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Indian Journal of Clinical Biochemistry logoLink to Indian Journal of Clinical Biochemistry
. 1998 Jan;13(1):46–51. doi: 10.1007/BF02873443

Salivary proteolytic activities in periodontitis, gingivitis and diabetes mellitus

Praveen Kumar Shetty 1,, T N Pattabiraman 1
PMCID: PMC3453535  PMID: 23105183

Abstract

Elastase activity was found to be significantly increased in periodontitis (0.872±0.4270 absorbance units/mg protein, mean±S. D., 1.05±0.61 units/ml saliva), gingivitis (0.772±0.416 units/mg protein, 1.515±0.952 units/ml) and diabetes (0.549±0.286 units/mg protein, 1.20±0.769 units/ml) compared to normals (0.255±0.089) units/mg protein, 0.264±0.079 units/ml). Chymotryptic activity was not found to be increased in these disease conditions over the normal level (0.284±0.096 units/mg protein). Aminopeptidase activity was elevated only in periodontitis (0.670+0.140 units/mg protein) compared to normals (0.349±0.100 units/mg protein). Trypsin-like activity was also found to be significantly raised in periodontitis compared to normals when Pro-Phe-Arg-p-nitroanilide (0.666±0.204 units/mg protein), Ile-Pro-Arg-p-nitroanilide (1.59±0.260 units/mg protein) and Pyroglu-Pro-Arg-p-nitroanilide (1.82±0.380 units/mg protein) were used as substrates. The normal values with these three substrates were respectively, 0.454±0.110, 1.04±0.231 and 1.15±0.312 units/mg protein. Total protein level in saliva was found to be significantly elevated in gingivitis (209±66.8 mg/dl) and diabetes (204±68.0) compared to normal values (107±20.7). Increase in periodontitis was marginal (127±28.3 mg/dl). Expression of proteolytic activities normalized to protein level was useful in differential diagnosis. Increase in elastase level in saliva is not a specific marker for periodontal diseases.

Key Words: Elastase, Proteases, Saliva, Periodontitis, Gingivitis, Diabetes mellitus

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Referneces

  • 1.Nakamura M., Slots J. Salivary enzymes: Origin and relationship to periodontal disease. J. Periodont. Res. 1983;18:559–569. doi: 10.1111/j.1600-0765.1983.tb00393.x. [DOI] [PubMed] [Google Scholar]
  • 2.Matsuda Y., Fujimoto Y., Watanabe Y., Obara T., Akhihama S. Human salivary kallikrein and submaxillary gland kallikreins. Adv. Expt. Med. Biol. 1989;247/B:169–175. doi: 10.1007/978-1-4615-9546-5_28. [DOI] [PubMed] [Google Scholar]
  • 3.Lijima K., Ando M., Nakashizuka J., Hayakawa T. Collagenase activity in human saliva. J. Dent. Res. 1983;62:709–712. doi: 10.1177/00220345830620060301. [DOI] [PubMed] [Google Scholar]
  • 4.Gustaffson A., Asman B., Bergstrom K., Soder P. O. Granulocyte elastase in gingival crevicular fluid. A possible discriminator between gingivitis and periodontitis. J. Clin. Periodont. 1992;19:535–540. doi: 10.1111/j.1600-051X.1992.tb00680.x. [DOI] [PubMed] [Google Scholar]
  • 5.Cox, S. W. Detection of cathepsin B and L, elastase, tryptase, trypsin and dipeptidyl peptidase IV like activities in crevicular fluid from gingivitis and periodontitis patients with peptidyl derivatives of 7-amino 4-trifluoromethyl coumarin. J. Periodont. Res. 24, 353–361. [DOI] [PubMed]
  • 6.Piotrowski J., Czajkowski A., Murty V. L., Slomiany A., Slomiany B. L. Identification of human salivary protease activity towards mucin. Differences with caries. Biochem. Int. 1992;28:939–947. [PubMed] [Google Scholar]
  • 7.Loesche W. J., Syed S. A., Stoll J. Trypsin-like activity in sublingual plaque. A diagnostic marker for spirochetes and periodontal disease. J. Periodontol. 1987;58:266–273. doi: 10.1902/jop.1987.58.4.266. [DOI] [PubMed] [Google Scholar]
  • 8.Palconis K. G., Larjava I. K., Wells B. R., Suggs K. A., Landis J. R., Chadwick D. E., Jeffcoat M. K. Elastase as an indicator of peridontal disease progression. J. Periodontol. 1992;63:237–242. doi: 10.1902/jop.1992.63.4.237. [DOI] [PubMed] [Google Scholar]
  • 9.Armitage G. C., Jeffcoat M. K., Chadwick D. E., Taggart E. J., Numabe Y., Landis J. R., Weaver S. L., Sharp T. J. Longitudinal evaluation of elastase as a marker for the progression of periodontitis. J. Periodontol. 1994;65:120–128. doi: 10.1902/jop.1994.65.2.120. [DOI] [PubMed] [Google Scholar]
  • 10.Uitto V. J., Nieminen A., Coil J., Hurttia H., Larja H. Oral fluid elastase activity as an idicator of periodontal health. J. Clin. Periodontol. 1996;23:30–37. doi: 10.1111/j.1600-051X.1996.tb00501.x. [DOI] [PubMed] [Google Scholar]
  • 11.Darany D. G., Beck F. M., Walters J. D. The relationship of gingival fluid leukocyte elastase activity to gingival fluid flow rate. J. Periodontol. 1992;63:743–747. doi: 10.1902/jop.1992.63.9.743. [DOI] [PubMed] [Google Scholar]
  • 12.Akalin F. A., Sengun D., Eratalay K., Renda N., Caglayan G. Hydroxyproline and total protein levels in gingiva and gingival crevicular fluid in patients with juvenile, rapidly progressive and adult periodontitis. J. Periodontol. 1993;64:323–329. doi: 10.1902/jop.1993.64.5.323. [DOI] [PubMed] [Google Scholar]
  • 13.Henskens Y. M. C., Velden U., Veerman E. C. I., Amerogen A. V. N. Protein albumin and cystatin concentrations in saliva of healthy subjects and of patients with gingivitis or periodontitis. J. Periodont. Res. 1993;28:43–48. doi: 10.1111/j.1600-0765.1993.tb01049.x. [DOI] [PubMed] [Google Scholar]
  • 14.Kertesz P., Banoczy J., Koesis L. Salivary proteins in healthy and diabetic subjects. J. Dent. Res. 1994;73:421–424. [Google Scholar]
  • 15.Smith K. P., Krohn I. R., Hermanson G. T., Mallia K. A., Gartner H. F., Provenzano D. M., Fujc moto K. E., Goekan N. M., Olson B. J., Klenk D. C. Measurement of protein using bicinchoninic acid. Anal. Biochem. 1985;150:76–82. doi: 10.1016/0003-2697(85)90442-7. [DOI] [PubMed] [Google Scholar]
  • 16.Rinderknecht H., Geokas M. C., Silverman P., Haverback B. J. A new ultra sensitive method for the determination of proteolytic activity. Clin. Chim. Acta. 1968;21(2):197–203. doi: 10.1016/0009-8981(68)90127-7. [DOI] [PubMed] [Google Scholar]
  • 17.Kabivitrum bulletin on synthetic chromogenic substrates, page 6, 1983.
  • 18.Erlanger R. F., Kokowsky N., Cohen W. The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 1961;95:271–278. doi: 10.1016/0003-9861(61)90145-X. [DOI] [PubMed] [Google Scholar]

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