Human Trypsins

Handbook of Proteolytic Enzymes

Volumn 3, Issue , 2013, Pages 2600-2609

  Chen, Jian Min ^a   Radisky, Evette S ^b   Férec, Claude ^a  

^a INSERM   (France)

^b MAYO CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84884835033     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-382219-2.00576-7     Document Type: Chapter

References (66)

1. Haverback B.J., Dyce B., Bundy H., Edmondson H.A. Trypsin, trypsinogen and trypsin inhibitor in human pancreatic juice: Mechanism for pancreatitis associated with hyperparathyroidism. Am. J. Med. 1960, 29(3):424-433.
2. Buck F.F., Bier M., Nord F.F. Some properties of human trypsin. Arch. Biochem. Biophys. 1962, 98:528-530.
3. Keller P.J., Allan B.J. The protein composition of human pancreatic juice. J. Biol. Chem. 1967, 242(2):281-287.
4. Figarella C., Clemente F., Guy O. On zymogens of human pancreatic juice. FEBS Lett. 1969, 3(5):351-353.
5. Guy O., Lombardo D., Bartelt D.C., Amic J., Figarella C. Two human trypsinogens. Purification, molecular properties, and N-terminal sequences. Biochemistry 1978, 17(9):1669-1675.
6. Rinderknecht H., Renner I.G., Carmack C. Trypsinogen variants in pancreatic juice of healthy volunteers, chronic alcoholics, and patients with pancreatitis and cancer of the pancreas. Gut 1979, 20(10):886-891.
7. Rinderknecht H., Renner I.G., Abramson S.B., Carmack C. Mesotrypsin: a new inhibitor-resistant protease from a zymogen in human pancreatic tissue and fluid. Gastroenterology 1984, 86(4):681-692.
8. Scheele G., Bartelt D., Bieger W. Characterization of human exocrine pancreatic proteins by two-dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis. Gastroenterology 1981, 80(3):461-473.
9. Chen J.M., Férec C. Genes, cloned cDNAs, and proteins of human trypsinogens and pancreatitis-associated cationic trypsinogen mutations. Pancreas 2000, 21(1):57-62.
10. Emi M., Nakamura Y., Ogawa M., Yamamoto T., Nishide T., Mori T., Matsubara K. Cloning, characterization and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens. Gene 1986, 41(2-3):305-310.
11. Tani T., Kawashima I., Mita K., Takiguchi Y. Nucleotide sequence of the human pancreatic trypsinogen III cDNA. Nucleic Acids Res. 1990, 18(6):1631.
12. Nyaruhucha C.N., Kito M., Fukuoka S.I. Identification and expression of the cDNA-encoding human mesotrypsin(ogen), an isoform of trypsin with inhibitor resistance. J. Biol. Chem. 1997, 272(16):10573-10578.
13. Rowen L., Koop B.F., Hood L. The complete 685-kilobase DNA sequence of the human beta T cell receptor locus. Science 1996, 272(5269):1755-1762.
14. Rowen L., Williams E., Glusman G., Linardopoulou E., Friedman C., Ahearn M.E., Seto J., Boysen C., Qin S., Wang K., Kaur A., Bloom S., Hood L., Trask B.J. Interchromosomal segmental duplications explain the unusual structure of PRSS3, the gene for an inhibitor-resistant trypsinogen. Mol. Biol. Evol. 2005, 22(8):1712-1720.
15. Chen J.M., Montier T., Férec C. Molecular pathology and evolutionary and physiological implications of pancreatitis-associated cationic trypsinogen mutations. Hum. Genet. 2001, 109(3):245-252.
16. Hartley B.S. Homologies in serine proteinases. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 1970, 257(813):77-87.
17. Chen J.M., Férec C. Wanted: a consensus nomenclature for cationic trypsinogen mutations. Gastroenterology 2000, 119(1):277-278.
18. Craik C.S., Largman C., Fletcher T., Roczniak S., Barr P.J., Fletterick R., Rutter W.J. Redesigning trypsin: alteration of substrate specificity. Science 1985, 228(4697):291-297.
19. Roach J.C., Wang K., Gan L., Hood L. The molecular evolution of the vertebrate trypsinogens. J. Mol. Evol. 1997, 45(6):640-652.
20. Gaboriaud C., Serre L., Guy-Crotte O., Forest E., Fontecilla-Camps J.C. Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151. J. Mol. Biol. 1996, 259(5):995-1010.
21. Katona G., Berglund G.I., Hajdu J., Gráf L., Szilágyi L. Crystal structure reveals basis for the inhibitor resistance of human brain trypsin. J. Mol. Biol. 2002, 315(5):1209-1218.
22. Higaki J.N., Gibson B.W., Craik C.S. Evolution of catalysis in the serine proteases. Cold Spring Harb. Symp. Quant. Biol. 1987, 52:615-621.
23. Szepessy E., Sahin-Toth M. Human mesotrypsin exhibits restricted S1' subsite specificity with a strong preference for small polar side chains. FEBS J. 2006, 273(13):2942-2954.
24. Koistinen H., Koistinen R., Zhang W.M., Valmu L., Stenman U.H. Nexin-1 inhibits the activity of human brain trypsin. Neuroscience 2009, 160(1):97-102.
25. Salameh M.A., Soares A.S., Hockla A., Radisky E.S. Structural basis for accelerated cleavage of bovine pancreatic trypsin inhibitor (BPTI) by human mesotrypsin. J. Biol. Chem. 2008, 283(7):4115-4123.
26. Szmola R., Kukor Z., Sahin-Toth M. Human mesotrypsin is a unique digestive protease specialized for the degradation of trypsin inhibitors. J. Biol. Chem. 2003, 278(49):48580-48589.
27. Grishina Z., Ostrowska E., Halangk W., Sahin-Toth M., Reiser G. Activity of recombinant trypsin isoforms on human proteinase-activated receptors (PAR): mesotrypsin cannot activate epithelial PAR-1, -2, but weakly activates brain PAR-1. Br. J. Pharmacol. 2005, 146(7):990-999.
28. Knecht W., Cottrell G.S., Amadesi S., Mohlin J., Skaregarde A., Gedda K., Peterson A., Chapman K., Hollenberg M.D., Vergnolle N., Bunnett N.W. Trypsin IV or mesotrypsin and p23 cleave protease-activated receptors 1 and 2 to induce inflammation and hyperalgesia. J. Biol. Chem. 2007, 282(36):26089-26100.
29. Salameh M.A., Robinson J.L., Navaneetham D., Sinha D., Madden B.J., Walsh P.N., Radisky E.S. The amyloid precursor protein/protease nexin 2 Kunitz inhibitor domain is a highly specific substrate of mesotrypsin. J. Biol. Chem. 2010, 285(3):1939-1949.
30. Salameh M.A., Soares A.S., Navaneetham D., Sinha D., Walsh P.N., Radisky E.S. Determinants of affinity and proteolytic stability in interactions of Kunitz family protease inhibitors with mesotrypsin. J. Biol. Chem. 2010, 285(47):36884-36896.
31. Kassell B., Kay J. Zymogens of proteolytic enzymes. Science 1973, 180(90):1022-1027.
32. Maroux S., Rovery M., Desnuelle P. An autolyzed and still active form of bovine trypsin. Biochim. Biophys. Acta 1967, 140(2):377-380.
33. Ru B.G., Du J.Z., Zeng Y.H., Chen L.S., Ni Y.S., Tan G.H., Zhang L.X. Active products of porcine trypsin after autolysis. Sci. Sin. 1980, 23(11):1453-1460.
34. Li X.F., Nie X., Tang J.G. Anti-autolysis of trypsin by modification of autolytic site Arg117. Biochem. Biophys. Res. Commun. 1998, 250(2):235-239.
35. Varallyay E., Pal G., Patthy A., Szilágyi L., Gráf L. Two mutations in rat trypsin confer resistance against autolysis. Biochem. Biophys. Res. Commun. 1998, 243(1):56-60.
36. Sahin-Toth M., Toth M. Gain-of-function mutations associated with hereditary pancreatitis enhance autoactivation of human cationic trypsnogen. Biochem. Biophys. Res. Commun. 2000, 278(2):286-289.
37. Szilágyi L., Kenesi E., Katona G., Kaslik G., Juhasz G., Gráf 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(27):24574-24580.
38. Kukor Z., Toth M., Sahin-Toth M. Human anionic trypsinogen: properties of autocatalytic activation and degradation and implications in pancreatic diseases. Eur. J. Biochem. 2003, 270(9):2047-2058.
39. Kukor Z., Toth M., Pal G., Sahin-Toth M. Human cationic trypsinogen. Arg(117) is the reactive site of an inhibitory surface loop that controls spontaneous zymogen activation. J. Biol. Chem. 2002, 277(8):6111-6117.
40. Szmola R., Sahin-Toth M. Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y. Proc. Natl. Acad. Sci. USA 2007, 104(27):11227-11232.
41. Colomb E., Figarella C., Guy O. The two human trypsinogens. Evidence of complex formation with basic pancreatic trypsin inhibitor-proteolytic activity. Biochim. Biophys. Acta 1979, 570(2):397-405.
42. Colomb E., Guy O., Deprez P., Michel R., Figarella C. The two human trypsinogens: catalytic properties of the corresponding trypsins. Biochim. Biophys. Acta 1978, 525(1):186-193.
43. Witt H., Luck W., Hennies H.C., Classen M., Kage A., Lass U., Landt O., Becker M. Mutations in the gene encoding the serine protease inhibitor, Kazal type 1 are associated with chronic pancreatitis. Nat. Genet. 2000, 25(2):213-216.
44. Rosendahl J., Witt H., Szmola R., Bhatia E., Ozsvari B., Landt O., Schulz H.U., Gress T.M., Pfutzer R., Lohr M., Kovacs P., Bluher M., Stumvoll M., Choudhuri G., Hegyi P., te Morsche R.H., Drenth J.P., Truninger K., Macek M., Puhl G., Witt U., Schmidt H., Buning C., Ockenga J., Kage A., Groneberg D.A., Nickel R., Berg T., Wiedenmann B., Bodeker H., Keim V., Mossner J., Teich N., Sahin-Toth M. Chymotrypsin C (CTRC) variants that diminish activity or secretion are associated with chronic pancreatitis. Nat. Genet. 2008, 40(1):78-82.
45. Masson E., Chen J.M., Scotet V., Le Maréchal C., Férec C. Association of rare chymotrypsinogen C (CTRC) gene variations in patients with idiopathic chronic pancreatitis. Hum. Genet. 2008, 123(1):83-91.
46. Sherwood M.W., Prior I.A., Voronina S.G., Barrow S.L., Woodsmith J.D., Gerasimenko O.V., Petersen O.H., Tepikin A.V. Activation of trypsinogen in large endocytic vacuoles of pancreatic acinar cells. Proc. Natl. Acad. Sci. USA 2007, 104(13):5674-5679.
47. van Acker G.J., Perides G., Steer M.L. Co-localization hypothesis: a mechanism for the intrapancreatic activation of digestive enzymes during the early phases of acute pancreatitis. World J. Gastroenterol. 2006, 12(13):1985-1990.
48. Greenbaum L.M., Hirshkowitz A., Shoichet I. The activation of trypsinogen by cathepsin B. J. Biol. Chem. 1959, 234:2885-2890.
49. Figarella C., Miszczuk-Jamska B., Barrett A.J. 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(Suppl):293-298.
50. Halangk W., Lerch M.M., Brandt-Nedelev B., Roth W., Ruthenbuerger M., Reinheckel T., Domschke W., Lippert H., Peters C., Deussing J. Role of cathepsin B in intracellular trypsinogen activation and the onset of acute pancreatitis. J. Clin. Invest. 2000, 106(6):773-781.
51. Kukor Z., Mayerle J., Kruger B., Toth M., Steed P.M., Halangk W., Lerch M.M., 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, 277(24):21389-21396.
52. Mahurkar S., Idris M.M., Reddy D.N., Bhaskar S., Rao G.V., Thomas V., Singh L., Chandak G.R. Association of cathepsin B gene polymorphisms with tropical calcific pancreatitis. Gut 2006, 55(9):1270-1275.
53. Weiss F.U., Behn C.O., Simon P., Ruthenburger M., Halangk W., Lerch M.M. Cathepsin B gene polymorphism Val26 is not associated with idiopathic chronic pancreatitis in European patients. Gut 2007, 56(9):1322-1323.
54. Witt H., Bhatia E. Genetic aspects of tropical calcific pancreatitis. Rev. Endocr. Metab. Disord. 2008, 9(3):213-226.
55. Bohe M., Borgstrom A., Lindstrom C., Ohlsson K. Pancreatic endoproteases and pancreatic secretory trypsin inhibitor immunoreactivity in human Paneth cells. J. Clin. Pathol. 1986, 39(7):786-793.
56. Wiegand U., Corbach S., Minn A., Kang J., Muller-Hill B. Cloning of the cDNA encoding human brain trypsinogen and characterization of its product. Gene 1993, 136(1-2):167-175.
57. Nemeth A.L., Medveczky P., Toth J., Siklodi E., Schlett K., Patthy A., Palkovits M., Ovadi J., Tokesi N., Nemeth P., Szilágyi L., Gráf L. Unconventional translation initiation of human trypsinogen 4 at a CUG codon with an N-terminal leucine. A possible means to regulate gene expression. FEBS J. 2007, 274(6):1610-1620.
58. Paju A., Stenman U.H. Biochemistry and clinical role of trypsinogens and pancreatic secretory trypsin inhibitor. Crit. Rev. Clin. Lab. Sci. 2006, 43(2):103-142.
59. Itkonen O. Human trypsinogens in the pancreas and in cancer. Scand. J. Clin. Lab. Invest. 2010, 70(2):136-143.
60. Koivunen E., Huhtala M.L., Stenman U.H. Human ovarian tumor-associated trypsin. Its purification and characterization from mucinous cyst fluid and identification as an activator of pro-urokinase. J. Biol. Chem. 1989, 264(24):14095-14099.
61. Paju A., Bjartell A., Zhang W.M., Nordling S., Borgstrom A., Hansson J., Stenman U.H. Expression and characterization of trypsinogen produced in the human male genital tract. Am. J. Pathol. 2000, 157(6):2011-2021.
62. Sahin-Toth M., Kukor Z., Nemoda Z. Human cationic trypsinogen is sulfated on Tyr154. FEBS J. 2006, 273(22):5044-5050.
63. Itkonen O., Helin J., Saarinen J., Kalkkinen N., Ivanov K.I., Stenman U.H., Valmu L. Mass spectrometric detection of tyrosine sulfation in human pancreatic trypsinogens, but not in tumor-associated trypsinogen. FEBS J. 2008, 275(2):289-301.
64. Chen J.M., Férec C. Trypsinogen genes: evolution. Nature Encyclopedia of the Human Genome 2003, vol. 5:645-650. Macmillan Publishers Ltd., Nature Publishing Group, London.
65. Nakanishi J., Yamamoto M., Koyama J., Sato J., Hibino T. Keratinocytes synthesize enteropeptidase and multiple forms of trypsinogen during terminal differentiation. J. Invest. Dermatol. 2010, 130(4):944-952.
66. Chen J.M., Férec C. Chronic pancreatitis: genetics and pathogenesis. Annu. Rev. Genomics Hum. Genet. 2009, 10:63-87.