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RESEARCH REPORT |
1 Department of Dental Basic Sciences, Academic Centre for Dentistry Amsterdam (ACTA), Van der Boechorststraat 7, 1081 BT Amsterdam, the Netherlands;
2 Department of Oral & Maxillofacial Surgery/Oral Pathology, University Medical Centre Vrije Universiteit (VUMC), Amsterdam, The Netherlands; and
3 Department of Immunology and Microbiology, Institute for Medical Biology, University of Southern Denmark, 5000 Odense C, Denmark;
*corresponding author, fj.bikker.obc.acta{at}med.vu.nl
Salivary agglutinin is a Streptococcus mutans binding protein and a member of the scavenger receptor cysteine-rich superfamily. It is identical to lung gp-340 and brain DMBT1, which possibly play a role in innate immunity and tumor suppression, respectively. The goal of this study was to localize salivary agglutinin in human salivary glands. Two monoclonal antibodies, directed against gp-340, were characterized. mAb 213-1 reacted with sialic acid epitopes and cross-reacted with MUC7. The reaction with mAb 213-6 disappeared after reduction, suggesting that a protein epitope was recognized. In the parotid gland, immunohistochemical labeling with mAb 213-6 was found in the duct cells. In the submandibular gland and labial gland, both serous acini and demilune cells were labeled. In the labial gland, labeling was found at the luminal side of the duct cells. Salivary agglutinin was distinctly localized in salivary glands, but in distinct glandular secretions, no differences in electrophoretic behavior were observed.
KEY WORDS: immunohistochemistry • saliva • salivary gland • scavenger receptors
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