Disease relevance of prtC

• In order to examine the potential role of bacterial collagenases in periodontal tissue destruction, we recently isolated a gene, prtC, from Porphyromonas gingivalis ATCC 53977, which expressed collagenase activity (N. Takahashi, T. Kato, and H. K. Kuramitsu, FEMS Microbiol. Lett. 84:135-138, 1991) [1].
• The PCR was also used for the detection of prtC sequences in dental plaque [2].
• In this study, the nucleotide sequences of the prtC genes of six clinical Porphyromonas gingivalis isolates obtained from patients with periodontitis and from reference strain 53977 were determined [3].
• A gene, prtC, has been isolated from Porphyromonas gingivalis ATCC 53977 in Escherichia coli utilizing the plasmid vector pPL-lambda [4].
• Crude endotoxin preparations from Haemophilus actinomycetemcomitans and Bacteroides gingivalis showed activity in the two principal bio-assays for interleukin 1--the lymphocyte activating factor assay and stimulation of chondrocyte collagenase synthesis [5].

High impact information on prtC

• An isogenic mutant lacking a functional tpr gene had a greatly reduced ability to hydrolyze the collagenase substrate [6].
• Effect of Porphyromonas gingivalis on epithelial cell MMP-9 type IV collagenase production [7].
• Collagenase secretion by the fibroblasts was assayed by incubating cell culture medium with soluble type I [3H]collagen at 25 degrees C followed by SDS-PAGE-fluorography analysis of the reaction products [8].
• 3. Inhibitor studies provided evidence that the breakdown of collagen involved the concerted action of both a collagenase and the trypsinlike enzyme [9].
• Enzymes with a specificity for gingival connective tissue (collagenase, hyaluronidase) were produced optimally at or below neutral pH, whereas trypsinlike activity increased with the growth pH and was maximal at pH 8 [9].

Chemical compound and disease context of prtC

• We previously reported that low-dose doxycycline (DOXY) therapy reduces host-derived collagenase activity in gingival tissue of adult periodontitis (AP) patients [10].
• Measurement of GCF flow rate, endotoxin, H2S, butyrate and a variety of enzymes (e.g., collagenase, arylsulfatase, B-glucuronidase) show good correlation with levels of gingivitis [11].
• In periodontitis, the most promising markers of tissue breakdown are prostaglandins of the E series, the enzymes collagenase and aspartate aminotransferase, sulfated glycosaminoglycans, osteoclastic activating factor and bone resorptive capacity of crevicular cells [11].
• Natural materials containing tannin were examined to determine whether they possessed any inhibitory activity against collagenase obtained from the culture supernatant of Bacteroides gingivalis [12].

Biological context of prtC

• Subcloning and deletion analysis located the prtC gene at one end of the P. gingivalis DNA insert on plasmid pS1 [4].
• The data presented here demonstrates that prtC genes are heterogeneous in their nucleotide sequence and therefore may be used as a target for molecular epidemiological studies [3].
• Of interest, Porphyromonas gingivalis collagenase was also inhibited by similar DOXY levels (IC50 = 15 microM), however the collagenase activity observed in the gingival tissue extracts was found to be of mammalian not bacterial origin based on the production of the specific alpha A (3/4) and alpha B (1/4) collagen degradation fragments [10].
• The virulence of P. gingivalis may be related to its production of collagenase [13].

Anatomical context of prtC

• Lipopolysaccharides purified from the crude endotoxins had reduced activity in the chondrocyte collagenase assay [5].
• This reflects proteolytic activation of leukocyte collagenase in dental plaque probably by other proteases derived from potent periodontopathogenic bacteria such as T. denticola or other PMN proteases such as cathepsin G.(ABSTRACT TRUNCATED AT 250 WORDS)[14]
• These results demonstrated that tea catechins containing galloyl radical possess the ability to inhibit both eukaryotic and prokaryotic cell derived collagenase [15].
• The collagenase activity in the gingival crevicular fluid from highly progressive adult periodontitis was completely inhibited by the addition of tea catechins [15].
• The crude tea catechins, which contain (+)-catechin (C), (-)-epicatechin (EC), (+)-gallocatechin (GC), (-)-epigallocatechin (EGC), (-)-epicatechin gallate (ECg), and (-)-epigallocatechin gallate (EGCg), were tested for their ability to inhibit the prokaryotic and eukaryotic cell derived collagenase activities [15].

Associations of prtC with chemical compounds

• These 16 P. gingivalis strains were confirmed as positive for prtC using DNA hybridization with a digoxigenin-labeled prtC PCR product as a probe [2].
• A recombinant collagenase antigen used for the immunoblot analysis was produced by using the plasmid pGEX-2T, which allows the fusion between the collagenase and glutathione S-transferase [16].
• Tetracycline, doxycycline, and chlorhexidine strongly inhibited collagenase activity [17].
• In contrast to ECg and EGCg, the other four tea catechins (C, EC, EGC, and GC) did not show any collagenase inhibitory effect [15].
• The resultant protease positive clone NHS1, harboring plasmid pS1 with a 5.9-kilobase P. gingivalis insert, expressed an enzyme capable of hydrolyzing the synthetic collagenase substrate PZ-PLGPA as well as solubilized type I collagen [4].

Analytical, diagnostic and therapeutic context of prtC

• Plaque samples from all groups were assessed by PCR with primers complementary to the collagenase-encoding gene prtC [16].
• In addition, Southern blot analysis indicated that the prtC gene is conserved among the three major serotypes of P. gingivalis [1].
• Therefore, the recombinant collagenase is a potential candidate for use in the serodiagnosis of periodontitis [16].
• There was no significant difference in collagenase-specific IgG antibody detection between samples from the EOP, AP, and control groups [16].
• Sequence analysis and characterization of the Porphyromonas gingivalis prtC gene, which expresses a novel collagenase activity [1].

References