Skip to main content
Log in

The measurement of serum immunoreactive pancreatic secretory trypsin inhibitor in gastrointestinal cancer and pancreatic disease

  • Reseach Papers
  • Published:
International journal of pancreatology Aims and scope Submit manuscript

Summary

The clinical usefulness of serum pancreatic secretory trypsin inhibitor (PSTI) in pancreatic disease and gastric and colorectal cancer has been examined.

The results showed that serum PSTI in acute pancreatitis was significantly higher than in normal subjects and it was also raised in acute exacerbations of chronic pancreatitis. Although the sensitivities of serum PSTI, amylase and elastase I were similar, serum PSTI in necrotizing hemorrhagic pancreatitis was 2.7 times higher than in mild acute pancreatitis. Only a few patients with chronic pancreatitis showed increased concentrations and the mean value was near normal.

The mean PSTI in patients with pancreatic and colorectal cancer was higher than normal, although that of gastric cancer was within normal limits. The sensitivity of serum PSTI measurements in patrents with these three malignant diseases was only about 30%.

The results suggested that the measurement of serum PSTI could be useful in the diagnosis of acute pancreatitis, but of limited value in the diagnosis of other disease which we examined.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Kazal LA, Spicer DS, Brakinsky RA. Isolation of a crystalline trypsin inhibitor/anticoagulant protein from pancreas. J Am Chem Soc 1948; 70:3034–3048.

    Article  PubMed  CAS  Google Scholar 

  2. Kitahara T, Takatsuka Y, Fugimoto K, Tanaka S, Ogawa M, Kosaki G. Radioimmunoassay for human pancreatic secretory trypsin inhibitor: Measurement of serum pancreatic secretory trypsin inhibitor in normal subjects and subjects with pancreatic disease. Clin Chim Acta 1980;103:135–143.

    Article  PubMed  CAS  Google Scholar 

  3. Eddeland A, Ohlsson K. A radioimmunoassay for measurement of human pancreatic secretory trypsin inhibitor in different body fluid. Hoppe Seyler's L Physiol Chem 1978;359:671–675.

    CAS  Google Scholar 

  4. Matsuda K, Ogawa M, Murata A, Kitahara T, Kosaki G. Elevation of serum immunoreactive pancreatic secretory trypsin inhibitor contents in various malignant disease. Res Commun Chem Pathol Pharmacol 1985;40:301–305.

    Google Scholar 

  5. Renner IG, Rinderknecht H, Douglas AP. Profiles of pure pancreatic secretion in patients with acute pancreatitis. The possible role of proteolytic enzymes in pathogenesis. Gastroenterology 1978;75:1090–1098.

    PubMed  CAS  Google Scholar 

  6. Allan BJ, Tournet R, White TT, Intraductal activation of pancreatic zymogens behind a carcinoma of the pancreas. Gastroenterology 1978;75:1090–1098.

    Google Scholar 

  7. Greene LJ, Giordans Jr JS. The structure of the bovine pancreatic secretory trypsin inhibitor-Kazal inhibitor. I. Isolation and amino acid sequences of the tryptic peptide from reduced aminoethylated inhibitor. J Biol Chem 1969;224:285–298.

    Google Scholar 

  8. Eddeland A, Ohlsson K. Purification of canine pancreatic secretory trypsin inhibitor and interaction in vitro with complexes of trypsin-α-macroglobulin. Scand J Clin Lab Invest 1976;46:815–820.

    Article  Google Scholar 

  9. Adham M, Dyce B, Wilding P, Wong T, Haverback BJ. Trypsin binding {ie331-1} patients with acute pancreatitis. Clin Res 1967;15:128.

    Google Scholar 

  10. Eddeland A, Ohlsson K. Studies on the pancreatic secretory trypsin inhibitor in plasma and in complex with trypsin in vivo and in vitro. Scan J Clin Lab Invest 1978;38:507–513.

    Article  CAS  Google Scholar 

  11. Eddeland A, Ohlsson K. The elimination in dogs of {ie331-2} complex inactivated by the Kazal or the Kunitz inhibitor. Hoppe-Seyler's L Physiol Chem 1978;359:379–384.

    CAS  Google Scholar 

  12. Marks WH, Ohlsson K. Elimination of pancreatic secretory trypsin inhibitor from the circulation. A study in man. Scand J Gastroenterol 1983;18:955–959.

    Article  PubMed  CAS  Google Scholar 

  13. Otsuki M, Oka T, Suehiro I, Okabayashi Y, Ohki A, Yuu H, Baba S. Serum pancreatic secretory trypsin inhibitor in acute pancreatitis. Lancet 1980;20:205.

    Google Scholar 

  14. Hunt LT, Barker WC, Dayhoff MO. Epidermoid growth factor: internal duplication and probable relationship to pancreatic secretory trypsin inhibitor. Biochem Biophys Res Commun 1974;60:1020–1028.

    Article  PubMed  CAS  Google Scholar 

  15. Scheving LA. Primary aminoacid sequence similarity between human epidermal growth factor-urogastrone. Human pancreatic secretory trypsin inhibitor and members of porcine secretin family. Arch Biochem Biophys 1983;226:411–413.

    Article  PubMed  CAS  Google Scholar 

  16. Ogawa M, Pancreatic secretory trypsin inhibitor—a historical review. The biliary Tract and Pancreas 1986;7:1–7.

    Google Scholar 

  17. Ogawa M, Malignant tumor and serum PSTI: Production and mechanism of PSTI in malignant tumor. In: Kosaki G, Ogawa M, eds. Pancreatic Secretory Trypsin Inhibitor Igakutoshoshupan Tokyo 1985;217–220.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Satake, K., Inui, A., Sogabe, T. et al. The measurement of serum immunoreactive pancreatic secretory trypsin inhibitor in gastrointestinal cancer and pancreatic disease. Int J Pancreatol 3, 323–331 (1988). https://doi.org/10.1007/BF02788466

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02788466

Key words

Navigation