Trypsinogen Activation Peptide

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  • novel prss1 mutation p p17t validates pathogenic relevance of ctrc mediated processing of the Trypsinogen Activation Peptide in chronic pancreatitis
    The American Journal of Gastroenterology, 2017
    Co-Authors: Balázs Németh, Akos Szucs, Peter Hegyi, Miklos Sahintoth
    Abstract:

    Novel PRSS1 Mutation p.P17T Validates Pathogenic Relevance of CTRC-Mediated Processing of the Trypsinogen Activation Peptide in Chronic Pancreatitis

  • tighter control by chymotrypsin c ctrc explains lack of association between human anionic Trypsinogen and hereditary pancreatitis
    Journal of Biological Chemistry, 2016
    Co-Authors: Zsanett Jancso, Miklos Sahintoth
    Abstract:

    The human pancreas expresses two major Trypsinogen isoforms, cationic Trypsinogen (PRSS1) and anionic Trypsinogen (PRSS2). Mutations in PRSS1 cause hereditary pancreatitis by altering cleavage of regulatory nick sites by chymotrypsin C (CTRC) resulting in reduced Trypsinogen degradation and increased autoActivation. Despite 90% identity with PRSS1 and a strong propensity for autoActivation, mutations in PRSS2 are not found in hereditary pancreatitis suggesting that Activation of this isoform is more tightly regulated. Here, we demonstrated that CTRC promoted degradation and thereby markedly suppressed autoActivation of human anionic Trypsinogen more effectively than previously observed with cationic Trypsinogen. Increased sensitivity of anionic Trypsinogen to CTRC-mediated degradation was due to an additional cleavage site at Leu-148 in the autolysis loop and the lack of the conserved Cys-139-Cys-206 disulfide bond. Significant stabilization of anionic Trypsinogen against degradation was achieved by simultaneous mutations of CTRC cleavage sites Leu-81 and Leu-148, autolytic cleavage site Arg-122, and restoration of the missing disulfide bridge. This stands in stark contrast to cationic Trypsinogen where single mutations of either Leu-81 or Arg-122 resulted in almost complete resistance to CTRC-mediated degradation. Finally, processing of the Trypsinogen Activation Peptide at Phe-18 by CTRC inhibited autoActivation of anionic Trypsinogen, although cationic Trypsinogen was strongly stimulated. Taken together, the observations indicate that human anionic Trypsinogen is controlled by CTRC in a manner that individual natural mutations are unlikely to increase stability enough to promote intra-pancreatic Activation. This unique biochemical property of anionic Trypsinogen explains the lack of association of PRSS2 mutations with hereditary pancreatitis.

  • robust autoActivation chymotrypsin c independence and diminished secretion define a subset of hereditary pancreatitis associated cationic Trypsinogen mutants
    FEBS Journal, 2013
    Co-Authors: Andrea Geisz, Peter Hegyi, Miklos Sahintoth
    Abstract:

    Mutations in human cationic Trypsinogen cause hereditary pancreatitis by altering its proteolytic regulation of Activation and degradation by chymotrypsin C (CTRC). CTRC stimulates Trypsinogen autoActivation by processing the Activation Peptide to a shorter form, but also promotes degradation by cleaving the calcium-binding loop in Trypsinogen. Mutations render Trypsinogen resistant to CTRC-mediated degradation and/or increase processing of the Activation Peptide by CTRC. Here we demonstrate that the Activation Peptide mutations D19A, D22G, K23R and K23_I24insIDK robustly increased the rate of Trypsinogen autoActivation, both in the presence and absence of CTRC. Degradation of the mutants by CTRC was unchanged, and processing of the Activation Peptide was increased fourfold in the D19A mutant only. Surprisingly, however, this increased processing had only a minimal effect on autoActivation. The tetra-aspartate motif in the Trypsinogen Activation Peptide binds calcium (KD of ~ 1.6 mm), which stimulates autoActivation. Unexpectedly, calcium binding was not compromised by any of the Activation Peptide mutations. Despite normal binding, autoActivation of mutants D22G and K23_I24insIDK was not stimulated by calcium. Finally, the Activation Peptide mutants exhibited reduced secretion from transfected cells, and secreted Trypsinogen levels were inversely proportional with autoActivation rates. We conclude that D19A, D22G, K23R and K23_I24insIDK form a mechanistically distinct subset of hereditary pancreatitis-associated mutations that exert their effect primarily through direct stimulation of autoActivation, independently of CTRC. The potentially severe clinical impact of the markedly increased autoActivation is offset by diminished secretion, resulting in a clinical phenotype that is indistinguishable from typical hereditary pancreatitis.

  • mutations of the Trypsinogen Activation Peptide in hereditary pancreatitis
    Pancreatology, 2013
    Co-Authors: Andrea Geisz, Peter Hegyi, Zoltan Rakonczay, Laszlo Czako, Miklos Sahintoth
    Abstract:

    s / Pancreatology 13 (2013) S2–S98 S56 Results: In CG animals during 12-48 h level of GTH in intestinal tissue was 40-55% lower (p<0,05) normal values, malone dialdehyde increased twice (p<0,05), BT was observed in 100% cases. GTH infusion (1 group) increased its concentration on 18-23% in comparison with CG, but it remained 1,5 time (p<0,05) lesser than in healthy animals, BT occurred in 65-85% after 24 h. In 2 group level of GTH and malon dialdehyde were not significantly differ from preoperative values, BT was diagnosed in 35-55% cases. Conclusion: Local delivery of GTH to intestinal mucosa by CNp can improve gut barrier function during SAP. PII-8 Abstract id: 70. Pathogenetic mechanisms acute pancreatitis I. Trubitsyna, T. Tarasova, L. Vinokurova, A. Smirnova. Central Research Institute of Gastroenterology, Russia Introduction: in the process of acute pancreatitis were essential membranodestruktivnye phenomena that lead to structural and functional changes in cells and tissues. Membranodestruktivnye processes are due to the intensification of lipid peroxidation, increased production of free radicals and lipid peroxidation products of low molecular weight, and hypoxia Aims: Reserch the changes of cytokines of inflamation and cytotoxyn Materials & methods: experimental research put on 25 white rats anesthetized peccant acute pancreatitis by application of acetic acid on the pancreas. Biochemical methods serotonin, IFM – proinflammatory cytokines IL-1b, TNFa, INFg. Results: 24 h increased the levels of serotonin in the blood serum of the pancreas and duodenal mucosa. In the dynamics of acute pancreatitis was observed intensification of lipid peroxidation, increased activity of phospholipase A2. Local and systemic increase in the content of 5-HT resulted in violation of the microvasculature of the pancreas. Reduction in the amount of blood flowing, increases venous engorgement. 5-HT violates the stability of biomembranes. There is an autoimmune component, which complicates the recovery of damaged tissue. Conclusion: Thus, the high content of serotonin, impaired blood flow and stability of biological membranes, increased proinflammatory cytokines either alone or together especially the combination of these factors is a pathogenetic factor in the development of acute pancreatitis. PII-10 Abstract id: 282. Mutations of the Trypsinogen Activation Peptide in hereditary pancreatitis Andrea Geisz , Peter Hegyi , Zoltan Rakonczay , L aszl o Czak o , Mikl os Sahin-T oth . 1 First Department of Medicine, University of Szeged, Szeged, Hungary, Hungary Department of Molecular and Cell Biology, Boston University Medical Center, Boston, MA, USA Introduction: Mutations in human cationic Trypsinogen cause hereditary pancreatitis by altering its proteolytic regulation by chymotrypsin C (CTRC). CTRC stimulates Trypsinogen autoActivation by processing the Activation Peptide to a shorter form but also promotes degradation by cleaving the calcium binding loop in Trypsinogen. Mutations render Trypsinogen resistant to CTRC-mediated degradation and/or increase processing of the Activation Peptide by CTRC. Aims: The present study was aimed at clarifying the role of CTRC in the mechanism of action of Activation Peptide mutations D19A, D22G, K23R and K23_I24insIDK. Materials & methods: Human pancreatic enzymes were produced recombinantly and purified to homogeneity. Trypsinogen Activation was followed by enzymatic assays and SDS-PAGE. Trypsinogen secretion was measured from transfected HEK 293T cells. Results: Activation Peptide mutations robustly increased Trypsinogen autoActivation, both in the presence and absence of CTRC. Degradation of Activation Peptide mutants by CTRC was unchanged and processing of the Activation Peptide was increased only in the D19A mutant by 4-fold. Surprisingly, however, increased processing had essentially no effect on autoActivation. Finally, the Activation Peptide mutants exhibited reduced secretion from transfected cells, and secreted Trypsinogen levels were inversely proportional with autoActivation rates. Conclusion: Activation Peptide mutations form a mechanistically distinct subset of hereditary pancreatitis associated mutations, which exert their effect primarily through direct stimulation of autoActivation, independently of CTRC. The potentially severe clinical impact of the markedly increased autoActivation is offset by diminished secretion, resulting in a clinical phenotype indistinguishable from typical hereditary pancreatitis. Supported by NIH, OTKA and NF€ U/T AMOP. PII-11 Abstract id: 25. Effects of exocrine pancreatic insufficiency (EPI) and pancreatic enzyme substitution on bone mineral content of growing pigs âV“ used as a model for children Anne M€ ossler , Annette Liesegang , Teresa Schwarzmaier , Peter Gregory , Josef Kamphues . 1 University of Veterinary Medicine, Hannover, Institute of Animal Nutrition, Germany University of Zurich, Institute of Animal Nutrition, Switzerland Abbott Laboratories GmbH (Germany), Germany Introduction: The pancreatic duct ligated (PL) minipig is an established model for studying effects of exocrine pancreatic insufficiency (EPI) in adults, but studies in juveniles are rare. Aims: This study aimed to test the effects of EPI on bone density in growing pigs. Materials & methods: In 8 pigs aged 8 weeks EPI was induced surgically (PL), another 4 pigs served as controls (C). Beginning from 3 weeks post OP 4 PL-pigs received Kreon (w6300 Ph.Eur.E lipase/g dietary fatÂ,(PLþE)) while 4 PL-pigs received no enzyme substitution therapy (PL0). Diet contained (per kg DM) 85 g crude fat; 10.5 g Ca, 5.68 g P and 1875 IU vitamin D. Every 2nd week all animals received parenteral vitamin supply. 11 weeks post OP all animals were slaughtered and left tibia was taken and analysed by peripheral quantitative computer tomography for total bone mineral content (BMC) and cortex mineral content (CMC). Results: BMC and CMC were significantly reduced in PL-0-pigs compared to C-pigs while in PLþE intermediate values not differing from C at large were observed at distal end of tibia: (mg/cm): C: 482 40.2a PL:295 25.6b, PLþE: 399 70.8ab] Conclusion: Even all animals received a complete diet and were supplemented parenterally with high dosed vitamins there was an impaired bone mineralization in PL-0 âV“ despite lack of clinical symptoms. Enzyme supplementation improved (but didnâV t normalize) bone mineralization presumably due to an improved total tract digestibility of fat (%: Control: 80.9; PL-0: 7.55; PLþE: 52.0) âV“ supposed to cause an increase of the absorption of vitamin D and calcium. PII-12 Abstract id: 310. Tributaryliths as a reason of peripheral ductal hypertension in chronic pancreatitis Aliaksandr Varabei , Anatoli Shuleika , Yury Arlouski , Egi Vizhinis , Natali Lagodich . 1 Prof., Belarus MD, Belarus

  • increased Activation of hereditary pancreatitis associated human cationic Trypsinogen mutants in presence of chymotrypsin c
    Journal of Biological Chemistry, 2012
    Co-Authors: Andras Szabo, Miklos Sahintoth
    Abstract:

    Mutations in human cationic Trypsinogen (PRSS1) cause autosomal dominant hereditary pancreatitis. Increased intrapancreatic autoActivation of Trypsinogen mutants has been hypothesized to initiate the disease. AutoActivation of cationic Trypsinogen is proteolytically regulated by chymotrypsin C (CTRC), which mitigates the development of trypsin activity by promoting degradation of both Trypsinogen and trypsin. Paradoxically, CTRC also increases the rate of autoActivation by processing the Trypsinogen Activation Peptide to a shorter form. The aim of this study was to investigate the effect of CTRC on the autoActivation of clinically relevant Trypsinogen mutants. We found that in the presence of CTRC, Trypsinogen mutants associated with classic hereditary pancreatitis (N29I, N29T, V39A, R122C, and R122H) autoactivated at increased rates and reached markedly higher active trypsin levels compared with wild-type cationic Trypsinogen. The A16V mutant, known for its variable disease penetrance, exhibited a smaller increase in autoActivation. The mechanistic basis of increased Activation was mutation-specific and involved resistance to degradation (N29I, N29T, V39A, R122C, and R122H) and/or increased N-terminal processing by CTRC (A16V and N29I). These observations indicate that hereditary pancreatitis is caused by CTRC-dependent dysregulation of cationic Trypsinogen autoActivation, which results in elevated trypsin levels in the pancreas.

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  • Linkage of oxidative and nonoxidative ethanol metabolism in the pancreas and toxicity of nonoxidative ethanol metabolites for pancreatic acinar cells.
    Surgery, 2001
    Co-Authors: Jens Werner, Mouris Saghir, Carlos Fernandez-del Castillo, Andrew L. Warshaw, Michael Laposata
    Abstract:

    Abstract Background. Alcohol abuse is a major cause of pancreatic damage. Recent experimental evidence suggests that fatty acid ethyl esters (FAEE), nonoxidative ethanol metabolites, injure pancreatic acinar cells. Linkage between oxidative and nonoxidative metabolism of ethanol in the pancreas may contribute to increased FAEE levels. Methods. To study the association between oxidative and nonoxidative ethanol metabolism, FAEE concentration and FAEE synthase activity in rat pancreatic and liver homogenates incubated with ethanol were evaluated with and without inhibitors of oxidative ethanol metabolism. For toxicity studies, Trypsinogen Activation Peptide synthesis as a measure of pancreatic cell injury was quantitated in unstimulated and cerulein-stimulated isolated pancreatic acinar cells incubated with ethanol or FAEE. Results. Inhibition of oxidative ethanol metabolism results in a 2- to 3-fold increase in nonoxidative ethanol metabolism to FAEE in pancreas and in liver. Both ethanol and FAEE induce increased intracellular Trypsinogen Activation by more than 50% in the presence of physiologic concentrations of cerulein in vitro. Conclusions. These findings demonstrate that the inhibition of oxidative ethanol metabolism results in an increase in flux through the nonoxidative pathway and support the proposition that alcohol-induced pancreatic injury is mediated at least in part by FAEE, which are important products of pancreatic ethanol metabolism.(Surgery 2001;129:736-44.)

  • elevated calcium and Activation of Trypsinogen in rat pancreatic acini
    Gut, 1997
    Co-Authors: Thomas W Frick, Carlos Fernandezdelcastillo, D Bimmler, Andrew L. Warshaw
    Abstract:

    Background—Acute pancreatitis associated with hypercalcaemia has been described in humans and experimental animals. It has been demonstrated that calcium dose dependently accelerates Trypsinogen Activation, and it is generally believed that ectopic Activation of digestive enzymes is an early event in the pathophysiology of acute pancreatitis. Aims and methods—Trypsinogen Activation Peptide (TAP) was measured in isolated rat pancreatic acini exposed to elevated extracellular calcium in order to investigate the association between calcium and Trypsinogen Activation in living cells. TAP was determined in the culture medium either before (extracellular compartment) or after (intracellular compartment) cell homogenisation. Results—Neither secretory stimulation nor elevated calcium alone caused an increase in TAP levels. Maximal cerulein or carbachol stimulation superimposed on high medium calcium, however, significantly increased intracellular Trypsinogen Activation twofold. This increase was inhibited by either N G -monomethyl-Larginine (L-NMMA) or verapamil. Acinar cell morphology and function remained intact as demonstrated by electron microscopy and secretagogue dose-response studies. Conclusions—These results support the hypothesis that increased intracellular Trypsinogen Activation is an early step in the pathogenesis of hypercalcaemia induced pancreatitis. The model may have a bearing on other types of pancreatitis as elevated cytosolic calcium is thought to be an early event in the pathogenesis of acute pancreatitis in general. (Gut 1997;41:339‐343)

  • urinary Trypsinogen Activation Peptide tap predicts severity in patients with acute pancreatitis
    International Journal of Pancreatology, 1997
    Co-Authors: Scott Tenner, Carlos Fernandez-del Castillo, Andrew L. Warshaw, William M Steinberg, John Hermontaylor, Jorge E Valenzuela, Mohammed Hariri, M Hughes, Peter A Banks
    Abstract:

    Conclusions Urinary TAP obtained within the first 48 h of the onset of symptoms can distinguish patients with severe acute pancreatitis.

  • antibiotic treatment improves survival in experimental acute necrotizing pancreatitis
    Gastroenterology, 1996
    Co-Authors: Kai Mithofer, David W Rattner, Fernandezdel C Castillo, Mary Jane Ferraro, Kent B Lewandrowski, Andrew L. Warshaw
    Abstract:

    Abstract BACKGROUND & AIMS: It is still unproven whether prophylactic antibiotics can reduce mortality from acute necrotizing pancreatitis (ANP). The aim of this study was to investigate whether antibiotic therapy can influence long-term outcome in ANP and how appropriate this therapy is. METHODS: ANP was induced in rats by standardized intraductal bile acid infusion and cerulein hyperstimulation. Serum Trypsinogen Activation Peptide levels were used to verify comparable disease severity. Starting 6 hours after induction, animals randomly received saline (n = 60), 20 mg/kg imipenem (n = 62), or 10 mg/kg ciprofloxacin (n = 60) every 8 hours for 7 days. On day 7, half of each group was killed so a quantitative pancreatic bacteriology could be conducted. The other half was analyzed at 21 days for long-term mortality, late bacteriologic changes, abscesses, and pseudocysts. RESULTS: Comparable Trypsinogen Activation Peptide increases confirmed equally severe ANP in each group before treatment. Imipenem and ciprofloxacin significantly reduced the number of infected pancreatic specimens, bacterial counts, and identified species at 1 week. At 3 weeks, pancreatic infection prevalence was lower in animals treated with antibiotics; abscess formation was reduced and pseudocysts were smaller and less frequently infected. Survival was significantly improved by imipenem and ciprofloxacin. CONCLUSIONS: Antibiotic treatment reduces early and late septic pancreatic complications and improves survival from experimental ANP. (Gastroenterology 1996 Jan;110(1):232-40)

  • quantitative assay of Trypsinogen by measurement of cleaved Activation Peptide after Activation with enterokinase
    Analytical Biochemistry, 1995
    Co-Authors: Kai Mithofer, Carlos Fernandezdelcastillo, U Mandavilli, David W Rattner, Andrew L. Warshaw
    Abstract:

    Measurement of Trypsinogen by quantitative immunosorbent assay of the highly specific and inert Trypsinogen Activation Peptide following complete Activation of Trypsinogen by enterokinase offers a simple and sensitive method that provides reliable results over a wide range of Trypsinogen concentrations. This method offers a significant advantage in being applicable to complex biological tissues.

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Esko Kemppainen - One of the best experts on this subject based on the ideXlab platform.

  • urinary Trypsinogen Activation Peptide as a marker of severe acute pancreatitis
    British Journal of Surgery, 2004
    Co-Authors: C D Johnson, Esko Kemppainen, Pauli Puolakkainen, Marko Lempinen, C W Imrie, Ross Carter, C Mckay
    Abstract:

    Background: Trypsinogen Activation Peptide (TAP) may be an early marker of severe pancreatitis. Previous studies have included all patients with organ failure in the group with severe pancreatitis, although patients with transient organ failure may have a good prognosis. The aim of this study was to determine the value of urinary TAP estimation for prediction of severity of acute pancreatitis, and to validate use of several markers of prediction of severity against a new, stringent definition of severity. Methods: Patients with acute pancreatitis were recruited within 24 h of onset of symptoms. Urine and blood samples were collected for 24 h, and Acute Physiology And Chronic Health Evaluation (APACHE) II (24 h), Ranson (48 h) and Glasgow (48 h) scores were calculated. Severe acute pancreatitis was defined by the presence of a local complication or the presence of organ failure for more than 48 h. Results: Urinary TAP levels were significantly greater in patients with severe pancreatitis than in those with mild disease during the first 36 h of admission. The highest of three estimations of TAP in the first 24 h was as effective as APACHE II at 24 h in predicting severity. At 24 h after admission, urinary TAP was better than C-reactive protein (CRP) in predicting severity. The combination of TAP and CRP at 24 h allowed identification of high- and low-risk groups. The new definition of severity excluded 24 of 190 patients with transient organ failure; none of these patients died. Conclusion: Use of TAP improved early prediction of the severity of acute pancreatitis. Organ failure that resolves within 48 h does not signify a severe attack of acute pancreatitis.

  • Trypsinogen-2 and Trypsinogen Activation Peptide (TAP) in urine of patients with acute pancreatitis
    The Journal of surgical research, 2003
    Co-Authors: Marko Lempinen, Pauli Puolakkainen, Reijo Haapiainen, Ulf-håkan Stenman, Patrik Finne, Esko Kemppainen
    Abstract:

    Abstract Background and aims. There is an obvious clinical need for a simple test that can identify patients at risk of developing severe acute pancreatitis. In this work we compared urinary Trypsinogen-2 with urinary Trypsinogen Activation Peptide (TAP) and serum C-reactive protein (CRP) for early differentiation between mild and severe acute pancreatitis. Patients and methods. The study population consisted of 127 consecutive patients with acute pancreatitis of whom 29 had severe disease. Urinary Trypsinogen-2 was measured by a quantitative immunofluorometric assay and TAP by a competitive immunoassay. Serum CRP was determined by immunoturbidimetry. Results. The sensitivity and specificity to identify severe acute pancreatitis on admission was 72% and 81% for urinary Trypsinogen-2, 64% and 82% for urinary TAP, and 29% and 93% for serum CRP, respectively. At 24 h after admission, the values were 82% and 78% for urinary Trypsinogen-2, 52% and 92% for urinary TAP, and 84% and 72% for serum CRP, respectively. Receiver-operating characteristics curve analysis showed that the area under the curve was larger for urinary Trypsinogen-2 than for urinary TAP and serum CRP on admission and 24 h after admission. On admission the positive likelihood ration for urinary trypsiongen-2 was 3.7, for urinary TAP 3.6, and 4.3 for serum CRP, respectively. The corresponding negative likelihood ratios were 0.34, 0.43, and 0.76, respectively. Conclusion. Urinary Trypsinogen-2 was superior to serum CRP and as god as or even better than urinary TAP and in the early prediction of disease severity in acute pancreatitis. These results suggest that it could be a valuable adjunct in the early assessment of the severity of acute pancreatitis.

  • early prediction of severity in acute pancreatitis by urinary Trypsinogen Activation Peptide a multicentre study
    The Lancet, 2000
    Co-Authors: John P Neoptolemos, Esko Kemppainen, Jens M Mayer, John M Fitzpatrick, Michael Raraty, J Slavin, H G Beger, A Hietaranta, Pauli Puolakkainen
    Abstract:

    Summary Background There is a pressing clinical requirement for an early simple test of severity in acute pancreatitis. We investigated the use of an assay of Trypsinogen Activation Peptide (TAP). Methods We undertook a multicentre study in 246 patients (172 with acute pancreatitis [35 with severe disease], 74 controls). We assessed the predictive value of urinary TAP concentrations measured by a validated competitive immunoassay. We compared the results with those for plasma C-reactive protein and three clinicobiochemical scoring systems. TAP and C-reactive protein concentrations were analysed at set times after symptom onset and compared with the clinicobiochemical systems scores at key times during hospital stay. Findings At 24 h after symptom onset, the median urinary TAP concentration was 37 nmol/L (IQR 17–110) for severe and 15 nmol/L (5–35) for mild disease (p 35 nmol/L), 58%, 73%, 39%, and 86%, respectively, and for C-reactive protein (>150 mg/L), 0%, 90%, 0%, and 75%. 48 h after admission the values for the clinicobiochemical scoring systems were: APACHE II (≥8), 56%, 64%, 30%, and 85%; Ranson score (≥3), 89%, 64%, 38%, and 96%; and Glasgow score (≥3), 77%, 75%, 44%, and 93%. At 48 h, the values for C-reactive protein were 86%, 61%, 37%, and 94% and for TAP were 83%, 72%, 44%, and 94%. Combined testing of C-reactive protein and TAP was not superior to TAP alone for accuracy. Interpretation Urinary TAP provided accurate severity prediction 24 h after onset of symptoms. This single marker of severity in acute pancreatitis deserves routine clinical application.

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