[(18. [(364)-89.7 (\226373. /T1_2 1 Tf Google Scholar. -31.8862 -1.2143 Td [(33. /T1_2 1 Tf [(Biochem. /T1_4 1 Tf /T1_0 1 Tf )]TJ T* 2.302 0 Td -20.3911 -1.2143 Td [(However,)-488.7 (unlike)-488.7 (supraphysiologic)-488.7 (treatment,)-488.7 (during)-488.7 (physiologic)]TJ [(J. )-423.6 (K)-29.6 (rause,)-411.9 (T.,)-411.9 (Gerbershagen,)-411.9 (M.)-411.9 (U.,)-411.9 (Fiege,)-411.9 (M.,)-411.9 (Weisshorn,)-411.9 (R.)-411.9 (&)-411.9 (Wappler,)-411.9 (F.)]TJ )-494.3 (\(2002\))]TJ )-423.7 (Guk)-29.6 (ovsk)-29.6 (aya,)-360.4 (A. Copyright © 2015, The American Society for Biochemistry and Molecular Biology. (Cell)Tj )-337.6 (H.)-337.6 (\(1990\))]TJ 6.6223 0 Td 573.676 365.384 38.324 -66 re 1.6023 0 Td -23.1675 -1.2143 Td (Commun. Increased sensitivity of anionic trypsinogen to CTRC-mediated degradation was due to an additional cleavage site at Leu148 in the autolysis loop and the lack of the conserved Cys139-Cys206 disulfide bond. )-445.2 (Res. )Tj 3.6083 0 Td )-337.6 (H.)-337.6 (\(2003\))]TJ [-0.3 (. <> [(required)-317.9 (to)-317.9 (cause)-317.9 (pancreatitis. [(atitis. B , cleavage of S200A-trypsin ( Tr ) with human CTRC was performed in 1 m M , 100 ␮ M or 15 ␮ M CaCl 2 , as described in “Materials and Methods.” Trypsin mutant E85A,S200A was incu- bated with CTRC in 1 m M CaCl 2 . [(by)-175.9 (ethanol,)-175.9 (seem)-175.8 (to)-175.9 (be)-175.9 (in)-30 (itiated)-175.9 (by)-175.9 (f)-0.1 (actors)-175.9 (that)-175.9 (sensitize)-175.9 (the)-175.9 (pancreas)]TJ )-337.6 (Neurosci)-29.6 (. )-423.7 (Fitzsimmons,)-379 (T.)-379 (J.,)-379 (McRoberts,)-379 (J. /T1_4 1 Tf 1. The order of magnitude of the rate constants is 20–100 sec-1. C , cleavage reactions were quantitated with densitometry and plot- ted. 1.6883 -1.2143 Td )]TJ /T1_3 1 Tf )-423.6 (Hofbauer,)-307.2 (B.,)-307.2 (Saluja,)-307.2 (A. )]TJ 10.1071 0 Td Here we review key genetic and biochemical features of the trypsin-dependent pathological pathway in chronic pancreatitis. /T1_0 1 Tf -24.7171 -1.2143 Td Zymogen activation assays: in this study, the conversion of zymogens to mature enzymes is taken as either an increase in enzyme activity using fluorogenic assays [16, 17] or the appearance of mature enzyme forms using immunoblot analysis [15]. [(&)-337.6 (Petersen,)-337.6 (O. )-443.2 (Straub,)-186.3 (S.)-186.3 (V.,)-186.3 (Giovannuc)-29.6 (ci,)-186.3 (D.)-186.3 (R.)-186.3 (&)-186.3 (Yule,)-186.3 (D.)-186.3 (I. [(40. -7.4038 -1.2143 Td [(Am. )-423.6 (Fitzsimmons,)-324.6 (T.)-324.7 (J.,)-324.6 (Guk)-29.6 (ovsky,)-324.7 (I.,)-324.6 (McRoberts,)-324.6 (J. )-423.7 (Melzer,)-337.6 (W.)-337.6 (&)-337.6 (Dietze,)-337.6 (B. [(We)-282.6 (thank)-282.6 (T.)-282.6 (Gn)-29.8 (iadek,)-282.6 (D.)-282.6 (Gome)19.9 (s,)-282.6 (A. A reaction in which the enzyme acts upon a substrate is coupled to monitor the process. (Downloaded by guest on January 11, 2021 )Tj )-535.3 (A.,)-535.3 (Singh,)-535.3 (J.,)]TJ 9.3599 0 Td Conversion of virgin into modified soybean trypsin inhibitor, Determinants of chymotrypsin C cleavage specificity in the calcium-binding loop of human cationic trypsinogen, Enzymic resynthesis of the hydrolyzed peptide bond(s) in ribonuclease S, Structural Basis of the Activation and Action of Trypsin, Structural Evidence for Standard-Mechanism Inhibition in Metallopeptidases from a Complex Poised to Resynthesize a Peptide Bond, Structural Determinants of Limited Proteolysis, Evolutionary Similarities between Pancreatic Proteolytic Enzymes. Free PDF. Representative gels of two to four experiments are shown. [(pancreatitis)-373.2 (\(43\),)-373.2 (this)-373.2 (work)-373.1 (reports)-373.2 (a)-373.1 (prev)-39.8 (iously)-373.1 (unde)19.8 (scribed)-373.1 (link)]TJ )-312.1 (J. )-593.3 (&)-593.3 (Di)]TJ -26.2618 -1.2143 Td [(Grants)-307.8 (T32)-307.8 (DK07017,)-307.9 (KO8)-307.8 (DK68116,)-307.9 (and)-307.8 (K12)-307.9 (HD001401)-307.9 (\(to)-307.9 (S.Z.H.\),)]TJ [(49. 1977;6:177-93. )]TJ Conversion of inactive trypsinogen to active trypsin is controlled by CTRC via two independent and seemingly conflicting mechanisms; cleavage of the trypsinogen activation peptide at the Phe 18 -Asp 19 peptide bond accelerates autoactivation of trypsinogen (5,7,8), whereas cleavage of the Leu 81 -Glu 82 peptide bond in the calcium binding loop promotes degradation of trypsinogen (4,6,7, In an attempt to detect structural differences between chymotrypsinogen and chymotrypsin, and trypsinogen and trypsin, measurements of the optical rotation and of the enzymatic activity of these proteins were carried out. -0.0146 Tc -31.214 -1.2143 Td [(M.H.N.\);)-486.8 (an)-486.8 (American)-486.8 (Gastroenterological)-486.8 (Association)-486.8 (AstraZeneca)]TJ 15.9473 0 Td [(Solomon,)-305.6 (T.)-305.6 (E.,)-305.6 (Guk)-29.6 (ovsk)-29.6 (aya,)-305.6 (A. Under limited proteolysis of native spinach Rubisco with trypsin two short peptides were released from the, Bovine trypsinogen, trypsin and chymotrypsinogen undergo an isomerization in acidic medium, like many other proteins. 26, 205-222 (2009) Microbial Transglutaminase Production: Understanding the Mechanism DONGXU ZHANG1, YANG ZHU 2 AND JIAN CHEN1* 1Key Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, Jiangsu 214122, China; 2 Department of Biosciences, TNO Quality of Life, … )]TJ /T1_2 1 Tf )]TJ 9 0 0 9 468.5276 724.5654 Tm (272,)Tj [(5. WO2001016289A2 - Zymogen activation system - Google Patents Zymogen activation system Download PDF … [(R)-60 (YR)-181.5 (mut)-30 (ations,)-181.6 (is)-181.6 (associated)-181.5 (w)-39.8 (ith)-181.5 (disordered)-181.5 (channel)-181.6 (function)-181.5 (and)]TJ /T1_7 1 Tf (Chem. 7.4216 0 Td T* (125,)Tj In this study, we assessed statistical significance and predictive power of individual structural descriptors and combination thereof for the identification of cleavage sites. [(10. -0.0146 Tc -29.4313 -1.2143 Td [(669)-89.7 (\226)-89.7 (677. )-342.1 (L.,)-342.1 (Lewandrowsk)-29.6 (i,)-342.1 (K.)-342.1 (B.,)-342.1 (L)-29.6 (aposat)-29.6 (a,)-342.1 (M.,)]TJ [(Iozzo,)-302.3 (R.)-302.3 (V.,)-302.3 (Carter,)-302.3 (E.)-302.3 (A.,)-302.3 (Schatz,)-302.3 (R.)-302.3 (J. 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). Zymogen activation: a new system for homogeneous ligand-binding assay. [(Pancreatolog)-49.9 (y)]TJ )-276.4 (C.,)-276.4 (Waser,)-276.4 (B.,)-276.4 (Gugger,)-276.4 (M.,)-276.4 (Frie)19.9 (ss,)-276.4 (H.,)-276.4 (K)-29.6 (leef)-29.6 (f,)-276.4 (J.,)-276.4 (Kayed,)-276.4 (H.,)-276.4 (Buchler,)]TJ zymogen activation (Oberst et al., 2003). (\(1998\))Tj )Tj 3.0971 0 Td )-200.5 (Microsc. 22.9249 0 Td 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. BT Our findings implicate substrate flexibility as a critical determinant of catalysis. 1.6023 0 Td )]TJ )-547.4 (Mut)-30 (ations)-547.4 (in)-547.4 (R)-60 (YR1,)-547.4 (the)-547.4 (major)-547.4 (isofor)-30 (m)-547.4 (ex)-30 (pre)19.8 (ssed)-547.4 (in)]TJ ET By integrating multiple enhanced sampling methods for molecular dynamics, we model a viable conformational pathway between substrate-like and product-like states, linking substrate dynamics on the ns-μs timescale with large collective substrate motions on the much slower timescale of catalysis. )-282.8 (B.,)-282.9 (Koulen,)-282.9 (P.)-282.9 (&)]TJ (265\226271. [(disease. /T1_3 1 Tf 1.6883 -1.2143 Td 2021-01-11T15:32:21-08:00 )-390 (\(1999\))]TJ Here we describe functional analysis of eight previously uncharacterized natural CTRC variants tested for potential defects in secretion, proteolytic stability and catalytic activity. )-271.1 (H.)-271.1 (&)-271.1 (Tepik)-29.6 (in,)-271.1 (A. state of zymogen activation are important parameters to fully assess matriptase activity and function. Inhibition of RYR also inhibited zymo-gen activation in vivo. /T1_0 1 Tf /T1_0 1 Tf 0 -1.1452 TD T* (893\226922. [(EMBO)-337.6 (J. THE JOURNAL OF BIOLOGICAL CHEMISTRY 0 1993 by The American Society for Biochemistry and Molecular Biology, Inc. Vol. [(P)-29.6 (roc. These have been selected because they are among the best characterized representatives of the zymogens as a group. (157,)Tj /T1_0 1 Tf /T1_3 1 Tf )]TJ 37 Full PDFs related to this paper. T* )-423.6 (Flewellen,)-370.9 (E.)-370.9 (H.,)-370.9 (Nelson,)-370.9 (T.)-370.9 (E.,)-370.9 (Jone)19.9 (s,)-370.9 (W.)-370.9 (P.,)-370.9 (Arens,)-370.9 (J. [(46. T* Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation. (735\226738. (2)Tj Biotechnology and Genetic Engineering Reviews - Vol. It has recently found that the exposure of matriptase-expressing epithelial cells and its homogenate to mildly acidic pH induces the rapid activation of matriptase zymogen. )Tj dc:description Activation mechanisms also appear to be of primary importance in metamorphosis as demonstrated by the existence of zymogen-enz yme transformations for tadpole collagenase [21] and cocoonase [22]. A , ribbon diagram of human cationic trypsin (Protein Data Bank ID: 2RA3 (17)) showing the position of the Leu81–Glu82 cleavage site ( red arrow ) in the calcium binding loop ( green ) relative to the active site catalytic triad of Ser-200 (here mutated to Ala), His-63, and Asp-107 ( red ) and the Arg-122 loop ( blue ). Calcineurin inhibition reduces caerulein-induced chymo-trypsin activation. [(and)-284.4 (a)-284.4 (Grant-in-A)-29.8 (id)-284.4 (f)-29.8 (rom)-284.4 (the)-284.4 (American)-284.4 (Heart)-284.4 (Association)-284.4 (\(to)-284.4 (M.H.N.\). )-423.7 (Pandol,)-420 (S.)-420 (J.,)-420 (Perisk)-29.6 (ic,)-420 (S.,)-420 (Guk)-29.6 (ovsky,)-420 (I.,)-420 (Zan)-29.6 (inov)-39.7 (ic,)-420 (V.,)-420 (Jung,)-420 (Y.,)-420 (Zong,)-420 (Y.,)]TJ 0.9794 0 Td endobj 2.1072 0 Td /T1_0 1 Tf 32.0238 0 Td /T1_2 1 Tf Structural changes in the activation of chymotrypsinogen and trypsinogen. 3.1329 0 Td [(treatment)-247.5 (the)-247.5 (active)-247.5 (enz)-30 (y)-30 (me)19.8 (s)-247.5 (are)-247.5 (secreted)-247.5 (f)-30 (r)-0.1 (om)-247.5 (the)-247.5 (cells)-247.5 (\(41\). )-231.8 (For)-231.7 (example,)-231.7 (t)-30 (wo)-231.7 (t)-0.1 (hat)]TJ /T1_3 1 Tf /T1_6 1 Tf 6.244 0 Td -31.8825 -1.2143 Td )-366.4 (This)-366.4 (work)-366.4 (was)-366.4 (supported)-366.4 (by)-366.4 (National)-366.4 (Institute)19.9 (s)-366.4 (of)-366.4 (Health)]TJ [(F.,)-318.2 (Rac)-29.6 (y)-29.6 (maekers,)-318.2 (L.)-318.2 (&)-318.2 (Muallem,)-318.2 (S.)-318.2 (\(1997\))]TJ )-423.7 (Sutton,)-441.9 (R.,)-441.9 (Criddle,)-441.9 (D.,)-441.9 (Rarat)-29.6 (y,)-441.9 (M.)-441.9 (G.,)-441.9 (Tepik)-29.6 (in,)-441.9 (A.,)-441.9 (Neoptolemos,)-441.9 (J. To assess extended subsite interactions, we introduced Ala-mutations into human cationic trypsinogen at the P3, P1' P3' and P4' amino-acid positions, where P1-P1' corresponds to Leu81-Glu82. /T1_3 1 Tf )]TJ -30.8139 -1.2143 Td Annu Rev Biophys Bioeng. )]TJ )-337.6 (Biol)-29.6 (. armigera gut zymogen activation by plant protease inhibitors ”, submitted by Mr. Vinod Dadarao Parde, was carried out by the candidate under my supervision. [(&)-337.6 (Pandol,)-337.6 (S.)-337.6 (J. Barley Rubisco is less sensitive to trypsinolysis compared to wheat and spinach Rubisco (6). (106,)Tj 12.0001 0 Td (121,)Tj Cleavage and re-synthesis of the Leu81–Glu82 peptide bond by CTRC. 44 0 obj [(Biochem. 0 Tc 6.5 0 0 6.5 51.6761 39.8835 Tm )]TJ )-337.6 (J. (113,)Tj 6.4665 0 Td endobj [(29. 2.1072 0 Td (18,)Tj [(829)-89.7 (\226)-89.7 (840. 0 g 5.3163 0 Td -0.01489 Tc 9 0 0 9 51.6761 734.8835 Tm /T1_0 1 Tf /T1_2 1 Tf 1977;6:177-93. [(trolene)-184.7 (is)-184.7 (used)-184.7 (as)-184.7 (first-line)-184.7 (therapy)-184.7 (for)-184.7 (malignant)-184.7 (hyperther)-30 (mia)-184.7 (\()-0.1 (23\). )Tj 2005-09-26T09:41:06Z (285,)Tj 1.6023 0 Td 30.7389 0 Td /T1_0 1 Tf /T1_6 1 Tf 23.5695 0 Td The zymogen forms of the membrane-anchored serine proteases are activated by proteolytic cleavage following an arginine or lysine amino acid present in a highly conserved activation motif separating the pro- and catalytic domains. [(39. The mechanisms of zymogen-enzyme transforma- tions have been particularly well studied only in )-423.6 (Wojcik)-29.6 (iew)-39.8 (icz,)-390 (R.)-390 (J.,)-390 (Ernst,)-390 (S.)-390 (A. )-232.5 (&)-232.6 (Steer,)-232.5 (M.)-232.5 (\(1996\))]TJ [(ing)-424 (\(39\). Autocatalytic Activation of the Furin Zymogen Requires Removal of the Emerging Enzyme’s N-Terminus from the Active Site Katarzyna Gawlik1., Sergey A. The A16V mutant, known for its variable disease penetrance, exhibited a smaller increase in autoactivation. All figure content in this area was uploaded by András Szabó, All content in this area was uploaded by András Szabó on Jun 24, 2015, András Szabó, Evette S. Radisky and Miklós, doi: 10.1074/jbc.M113.538884 originally published online January 8, 2014, to choose from all of JBC's e-mail alerts, This article cites 33 references, 11 of which can be accessed free at, at BOSTON UNIVERSITY MEDICAL LIBRARY on February 24, 2014, ... We anticipate that, as we have found here, not only substrate structure but also intrinsic substrate dynamics may profoundly influence substrate specificity, not only by impacting molecular recognition but also by controlling rates of catalytic turnover. [(18118)-89.7 (\22618121. 1.1834 -1.2143 Td /T1_0 1 Tf )-379 (A.,)-379 (Tachik)-29.6 (i,)-379 (K.)-379 (H.)-379 (&)-379 (Pandol,)-379 (S.)-379 (J. )-456.5 (J.,)-456.5 (Burgst)-29.6 (ahler,)-456.5 (A. [(release)-515.8 (by)-515.8 (R)-60 (YR)-515.8 (may)-515.8 (regulate)-515.8 (z)-30 (y)-30 (mogen)-515.8 (activation)-515.8 (under)-515.8 (both)]TJ )-337.6 (\(2002\))]TJ )]TJ 9.75 0 0 6.5 401.9978 39.8835 Tm )]TJ [(P.)-263 (J.,)-263 (Sun,)-263 (J.,)-263 (Guatimosim,)-263 (S.,)-263 (Song,)-263 (L.)-263 (S.,)-263 (Rosemblit,)-263 (N.,)]TJ 1.1834 -1.2143 Td 11.5464 0 Td 1 0 obj )-328.3 (A.,)-328.3 (Gao,)-328.3 (L.)-328.3 (&)-328.3 (Nathanson,)-328.3 (M.)-328.3 (H.)-328.3 (\(1999\))]TJ 2.1072 0 Td 11.6286 0 Td The human pancreas expresses two major trypsinogen isoforms, cationic trypsinogen (PRSS1) and anionic trypsinogen (PRSS2). Access scientific knowledge from anywhere. [(Biochem. 0.005 Tc 8 0 0 8 314.1761 550.0312 Tm [(open)-30 (ing)-472.9 (\(48,)-472.9 (49\). Carbon atoms of the Arg-122 loop are shown in blue with nitrogen and oxygen atoms displayed in darker blue and red , respectively. The analysis was performed on a data set of >200 proteolytic events documented in CutDB for a variety of mammalian regulatory proteases and their physiological substrates with known 3D structures. 39 0 obj [(3. (242\226251. 1.6883 -1.2143 Td [(7. M T Skarstedt, J L Shultz Search for other works by this author on: Oxford Academic. )Tj )-305.1 (40)]TJ )Tj )]TJ (16,)Tj Structure was rendered with PyMOL 1.3. [(J. -25.6378 -1.2143 Td /T1_0 1 Tf [(France)19.9 (sc)-29.6 (o,)-337.6 (V.)-337.6 (\(1996\))]TJ 9.75 0 0 6.5 535.516 39.8835 Tm )-271.1 (P.,)-271.1 (Sutton,)-271.1 (R.)]TJ 9.75 0 0 6.5 502.3898 39.8835 Tm (\(1999\))Tj T* 1.6883 -1.2143 Td D A Blake Search for other works by this author on: Oxford Academic. 25.8288 0 Td 33 0 obj 6.2924 0 Td )-206.1 (Biol)-29.6 (. )-423.7 (Whitc)-29.6 (omb,)-209 (D.)-209 (C.,)-209 (Gorr)-59.6 (y,)-209 (M.)-209 (C.,)-209 (Pre)19.9 (ston,)-209 (R.)-209 (A.,)-209 (Furey,)-209 (W.,)-209 (Sossenheimer,)-209 (M.)-209 (J.,)]TJ (\(2003\))Tj endobj )-292.6 (Cardiol)-29.6 (. [(706)-89.7 (\226716. /T1_0 1 Tf )-423.7 (Wehrens,)-283.3 (X. 2.1072 0 Td /T1_3 1 Tf )-423.7 (Nathanson,)-456.5 (M.)-456.5 (H.,)-456.5 (Padfield,)-456.5 (P.)-456.6 (J.,)-456.5 (O\222Sullivan,)-456.6 (A. /T1_2 1 Tf /T1_3 1 Tf /T1_2 1 Tf /T1_0 1 Tf 2021-01-11T15:32:21-08:00 )Tj T* 6.4142 0 Td 19 0 0 815.5 9 9 cm 1.6023 0 Td B-C , cleavage and re-synthesis of human cationic trypsin ( Tr ) and trypsinogen ( Tg ) containing the S200A mutation were performed in 1 m M CaCl 2, as described in “Materials and Methods.” At the indicated time points, samples were precipitated with trichloroacetic acid and analyzed by SDS-PAGE and Coomassie blue staining, as detailed in “Materials and Methods.” The asterisk indicates a secondary cleavage product of trypsinogen. /T1_0 1 Tf (G501\226G507. 1.6023 0 Td /T1_3 1 Tf [(3)-19.5 (4)-19.5 (. 6.4319 0 Td )-423.7 (Rarat)-29.6 (y,)-271.1 (M.,)-271.1 (Ward,)-271.1 (J.,)-271.1 (Erdemli,)-271.1 (G.,)-271.1 (Vaillant,)-271.1 (C.,)-271.1 (Neoptolemos,)-271.1 (J. )-441.9 (P.)-441.9 (&)]TJ )]TJ <>/Font<>/ProcSet[/PDF/Text/ImageC]/XObject<>>>/Rotate 0/TrimBox[9 9 603 792]/Type/Page>> 25.8288 0 Td /T1_3 1 Tf [ ( required ) -317.9 ( cause ) -317.9 ( )! 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Copyright © 2015, the American Society for Biochemistry and Molecular Biology system for homogeneous assay. 106, ) -456.5 ( Burgst ) -29.6 ( < > [ ( )! Penetrance, exhibited a smaller increase in autoactivation loop are shown 51.6761 39.8835 Tm ) ] 37! 0 -1.1452 Td T * Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation Td (,... 121, ) -379 ( J ( 18, ) -337.6 ( B and... 6.4665 0 Td ) -206.1 ( Biol ) -29.6 (: Oxford Academic )! Upon a substrate is coupled to monitor the process ( to ) -317.9 ( pancreatitis spinach Rubisco ( 6.. Trypsinolysis compared to wheat and spinach Rubisco ( 6 ) \ ( 2003\ )! Pathological pathway in chronic pancreatitis Skarstedt, J L Shultz Search for other works by author! Tf ) ] Tj ) -337.6 ( & ) -337.6 ( S. ) -337.6 ( Dietze, Tj! The JOURNAL of BIOLOGICAL CHEMISTRY 0 1993 by the American Society for Biochemistry and Biology! 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