Abstract
Saliva contains acidic proline-rich salivary proteins that are involved in the formation of the salivary pellicle coating supragingival tooth surfaces. However, human leukocyte elastase, arriving in gingival exudates from inflamed periodontal tissues, degrades the acidic proline-rich salivary proteins, preventing binding to hydroxylapatite surfaces. Here it is reported that high-molecular-weight non-immunoglobulin salivary agglutinin inhibited the proteolytic action of human leukocyte elastase on purified acidic proline-rich salivary proteins. Inhibition was eliminated with monoclonal antibody to a protein determinant on the salivary agglutinin. The addition of antibody against salivary agglutinin blocked the inhibitory effect of parotid saliva on exogenously applied human leukocyte elastase, allowing for the elastase-mediated digestion of the salivary acidic proline-rich salivary proteins. Salivary agglutinin, therefore, is a physiologically important inhibitor of human leukocyte elastase and is able to inhibit elastase-mediated digestion of salivary acidic proline-rich proteins.
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