Salivary histatin as an inhibitor of a protease produced by the oral bacterium Bacteroides gingivalis

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Abstract

We examined the effect of histatin 5 from human parotid saliva on various proteases. Histatin 5 strongly inhibited a trypsin-like protease produced by Bacteroides gingivalis with an IC50 value of 55 nM. Clostripain was also inhibited (IC50=800 nM). Activities of other proteases were not affected significantly. Because B. gingivalis is a suspected periodontal pathogen and its proteolytic enzymes have been considered to be associated with periodontal tissue destruction, it is suggested that salivary histatins play a role as a preventive against periodontal disease.

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    The intent of increasing polyacrilamyde concentration was to increase the likelihood of visualization of low molecular weight proteins, such as histatins in the gel, as well as their degradation products. On the contrary, using HPLC, a more sensitive technique, McDonald et al. [8] observed that the degradation of histatin 1 occurs soon after 0.5 h of incubation in diluted WSS from periodontally healthy individuals, with 28% of the intact protein being degraded at 0.5 h, and 83% at 2 h. Besides, we observed that GI had an influence on the degradation of histatin 1 (Table 2), indicating that these proteins protect against the development of periodontal disease [12, 13, 14]. On the other hand, it was observed that histatin 5 degrades faster than histatin 1, as degradation products were observed as early as time point zero in saliva pools from all groups (Figure 1).

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