Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0031099 (periodontitis)
 12,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Gingival tissue and gingival crevicular fluid were collected from patients with chronic periodontitis. Gel filtration chromatography of crude tissue extracts yielded separate fractions active against Lys-Ala-7-amino-4-trifluoromethyl-coumarylamide (AFC) at acid pH and Gly-Pro-AFC at alkaline pH. The molecular weights, pH optima and inhibitor responses of these activities were consistent with those of dipeptidyl peptidases (DPP) II and IV, respectively. When tested with the same substrates, crevicular fluid was also found to contain DPP II- and IV-like activities with very similar pH profiles and inhibitor responses to those in tissue. The close resemblance suggested that the crevicular fluid enzymes were derived mainly from inflamed gingival tissues. Slight differences in the DPP II-like activities might be explained by the additional presence in crevicular fluid of enzymes from subgingival bacteria. With use of appropriate buffers, a third substrate, Ala-Pro-AFC, gave selective detection of both DPP II- and IV-like activities in tissue and crevicular fluid. Assays with Ala-Pro-AFC had the advantage of greater sensitivity, especially with DPP II-like activity. Raised levels of this enzyme have previously been found in the gingiva of periodontitis patients and thus DPP II-like activity in crevicular fluid might prove of value in monitoring disease activity.
 ...
PMID:Dipeptidyl peptidase II- and IV-like activities in gingival tissue and crevicular fluid from human periodontitis lesions. 135 Jan 93

The activity of DPP II was higher in gingiva from patients with periodontitis, but the activity of DPP IV, post-proline cleaving enzyme and collagenase-like peptidase was not significantly higher than that of the control group. As DPP II activity is known to be altered in immunological diseases, these findings may suggest some role for DPP II in the pathogenesis of chronic marginal periodontitis.
 ...
PMID:Activity of dipeptidyl peptidase II and dipeptidyl peptidase IV in human gingiva with chronic marginal periodontitis. 198 Aug 11

Earlier work has shown that gingival crevicular fluid (GCF) contains dipeptidyl peptidase (DPP) activities that resemble those in host tissue. Here, further comparisons were made with enzymes from suspected periodontal pathogens. Gingival tissue and GCF were collected from patients with chronic periodontitis. DPP II and DPP IV fractions with acid and alkaline pH optima, respectively, were separated from crude tissue extracts by gel-filtration chromatography. Bacterial cell sonicates were prepared from broth cultures of reference strains. There was moderate to strong DPP activity with Capnocytophaga spp., Porphyromonas gingivalis and Prevotella spp., very weak activity with Treponema denticola and no detectable activity with Actinobacillus actinomycetemcomitans or Fusobacterium nucleatum. Banding patterns in GCF, tissue and bacterial samples were compared on substrate-impregnated overlay membranes applied to isoelectric focusing gels. In gels washed with acid buffer, GCF had bands corresponding to tissue DPP II. Use of an alkaline washing buffer showed GCF activity which closely matched tissue DPP IV that had been pretreated with neuraminidase, an enzyme found by others in the gingival crevice. P. Gingivalis gave multiple bands and several of these had counterparts in GCF. The apparent presence in GCF of the DPP from P. gingivalis is consistent with the association of this organism with destructive periodontitis.
 ...
PMID:Comparison of host tissue and bacterial dipeptidyl peptidases in human gingival crevicular fluid by analytical isoelectric focusing. 748 74

Dipeptidyl peptidase (DPP) II and IV activities were demonstrated in unfixed cryostat sections of gingival tissue from chronic periodontitis patients using histochemistry with 2-methoxy-4-naphthylamine (MNA) substrates. In the case of DPP IV, enzyme localization was confirmed by immunocytochemistry with mouse monoclonal antihuman DPP IV (CD26) antibody. Inflammatory cells containing enzyme were identified in adjacent sections with mouse monoclonal antibodies directed against leukocyte differentiation antigens. Lys-Ala-MNA and Ala-Pro-MNA staining in acid buffer for DPP II was only found in a few fibroblasts in superficial tissue. Staining with Gly-Pro-MNA and Ala-Pro-MNA in alkaline buffer for DPP IV was localized in some CD4 and CD8 positive T lymphocytes, CD68 positive macrophages, and fibroblasts and these cells also reacted with the enzyme antibody. DPP IV-containing macrophages and T lymphocytes were seen in the epithelium. In deeper granulomatous tissue Gram positive and negative bacteria stained with the histochemical substrates, but not the DPP IV antibody. Fibroblast DPP II and IV might participate in cellular interactions with collagen, while T lymphocyte DPP IV may be involved in cell signalling.
 ...
PMID:Histochemical and immunocytochemical localization of dipeptidyl peptidases II and IV in human gingiva. 888 40