Journal of Dental Research, Vol 80, 1550-1554, Copyright © 2001 by International & American Associations for Dental Research Online Journals
Salivary non-immunoglobulin agglutinin inhibits human leukocyte elastase digestion of acidic proline-rich salivary proteins
R. J. Boackle, S. L. Dutton, H. Fei, J. Vesely, D. Malamud and A. R. Furness
Department of Stomatology, Medical University of South Carolina, Charleston 29425, USA. boacklrj@musc.edu
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.
