PMN responses in chronic periodontal disease: evaluation by gingival crevicular fluid enzymes and elastase-alpha-1-proteinase inhibitor complex.
OBJECTIVE
In the present trial, the hypothesis was examined that the local PMN responses in untreated and treated chronic periodontitis can be differentiated by gingival crevicular fluid lysosomal enzyme activities and elastase-alpha-1-proteinase inhibitor complex.


METHODS
In nine subjects (average age 49.2 +/- 7.1 years) with chronic periodontitis, clinical parameters and markers of the PMN-derived inflammatory tissue response in gingival crevicular fluid (GCF) were assessed before and 6 months after surgical periodontal therapy. Myeloperoxidase (MPO), beta-N-acetyl-hexosaminidase (beta-NAH) and cathepsin D (CD) were analyzed as indicators of the PMN-associated host tissue destruction, and elastase-alpha-1-proteinase inhibitor complex (alpha-1-EPI) as the major serum protein inactivating PMN elastase. The total activities of the lysosomal enzymes MPO and beta-NAH were evaluated spectrophotometrically, the CD levels by liquid scintillation counting with [14C] hemoglobin as substrate, and the total alpha-1-proteinase inhibitor complex using a sandwich-immunoassay.


RESULTS
The clinical parameters revealed a statistical significant decrease at the 6-month reexamination. PD levels dropped from 5.40 to 2.88 mm (change 2.52 +/- 1.04 mm), the CAL scores from 6.67 to 4.43 mm (change 2.24 +/- 0.77 mm). The 30 s GCF volumes dropped from 129.8 to 68.6, displaying a change of 61.1 +/- 18.6, p </= 0.05. The decrease in total MPO, beta-NAH and CD levels (medians: 1.7/0.6 micro U MPO, 0.035/0.020 micro U beta-NAH, 1.3/0.5 ng CD) following therapy was associated with a significant drop in total GCF amounts of alpha-1-EPI from 76.3 ng at baseline to 52.4 ng after 6 months.


CONCLUSIONS
The clinical healing in chronic periodontal disease is associated with a downregulation of the local PMN responses following periodontal therapy. The reorganization of periodontal tissues is characterized by a decrease of lysosomal enzyme activities and the alpha-1-proteinase inhibitor complex in gingival crevicular fluid.
Buchmann
Rainer
R
Department of Periodontology and Oral Biology, Goldman School of Dental Medicine, Boston University, Boston, MA, USA. rainerbuhmann.yahoo.de
Hasilik
Andrej
A
Nunn
Martha E
ME
Van Dyke
Thomas E
TE
Lange
Dieter E
DE
D000328:Adult; D002250:Carbon Radioisotopes; D002402:Cathepsin D / Q000032:analysis; D002908:Chronic Disease; D015536:Down-Regulation; D005260:Female; D005500:Follow-Up Studies; D005883:Gingival Crevicular Fluid / Q000201:enzymology*; D006801:Humans; D019272:Leukocyte Elastase / Q000032:analysis*; D008247:Lysosomes / Q000201:enzymology; D008297:Male; D008875:Middle Aged; D018375:Neutrophil Activation / Q000502:physiology; D009504:Neutrophils / Q000502:physiology*; D017622:Periodontal Attachment Loss / Q000601:surgery; D010514:Periodontal Pocket / Q000601:surgery; D010518:Periodontitis / Q000503:physiopathology* / Q000601:surgery; D009195:Peroxidase / Q000032:analysis; D019275:Radiopharmaceuticals; D013053:Spectrophotometry; D018709:Statistics, Nonparametric; D014945:Wound Healing; D000515:alpha 1-Antitrypsin / Q000032:analysis*; D001619:beta-N-Acetylhexosaminidases / Q000032:analysis
D002250:Carbon Radioisotopes; D019275:Radiopharmaceuticals; D000515:alpha 1-Antitrypsin; C037741:alpha 1-antitrypsin-leukocyte elastase complex; D009195:Peroxidase; D001619:beta-N-Acetylhexosaminidases; D019272:Leukocyte Elastase; D002402:Cathepsin D