메뉴 건너뛰기




Volumn 288, Issue 33, 2013, Pages 24049-24062

Autoactivation of mouse trypsinogens is regulated by chymotrypsin C via cleavage of the autolysis loop

Author keywords

[No Author keywords available]

Indexed keywords

AUTOACTIVATION; AUTOLYSIS LOOP; BIOCHEMICAL EFFECTS; DIFFERENT MECHANISMS;

EID: 84882398089     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.478800     Document Type: Article
Times cited : (32)

References (34)
  • 2
    • 33747010658 scopus 로고    scopus 로고
    • Mutations of human cationic trypsinogen (PRSS1) and chronic pancreatitis
    • Teich, N., Rosendahl, J., Tóth, M., Mössner, J., and Sahin-Tóth, M. (2006) Mutations of human cationic trypsinogen (PRSS1) and chronic pancreatitis. Hum. Mutat. 27, 721-730
    • (2006) Hum. Mutat. , vol.27 , pp. 721-730
    • Teich, N.1    Rosendahl, J.2    Tóth, M.3    Mössner, J.4    Sahin-Tóth, M.5
  • 3
    • 84862017112 scopus 로고    scopus 로고
    • Increased activation of hereditary pancreatitis-associated human cationic trypsinogen mutants in presence of chymotrypsin C
    • Szabó, A., and Sahin-Tóth, M. (2012) Increased activation of hereditary pancreatitis-associated human cationic trypsinogen mutants in presence of chymotrypsin C. J. Biol. Chem. 287, 20701-20710
    • (2012) J. Biol. Chem. , vol.287 , pp. 20701-20710
    • Szabó, A.1    Sahin-Tóth, M.2
  • 4
    • 33744960876 scopus 로고    scopus 로고
    • ChymotrypsinC(caldecrin) stimulates autoactivation of human cationic trypsinogen
    • Nemoda, Z., and Sahin-Tóth, M. (2006) ChymotrypsinC(caldecrin) stimulates autoactivation of human cationic trypsinogen. J. Biol. Chem. 281, 11879-11886
    • (2006) J. Biol. Chem. , vol.281 , pp. 11879-11886
    • Nemoda, Z.1    Sahin-Tóth, M.2
  • 5
    • 34547437254 scopus 로고    scopus 로고
    • ChymotrypsinC(caldecrin) promotes degradation of human cationic trypsin: Identity with Rinderknecht's enzyme y
    • Szmola, R., and Sahin-Tóth, M. (2007) ChymotrypsinC(caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y. Proc. Natl. Acad. Sci. U.S.A. 104, 11227-11232
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 11227-11232
    • Szmola, R.1    Sahin-Tóth, M.2
  • 7
    • 33845664588 scopus 로고    scopus 로고
    • A mouse model of hereditary pancreatitis generated by transgenic expression of R122H trypsinogen
    • Archer, H., Jura, N., Keller, J., Jacobson, M., and Bar-Sagi, D. (2006) A mouse model of hereditary pancreatitis generated by transgenic expression of R122H trypsinogen. Gastroenterology 131, 1844-1855
    • (2006) Gastroenterology , vol.131 , pp. 1844-1855
    • Archer, H.1    Jura, N.2    Keller, J.3    Jacobson, M.4    Bar-Sagi, D.5
  • 8
    • 0020418778 scopus 로고
    • Purification and properties of multiple forms of mouse trypsinogen
    • Watanabe, T., and Ogasawara, N. (1982) Purification and properties of multiple forms of mouse trypsinogen. Biochim. Biophys. Acta 717, 439-444
    • (1982) Biochim. Biophys. Acta , vol.717 , pp. 439-444
    • Watanabe, T.1    Ogasawara, N.2
  • 9
    • 0023047215 scopus 로고
    • Sequence organisation and transcriptional regulation of the mouse elastase II and trypsin genes
    • Stevenson, B. J., Hagenbüchle, O., and Wellauer, P. K. (1986) Sequence organisation and transcriptional regulation of the mouse elastase II and trypsin genes. Nucleic Acids Res. 14, 8307-8330
    • (1986) Nucleic Acids Res. , vol.14 , pp. 8307-8330
    • Stevenson, B.J.1    Hagenbüchle, O.2    Wellauer, P.K.3
  • 11
    • 0032883785 scopus 로고    scopus 로고
    • A homologue of pancreatic trypsin is localized in the acrosome of mammalian sperm and is released during acrosome reaction
    • Ohmura, K., Kohno, N., Kobayashi, Y., Yamagata, K., Sato, S., Kashiwabara, S., and Baba, T. (1999) A homologue of pancreatic trypsin is localized in the acrosome of mammalian sperm and is released during acrosome reaction. J. Biol. Chem. 274, 29426-29432
    • (1999) J. Biol. Chem. , vol.274 , pp. 29426-29432
    • Ohmura, K.1    Kohno, N.2    Kobayashi, Y.3    Yamagata, K.4    Sato, S.5    Kashiwabara, S.6    Baba, T.7
  • 12
    • 81855228093 scopus 로고    scopus 로고
    • Intra-acinar trypsinogen activation mediates early stages of pancreatic injury but not inflammation in mice with acute pancreatitis
    • Dawra, R., Sah, R. P., Dudeja, V., Rishi, L., Talukdar, R., Garg, P., and Saluja, A. K. (2011) Intra-acinar trypsinogen activation mediates early stages of pancreatic injury but not inflammation in mice with acute pancreatitis. Gastroenterology 141, 2210-2217
    • (2011) Gastroenterology , vol.141 , pp. 2210-2217
    • Dawra, R.1    Sah, R.P.2    Dudeja, V.3    Rishi, L.4    Talukdar, R.5    Garg, P.6    Saluja, A.K.7
  • 13
    • 84876493374 scopus 로고    scopus 로고
    • Caeruleininduced chronic pancreatitis does not require intra-acinar activation of trypsinogen in mice
    • Sah, R. P., Dudeja, V., Dawra, R. K., and Saluja, A. K. (2013) Caeruleininduced chronic pancreatitis does not require intra-acinar activation of trypsinogen in mice. Gastroenterology 144, 1076-1085
    • (2013) Gastroenterology , vol.144 , pp. 1076-1085
    • Sah, R.P.1    Dudeja, V.2    Dawra, R.K.3    Saluja, A.K.4
  • 14
    • 33646884384 scopus 로고    scopus 로고
    • Expression of human cationic trypsinogen with an authentic N terminus using intein-mediated splicing in aminopeptidase P-deficient Escherichia coli
    • Király, O., Guan, L., Szepessy, E., Tóth, M., Kukor, Z., and Sahin-Tóth, M. (2006) Expression of human cationic trypsinogen with an authentic N terminus using intein-mediated splicing in aminopeptidase P-deficient Escherichia coli. Protein Expr. Purif. 48, 104-111
    • (2006) Protein Expr. Purif. , vol.48 , pp. 104-111
    • Király, O.1    Guan, L.2    Szepessy, E.3    Tóth, M.4    Kukor, Z.5    Sahin-Tóth, M.6
  • 15
    • 0034725697 scopus 로고    scopus 로고
    • Human cationic trypsinogen. Role of Asn-21 in zymogen activation and implications in hereditary pancreatitis
    • Sahin-Tóth, M. (2000) Human cationic trypsinogen. Role of Asn-21 in zymogen activation and implications in hereditary pancreatitis. J. Biol. Chem. 275, 22750-22755
    • (2000) J. Biol. Chem. , vol.275 , pp. 22750-22755
    • Sahin-Tóth, M.1
  • 16
    • 0034687560 scopus 로고    scopus 로고
    • Gain-of-function mutations associated with hereditary pancreatitis enhance autoactivation of human cationic trypsinogen
    • Sahin-Tóth, M., and Tóth, M. (2000) Gain-of-function mutations associated with hereditary pancreatitis enhance autoactivation of human cationic trypsinogen. Biochem. Biophys. Res. Commun. 278, 286-289
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 286-289
    • Sahin-Tóth, M.1    Tóth, M.2
  • 18
    • 0032029774 scopus 로고    scopus 로고
    • Affinity purification of recombinant trypsinogen using immobilized ecotin
    • Lengyel, Z., Pál, G., and Sahin-Tóth, M. (1998) Affinity purification of recombinant trypsinogen using immobilized ecotin. Protein Expr. Purif. 12, 291-294
    • (1998) Protein Expr. Purif. , vol.12 , pp. 291-294
    • Lengyel, Z.1    Pál, G.2    Sahin-Tóth, M.3
  • 19
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 20
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum, H., Beier, H., and Gross, H. J. (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 21
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, V., Arold, N., Taube, D., and Ehrhardt, W. (1988) Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9, 255-262
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 22
    • 79952471865 scopus 로고    scopus 로고
    • Expression of recombinant proteins with uniform N termini
    • Király, O., Guan, L., and Sahin-Tóth, M. (2011) Expression of recombinant proteins with uniform N termini. Methods Mol. Biol. 705, 175-194
    • (2011) Methods Mol. Biol. , vol.705 , pp. 175-194
    • Király, O.1    Guan, L.2    Sahin-Tóth, M.3
  • 23
    • 84870056923 scopus 로고    scopus 로고
    • Determinants of chymotrypsin C cleavage specificity in the calcium-binding loop of human cationic trypsinogen
    • Szabó, A., and Sahin-Tóth, M. (2012) Determinants of chymotrypsin C cleavage specificity in the calcium-binding loop of human cationic trypsinogen. FEBS J. 279, 4283-4292
    • (2012) FEBS J. , vol.279 , pp. 4283-4292
    • Szabó, A.1    Sahin-Tóth, M.2
  • 24
    • 79959353475 scopus 로고    scopus 로고
    • High affinity small protein inhibitors of human chymotrypsin C (CTRC) selected by phage display reveal unusual preference for P4+ acidic residues
    • Szabó, A., Héja, D., Szakács, D., Zboray, K., Kékesi, K. A., Radisky, E. S., Sahin-Tóth, M., and Pál, G. (2011) High affinity small protein inhibitors of human chymotrypsin C (CTRC) selected by phage display reveal unusual preference for P4+ acidic residues. J. Biol. Chem. 286, 22535-22545
    • (2011) J. Biol. Chem. , vol.286 , pp. 22535-22545
    • Szabó, A.1    Héja, D.2    Szakács, D.3    Zboray, K.4    Kékesi, K.A.5    Radisky, E.S.6    Sahin-Tóth, M.7    Pál, G.8
  • 25
    • 0038029879 scopus 로고    scopus 로고
    • Human anionic trypsinogen: Properties of autocatalytic activation and degradation and implications in pancreatic diseases
    • Kukor, Z., Tóth, M., and Sahin-Tóth, M. (2003) Human anionic trypsinogen: properties of autocatalytic activation and degradation and implications in pancreatic diseases. Eur. J. Biochem. 270, 2047-2058
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2047-2058
    • Kukor, Z.1    Tóth, M.2    Sahin-Tóth, M.3
  • 26
    • 0040625000 scopus 로고    scopus 로고
    • Hereditary pancreatitis-associated mutation Asn21 Ile stabilizes rat trypsinogen in vitro
    • Sahin-Tóth, M. (1999) Hereditary pancreatitis-associated mutation Asn21 Ile stabilizes rat trypsinogen in vitro. J. Biol. Chem. 274, 29699-29704
    • (1999) J. Biol. Chem. , vol.274 , pp. 29699-29704
    • Sahin-Tóth, M.1
  • 27
    • 0014511660 scopus 로고
    • On some autolyzed derivatives of bovine trypsin
    • Maroux, S., and Desnuelle, P. (1969) On some autolyzed derivatives of bovine trypsin. Biochim. Biophys. Acta 181, 59-72
    • (1969) Biochim. Biophys. Acta , vol.181 , pp. 59-72
    • Maroux, S.1    Desnuelle, P.2
  • 28
    • 0037155148 scopus 로고    scopus 로고
    • Human cationic trypsinogen. Arg-117 is the reactive site of an inhibitory surface loop that controls spontaneous zymogen activation
    • Kukor, Z., Tóth, M., Pál, G., and Sahin-Tóth, M. (2002) Human cationic trypsinogen. Arg-117 is the reactive site of an inhibitory surface loop that controls spontaneous zymogen activation. J. Biol. Chem. 277, 6111-6117
    • (2002) J. Biol. Chem. , vol.277 , pp. 6111-6117
    • Kukor, Z.1    Tóth, M.2    Pál, G.3    Sahin-Tóth, M.4
  • 30
    • 77951785123 scopus 로고    scopus 로고
    • Relationship of straindependent susceptibility to experimentally induced acute pancreatitis with regulation of Prss1 and Spink3 expression
    • Wang, J., Ohmuraya, M., Suyama, K., Hirota, M., Ozaki, N., Baba, H., Nakagata, N., Araki, K., and Yamamura, K. (2010) Relationship of straindependent susceptibility to experimentally induced acute pancreatitis with regulation of Prss1 and Spink3 expression. Lab. Invest. 90, 654-664
    • (2010) Lab. Invest. , vol.90 , pp. 654-664
    • Wang, J.1    Ohmuraya, M.2    Suyama, K.3    Hirota, M.4    Ozaki, N.5    Baba, H.6    Nakagata, N.7    Araki, K.8    Yamamura, K.9
  • 33
    • 84876005351 scopus 로고    scopus 로고
    • Long-range electrostatic complementarity governs substrate recognition by human chymotrypsin C, a key regulator of digestive enzyme activation
    • Batra, J., Szabó, A., Caulfield, T. R., Soares, A. S., Sahin-Tóth, M., and Radisky, E. S. (2013) Long-range electrostatic complementarity governs substrate recognition by human chymotrypsin C, a key regulator of digestive enzyme activation. J. Biol. Chem. 288, 9848-9859
    • (2013) J. Biol. Chem. , vol.288 , pp. 9848-9859
    • Batra, J.1    Szabó, A.2    Caulfield, T.R.3    Soares, A.S.4    Sahin-Tóth, M.5    Radisky, E.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.