Relevant bibliographies by topics / Proteolysis

Academic literature on the topic 'Proteolysis'

Author: Grafiati
Published: 4 June 2021
Last updated: 9 March 2023

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Journal articles on the topic "Proteolysis"

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Navegantes, Luiz Carlos C., Neusa M. Z. Resano, Renato H. Migliorini, and Isis C. Kettelhut. "Effect of guanethidine-induced adrenergic blockade on the different proteolytic systems in rat skeletal muscle." American Journal of Physiology-Endocrinology and Metabolism 277, no. 5 (November 1, 1999): E883—E889. http://dx.doi.org/10.1152/ajpendo.1999.277.5.e883.

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Overall proteolysis and the activity of skeletal muscle proteolytic systems were investigated in rats submitted to guanethidine-induced adrenergic blockade for 4 days. In soleus, overall proteolysis increased by 15–20% during the first 2 days of guanethidine treatment but decreased to levels below control values after 4 days. Extensor digitorum longus (EDL) did not show the initial increase in total proteolysis, which was already reduced after 2 days of guanethidine treatment. The initial rise in the rate of protein degradation in soleus was accompanied by an increased activity of the Ca2+-dependent proteolytic pathway. In both soleus and EDL, the reduction in overall proteolysis was paralleled by decreased activities of the Ca2+-dependent and ATP-dependent proteolytic processes. No change was observed in the activity of the lysosomal proteolytic system. Overall proteolysis in soleus and EDL from nontreated rats was partially inhibited by isoproterenol, in vitro. The data suggest an acute inhibitory control of skeletal muscle proteolysis by the adrenergic system, well evident in the oxidative muscle, with an important participation of the Ca2+-dependent pathway.
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Navegantes, Luiz Carlos C., Neusa M. Z. Resano, Renato H. Migliorini, and Ísis C. Kettelhut. "Catecholamines inhibit Ca2+-dependent proteolysis in rat skeletal muscle through β2-adrenoceptors and cAMP." American Journal of Physiology-Endocrinology and Metabolism 281, no. 3 (September 1, 2001): E449—E454. http://dx.doi.org/10.1152/ajpendo.2001.281.3.e449.

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Overall proteolysis and the activity of skeletal muscle proteolytic systems were investigated in rats 1, 2, or 4 days after adrenodemedullation. Adrenodemedullation reduced plasma epinephrine by 95% and norepinephrine by 35% but did not affect muscle norepinephrine content. In soleus and extensor digitorum longus (EDL) muscles, rates of overall proteolysis increased by 15–20% by 2 days after surgery but returned to normal levels after 4 days. The rise in rates of protein degradation was accompanied by an increased activity of Ca2+-dependent proteolysis in both muscles, with no significant change in the activity of lysosomal and ATP-dependent proteolytic systems. In vitro rates of Ca2+-dependent proteolysis in soleus and EDL from normal rats decreased by ∼35% in the presence of either 10−5 M clenbuterol, a β2-adrenergic agonist, or epinephrine or norepinephrine. In the presence of dibutyryl cAMP, proteolysis was reduced by 62% in soleus and 34% in EDL. The data suggest that catecholamines secreted by the adrenal medulla exert an inhibitory control of Ca2+-dependent proteolysis in rat skeletal muscle, mediated by β2-adrenoceptors, with the participation of a cAMP-dependent pathway.
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LARBAUD, Daniel, Michèle BALAGE, Daniel TAILLANDIER, Lydie COMBARET, Jean GRIZARD, and Didier ATTAIX. "Differential regulation of the lysosomal, Ca2+-dependent and ubiquitin/proteasome-dependent proteolytic pathways in fast-twitch and slow-twitch rat muscle following hyperinsulinaemia." Clinical Science 101, no. 6 (October 26, 2001): 551–58. http://dx.doi.org/10.1042/cs1010551.

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In order to characterize the poorly defined mechanisms that account for the anti-proteolytic effects of insulin in skeletal muscle, we investigated in rats the effects of a 3h systemic euglycaemic hyperinsulinaemic clamp on lysosomal, Ca2+-dependent proteolysis, and on ubiquitin/proteasome-dependent proteolysis. Proteolysis was measured in incubated fast-twitch mixed-fibre extensor digitorum longus (EDL) and slow-twitch red-fibre soleus muscles harvested at the end of insulin infusion. Insulin inhibited proteolysis (P < 0.05) in both muscles. This anti-proteolytic effect disappeared in the presence of inhibitors of the lysosomal/Ca2+-dependent proteolytic pathways in the soleus, but not in the EDL, where only the proteasome inhibitor MG 132 (benzyloxycarbonyl-leucyl-leucyl-leucinal) was effective. Furthermore, insulin depressed ubiquitin mRNA levels in the mixed-fibre tibialis anterior, but not in the red-fibre diaphragm muscle, suggesting that insulin inhibits ubiquitin/proteasome-dependent proteolysis in mixed-fibre muscles only. However, depressed ubiquitin mRNA levels in such muscles were not associated with significant decreases in the amount of ubiquitin conjugates, or in mRNA levels or protein content for the 14kDa ubiquitin-conjugating enzyme E2 and 20S proteasome subunits. Thus alternative, as yet unidentified, mechanisms are likely to contribute to inhibit the ubiquitin/proteasome system in mixed-fibre muscles.
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Kominami, Yuri, Tatsuya Hayashi, Tetsuji Tokihiro, and Hideki Ushio. "A Novel Analysis of the Peptide Terminome Characterizes Dynamics of Proteolytic Regulation in Vertebrate Skeletal Muscle Under Severe Stress." Proteomes 7, no. 1 (February 13, 2019): 6. http://dx.doi.org/10.3390/proteomes7010006.

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In healthy cells, proteolysis is orderly executed to maintain basal homeostasis and normal physiology. Dyscontrol in proteolysis under severe stress condition induces cell death, but the dynamics of proteolytic regulation towards the critical phase remain unclear. Teleosts have been suggested an alternative model for the study of proteolysis under severe stress. In this study, horse mackerel (Trachurus japonicus) was used and exacerbated under severe stress conditions due to air exposure. Although the complete genome for T. japonicus is not available, a transcriptomic analysis was performed to construct a reference protein database, and the expression of 72 proteases were confirmed. Quantitative peptidomic analysis revealed that proteins related to glycolysis and muscle contraction systems were highly cleaved into peptides immediately under the severe stress. Novel analysis of the peptide terminome using a multiple linear regression model demonstrated profiles of proteolysis under severe stress. The results indicated a phase transition towards dyscontrol in proteolysis in T. japonicus skeletal muscle during air exposure. Our novel approach will aid in investigating the dynamics of proteolytic regulation in skeletal muscle of non-model vertebrates.
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Portbury, Andrea L., Monte S. Willis, and Cam Patterson. "Tearin' Up My Heart: Proteolysis in the Cardiac Sarcomere." Journal of Biological Chemistry 286, no. 12 (January 21, 2011): 9929–34. http://dx.doi.org/10.1074/jbc.r110.170571.

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Proteolysis within the cardiac sarcomere is a constantly evolving area of research. Three major pathways of proteolysis have been identified as being active within the cardiac sarcomere, namely the ubiquitin-proteasome system, autophagy, and the calpain system. The role of ubiquitin-proteasome system-mediated proteolysis in cardiovascular health and disease has been known for some time; however, it is now apparent that other proteolytic systems also aid in the stabilization of cardiac sarcomere structure and function. This minireview focuses on the individual as well as cooperative involvement of each of these three major pathways of proteolysis within the cardiac sarcomere.
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Sun, Z., W. Carpiaux, D. Fan, Y. Fan, R. Lakshminarayanan, and J. Moradian-Oldak. "Apatite Reduces Amelogenin Proteolysis by MMP-20 and KLK4 in vitro." Journal of Dental Research 89, no. 4 (February 16, 2010): 344–48. http://dx.doi.org/10.1177/0022034509360660.

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Two enamel proteases, matrix metalloproteinase-20 (MMP-20) and kallikrein 4 (KLK4), are known to cleave amelogenin and are necessary for proper enamel formation. However, the effect of hydroxyapatite (HAP) on the proteolytic activity of these enzymes remains unclear. To investigate whether apatite affects normal amelogenin proteolysis, we used 2 different isoforms of amelogenin combined with the appropriate enzymes to analyze proteolytic processing rates in the presence or absence of synthetic hydroxyapatite (HAP) crystals (N = 3). We found a distinct dose-dependent relationship between the amount of HAP present in the proteolysis mixture and the rate of rP172 degradation by rpMMP-20, whereas the effect of HAP on proteolysis of either rP172 or rP148 by rhKLK4 was less prominent.
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Picard, Catherine, Isabelle Plard, Dominique Rongdaux-Gaida, and Jean-Claude Collin. "Detection of proteolysis in raw milk stored at low temperature by an inhibition ELISA." Journal of Dairy Research 61, no. 3 (August 1994): 395–404. http://dx.doi.org/10.1017/s0022029900030818.

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SummaryAn inhibition ELISA (enzyme-linked immunosorbent assay) was developed for the determination of caseinomacropeptide (CMP) in order to estimate the proteolysis of κ-casein due to the enzymes of psychrotrophic bacteria in bulk raw milk. The CMP present in milk was quantified specifically by an antibody. The limit of detection was ∽ 0·1 μg/ml and the CV was < 10%. This method was used to study the proteolytic activity of three strains of psychrotrophic Pseudomonas fluorescens in raw milk and to analyse different raw milk samples supplied by four dairy plants. The proteolytic activity for different strains of psychrotrophs and for different milk samples varied considerably, but no correlation was established between the level of microbial flora and κ-casein proteolysis. It is thus not possible to determine the extent of proteolysis from the bacterial count alone. However, by CMP determination in bulk raw milk samples after 6 d storage at 4°C, the mean κ-casein proteolysis was ∽ 4%. Among the milk samples analysed that contained < 107 cfu psychrotrophs/ml, 30% exhibited a proteolysis of κ-casein < 0·5%, i.e. < 5μg CMP/ml.
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Solioz, M. "Role of proteolysis in copper homoeostasis." Biochemical Society Transactions 30, no. 4 (August 1, 2002): 688–91. http://dx.doi.org/10.1042/bst0300688.

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The cop operon of Enterococcus hirae controls cytoplasmic copper levels. It encodes two copper ATPases, a repressor, and the CopZ metallo-chaperone. Transcription of these genes is induced by copper. However, at higher copper concentrations, CopZ is degraded by a copper-activated proteolytic activity. This specific proteolysis of CopZ can also be demonstrated in vitro with E. hirae extracts. Growth of the cells in copper increases the copper-inducible proteolytic activity in extracts. Zymography reveals the presence of a copper-dependent protease in crude cell lysates. Copper-stimulated proteolysis of CopZ appears to play an important role in copper homoeostasis by E. hirae.
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Shang, F., and A. Taylor. "Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells." Biochemical Journal 307, no. 1 (April 1, 1995): 297–303. http://dx.doi.org/10.1042/bj3070297.

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Roles for ubiquitin (an 8.5 kDa polypeptide) involve its conjugation to proteins as a signal to initiate degradation and as a stress protein. We investigated ubiquitin conjugation and ubiquitin-dependent proteolytic activities in cultured bovine lens epithelial cells (BLECs) upon oxidative challenge. A 44% decrease in intracellular glutathione confirmed oxidative stress upon incubation with 1 mM H2O2. After 30 min incubation, endogenous high-molecular-mass ubiquitin conjugates decreased 73%, and intracellular proteolysis decreased about 50%. In the supernatants of the oxidatively treated BLECs, the ability to form high-molecular-mass ubiquitin conjugates with exogenous 125I-labelled ubiquitin decreased 28%, and ATP-dependent degradation of oxidized alpha-crystallin decreased 36%. When the H2O2-treated BLECs were allowed to recover for 60 min, intracellular proteolysis returned to the level of control cells. There was also a subsequent transient enhancement of intracellular proteolysis and a simultaneous recovery of endogenous high-molecular-mass ubiquitin conjugates. In parallel cell-free experiments, conjugating activity with exogenous 125I-labelled ubiquitin and ATP-dependent degradation of oxidized alpha-crystallin increased 35% and 72% respectively compared with non-oxidatively treated BLECs. ATP-independent proteolysis showed little response to exposure or removal of H2O2. These results indicate that (1) the rate of intracellular proteolysis in BLECs is associated with the level of endogenous high-molecular-mass ubiquitin conjugates and (2) oxidative stress may inactivate the ubiquitin conjugation activity with coordinate depression of proteolytic capability. Enhancement in ubiquitin conjugation and proteolytic activities during recovery from oxidative stress may be important in removal of damaged proteins and restoration of normal function of BLECs. The inactivation of ubiquitin-dependent proteolysis by oxidation may be involved in the accumulation of altered proteins and other adverse sequelae in the oxidatively challenged aging lens.
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Mitch, William E., James L. Bailey, Xiaonan Wang, Claudine Jurkovitz, David Newby, and S. Russ Price. "Evaluation of signals activating ubiquitin-proteasome proteolysis in a model of muscle wasting." American Journal of Physiology-Cell Physiology 276, no. 5 (May 1, 1999): C1132—C1138. http://dx.doi.org/10.1152/ajpcell.1999.276.5.c1132.

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The ubiquitin-proteasome proteolytic system is stimulated in conditions causing muscle atrophy. Signals initiating this response in these conditions are unknown, although glucocorticoids are required but insufficient to stimulate muscle proteolysis in starvation, acidosis, and sepsis. To identify signals that activate this system, we studied acutely diabetic rats that had metabolic acidosis and increased corticosterone production. Protein degradation was increased 52% ( P < 0.05), and mRNA levels encoding ubiquitin-proteasome system components, including the ubiquitin-conjugating enzyme E214k, were higher (transcription of the ubiquitin and proteasome subunit C3 genes in muscle was increased by nuclear run-off assay). In diabetic rats, prevention of acidemia by oral NaHCO3 did not eliminate muscle proteolysis. Adrenalectomy blocked accelerated proteolysis and the rise in pathway mRNAs; both responses were restored by administration of a physiological dose of glucocorticoids to adrenalectomized, diabetic rats. Finally, treating diabetic rats with insulin for ≥24 h reversed muscle proteolysis and returned pathway mRNAs to control levels. Thus acidification is not necessary for these responses, but glucocorticoids and a low insulin level in tandem activate the ubiquitin-proteasome proteolytic system.
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Dissertations / Theses on the topic "Proteolysis"

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El-Daher, Marie-Thérèse. "Huntingtin proteolysis and toxicity." Thesis, Paris 11, 2013. http://www.theses.fr/2013PA11T029/document.

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La maladie de Huntington (MH) est une maladie neurodégénérative héréditaire autosomique dominante. Elle est due à l’expansion anormale de polyglutamine dans la partie N-terminal de la protéine huntingtine (HTT). Une des étapes clés de la pathologie est le clivage de la HTT pleine longueur en fragments N-terminaux plus petits, contenant l’expansion de polyglutamine, et qui sont toxiques pour les neurones. En effet, les clivages de la HTT mutée génère des fragments N-terminaux (N-ter) de tailles comprises entre les acides aminés 1-105 et 1-586 observés dans des extraits de cerveaux de patients MH post-mortem et dont l’implication dans la mort neuronal est bien caractérisée. Mes travaux de thèse ont visé à modéliser le clivage de la HTT et à évaluer les conséquences sur la survie neuronale.Au cours de ma thèse, j’ai développé un outil permettant de contrôler le clivage de la HTT dans le temps et à des sites spécifiques. J’ai étudié le clivage de la HTT à deux sites stratégiques : les positions clivées par la caspase-6 et par la bléomycine hydrolase/cathepsine Z. A l’aide de cet outil, j’ai montré que le clivage de la HTT confère une toxicité cellulaire qui dépend du profil du clivage. Plus précisément, J’ai décrit une interaction intramoléculaire au sein des domaines de la HTT. Mes résultats indiquent que cette interaction protège les cellules de la toxicité induite par le clivage de la HTT mutée. En effet, les clivages successifs de la HTT annulent cette interaction, ce qui induit la libération des fragments N-ter mutants et provoque la mort cellulaire à l’issue de leur translocation nucléaire. Pour conclure, au cours de ma thèse, j’ai montré que la protéolyse successive de la HTT induit des processus cytotoxiques différents
Huntington’s disease (HD) is an autosomal dominant inherited neurodegenerative disorder caused by an abnormal polyglutamine (polyQ) expansion in the N-terminus of the protein huntingtin (HTT). A crucial step in HD pathogenesis is the cleavage of full-length HTT into smaller N-terminal (N-ter) fragments that contain the polyQ stretch and that are toxic to neurons. HTT cleavage generates short N-ter fragments whose amino-acid positions range from 1-105 to 1-586. These fragments are observed in HD post mortem brain samples and their participation in neuronal death in HD is well characterized. During my PhD research, I investigated the consequences of full-length mutant HTT proteolysis by developing a time and site-specific controlled system for HTT proteolysis. I have assessed HTT cleavage on two sites caspase-6 and cathepsin Z. My results show that HTT cleavage induces neurotoxicity in vitro as well as in vivo, toxicity which depends on HTT proteolysis pattern. Briefly, we described an intramolecular interaction within the HTT domains which is impaired upon successive proteolysis of HTT. We found that HTT intramolecular interaction buffer mutant N-ter HTT-induced toxicity. Moreover, specific cleavages of the mutant HTT generated toxic N-ter fragments as they translocate into the nucleus. To conclude, my PhD work has shown that additional cleavage of mutant HTT induces cytotoxicity by different mechanisms
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Clay, L. "CDC20 function, regulation and proteolysis." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.597750.

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The destruction of mitotic cyclins and other key regulators uses ubiquitin mediated proteolysis controlled via the activation of the ubiquitin ligase the Anaphase Promoting Complex/Cyclosome (APC/C), and its adaptor proteins Cdc20 and Cdh1. The spindle assembly checkpoint coordinates the APC/C with microtubule attachment and sets the timing from NEBD to anaphase. Cdc20 is inactivated by the spindle assembly checkpoint to prevent premature anaphase onset. Once the spindle assembly checkpoint is satisfied, Cdc20 can be released and activate the APC/C. However, cyclin A is degraded independently of the spindle assembly checkpoint before cyclin B1 and the anaphase inhibitor Securin. How Cdc20 can target different substrates for degradation at different times during mitosis is not yet clear. Using live-cell imaging and RNA interference and immunofluorescence techniques, I have studied the degradation of endogenous and ectopicly expressed APC/C substrates in cells with reduced Cdc20 levels. In this dissertation, I show that cyclin A degradation strongly depends on Cdc20, whereas cyclin B1 and Securin degradation do not. I identified the region of Cdc20 required for cyclin A binding and by mutating this site, I found that Cdc20 was no longer properly localised. I also show that Cdc20 proteolysis in human somatic cells does not require the KEN motif and gone on to find the motif required for Cdc20 degradation. I also show that the function of Cdc20 in the spindle assembly checkpoint can be influenced by the serine/threonine kinase Aurora A. Co-expression of a fluorescently tagged Cdc20 and Aurora A in human somatic cells causes an accelerated progression through mitosis and premature substrate degradation.
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Slee, Adrian. "Regulation of skeletal muscle proteolysis." Thesis, University of Nottingham, 2005. http://eprints.nottingham.ac.uk/13105/.

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Proteolysis is a component of protein turnover, controlled by multiple proteolytic systems. Alterations in system components within skeletal muscle has been associated with hypertrophy, remodelling, atrophy, apoptosis and metabolic dysregulation. Key components may have novel regulatory roles, e. g. calpain-3 and cathepsin-L. Experiments described within this thesis investigated the hypothesis that the gene expression of specific proteolytic system components within skeletal muscle may be co-ordinately regulated and altered during nutritional and pharmacological states known to modify protein turnover and induce muscle growth. Gene expression for multiple components of the calpain system was analysed in calf LD (Longissmus dorsi) by Quantitative Real-Time PCR in a plane of nutrition trial. There were three groups: low (LOW), high (HIGH) plane of nutrition and LOW to HIGH (REFED). Half of each group were slaughtered 48 hrs after refeeding, whilst the remainder were slaughtered 13 days later. Total RNA yield/g LD increased (P < 0.05) across all groups between slaughter dates. Calpain-3 expression increased in LOW and REFED and calpastatin in all groups between slaughter dates, with a trend towards significance (P = 0.073, P=0.085, respectively). In the 1St slaughter, calpain-3 expression had a trend to be lower in the LOW group and values for REFED were similar to HIGH value level. cDNA probes for unique and novel proteolytic system components were generated by RT-PCR and used to investigate the effects of acute and chronic Q-adrenergic stimulation, on the gene expression of those specific components in pig LD, by northern blotting. The ß2-adrenergic agonist clenbuterol (5 ppm) decreased glycogen levels (mg/g LD) (P < 0.001), increased cathepsin-L expression (P < 0.001) and increased E2G 1 values numerically within 24 hrs of treatment. Cathepsin-L was unchanged by adrenaline administration. Calpain-3 was unchanged with either clenbuterol or adrenaline treatment. The significance and implications of the data are discussed.
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Andréasson, Claes. "Ligand-activated proteolysis in nutrient signaling /." Stockholm, 2004. http://diss.kib.ki.se/2004/91-7140-075-3/.

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Hutton, David Alan. "Studies on mucin isolation and proteolysis." Thesis, University of Newcastle Upon Tyne, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.287272.

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Canning, Mary. "Ubiquitin-mediated proteolysis and Drosophila embryogenesis." Thesis, University of Edinburgh, 2000. http://hdl.handle.net/1842/13305.

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Ubiquitination provides a means of rapidly and irreversibly eliminating an unwanted protein from the cell, and is therefore a potentially effective tool for regulating cellular behaviour. Ubiquitin-mediated proteolysis is involved in such diverse physiological functions as growth control, cell signalling, differentiation and the immune response. The aim of this research has been to investigate its role in Drosophila embryogenesis. Protein ubiquitination is a stepwise process carried out by three classes of enzyme known as E1s, E2s and E3s. The E1 (ubiquitin-activating enzyme), generates a thiolester linkage with a ubiquitin cysteine residue. The activated ubiquitin is then transferred to an E2 (ubiquitin-conjugating enzyme) which, with the help of an E3 (ubiquitin-protein ligase), recruits the substrate protein which is to be degraded. I examined the embryonic expression patterns of several known and novel genes encoding each type of ubiquitinating enzyme. The E2 UbcD4 is transcribed during early to mid-embryogenesis in a variety of tissues, with specific germcell expression in stage 10 embryos. This suggested a possible role for UbcD4 in germ cell migration towards the somatic gonadal precursors. UbcD4 mRNA was also abundant in git and nervous system during germband retraction and dorsal closure. I screened for UbcD4 - interacting proteins using the yeast two-hybrid system, and identified several putative substrates for, as well as ancillary factors involved in, ubiquitination by UbcD4. These included a novel E3 of the Hect-domain family. In an attempt to examine the function of UbcD4 directly, I used RNA interference to disrupt UbcD4 function. The results suggest a post-germband retraction requirement for UbcD4.
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Smith, Kate L. "Tumour associated proteolysis and protein metabolism." Thesis, Aston University, 1992. http://publications.aston.ac.uk/12604/.

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The effect of cancer cachexia on protein metabolism has been studied in mice transplanted with the MAC16 adenocarcinoma. The progressive cachexia induced by the MAC16 tumour was characterised by a reduction in carcass nitrogen between 16-30% weight loss and a reciprocal increase in tumour nitrogen content. Carcass nitrogen loss was accompanied by a concomitant decrease in gastrocnemius muscle weight and nitrogen content and also by a decrease in liver nitrogen content. The loss of gastrocnemius muscle throughout the progression of cachexia was attributable to a 60% decrease in the rate of protein synthesis and a 240% increase in the rate of protein degradation. The loss of skeletal muscle protein that may be mediated by an increased rate of protein degradation has been correlated with a circulatory catabolic factor present only in cachectic tumour-bearing animals, that degrades host muscle in vitro. The proteolysis-inducing factor was found to be heat stable, not a serine protease and was inhibited by indomethacin and eicosapentaenoic acid (EPA) in a dose-related manner. The proteolytic factor induced prostaglandin E2 formation in the gastrocnemius muscle of non tumour-bearing animals and this effect was inhibited by indomethacin and EPA. In vivo studies show EPA (2.0g/kg-1 by gavage) to effectively reverse the decrease in body weight in animals bearing the MAC16 tumour with a concomitant reduction in tumour growth. Muscle from animals treated with EPA showed a decrease (60%) in protein degradation without an effect on protein synthesis. The action of the factor was largely mimicked by triarachidonin and trilinoleia. The increased serum levels of arachidonic acid in cachectic tumour-bearing animals may thus be responsible for increased protein degradation through prostanoid metabolism.
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Lemberg, Marius Kaspar. "Intramembrane proteolysis by the aspartic protease SPP /." Zürich, 2003. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=15327.

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Potocka, Isabel. "Cell-cycle regulated proteolysis in Caulobacter crescentus." Thesis, Imperial College London, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.252229.

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Campbell, William. "Characterisation of the proteolysis of chromogranin A." Thesis, Queen's University Belfast, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.301777.

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Books on the topic "Proteolysis"

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Specificity of proteolysis. Berlin: Springer-Verlag, 1992.

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Chemistry of proteolysis. Berlin: Springer-Verlag, 1993.

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Chondrogianni, Niki, Elah Pick, and Anna Gioran. Proteostasis and Proteolysis. Boca Raton: CRC Press, 2021. http://dx.doi.org/10.1201/9781003048138.

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Antonov, Vladimir K. Chemistry of Proteolysis. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-00979-6.

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Keil, Borivoj. Specificity of Proteolysis. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-48380-6.

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Abatangelo, G., L. Donati, and W. Vanscheidt, eds. Proteolysis in Wound Repair. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61130-8.

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Dougan, David A., ed. Regulated Proteolysis in Microorganisms. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-5940-4.

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K, Hopsu-Havu Väinö, Järvinen M, Kirschke Heidrun, and International Conference on Proteolysis and Protein Turnover (11th : 1996 : Turku, Finland), eds. Proteolysis in cell functions. Amsterdam: IOS Press, 1997.

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1946-, Mellgren Ronald L., and Murachi Takashi 1926-, eds. Intracellular calcium-dependent proteolysis. Boca Raton, Fla: CRC Press, 1990.

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C, Taylor Joseph, and Mittman Charles, eds. Pulmonary emphysema and proteolysis, 1986. Orlando: Academic Press, 1987.

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Book chapters on the topic "Proteolysis"

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Bond, Judith S., Timothy R. Keiffer, and Qi Sun. "Pericellular Proteolysis." In Extracellular Matrix Degradation, 75–94. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16861-1_4.

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Brix, Klaudia, Christopher J. Scott, and Margarete M. S. Heck. "Compartmentalization of Proteolysis." In Proteases: Structure and Function, 85–125. Vienna: Springer Vienna, 2013. http://dx.doi.org/10.1007/978-3-7091-0885-7_3.

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Tatsuta, Takashi, and Thomas Langer. "Studying Proteolysis Within Mitochondria." In Methods in Molecular Biology, 343–60. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-365-3_25.

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Bøgh, Katrine Lindholm, and Jeppe Madura Larsen. "Reducing Allergenicity by Proteolysis." In Agents of Change, 499–523. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-55482-8_19.

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Lindon, Catherine, and Barbara Di Fiore. "Measuring Proteolysis in Mitosis." In Methods in Molecular Biology, 259–70. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-993-2_16.

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Rodriguez-Gonzalez, Agustin, and Kathleen M. Sakamoto. "Proteolysis Targeting Chimeric Molecules." In Modulation of Protein Stability in Cancer Therapy, 147–60. New York, NY: Springer US, 2009. http://dx.doi.org/10.1007/978-0-387-69147-3_9.

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Antonov, Vladimir K. "Introduction." In Chemistry of Proteolysis, 1–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-00979-6_1.

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Antonov, Vladimir K. "Substrates." In Chemistry of Proteolysis, 5–31. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-00979-6_2.

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Antonov, Vladimir K. "Enzymes." In Chemistry of Proteolysis, 33–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-00979-6_3.

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Antonov, Vladimir K. "Nonenzymatic Hydrolysis. Models." In Chemistry of Proteolysis, 97–144. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-00979-6_4.

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Conference papers on the topic "Proteolysis"

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Batlle, J., M. F. López-Fernández, C. López-Berges, S. D. Berkowitz, Z. M. Ruggeri, and T. S. Zimmerman. "PROTEOLYTIC DEGRADATION OF VON WILLEBRAND FACTOR AFTER DDAVP ADMINISTRATION IN NORMAL INDIVIDUALS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644121.

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The infusion of l-Deamino-8-D-Arginine Vasopressin (DDAVP) in normal individuals is followed by an increase in factor VIII/von Willebrand factor in plasma and by the appearance of larger multimers of von Willebrand factor (vWF) than those seen in the resting state. Since the larger multimers are rapidly cleared and proteolysis is known to cause disaggregation of large multimers, we evaluated the degree of vWF proteolysis after DDAVP. DDAVP was infused into eight normal adult volunteers and the relative proportions of the intact 225 kDa subunit and the 189, 176 and 140 kDa fragments were compared before and at different times after DDAVP infusion. The relative proportion of the 176 kDa fragment was increased while that of the other species was decreased, indicating that proteolytic fragmentation had occurred. However, plasmin did not appear to be responsible because the vWF fragments characteristically produced by this enzyme could not be detected. Concomitant analysis of vWF multimeric structure showed that these changes were accompanied by an increase in the relative proportion of the satellite bands suggesting that they were ptoteolytically generated. Proteolysis may explain, at least in part, rapid clearance of larger vWF multimers released by DDAVP.
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Bischel, Kristen Moriah, Philip Emmerich, Tonela Qyli, Stephanie McGregor, Mitchell Depke, Nathaniel Verhagen, Dustin Deming, et al. "Abstract 403: Versican proteolysis in endometrial cancer." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-403.

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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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Roslan, Nur Farhana, Bee Lyn Chew, Hoe-Han Goh, and Nurulhikma Md Isa. "Sequence analysis of PROTEOLYSIS 6 from Solanum lycopersicum." In THE 2017 UKM FST POSTGRADUATE COLLOQUIUM: Proceedings of the University Kebangsaan Malaysia, Faculty of Science and Technology 2017 Postgraduate Colloquium. Author(s), 2018. http://dx.doi.org/10.1063/1.5027977.

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Berkowitz, S. D., H. Nozaki, K. Titani, T. Murachi, and T. S. Zimmerman. "CALPAIN AND ELASTASE ARE NOT RESPONSIBLE FOR THE VON WILLEBRAND FACTOR FRAGMENTS IN NORMAL PLASMA AND IIA VON WILLEBRAND DISEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644103.

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Recent evidence suggests that proteolysis plays an important role in some forms of inherited and acquired von Willebrand disease (vWD). Using monoclonal epitope mapping, we have examined the proteolysis of the von Willebrand factor (vWF) subunit with platelet calcium activated neutral protease (CANP) and human leukocyte elastase and found that they are not responsible for the proteolytic cleavage sejen in normal individuals and IIA vWD. Previously we have shown that in vivo proteolysis of vWF is a normal event with a small but consistent proportion of plasma vWF being composed of 189, 176, and 140 kD fragments cleaved from the 225 kD subunit. In IIA vWD the proportion of cleaved vWF is increased. Because calcium activated neutral protease (CANP, calpain) and one or more enzymes released from polymorphonuclear leukocytes are known to proteolyze vWF in vitro with resultant loss of large multimers similar to that seen in IIA vWD, they have been suggested as being responsible for the proteolysis in vivo. We have now digested highly purified vWF with porcine CANP I and II and performed monoclonal epitope mapping on the resulting fragments. We found no difference in the size, location, and quantity of the fragments produced by calpain I versus calpain II. New fragments were detected of approximately 200, 170, 150, and 125 kD. There was no evidence for generation of the native fragments. Mapping of the 170 and 150 kD calpain-cleaved fragments revealed them to be from different parts of the molecule than the native 176 and 140 kD fragments. Digestion of vWF with human leukocyte elastase produced new fragments at 210/205, 190, 165, 145/140, and 130/125 kD. No generation of native fragments was detected. Monoclonal epitope mapping of the 190 and 145/140 kD elastase-cleaved bands proved that they come from opposite ends of the vWF molecule than the native 189 and 140 kD fragments, respectively. Therefore, CANP and human leukocyte elastase do not produce the proteolyzed fragments present in normal and IIA vWD and probably do not cause the loss of large multimers seen in that disorder.
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Hou, Li-Xia, Ying-Ying Wang, Yu-Lan Liu, and Xiao-Kun Wang. "Effect of Sonication on Proteolysis of Peanut Protein Isolate." In 2015 International Conference on Medicine and Biopharmaceutical. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789814719810_0147.

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Peyrot, V., C. Briand, and J. M. Andreu. "Limited proteolysis of tubulin by subtilisin induces ring formation." In The living cell in four dimensions. AIP, 1991. http://dx.doi.org/10.1063/1.40597.

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Babiarz, Christopher P., Philip B. Emmerich, Carley M. Sprackling, Cheri A. Pasch, Linda Clipson, Kristina A. Matkowskyj, Fotis Asimakopoulos, and Dustin A. Deming. "Abstract 4583: Versican accumulation and proteolysis in neuroendocrine tumors." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4583.

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Babiarz, Christopher P., Philip B. Emmerich, Carley M. Sprackling, Cheri A. Pasch, Linda Clipson, Kristina A. Matkowskyj, Fotis Asimakopoulos, and Dustin A. Deming. "Abstract 4583: Versican accumulation and proteolysis in neuroendocrine tumors." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4583.

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"Proteolysis Targeting Chimeras (PROTACs): Emerging Therapeutics for Pancreatic Cancer." In 2022 International Conference on Biotechnology, Life Science and Medical Engineering. Clausius Scientific Press, 2022. http://dx.doi.org/10.23977/blsme.2022015.

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Reports on the topic "Proteolysis"

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Harper, Jeffrey. Identification of Genes Regulated by Proteolysis. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada408062.

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Carlson, Kelsey, Kenneth J. Prusa, Chris A. Fedler, Ed M. Steadham, Amanda C. Outhouse, Elisabeth J. Huff-Lonergan, and Steven M. Lonergan. Proteolysis Influences Tenderness of Aged Pork Loins. Ames (Iowa): Iowa State University, January 2017. http://dx.doi.org/10.31274/ans_air-180814-328.

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Mudryj, Maria. Calpain-Dependent Proteolysis of the Androgen Receptor. Fort Belvoir, VA: Defense Technical Information Center, November 2009. http://dx.doi.org/10.21236/ada517269.

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Strohmaier, Heimo M., and Steven Reed. The Role of Deregulated Cyclin E Proteolysis in Breast Cancer Development. Fort Belvoir, VA: Defense Technical Information Center, May 2002. http://dx.doi.org/10.21236/ada409788.

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Drogen, Frank van, Steven Reed, and Heimo M. Strohmaier. The Role of Deregulated Cyclin E Proteolysis in Breast Cancer Development. Fort Belvoir, VA: Defense Technical Information Center, May 2003. http://dx.doi.org/10.21236/ada418341.

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Spruck, Charles H. Identification of Substances for Ubiquitin-Dependent Proteolysis During Breast Tumor Progression. Fort Belvoir, VA: Defense Technical Information Center, October 2008. http://dx.doi.org/10.21236/ada510763.

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Srikanth, Appikonda. The Role of Ubiquitin-Mediated Proteolysis of Cyclin D in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, April 2005. http://dx.doi.org/10.21236/ada455151.

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Block, Karen L. The Role of Ubiquitin-Mediated Proteolysis of Cyclin D in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, April 2003. http://dx.doi.org/10.21236/ada416662.

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Khokha, Rama. Molecular Tracking of Proteolysis During Breast Cancer Cell Extravasation: Blockage of Therapeutic Inhibitors. Fort Belvoir, VA: Defense Technical Information Center, August 2002. http://dx.doi.org/10.21236/ada411429.

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Xiong, Yue. G1 Cell Cycle Control by Regulated Proteolysis in Normal and Tumorigenic Breast Cells. Fort Belvoir, VA: Defense Technical Information Center, September 2002. http://dx.doi.org/10.21236/ada415516.

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