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Volumn 2, Issue , 2002, Pages

Cathepsin B cleavage of the trypsinogen activation peptide

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN B; MUTANT PROTEIN; TRYPSINOGEN ACTIVATION PEPTIDE; OLIGOPEPTIDE;

EID: 18744403442     PISSN: 1471230X     EISSN: 1471230X     Source Type: Journal    
DOI: 10.1186/1471-230X-2-16     Document Type: Article
Times cited : (27)

References (19)
  • 2
    • 0032993541 scopus 로고    scopus 로고
    • A signal peptide cleavage site mutation in the cationic trypsinogen gene is strongly associated with chronic pancreatitis
    • Witt H, Luck W, Becker M: A signal peptide cleavage site mutation in the cationic trypsinogen gene is strongly associated with chronic pancreatitis. Gastroenterology 1999, 117:7-10
    • (1999) Gastroenterology , vol.117 , pp. 7-10
    • Witt, H.1    Luck, W.2    Becker, M.3
  • 3
    • 0033866202 scopus 로고    scopus 로고
    • Chronic pancreatitis associated with an activation peptide mutation that facilitates trypsin activation
    • Teich N, Ockenga J, Hoffmeister A, Manns M, Mössner J, Keim V: Chronic pancreatitis associated with an activation peptide mutation that facilitates trypsin activation. Gastroenterology 2000, 119:461-465
    • (2000) Gastroenterology , vol.119 , pp. 461-465
    • Teich, N.1    Ockenga, J.2    Hoffmeister, A.3    Manns, M.4    Mössner, J.5    Keim, V.6
  • 5
    • 0023904236 scopus 로고
    • Possible lysosomal activation of pancreatic zymogens. Activation of both human trypsinogens by cathepsin B and spontaneous acid. Activation of human trypsinogen 1
    • Figarella C, Miszczuk-Jamska B, Barrett AJ: Possible lysosomal activation of pancreatic zymogens. Activation of both human trypsinogens by cathepsin B and spontaneous acid. Activation of human trypsinogen 1. Biol Chem Hoppe Seyler 1988, 369:293-298
    • (1988) Biol. Chem. Hoppe Seyler , vol.369 , pp. 293-298
    • Figarella, C.1    Miszczuk-Jamska, B.2    Barrett, A.J.3
  • 8
    • 0037077262 scopus 로고    scopus 로고
    • Presence of cathepsin B in the human pancreatic secretory pathway and its role in trypsinogen activation during hereditary pancreatitis
    • Kukor Z, Mayerle J, Kruger B, Toth M, Steed PM, Halangk W, Lerch MM, Sahin-Toth M: Presence of cathepsin B in the human pancreatic secretory pathway and its role in trypsinogen activation during hereditary pancreatitis. J Biol Chem 2002
    • (2002) J. Biol. Chem.
    • Kukor, Z.1    Mayerle, J.2    Kruger, B.3    Toth, M.4    Steed, P.M.5    Halangk, W.6    Lerch, M.M.7    Sahin-Toth, M.8
  • 9
    • 0017229711 scopus 로고
    • The roles of cathepsins B1 and D in the digestion of cytoplasmic proteins in vitro by lysosomal extracts
    • Dean RT: The roles of cathepsins B1 and D in the digestion of cytoplasmic proteins in vitro by lysosomal extracts. Biochem Biophys Res Commun 1976, 68:518-523
    • (1976) Biochem. Biophys. Res. Commun. , vol.68 , pp. 518-523
    • Dean, R.T.1
  • 10
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S, Poole B: Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc Natl Acad Sci U S A 1978, 75:3327-3331
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 11
    • 0019887961 scopus 로고
    • ATP-dependent acidification of intact and disrupted lysosomes. Evidence for an ATP-driven proton pump
    • Schneider DL: ATP-dependent acidification of intact and disrupted lysosomes. Evidence for an ATP-driven proton pump. J Biol Chem 1981, 256:3858-3864
    • (1981) J. Biol. Chem. , vol.256 , pp. 3858-3864
    • Schneider, D.L.1
  • 12
    • 0025925346 scopus 로고
    • Alterations in the structure, physicochemical properties, and pH of hepatocyte lysosomes in experimental iron overload
    • Myers BM, Prendergast FG, Holman R, Kuntz SM, LaRusso NF: Alterations in the structure, physicochemical properties, and pH of hepatocyte lysosomes in experimental iron overload. J Clin Invest 1991, 88:1207-1215
    • (1991) J. Clin. Invest. , vol.88 , pp. 1207-1215
    • Myers, B.M.1    Prendergast, F.G.2    Holman, R.3    Kuntz, S.M.4    LaRusso, N.F.5
  • 13
  • 14
    • 0026530387 scopus 로고
    • Involvement of a non-proton pump factor (possibly Donnan-type equilibrium) in maintenance of an acidic pH in lysosomes
    • Moriyama Y, Maeda M, Futai M: Involvement of a non-proton pump factor (possibly Donnan-type equilibrium) in maintenance of an acidic pH in lysosomes. FEBS Lett 1992, 302:18-20
    • (1992) FEBS Lett. , vol.302 , pp. 18-20
    • Moriyama, Y.1    Maeda, M.2    Futai, M.3
  • 15
    • 0035816544 scopus 로고    scopus 로고
    • Comparative in vitro studies on native and recombinant human cationic trypsins. Cathepsin B is a possible pathological activator of trypsinogen in pancreatitis
    • Szilagyi L, Kenesi E, Katona G, Kaslik G, Juhasz G, Graf L: Comparative in vitro studies on native and recombinant human cationic trypsins. Cathepsin B is a possible pathological activator of trypsinogen in pancreatitis. J Biol Chem 2001, 276:24574-24580
    • (2001) J. Biol. Chem. , vol.276 , pp. 24574-24580
    • Szilagyi, L.1    Kenesi, E.2    Katona, G.3    Kaslik, G.4    Juhasz, G.5    Graf, L.6
  • 16
    • 0017138322 scopus 로고
    • Crystal structure of bovine trypsinogen at 1-8 A resolution. I. Data collection, application of patterson search techniques and preliminary structural interpretation
    • Bode W, Fehlhammer H, Huber R: Crystal structure of bovine trypsinogen at 1-8 A resolution. I. Data collection, application of patterson search techniques and preliminary structural interpretation. J Mol Biol 1976, 106:325-335
    • (1976) J. Mol. Biol. , vol.106 , pp. 325-335
    • Bode, W.1    Fehlhammer, H.2    Huber, R.3
  • 17
    • 0014500844 scopus 로고
    • The mechanism of activation of trypsinogen. The role of the four N-terminal aspartyl residues
    • Abita JP, Delaage M, Lazdunski M: The mechanism of activation of trypsinogen. The role of the four N-terminal aspartyl residues. Eur J Biochem 1969, 8:314-324
    • (1969) Eur. J. Biochem. , vol.8 , pp. 314-324
    • Abita, J.P.1    Delaage, M.2    Lazdunski, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.