam applications with Annubar primary elements, conventional wisdom dictates that the Annubar primary element and transmitter be positioned below the pipe. The previously recommended orientation has a number of issues particularly with geothermal steam and its constituents (silica scale, non-condensable gases,) plus the likelihood that pockets of condensate will form and lead to metallurgical issues including stress corrosion cracking, thus shortening the life of the primary element. The installation can be further enhanced with an automated nitrogen purge system that blows nitrogen through the Annubar primary element to ensure the ports remain clear. The MSL flow measurement is critical for regulatory compliance and performance monitoring. Knowing with precision and repeatability the volumetric steam flow rate is critical. The top-mounted Annubar flowmeter with nitrogen purge system, which has been in service for more than a year, has proven to be reliable and has provided precise, repeatable measurement of steam flow.
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