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

Crevicular fluid was collected from gingivitis and periodontitis patients on filter paper strips and then eluted into buffer. The eluates hydrolyzed ZAlaArgArgAFC at alkaline pH and the effector response at pH 8.5 indicated serine proteinase activity. The results, particularly the substantial increase in activity produced by heparin, were suggestive of mast cell tryptase. They were also consistent with the properties of the tryptase-like enzyme identified in extracts of inflamed human gingiva (Cox and Eley, Arch Oral Biol, in press). Partial inhibition of crevicular fluid eluate activity by soybean trypsin inhibitor suggested the additional presence of a second trypsin-like enzyme which might be of host or bacterial origin.
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PMID:Tryptase-like activity in crevicular fluid from gingivitis and periodontitis patients. 252 68

Porphyromonas gingivalis is known to be a major etiologic agent in the onset and progression of chronic periodontitis. Among various virulence factors that this bacterium produces, Arg- and Lys-specific cysteine proteinases (gingipains) are believed to be major determinants of the pathogenicity of P. gingivalis. Here, we report on our finding that there are inhibitors of these cysteine proteinases in a rice protein fraction. Comprehensive affinity chromatography and MS analyses resulted in the identification of 17 Arg-gingipain (Rgp)-interacting proteins in the rice endosperm. Of these, four proteins (i.e., a 26 kDa globulin, a plant lipid transfer/trypsin-alpha amylase inhibitor, the RA17 seed allergen, and an alpha amylase/trypsin inhibitor) were estimated to account for 90% of the Rgp inhibitory activity in the rice protein fraction, using a two-dimensional gel system of double-layer reverse zymography. In addition, a synthetic peptide derived from an Rgp-interacting protein, cyanate hydratase, could inhibit the growth of P. gingivalis and showed inhibitory activity against both the Arg- and Lys-gingipains. These results suggest that these rice proteins may be useful as nutraceutical ingredients for the prevention and management of periodontal diseases.
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PMID:Identification of proteinaceous inhibitors of a cysteine proteinase (an Arg-specific gingipain) from Porphyromonas gingivalis in rice grain, using targeted-proteomics approaches. 1969 Dec 86