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Journal articles on the topic 'Proteolysis'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

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 (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+-dep

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Navegantes, Luiz Carlos C., Neusa M. Z. Resano, Renato H. Migliorini та 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, № 3 (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 chan

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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 (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

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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 (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

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Volodymyr, Yukalo, Datsyshyn Kateryna, and Storozh Liudmyla. "COMPARISON OF PRODUCTS OF WHEY PROTEINS CONCENTRATE PROTEOLYSIS, OBTAINED BY DIFFERENT PROTEOLYTIC PREPARATIONS." Eastern-European Journal of Enterprise Technologies 5, no. 11 (101) (2019): 40–47. https://doi.org/10.15587/1729-4061.2019.177314.

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An important source of bioactive peptides is hydrolyzed products based on milk whey: hypoallergenic products, hydrolyzates for baby food, and products for athletes. However, in their production, proteolytic preparations of different origin are used. This may affect the degree of proteolysis of the biologically active peptides (BAP) proteins-precursors, the proteolysis products molecular weight distribution and, accordingly, the probability of BAP formation. A comparison of the degree of whey protein concentrate (WPC) proteins proteolysis and the molecular weight distribution of proteolysis pro

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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 (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

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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 (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 am

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8

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 (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

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Adasheva, Daria A., Olga S. Lebedeva, Daria V. Goliusova, et al. "PAPP-A-Specific IGFBP-4 Proteolysis in Human Induced Pluripotent Stem Cell-Derived Cardiomyocytes." International Journal of Molecular Sciences 24, no. 9 (2023): 8420. http://dx.doi.org/10.3390/ijms24098420.

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The insulin-like growth factors IGF-I and IGF-II—as well as their binding proteins (IGFBPs), which regulate their bioavailability—are involved in many pathological and physiological processes in cardiac tissue. Pregnancy-associated plasma protein A (PAPP-A) is a metalloprotease that preferentially cleaves IGFBP-4, releasing IGF and activating its biological activity. Previous studies have shown that PAPP-A-specific IGFBP-4 proteolysis is involved in the pathogenesis of cardiovascular diseases, such as ischemia, heart failure, and acute coronary syndrome. However, it remains unclear whether PAP

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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 (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

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Vorob’ev, Mikhail M. "Towards a Quantitative Description of Proteolysis: Contribution of Demasking and Hydrolysis Steps to Proteolysis Kinetics of Milk Proteins." Foods 14, no. 1 (2025): 93. https://doi.org/10.3390/foods14010093.

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The hydrolysis of proteins by proteases (proteolysis) plays a significant role in biology and food science. Despite the importance of proteolysis, a universal quantitative model of this phenomenon has not yet been created. This review considers approaches to modeling proteolysis in a batch reactor that take into account differences in the hydrolysis of the individual peptide bonds, as well as the limited accessibility (masking) for the enzymes of some hydrolysis sites in the protein substrate. Kinetic studies of the proteolysis of β-casein and β-lactoglobulin by various proteolytic enzymes thr

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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 (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 E21

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Franch, Harold A., Xiaonan Wang, Sira Sooparb, Nikia S. Brown, and Jie Du. "Phosphatidylinositol 3-Kinase Activity Is Required for Epidermal Growth Factor to Suppress Proteolysis." Journal of the American Society of Nephrology 13, no. 4 (2002): 903–9. http://dx.doi.org/10.1681/asn.v134903.

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ABSTRACT. Suppression of protein breakdown occurs commonly in cell growth, but the pathways responsible for controlling proteolysis are poorly understood. Protein breakdown in NRK-52E renal epithelial cells treated with epidermal growth factor (EGF) and intracellular signaling inhibitors or dominant negative signaling molecules contained in an adenoviral vector were measured. The tyrosine kinase inhibitor, herbimycin A, eliminated the suppression of proteolysis induced by EGF. In contrast, the Src inhibitor, PP1, had no effect. Expression of dominant negative H-RasY57 blocked the ability of EG

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Solioz, M. "Role of proteolysis in copper homoeostasis." Biochemical Society Transactions 30, no. 4 (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 proteo

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15

Lockwood, Thomas D. "Redox-dependent and redox-independent subcomponents of protein degradation in perfused myocardium." American Journal of Physiology-Endocrinology and Metabolism 276, no. 5 (1999): E945—E954. http://dx.doi.org/10.1152/ajpendo.1999.276.5.e945.

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The integration of proteolytic pathways with metabolism was investigated in perfused rat myocardium. After a 10-min incorporation period, the minute-to-minute release of [3H]leucine from myocardial proteins was measured in nonrecirculating effluent perfusate. The nontoxic pro-oxidant probe diamide (100 μM) or a supraphysiological concentration of the endogenous oxidative metabolite dehydroascorbic acid (200 μM) reversibly inhibited 75% of myocardial proteolysis consisting of several known subcomponents (redox dependent); however, 25% of proteolysis was diamide insensitive (redox independent).

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Christensen, M., P. Henckel, and P. P. Purslow. "Postmortem proteolysis in pork does not depend on fibre type distribution." Proceedings of the British Society of Animal Science 2001 (2001): 79. http://dx.doi.org/10.1017/s1752756200004610.

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Proteolytic degradation is known to be faster in white muscles than in red muscles (Whipple & Koohmaraie, 1992). Variation in eating quality between muscles has often been correlated to their metabolic properties, as determined by the fibre type distribution. Correlations between fibre type distribution and postmortem proteolysis could result from two possible effects: (1) Due to their inherent differences in metabolic potential, composition and content of proteolytic enzymes, fibres of some types may degrade more than others. (2) The balance of fibre types controls postmortem (p.m.) metab

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Manfredi, L. H., D. Lustrino, J. Machado, et al. "Adrenodemedullation activates the Ca2+-dependent proteolysis in soleus muscles from rats exposed to cold." Journal of Applied Physiology 122, no. 2 (2017): 317–26. http://dx.doi.org/10.1152/japplphysiol.00198.2016.

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Previous studies have shown that catecholamines in vivo and in vitro inhibit the activity of Ca2+-dependent proteolysis in skeletal muscles under basal conditions. In the present study we sought to investigate the role of catecholamines in regulating the Ca2+-dependent proteolysis in soleus and extensor digitorum longus (EDL) muscles from rats acutely exposed to cold. Overall proteolysis, the activity of proteolytic systems, protein levels and gene expression of different components of the calpain system were investigated in rats submitted to adrenodemedullation (ADMX) and exposed to cold for

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Artemyeva, K. A., E. I. Goufman, I. I. Stepanova, et al. "The level of IgG proteolytic fragments as an additional prognostic biomarker of prostate cancer." CLINICAL AND EXPERIMENTAL MORPHOLOGY 11, no. 2 (2022): 22–31. http://dx.doi.org/10.31088/cem2022.11.2.22-31.

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Introduction. Prostate cancer (PC) leads the world structure of male cancer mortality. Understanding the prognosis for PC patients is vitally important and requires diagnostic enhancements such as developing biomarker panels. The studyaimed to estimate sensitivity, specificity, and prognostic significance of the level of immunoglobulin G (IgG) proteolysis products in the blood serum depending on PC Gleason score and detect how the levels of IgG proteolytic fragments were associated with the diagnostic marker expression. Materials and methods. The study included 90 PC patients. We used the Glea

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Moazed, Bita, and M. Desautels. "Control of proteolysis by norepinephrine and insulin in brown adipocytes: role of ATP, phosphatidylinositol 3-kinase, and p70 S6K." Canadian Journal of Physiology and Pharmacology 80, no. 6 (2002): 541–52. http://dx.doi.org/10.1139/y02-078.

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The objective of this study was to evaluate some of the mechanisms by which norepinephrine (NE) and insulin may influence protein degradation in mouse brown adipocytes differentiated in cultures. The effects of NE and insulin, alone or in combination, on three factors known to influence proteolysis (maintenance of cell ATP and 1-phosphatidylinositol 3-kinase (PI 3-kinase) and p70 ribosomal S6-kinase (p70 S6K) activities) were examined. It was proposed that NE affects proteolysis indirectly by decreasing cell ATP from activation of uncoupling protein-1 (UCP1)-dependent mitochondrial respiration

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Zamir, Oded, Per-Olof Hasselgren, Takashi Higashiguchi, Janice A. Frederick, and Josef E. Fischer. "Tumour necrosis factor (TNF) and interleukin-1 (IL-1) induce muscle proteolysis through different mechanisms." Mediators of Inflammation 1, no. 4 (1992): 247–50. http://dx.doi.org/10.1155/s0962935192000371.

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The purpose of this study was to test the hypothesis that muscle proteolysis induced by TNF or IL-1 is mediated by glucocorticoids. Rats were treated with 300 μg kg−1of recombinant human preparations of IL-1α (rIL-1α) or TNFα (rTNFα) divided into three equal intraperitoneal doses given over 16 h. Two hours before each cytokine injection, rats were given 5 mg kg−1of the glucocorticoid receptor blocker mifepristone RU 38486, by gavage or were gavaged with the vehicle. Eighteen hours after the first cytokine injection, total and myofibrillar protein breakdown rates were determined in incubated ex

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Fagan, J. M., and A. L. Goldberg. "The rate of protein degradation in isolated skeletal muscle does not correlate with reduction-oxidation status." Biochemical Journal 227, no. 3 (1985): 689–94. http://dx.doi.org/10.1042/bj2270689.

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It has been suggested that the cytoplasmic reduction-oxidation state correlates with, and may regulate, rates of protein breakdown in skeletal muscle. To test whether an increased lactate/pyruvate ratio is in fact generally associated with low proteolytic rates, this ratio was measured in rat extensor digitorum longus muscles incubated under conditions that rates of protein breakdown. Treatment with the calcium ionophore A23187 caused similar large increases in the lactate/pyruvate ratio at 2 microM, where proteolysis did not change, and at 20 microM, where proteolysis was greatly accelerated.

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Barrett, E. J., L. A. Jahn, D. M. Oliveras, and D. A. Fryburg. "Chloroquine does not exert insulin-like actions on human forearm muscle metabolism." American Journal of Physiology-Endocrinology and Metabolism 268, no. 5 (1995): E820—E824. http://dx.doi.org/10.1152/ajpendo.1995.268.5.e820.

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Insulin's anabolic action on skeletal muscle and whole body protein is attributable to its action to slow tissue proteolysis. The antimalarial chloroquine inhibits lysosomal proteolysis and is reported to improve glycemia in poorly controlled diabetic patients. We infused chloroquine into the brachial artery of seven healthy postabsorptive volunteers over 3 h during a steady-state infusion of L-[ring-2,6-3H]phenylalanine (Phe) to study its effect on muscle glucose and protein turnover. Compared with basal, chloroquine increased forearm blood flow (P < 0.01) but did not change glucose uptake

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TAILLANDIER, Daniel, Eveline AUROUSSEAU, Dominique MEYNIAL-DENIS, et al. "Coordinate activation of lysosomal, Ca2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle." Biochemical Journal 316, no. 1 (1996): 65–72. http://dx.doi.org/10.1042/bj3160065.

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Nine days of hindlimb suspension resulted in atrophy (55%) and loss of protein (53%) in rat soleus muscle due to a marked elevation in protein breakdown (66%, P < 0.005). To define which proteolytic system(s) contributed to this increase, soleus muscles from unweighted rats were incubated in the presence of proteolytic inhibitors. An increase in lysosomal and Ca2+-activated proteolysis (254%, P < 0.05) occurred in the atrophying incubated muscles. In agreement with the measurements in vitro, cathepsin B, cathepsins B+L and m-calpain enzyme activities increased by 111%, 92% and 180% (P &l

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Mañas-García, Laura, Charlotte Denhard, Javier Mateu, Xavier Duran, Joaquim Gea, and Esther Barreiro. "Beneficial Effects of Resveratrol in Mouse Gastrocnemius: A Hint to Muscle Phenotype and Proteolysis." Cells 10, no. 9 (2021): 2436. http://dx.doi.org/10.3390/cells10092436.

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We hypothesized that the phenolic compound resveratrol mitigates muscle protein degradation and loss and improves muscle fiber cross-sectional area (CSA) in gastrocnemius of mice exposed to unloading (7dI). In gastrocnemius of mice (female C57BL/6J, 10 weeks) exposed to a seven-day period of hindlimb immobilization with/without resveratrol treatment, markers of muscle proteolysis (tyrosine release, systemic troponin-I), atrophy signaling pathways, and muscle phenotypic features and function were analyzed. In gastrocnemius of unloaded mice treated with resveratrol, body and muscle weight and fu

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van de Winkel, J. G., R. van Ommen, T. W. Huizinga, et al. "Proteolysis induces increased binding affinity of the monocyte type II FcR for human IgG." Journal of Immunology 143, no. 2 (1989): 571–78. http://dx.doi.org/10.4049/jimmunol.143.2.571.

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Abstract Human monocytes express two types of IgG FcR, Fc gamma RI and Fc gamma RII. These can be assayed by using indicator E sensitized by human IgG (EA-human IgG) or mouse IgG1, (EA-mouse IgG1), respectively. On mouse macrophages, Fc gamma RI is sensitive to trypsin, whereas Fc gamma RII is trypsin resistant. We studied the effects of the proteolytic enzymes pronase and trypsin on human monocyte Fc gamma R. Neither enzyme caused a decrease in rosetting mediated by monocyte Fc gamma RI. Human Fc gamma RII is polymorphic, and monocytes interact either strongly or weakly with mouse IgG1. The i

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Myagkonosov, D. S., I. T. Smykov, D. V. Abramov, and I. N. Delitskaya. "Influence of different types of fermentation-produced chymosin on quality of soft cheeses." IOP Conference Series: Earth and Environmental Science 1052, no. 1 (2022): 012076. http://dx.doi.org/10.1088/1755-1315/1052/1/012076.

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Abstract The disadvantage of soft cheeses is their short shelf life. In soft cheeses with a high moisture content, proteolysis occurs at a high rate, as a result of which the cheeses quickly overripe. The main proteolytic agent in soft cheeses is the milk-clotting enzyme (MCE). Increasing the shelf life of cheeses can be achieved by using MCE types having low proteolytic activity (PA). We have studied the effect of MCE based on different types of fermentation-produced chymosin: Chy-max® Extra (bovine chymosin), Chy-max® M (camel chymosin), Chy-max® Supreme (“modified” chymosin) on the dynamics

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TOURNU, Cécile, Alain OBLED, Marie-Paule ROUX, Marc FERRARA, Satoshi OMURA, and Daniel M. BÉCHET. "Glucose regulates protein catabolism in ras-transformed fibroblasts through a lysosomal-dependent proteolytic pathway." Biochemical Journal 357, no. 1 (2001): 255–61. http://dx.doi.org/10.1042/bj3570255.

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Transformed cells are exposed to heterogeneous microenvironments, including low d-glucose (Glc) concentrations inside tumours. The regulation of protein turnover is commonly impaired in many types of transformed cells, but the role of Glc in this regulation is unknown. In the present study we demonstrate that Glc controls protein turnover in ras-transformed fibroblasts (KBALB). The regulation by Glc of protein breakdown was correlated with modifications in the levels of lysosomal cathepsins B, L and D, while autophagic sequestration and non-lysosomal proteolytic systems (m- and μ-calpains and

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Lavatelli, Francesca, Giulia Mazzini, Stefano Ricagno, et al. "Mass spectrometry characterization of light chain fragmentation sites in cardiac AL amyloidosis: insights into the timing of proteolysis." Journal of Biological Chemistry 295, no. 49 (2020): 16572–84. http://dx.doi.org/10.1074/jbc.ra120.013461.

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Amyloid fibrils are polymeric structures originating from aggregation of misfolded proteins. In vivo, proteolysis may modulate amyloidogenesis and fibril stability. In light chain (AL) amyloidosis, fragmented light chains (LCs) are abundant components of amyloid deposits; however, site and timing of proteolysis are debated. Identification of the N and C termini of LC fragments is instrumental to understanding involved processes and enzymes. We investigated the N and C terminome of the LC proteoforms in fibrils extracted from the hearts of two AL cardiomyopathy patients, using a proteomic appro

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Hutton, D. A., J. P. Pearson, A. Allen, and S. N. E. Foster. "Mucolysis of the colonic mucus barrier by faecal proteinases: Inhibition by interacting polyacrylate." Clinical Science 78, no. 3 (1990): 265–71. http://dx.doi.org/10.1042/cs0780265.

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1. Mucolytic (mucus solubilizing) activity in human faeces has been characterized with both purified human and pig colonic mucin and shown to be mediated by proteolysis. 2. Mucolytic activity was demonstrated by: (i) a drop in mucin viscosity; (ii) a substantial reduction in mucin size, from polymer to degraded subunit, as assessed by Sepharose CL-2B gel filtration; (iii) formation of new N-terminal peptides. 3. Mucolytic activity was also followed in faecal extracts by its proteolytic activity using standard succinyl albumin substrate. Proteolysis extended over the pH range 4.5–11.0. Proteoly

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Ewald, S. J., and P. H. Refling. "Co-immunoprecipitation of the Ly-5 molecule and an endogenous protease: a proteolytic system requiring a reducing agent and Ca2+1." Journal of Immunology 134, no. 4 (1985): 2513–19. http://dx.doi.org/10.4049/jimmunol.134.4.2513.

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Abstract Sodium [3H]borohydride- and [35S]methionine-labeled Ly-5 molecules from mouse thymocytes and T lymphoma cells were isolated with specific antibody and Staphylococcus aureus Cowan I (SaCI) strain; after extensive washing of the complexes, elution with Laemmli's reducing buffer (0.05 M Tris [pH 6.8 or 6.0], 4% sodium dodecyl sulfate [SDS], and 2% 2-mercaptoethanol [2-ME]) resulted in partial breakdown of the isolated Ly-5 molecules from a Mr = 175,000 to 150,000. Other proteins present during the elution step showed no evidence of proteolysis. 2-ME and SDS were required for proteolysis;

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Baracos, V. E., C. DeVivo, D. H. Hoyle, and A. L. Goldberg. "Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma." American Journal of Physiology-Endocrinology and Metabolism 268, no. 5 (1995): E996—E1006. http://dx.doi.org/10.1152/ajpendo.1995.268.5.e996.

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Rats implanted with Yoshida ascites hepatoma (YAH) show a rapid and selective loss of muscle protein due mainly to a marked increase (63-95%) in the rate of protein degradation (compared with rates in muscles of pair-fed controls). To define which proteolytic pathways contribute to this increase, epitrochlearis muscles from YAH-bearing and control rats were incubated under conditions that modify different proteolytic systems. Overall proteolysis in either group of rats was not affected by removal of Ca2+ or by blocking the Ca(2+)-dependent proteolytic system. Inhibition of lysosomal function w

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Baracos, V., R. E. Greenberg, and A. L. Goldberg. "Influence of calcium and other divalent cations on protein turnover in rat skeletal muscle." American Journal of Physiology-Endocrinology and Metabolism 250, no. 6 (1986): E702—E710. http://dx.doi.org/10.1152/ajpendo.1986.250.6.e702.

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When rat muscles were incubated in Ca2+-free media, their rates of protein break-down were significantly lower than in complete medium (2.58 mM Ca2+). Dantrolene and 3,4,5-trimethoxybenzoic acid 8-(diethylamino)octyl ester, inhibitors of Ca2+ release from the sarcoplasmic reticulum, also reduced muscle proteolysis. When Ca2+ was added (up to 5.16 mM), proteolysis increased progressively up to 70% in the intact soleus and extensor digitorum longus muscles and up to 300% in the cut diaphragm preparation. Addition of Ca2+ did not affect the muscles' ATP or phosphocreatine content and increased pr

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Sun, Hong, and Hui Zhang. "Lysine Methylation-Dependent Proteolysis by the Malignant Brain Tumor (MBT) Domain Proteins." International Journal of Molecular Sciences 25, no. 4 (2024): 2248. http://dx.doi.org/10.3390/ijms25042248.

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Lysine methylation is a major post-translational protein modification that occurs in both histones and non-histone proteins. Emerging studies show that the methylated lysine residues in non-histone proteins provide a proteolytic signal for ubiquitin-dependent proteolysis. The SET7 (SETD7) methyltransferase specifically transfers a methyl group from S-Adenosyl methionine to a specific lysine residue located in a methylation degron motif of a protein substrate to mark the methylated protein for ubiquitin-dependent proteolysis. LSD1 (Kdm1a) serves as a demethylase to dynamically remove the methyl

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Maupin-Furlow, Julie A. "Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme." Emerging Topics in Life Sciences 2, no. 4 (2018): 561–80. http://dx.doi.org/10.1042/etls20180025.

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Archaea are phylogenetically distinct from bacteria, and some of their proteolytic systems reflect this distinction. Here, the current knowledge of archaeal proteolysis is reviewed as it relates to protein metabolism, protein homeostasis, and cellular regulation including targeted proteolysis by proteasomes associated with AAA-ATPase networks and ubiquitin-like modification. Proteases and peptidases that facilitate the recycling of peptides to amino acids as well as membrane-associated and integral membrane proteases are also reviewed.

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Rivera, G. M., and J. E. Fortune. "Selection of the Dominant Follicle and Insulin-Like Growth Factor (IGF)-Binding Proteins: Evidence that Pregnancy-Associated Plasma Protein A Contributes to Proteolysis of IGF-Binding Protein 5 in Bovine Follicular Fluid." Endocrinology 144, no. 2 (2003): 437–46. http://dx.doi.org/10.1210/en.2002-220657.

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Development of a dominant follicle is associated with decreased intrafollicular low molecular weight IGF-binding proteins (namely IGFBP-2, -4, and -5) and increased proteolysis of IGFBP-4 by pregnancy-associated plasma protein A (PAPP-A). In addition to IGFBP-4 proteolytic activity, bovine follicular fluid contains strong proteolytic activity for IGFBP-5, but not for IGFBP-2. Here we show that the IGFBP-5 protease present in bovine follicular fluid is a neutral/basic pH-favoring, Zn2+ metalloprotease very similar to the previously described IGFBP-4 protease. We hypothesized that immunoneutrali

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SIVANANDAM, Arun S., Subburaman MOHAN, Hirohito KITA, et al. "Studies on regulation of IGF (insulin-like growth factor)-binding protein (IGFBP) 4 proteolysis by pregnancy-associated plasma protein-A (PAPP-A) in cells treated with phorbol ester." Biochemical Journal 379, no. 1 (2004): 57–64. http://dx.doi.org/10.1042/bj20030937.

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PAPP-A (pregnancy-associated plasma protein-A) is produced by hSFs (human skin fibroblasts) and hOBs (human osteoblasts) and enhances the mitogenic activity of IGFs (insulin-like growth factors) by degradation of IGFBP-4 (insulin-like growth factor-binding protein 4). PKC (protein kinase C) activation in these cells led to reduction in IGFBP-4 proteolysis. This study was undertaken to determine the mechanism by which activation of PKC suppresses IGFBP-4 proteolysis. Treatment of hSFs/hOBs with TPA (PMA; 100 nM) reduced IGFBP-4 proteolysis without significantly decreasing the PAPP-A level in th

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Germain, D., J. Hendley, and B. Futcher. "DNA damage inhibits proteolysis of the B-type cyclin Clb5 in S. cerevisiae." Journal of Cell Science 110, no. 15 (1997): 1813–20. http://dx.doi.org/10.1242/jcs.110.15.1813.

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Cell cycle progression is mediated by waves of specific cyclin dependent kinases (CDKs) in all eukaryotes. Cyclins are degraded by the ubiquitin pathway of proteolysis. The recent identification of several components of the cyclin proteolysis machinery has highlighted both the importance of proteolysis at multiple transition points in the cell cycle and the involvement of other substrates degraded by the same machinery. In this study, we have investigated the effects of DNA damage on the cyclin proteolytic machinery in Saccharomyces cerevisiae. We find that the half-life of the B-type cyclin C

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Fontana, Angelo, Patrizia Polverino De Laureto, Barbara Spolaore, Erica Frare, Paola Picotti, and Marcello Zambonin. "Probing protein structure by limited proteolysis." Acta Biochimica Polonica 51, no. 2 (2004): 299–321. http://dx.doi.org/10.18388/abp.2004_3573.

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Limited proteolysis experiments can be successfully used to probe conformational features of proteins. In a number of studies it has been demonstrated that the sites of limited proteolysis along the polypeptide chain of a protein are characterized by enhanced backbone flexibility, implying that proteolytic probes can pinpoint the sites of local unfolding in a protein chain. Limited proteolysis was used to analyze the partly folded (molten globule) states of several proteins, such as apomyoglobin, alpha-lactalbumin, calcium-binding lysozymes, cytochrome c and human growth hormone. These protein

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Tawa, N. E., I. C. Kettelhut, and A. L. Goldberg. "Dietary protein deficiency reduces lysosomal and nonlysosomal ATP-dependent proteolysis in muscle." American Journal of Physiology-Endocrinology and Metabolism 263, no. 2 (1992): E326—E334. http://dx.doi.org/10.1152/ajpendo.1992.263.2.e326.

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When rats are fed a protein deficient (PD) diet for 7 days, rates of proteolysis in skeletal muscle decrease by 40-50% (N. E. Tawa, Jr., and A. L. Goldberg. Am. J. Physiol. 263 (Endocrinol. Metab. 26): E317-325, 1992). To identify the underlying biochemical adaptations, we measured different proteolytic processes in incubated muscles. The capacity for intralysosomal proteolysis, as shown by sensitivity to methylamine or lysosomal protease inhibitors, fell 55-75% in muscles from PD rats. Furthermore, extracts of muscles of PD rats showed 30-70% lower activity of many lysosomal proteases, includ

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Li, Anguo, and Tze-Chein Wun. "Proteolysis of Tissue Factor Pathway Inhibitor (TFPI) by Plasmin: Effect on TFPI Activity." Thrombosis and Haemostasis 80, no. 09 (1998): 423–27. http://dx.doi.org/10.1055/s-0037-1615224.

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SummaryAn important regulator of the initiation of blood coagulation is the plasma glycoprotein, tissue factor pathway inhibitor (TFPI). TFPI inhibits factor Xa and factor VIIa/tissue factor complex, thereby dampens the proteolytic cascade of the tissue factor pathway. Plasma clot lysis is primarily mediated by the fibrinolytic enzyme, plasmin, which is generated through limited proteolysis of plasminogen by endogenous or exogenously administered plaminogen activators. In this study, the interaction of plasmin with recombinant E. coli-derived TFPI (rTFPI) was examined. Plasmin was found to cau

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Cortesio, Christa L., Lindsy R. Boateng, Timothy M. Piazza, David A. Bennin, and Anna Huttenlocher. "Calpain-mediated Proteolysis of Paxillin Negatively Regulates Focal Adhesion Dynamics and Cell Migration." Journal of Biological Chemistry 286, no. 12 (2011): 9998–10006. http://dx.doi.org/10.1074/jbc.m110.187294.

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The dynamic turnover of integrin-mediated adhesions is important for cell migration. Paxillin is an adaptor protein that localizes to focal adhesions and has been implicated in cell motility. We previously reported that calpain-mediated proteolysis of talin1 and focal adhesion kinase mediates adhesion disassembly in motile cells. To determine whether calpain-mediated paxillin proteolysis regulates focal adhesion dynamics and cell motility, we mapped the preferred calpain proteolytic site in paxillin. The cleavage site is between the paxillin LD1 and LD2 motifs and generates a C-terminal fragme

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Mahmoud, Samar A., and Peter Chien. "Regulated Proteolysis in Bacteria." Annual Review of Biochemistry 87, no. 1 (2018): 677–96. http://dx.doi.org/10.1146/annurev-biochem-062917-012848.

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Regulated proteolysis is a vital process that affects all living things. Bacteria use energy-dependent AAA+ proteases to power degradation of misfolded and native regulatory proteins. Given that proteolysis is an irreversible event, specificity and selectivity in degrading substrates are key. Specificity is often augmented through the use of adaptors that modify the inherent specificity of the proteolytic machinery. Regulated protein degradation is intricately linked to quality control, cell-cycle progression, and physiological transitions. In this review, we highlight recent work that has she

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ČERVEK, Matjaž, D. ATTAIX, and Jasna M. A. STEKAR. "Glavne poti razkroja beljakovin v skeletnem mišičju." Acta agriculturae Slovenica 70, no. 1 (1997): 201–9. http://dx.doi.org/10.14720/aas.1997.70.1.16157.

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Skeletal muscle contains multiple proteolytic systems that are presumably responsible for the breakdown of specific proteins. Three major proteolitic pathways operate in skeletal muscle, although such a simple division is too simplified. The best known proteolytic system is the lysosomal pathway. Lysosomes are particularly abundant in liver, and they are not involved in the degradation of myofibrillar proteins. The Ca2+-dependent proteolytic process does not contribute significantly to overall proteolysis in muscles from control and catabolic animals. In fact, there is now growing evidence tha

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Mosoni, L., T. Malmezat, M. C. Valluy, M. L. Houlier, D. Attaix, and P. Patureau Mirand. "Lower recovery of muscle protein lost during starvation in old rats despite a stimulation of protein synthesis." American Journal of Physiology-Endocrinology and Metabolism 277, no. 4 (1999): E608—E616. http://dx.doi.org/10.1152/ajpendo.1999.277.4.e608.

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Sarcopenia could result from the inability of an older individual to recover muscle lost during catabolic periods. To test this hypothesis, we compared the capacity of 5-day-refed 12- and 24-mo-old rats to recover muscle mass lost after 10 days without food. We measured gastrocnemius and liver protein synthesis with the flooding-dose method and also measured nitrogen balance, 3-methylhistidine excretion, and the gene expression of components of proteolytic pathways in muscle comparing fed, starved, and refed rats at each age. We show that 24-mo-old rats had an altered capacity to recover muscl

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Reboul, A., J. Arvieux, J. F. Wright, and M. G. Colomb. "Proteolytic fragmentation of tetanus toxin by subcellular fractions of JY, a B lymphoblastoid cell line." Biochemical Journal 277, no. 1 (1991): 47–51. http://dx.doi.org/10.1042/bj2770047.

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Proteolysis of 125I-labelled tetanus toxin by subcellular fractions from an Epstein-Barr-virus-transformed B lymphoblastoid cell line, JY, was investigated. Fractions enriched in lysosomes and plasma membranes cleaved the toxin molecule at several sites, with a pH optimum of 5.5. N-Terminal sequence analysis of Mr-81,000, -45,000 and -35,000 proteolytic fragments indicated cleavage of the Asp-460-Leu-461, Asp-872-Glu-873 and Ile-1013-Thr-1014 peptide bonds, all sites located within the heavy chain of the toxin molecule. Additional sites near the C-terminus of the heavy chain, giving rise to lo

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Librando, Vito, Danilo Gullotto, and Zelica Minniti. "Automated Molecular Library Generation of Proteic Fragments by Virtual Proteolysis for Molecular Modelling Studies." In Silico Biology: Journal of Biological Systems Modeling and Multi-Scale Simulation 6, no. 5 (2006): 449–57. https://doi.org/10.3233/isb-00257.

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This paper presents a computer aided design method useful for simulation of a set of proteolytic cleavages upon target proteins obtained from the Brookhaven Data Bank. The method was developed by using algorithms that are able to interface themselves with other software environments, in order to assist computer analyses in the molecular modelling field, and allowing the generation of molecular libraries containing protein fragments produced by simulated proteolysis. These libraries include structures that differ for several amino acid deletions upon specified regions of the primary sequence. T

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Katrukha, Aleksei G., Anastasia V. Bereznikova, Vladimir L. Filatov, et al. "Degradation of cardiac troponin I: implication for reliable immunodetection." Clinical Chemistry 44, no. 12 (1998): 2433–40. http://dx.doi.org/10.1093/clinchem/44.12.2433.

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Abstract We have analyzed by different immunological methods the proteolytic degradation of cardiac troponin I (cTnI) in human necrotic tissue and in serum. cTnI is susceptible to proteolysis, and its degradation leads to the appearance of a wide diversity of proteolytic peptides with different stabilities. N- and C-terminal regions were rapidly cleaved by proteases, whereas the fragment located between residues 30 and 110 demonstrated substantially higher stability, possibly because of its protection by TnC. We conclude that antibodies selected for cTnI sandwich immunoassays should preferenti

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Voelkel-Johnson, C., A. J. Entingh, W. S. Wold, L. R. Gooding, and S. M. Laster. "Activation of intracellular proteases is an early event in TNF-induced apoptosis." Journal of Immunology 154, no. 4 (1995): 1707–16. http://dx.doi.org/10.4049/jimmunol.154.4.1707.

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Abstract The serine protease inhibitor tosyl-argenine methyl ester inhibits TNF-induced apoptosis, suggesting that proteolysis is necessary for this response. To test this hypothesis, we asked whether protein fragmentation occurs during the death of C3HA fibroblasts, a 3T3-like cell that was rendered sensitive to TNF by cycloheximide. Our results show that the binding of fluorescamine, which binds primary amines, was increased in apoptotic cells by approximately 50%. We also found that 10-15% of the protein in apoptotic cells was no longer precipitable by TCA. Evidence for proteolysis was also

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Mañas-García, Laura, Nuria Bargalló, Joaquim Gea, and Esther Barreiro. "Muscle Phenotype, Proteolysis, and Atrophy Signaling During Reloading in Mice: Effects of Curcumin on the Gastrocnemius." Nutrients 12, no. 2 (2020): 388. http://dx.doi.org/10.3390/nu12020388.

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We hypothesized that curcumin may mitigate muscle protein degradation and loss through attenuation of proteolytic activity in limb muscles of mice exposed to reloading (7dR) following immobilization (7dI). In gastrocnemius of mice (female C57BL/6J, 10 weeks) exposed to recovery following a seven-day period of hindlimb immobilization with/without curcumin treatment, markers of muscle proteolysis (systemic troponin-I), atrophy signaling pathways and histone deacetylases, protein synthesis, and muscle phenotypic characteristics and function were analyzed. In gastrocnemius of reloading mice compar

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Mintoo, Mubashir, Amritangshu Chakravarty, and Ronak Tilvawala. "N-Terminomics Strategies for Protease Substrates Profiling." Molecules 26, no. 15 (2021): 4699. http://dx.doi.org/10.3390/molecules26154699.

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Proteases play a central role in various biochemical pathways catalyzing and regulating key biological events. Proteases catalyze an irreversible post-translational modification called proteolysis by hydrolyzing peptide bonds in proteins. Given the destructive potential of proteolysis, protease activity is tightly regulated. Dysregulation of protease activity has been reported in numerous disease conditions, including cancers, neurodegenerative diseases, inflammatory conditions, cardiovascular diseases, and viral infections. The proteolytic profile of a cell, tissue, or organ is governed by pr

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