Skip to main content
Mediators of Inflammation logoLink to Mediators of Inflammation
. 1999;8(3):147–151. doi: 10.1080/09629359990478

Production of secretory leucocyte protease inhibitor (SLPI) in human pancreatic beta-cells.

M Nyström 1, M Bergenfeldt 1, I Ljungcrantz 1, A Lindeheim 1, K Ohlsson 1
PMCID: PMC1781797  PMID: 10704052

Abstract

Secretory leucocyte protease inhibitor (SLPI) is a potent inhibitor of granulocyte elastase and cathepsin G, and also an inhibitor of pancreatic enzymes like trypsin, chymotrypsin and pancreatic elastase. SLPI has also been shown to inhibit HIV-1 infections by blocking viral DNA synthesis. Since SLPI is an inhibitor of pancreatic proteases we wished to investigate whether SLPI was also actually produced in the pancreas. M-RNA from human pancreatic tissue showed evidence of SLPI production using the reverse transcriptase polymer chain reaction technique (RT-PCR). Using immunohistochemical methods SLPI was demonstrated in the beta-cells of the islets of Langerhans. The function could be local protease/antiprotease regulation or antiviral/antibacterial defence in the close vicinity of the cell surface, or even inside the beta-cell itself.

Full Text

The Full Text of this article is available as a PDF (739.0 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bergenfeldt M., Nyström M., Bohe M., Lindström C., Polling A., Ohlsson K. Localization of immunoreactive secretory leukocyte protease inhibitor (SLPI) in intestinal mucosa. J Gastroenterol. 1996 Feb;31(1):18–23. doi: 10.1007/BF01211182. [DOI] [PubMed] [Google Scholar]
  2. Casslén B., Rosengren M., Ohlsson K. Localization and quantitation of a low molecular weight proteinase inhibitor, antileukoprotease, in the human uterus. Hoppe Seylers Z Physiol Chem. 1981 Jul;362(7):953–961. doi: 10.1515/bchm2.1981.362.2.953. [DOI] [PubMed] [Google Scholar]
  3. De Water R., Willems L. N., Van Muijen G. N., Franken C., Fransen J. A., Dijkman J. H., Kramps J. A. Ultrastructural localization of bronchial antileukoprotease in central and peripheral human airways by a gold-labeling technique using monoclonal antibodies. Am Rev Respir Dis. 1986 May;133(5):882–890. [PubMed] [Google Scholar]
  4. Dietze S. C., Sommerhoff C. P., Fritz H. Inhibition of histamine release from human mast cells ex vivo by natural and synthetic chymase inhibitors. Biol Chem Hoppe Seyler. 1990 May;371 (Suppl):75–79. [PubMed] [Google Scholar]
  5. Fink E., Nettelbeck R., Fritz H. Inhibition of mast cell chymase by eglin c and antileukoprotease (HUSI-I). Indications for potential biological functions of these inhibitors. Biol Chem Hoppe Seyler. 1986 Jul;367(7):567–571. doi: 10.1515/bchm3.1986.367.2.567. [DOI] [PubMed] [Google Scholar]
  6. Franken C., Meijer C. J., Dijkman J. H. Tissue distribution of antileukoprotease and lysozyme in humans. J Histochem Cytochem. 1989 Apr;37(4):493–498. doi: 10.1177/37.4.2926127. [DOI] [PubMed] [Google Scholar]
  7. Fryksmark U., Ohlsson K., Polling A., Tegner H. Distribution of antileukoprotease in upper respiratory mucosa. Ann Otol Rhinol Laryngol. 1982 May-Jun;91(3 Pt 1):268–271. doi: 10.1177/000348948209100308. [DOI] [PubMed] [Google Scholar]
  8. Haendle H., Fritz H., Trautschold I., Werle E. Uber einen hormonabhängigen Inhibitor für proteolytische Enzyme in männlichen accessorischen Geschlechtsdrüsen und im Sperma. Hoppe Seylers Z Physiol Chem. 1965;343(1):185–188. [PubMed] [Google Scholar]
  9. Haendle H., Ingrisch H., Werle E. Uber einen neuen Trypsin-Chymotrypsin-Inhibitor im Cervixsekret der RFrau. Hoppe Seylers Z Physiol Chem. 1970 Apr;351(4):545–546. [PubMed] [Google Scholar]
  10. Hiemstra P. S., Maassen R. J., Stolk J., Heinzel-Wieland R., Steffens G. J., Dijkman J. H. Antibacterial activity of antileukoprotease. Infect Immun. 1996 Nov;64(11):4520–4524. doi: 10.1128/iai.64.11.4520-4524.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hochstrasser K., Reichert R., Schwarz S., Werle E. isolierung und Charakterisierung eines Proteaseninhibitors aus menschlichen Bronchialsekret. Hoppe Seylers Z Physiol Chem. 1972 Feb;353(2):221–226. [PubMed] [Google Scholar]
  12. Håkansson H. O., Ohlsson K. Influence of plasma proteinase inhibitors and the secretory leucocyte proteinase inhibitor on pancreatic elastase-induced degradation of some plasma proteins. Gastroenterol Jpn. 1992 Oct;27(5):652–656. doi: 10.1007/BF02774981. [DOI] [PubMed] [Google Scholar]
  13. Kramps J. A., Franken C., Meijer C. J., Dijkman J. H. Localization of low molecular weight protease inhibitor in serous secretory cells of the respiratory tract. J Histochem Cytochem. 1981 Jun;29(6):712–719. doi: 10.1177/29.6.6788837. [DOI] [PubMed] [Google Scholar]
  14. Masuda K., Kamimura T., Watanabe K., Suga T., Kanesaki M., Takeuchi A., Imaizumi A., Suzuki Y. Pharmacological activity of the C-terminal and N-terminal domains of secretory leukoprotease inhibitor in vitro. Br J Pharmacol. 1995 Jul;115(6):883–888. doi: 10.1111/j.1476-5381.1995.tb15892.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. McNeely T. B., Shugars D. C., Rosendahl M., Tucker C., Eisenberg S. P., Wahl S. M. Inhibition of human immunodeficiency virus type 1 infectivity by secretory leukocyte protease inhibitor occurs prior to viral reverse transcription. Blood. 1997 Aug 1;90(3):1141–1149. [PubMed] [Google Scholar]
  16. Nyström M., Bergenfeldt M., Ohlsson K. The elimination of secretory leukocyte protease inhibitor (SLPI) from the gastrointestinal tract in man. Scand J Clin Lab Invest. 1997 Apr;57(2):119–125. doi: 10.1080/00365519709056379. [DOI] [PubMed] [Google Scholar]
  17. Ohlsson K., Bjartell A., Lilja H. Secretory leucocyte protease inhibitor in the male genital tract: PSA-induced proteolytic processing in human semen and tissue localization. J Androl. 1995 Jan-Feb;16(1):64–74. [PubMed] [Google Scholar]
  18. Ohlsson K., Tegner H. Inhibition of elastase from granulocytes by the low molecular weight bronchial protease inhibitor. Scand J Clin Lab Invest. 1976 Sep;36(5):437–445. doi: 10.3109/00365517609054461. [DOI] [PubMed] [Google Scholar]
  19. Ohlsson M., Fryksmark U., Polling A., Tegner H., Ohlsson K. Localization of antileukoprotease in the parotid and the submandibular salivary glands. Acta Otolaryngol. 1984 Jul-Aug;98(1-2):147–151. doi: 10.3109/00016488409107547. [DOI] [PubMed] [Google Scholar]
  20. Ohlsson M., Rosengren M., Tegner H., Ohlsson K. Quantification of granulocyte elastase inhibitors in human mixed saliva and in pure parotid secretion. Hoppe Seylers Z Physiol Chem. 1983 Sep;364(9):1323–1328. doi: 10.1515/bchm2.1983.364.2.1323. [DOI] [PubMed] [Google Scholar]
  21. Schiessler H., Arnhold M., Ohlsson K., Fritz H. Inhibitors of acrosin and granulocyte proteinases from human genital tract secretions. Hoppe Seylers Z Physiol Chem. 1976 Sep;357(9):1251–1260. doi: 10.1515/bchm2.1976.357.2.1251. [DOI] [PubMed] [Google Scholar]
  22. Thompson R. C., Ohlsson K. Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6692–6696. doi: 10.1073/pnas.83.18.6692. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Wallner O., Fritz H. Characterization of an acid-stable proteinase inhibitor in human cervical mucus. Hoppe Seylers Z Physiol Chem. 1974 Jun;355(6):709–715. doi: 10.1515/bchm2.1974.355.1.709. [DOI] [PubMed] [Google Scholar]

Articles from Mediators of Inflammation are provided here courtesy of Wiley

RESOURCES