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Elevated serum levels of immunoreactive anionic trypsin (but not cationic trypsin) signals pancreatic disease

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Summary

Pancreatic juice from most studied species contains two major forms of trypsin, one with anionic electrophoretic mobility and one with cationic mobility. They are referred to as anionic and cationic trypsin(ogen). The purpose of this study was to measure immunoreactive anionic trypsin (irAT) and immunoreactive cationic trypsin (irCT) in sera from patients with pancreatic cancer (n=39) and chronic pancreatitis (n=32) using two specific ELISA methods. Sera from 72 healthy persons were used as controls. Patients with pancreatic cancer showed significantly elevated serum levels of irAT median level 39 vs 20.5 μg/L in the control group (p<0.001). No differences in irCT levels were found. The ratio between irAT and irCT in serum was significantly increased (p<0.001). Patients with chronic pancreatitis showed a wide range of both irAT and irCT levels, but no significant differences compared to the control group. The ratio between irAT and irCT was, however, significantly increased also in this group of patients. The results suggest a nonparallel secretion of anionic and cationic trypsinogen in pancreatic disease. This is a pattern that has been observed in experimental forms of chronic “hyperCCKemia.”

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Abbreviations

irAT:

immunoreactive anionic trypsin

irCT:

immunoreactive cationic trypsin

References

  1. Guy O, Lombardo D, Bartelt D, Amic J, Figarella C. Two human trypsinogens. Purification, molecular properties and N-terminal sequences.Biochemistry 1978; 17: 1669–1675.

    Article  PubMed  CAS  Google Scholar 

  2. Fletcher T, Alhadeff M, Craik C, Largman C. Isolation and characterisation of a cDNA encoding rat cationic trypsinogen.Biochemistry 1987; 26: 3081–3086.

    Article  PubMed  CAS  Google Scholar 

  3. Emi M, Nakamura Y, Ogawa M, Yamamoto T, Nishide T, Mori T, Matsubara K. Cloning, characterisation and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens. Gene 1986; 41: 305–310.

    Article  PubMed  CAS  Google Scholar 

  4. 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: 186–193.

    PubMed  CAS  Google Scholar 

  5. Figarella C, Negri GA, Guy O. The two human trypsinogens. Inhibition spectra of the two human trypsins derived from their purified zymogens.Eur J Biochem 1975: 53; 457–463.

    Article  PubMed  CAS  Google Scholar 

  6. Borgström A. Purification and N-terminal amino acid sequence determination of anionic and cationic canine trypsinogens.Hoppe-Seyler’s Z Physiol Chem 1979; 360: 657–661.

    PubMed  Google Scholar 

  7. Rinderknecht H, Renner IG, Carmack C. Trypsinogen variants in pancreatic juice of healthy volunteers, chronic alcoholics and patients with pancreatitis and cancer of the pancreas.Gut 1979; 20: 886–891.

    Article  PubMed  CAS  Google Scholar 

  8. Kimland M, Russick C, Marks WH, Borgström A. Immunoreactive anionic and cationic trypsin in human serum.Clin Chim Acta 1989; 184: 31–46.

    Article  PubMed  CAS  Google Scholar 

  9. Borgström A, Whelin L. Correlation between serum concentrations of three specific exocrine pancreatic proteins and pancreatic duct morphology at ERCP examinations.Scand J Gastroenterol 1984; 19: 220–227.

    PubMed  Google Scholar 

  10. Möller-Petersen J, Pedersen JO, Pedersen NT, Andersen BN. Serum cathodic trypsin-like immunoreactivity, pancreatic lipase and pancreatic isoamylase as diagnostic tests of chronic pancreatitis or pancreatic steatorrhea.Scand J Gastroenterol 1988; 23: 287–296.

    Article  PubMed  Google Scholar 

  11. Marks WH, Borgström A, Sollinger H, Marks C. Serum immunoreactive anodal trypsinogen and urinary amylase as biochemical markers for rejection of clinical whole-organ pancreas allografts having exocrine drainage into the urinary bladder.Transplantation 1990; 49: 112–115.

    Article  PubMed  CAS  Google Scholar 

  12. Borgström A, Marks WH, Dafoe DC, Campbell DA, Turcotte JG. Immunoreactive anionic and cationic trypsins in serum after experimental porcine pancreatic transplantation.Surgery 1986; 100: 841–848.

    PubMed  Google Scholar 

  13. Landin-Olsson M, Borgström A, Blom L, Sundqvist G, Lernmark Å. Immunoreactive trypsinogen in the sera of children with recent onset insulin dependent diabetes and matched controls.Pancreas 1990; 5: 241–247.

    Article  PubMed  CAS  Google Scholar 

  14. Fernandez E, Fallon MJ, Frazier ML, de Llorens R, Cuchillo CM. Expression of acinar and ductal products in Capan-1 cells growing in synthetic serum and serum-free media.Cancer 1994; 73: 2285–2295.

    Article  PubMed  CAS  Google Scholar 

  15. Marks WH, Ohlsson K, Polling Å. Immunocytochemical distribution of trypsinogen and pancreatic secretory trypsin inhibitor (PSTI) in normal and neoplastic tissue in man.Scand J Gastroenterol 1984; 19: 673–676.

    PubMed  CAS  Google Scholar 

  16. Otha T, Terada T, Nagakawa T, Tajima H, Itho H, Foneseca L, Miyazaki I. Pancreatic trypsinogen and cathepsin B in human pancreatic carcinomas and associated metastatic lesions.Br J Cancer 1994; 69: 152–156.

    Google Scholar 

  17. Schick J, Kern H, Scheele G. Hormonal stimulation in the exocrine pancreas results in coordinate and anticoordinate regulation of protein synthesis.J Cell Biol 1984; 99: 1569–1574.

    Article  PubMed  CAS  Google Scholar 

  18. Dakka N, Wicker C, Puigserver A. Specific response of serine protease mRNA to a protein-free diet in the rat pancreas.Eur J Biochem 1988; 176: 231–236

    Article  PubMed  CAS  Google Scholar 

  19. Borgström A, Axelson J, Ihse I, Rehfeld JF. The ratio between anionic and cationic trypsin in rat pancreas varies with CCK stimulation.Pancreas 1995; 11: 179–184.

    Article  PubMed  Google Scholar 

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Borgström, A., Andrén-Sandberg, Å. Elevated serum levels of immunoreactive anionic trypsin (but not cationic trypsin) signals pancreatic disease. Int J Pancreatol 18, 221–225 (1995). https://doi.org/10.1007/BF02784945

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  • DOI: https://doi.org/10.1007/BF02784945

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