Skip to main content
Infection and Immunity logoLink to Infection and Immunity
. 1985 May;48(2):389–394. doi: 10.1128/iai.48.2.389-394.1985

Levels of salivary lysozyme, lactoperoxidase, and lactoferrin in diabetic hamsters.

K Muratsu, T Morioka
PMCID: PMC261321  PMID: 2580790

Abstract

In an attempt to clarify the mechanism(s) of increased susceptibility to oral infection in diabetics, we examined the levels of salivary antibacterial factors, including lysozyme, lactoperoxidase, and lactoferrin, in diabetic hamsters whose condition was induced with streptozotocin. Saliva was collected from these hamsters periodically for 19 weeks after the administration of streptozotocin. Diabetes persisted with significant hyperglycemia throughout the experiment after a single injection of streptozotocin. There was no significant difference between groups in the amount of saliva secreted. In diabetic hamsters, lysozyme activity decreased by 56% and lactoperoxidase activity decreased by 53% compared with the control hamsters 19 weeks after the administration of streptozotocin. There was no significant difference between groups in the amount of salivary lactoferrin. However, the ratio of lactoferrin to total protein increased to approximately double the amount of that of the control hamsters. Insulin treatment had a significant effect on lysozyme and lactoperoxidase activity, recovering 73 and 74% those of the controls, respectively, and the ratio of lactoferrin to total salivary protein reverted to normal values. Growth inhibition of Lactobacillus plantarum ATCC 8014 with whole saliva and amylase activity significantly decreased in diabetic hamsters. The position of each protein band of whole saliva on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was almost the same for control and diabetic hamsters; however, there was some variability in band intensity.

Full text

PDF
389

Images in this article

Selected References

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

  1. Arnold R. R., Brewer M., Gauthier J. J. Bactericidal activity of human lactoferrin: sensitivity of a variety of microorganisms. Infect Immun. 1980 Jun;28(3):893–898. doi: 10.1128/iai.28.3.893-898.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Aune T. M., Thomas E. L. Accumulation of hypothiocyanite ion during peroxidase-catalyzed oxidation of thiocyanate ion. Eur J Biochem. 1977 Oct 17;80(1):209–214. doi: 10.1111/j.1432-1033.1977.tb11873.x. [DOI] [PubMed] [Google Scholar]
  3. BYBEE J. D., ROGERS D. E. THE PHAGOCYTIC ACTIVITY OF POLYMORPHONUCLEAR LEUKOCYTES OBTAINED FROM PATIENTS WITH DIABETES MELLITUS. J Lab Clin Med. 1964 Jul;64:1–13. [PubMed] [Google Scholar]
  4. Bagdade J. D., Root R. K., Bulger R. J. Impaired leukocyte function in patients with poorly controlled diabetes. Diabetes. 1974 Jan;23(1):9–15. doi: 10.2337/diab.23.1.9. [DOI] [PubMed] [Google Scholar]
  5. Björck L., Rosén C., Marshall V., Reiter B. Antibacterial activity of the lactoperoxidase system in milk against pseudomonads and other gram-negative bacteria. Appl Microbiol. 1975 Aug;30(2):199–204. doi: 10.1128/am.30.2.199-204.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bullen J. J., Rogers H. J., Leigh L. Iron-binding proteins in milk and resistance to Escherichia coli infection in infants. Br Med J. 1972 Jan 8;1(5792):69–75. doi: 10.1136/bmj.1.5792.69. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Casey J. I., Heeter B. J., Klyshevich K. A. Impaired response of lymphocytes of diabetic subjects to antigen of Staphylococcus aureus. J Infect Dis. 1977 Oct;136(4):495–501. doi: 10.1093/infdis/136.4.495. [DOI] [PubMed] [Google Scholar]
  8. Cutler L. S., Pinney H. E., Christian C., Russotto S. B. Ultrastructural studies of the rat submandibular gland in streptozotocin induced diabetes mellitus. Virchows Arch A Pathol Anat Histol. 1979 Jun 29;382(3):301–311. doi: 10.1007/BF00430406. [DOI] [PubMed] [Google Scholar]
  9. Dawes C. The composition f human saliva secreted in response to a gustatory stimulus and to pilocaprine. J Physiol. 1966 Mar;183(2):360–368. doi: 10.1113/jphysiol.1966.sp007870. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Delespesse G., Duchateau J., Bastenie P. A., Lauvaux J. P., Collet H., Govaerts A. Cell-mediated immunity in diabetes mellitus. Clin Exp Immunol. 1974 Dec;18(4):461–467. [PMC free article] [PubMed] [Google Scholar]
  11. Golub L. M., Schneir M., Ramamurthy N. S. Enhanced collagenase activity in diabetic rat gingiva: in vitro and in vivo evidence. J Dent Res. 1978 Mar;57(3):520–525. doi: 10.1177/00220345780570032101. [DOI] [PubMed] [Google Scholar]
  12. Hoogendoorn H., Piessens J. P., Scholtes W., Stoddard L. A. Hypothiocyanite ion; the inhibitor formed by the system lactoperoxidase-thiocyanate-hydrogen peroxide. I. Identification of the inhibiting compound. Caries Res. 1977;11(2):77–84. doi: 10.1159/000260252. [DOI] [PubMed] [Google Scholar]
  13. Hugoson A., Koch G., Thilander H., Hoogendoorn H. Lactoperoxidase in the prevention of plaque accumulation, gingivitis and dental caries. 3. Effect of mouthrinses with amyloglucosidase and glucoseoxidase in the model system of experimental gingivitis and caries in man. Odontol Revy. 1974;25(1):69–80. [PubMed] [Google Scholar]
  14. Iacono V. J., MacKay B. J., DiRienzo S., Pollock J. J. Selective antibacterial properties of lysozyme for oral microorganisms. Infect Immun. 1980 Aug;29(2):623–632. doi: 10.1128/iai.29.2.623-632.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Iwamoto Y., Matsumura T. Purification and characterization of the salivary antibacterial factor (S.A. factor). Arch Oral Biol. 1966 Jul;11(7):667–676. doi: 10.1016/0003-9969(66)90092-6. [DOI] [PubMed] [Google Scholar]
  16. Koch G., Edlund K., Hoogendoorn H. Lactoperoxidase in the prevention of plaque accumulation, gingivitis and dental caries. II. Effect of mouthrinses with amyloglucosidase and glucoseoxidase on plaque accumulation on teeth in individuals on a sucrose diet. Odontol Revy. 1973;24(4):367–372. [PubMed] [Google Scholar]
  17. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  18. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  19. Lehrer R. I. Antifungal effects of peroxidase systems. J Bacteriol. 1969 Aug;99(2):361–365. doi: 10.1128/jb.99.2.361-365.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. MacCuish A. C., Urbaniak S. J., Campbell C. J., Duncan L. J., Irvine W. J. Phytohemagglutinin transformation and circulating lymphocyte subpopulations in insulin-dependent diabetic patients. Diabetes. 1974 Aug;23(8):708–712. doi: 10.2337/diab.23.8.708. [DOI] [PubMed] [Google Scholar]
  21. Mahmoud A. A., Cheever A. W., Warren K. S. Streptozotocin-induced diabetes mellitus and the host-parasite relation in murine schistosomiasis mansoni. J Infect Dis. 1975 Jun;131(6):634–642. doi: 10.1093/infdis/131.6.634. [DOI] [PubMed] [Google Scholar]
  22. Mancini G., Carbonara A. O., Heremans J. F. Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry. 1965 Sep;2(3):235–254. doi: 10.1016/0019-2791(65)90004-2. [DOI] [PubMed] [Google Scholar]
  23. Manouchehr-Pour M., Spagnuolo P. J., Rodman H. M., Bissada N. F. Impaired neutrophil chemotaxis in diabetic patients with severe periodontitis. J Dent Res. 1981 Mar;60(3):729–730. doi: 10.1177/00220345810600031101. [DOI] [PubMed] [Google Scholar]
  24. Marder M. Z., Abelson D. C., Mandel I. D. Salivary alterations in diabetes mellitus. J Periodontol. 1975 Sep;46(9):567–569. doi: 10.1902/jop.1975.46.9.567. [DOI] [PubMed] [Google Scholar]
  25. Matsumura T. [Analyses of monosaccharides in parotid saliva obtained from normal and diabetic animals]. Osaka Daigaku Shigaku Zasshi. 1979 Jun;24(1):40–53. [PubMed] [Google Scholar]
  26. Mowat A., Baum J. Chemotaxis of polymorphonuclear leukocytes from patients with diabetes mellitus. N Engl J Med. 1971 Mar 25;284(12):621–627. doi: 10.1056/NEJM197103252841201. [DOI] [PubMed] [Google Scholar]
  27. Nolan C. M., Beaty H. N., Bagdade J. D. Further characterization of the impaired bactericidal function of granulocytes in patients with poorly controlled diabetes. Diabetes. 1978 Sep;27(9):889–894. doi: 10.2337/diab.27.9.889. [DOI] [PubMed] [Google Scholar]
  28. Pruitt K. M., Adamson M., Arnold R. Lactoperoxidase binding to streptococci. Infect Immun. 1979 Jul;25(1):304–309. doi: 10.1128/iai.25.1.304-309.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. RAKIETEN N., RAKIETEN M. L., NADKARNI M. R. Studies on the diabetogenic action of streptozotocin (NSC-37917). Cancer Chemother Rep. 1963 May;29:91–98. [PubMed] [Google Scholar]
  30. ROGOSA M., MITCHELL J. A., WISEMAN R. F. A selective medium for the isolation and enumeration of oral lactobacilli. J Dent Res. 1951 Oct;30(5):682–689. doi: 10.1177/00220345510300051201. [DOI] [PubMed] [Google Scholar]
  31. SALTON M. R. The anatomy of the bacterial surface. Bacteriol Rev. 1961 Jun;25:77–99. doi: 10.1128/br.25.2.77-99.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. SMOLELIS A. N., HARTSELL S. E. Factors affecting the lytic activity of lysozyme. J Bacteriol. 1952 May;63(5):665–674. doi: 10.1128/jb.63.5.665-674.1952. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Steele W. F., Morrison M. Antistreptococcal activity of lactoperoxidase. J Bacteriol. 1969 Feb;97(2):635–639. doi: 10.1128/jb.97.2.635-639.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Tabak L., Mandel I. D., Herrera M., Baurmash H. Changes in lactoferrin and other proteins in a case of chronic recurrent parotitis. J Oral Pathol. 1978 Apr;7(2):91–99. doi: 10.1111/j.1600-0714.1978.tb01583.x. [DOI] [PubMed] [Google Scholar]
  35. Tabak L., Mandel I. D., Karlan D., Baurmash H. Alterations in lactoferrin in salivary gland disease. J Dent Res. 1978 Jan;57(1):43–47. doi: 10.1177/00220345780570011801. [DOI] [PubMed] [Google Scholar]
  36. Tenovuo J., Mansson-Rahemtulla B., Pruitt K. M., Arnold R. Inhibition of dental plaque acid production by the salivary lactoperoxidase antimicrobial system. Infect Immun. 1981 Oct;34(1):208–214. doi: 10.1128/iai.34.1.208-214.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Wolf J. Dental and periodontal conditions in diabetes mellitus. A clinical and radiographic study. Proc Finn Dent Soc. 1977;73(4-6):1–56. [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES