Immunohistochemical Detection and Distribution of Enamelysin (MMP-20) in Human Odontogenic Tumors

• Published in: Journal of dental research 2000-08, Vol.79 (8), p.1608-1613
• Main Authors: Takata, T., Zhao, M., Uchida, T., Wang, T., Aoki, T., Bartlett, J.D., Nikai, H.
• Format: Article
• Language: English
• Subjects: Ameloblastoma - enzymology; Amino Acid Sequence; Antibodies, Monoclonal; Blotting, Western; Dental Enamel Proteins - analysis; Dental Enamel Proteins - metabolism; Dentistry; Humans; Immunohistochemistry; Matrix Metalloproteinase 20; Matrix Metalloproteinases - analysis; Matrix Metalloproteinases - chemistry; Matrix Metalloproteinases - metabolism; Molecular Sequence Data; Odontogenic Cyst, Calcifying - enzymology; Odontogenic Tumors - chemistry; Odontogenic Tumors - enzymology; Odontoma - enzymology; Recombinant Proteins - metabolism
• ISSN: 0022-0345; 1544-0591
• DOI: 10.1177/00220345000790081401

Enamelysin is a tooth-specific protease that was initially isolated from porcine enamel organ and subsequently from human odontoblasts. Since this protease is thought to play important roles in tooth development, the evaluation of enamelysin in odontogenic tumors may aid our understanding of the histogenesis and cell differentiation of such lesions. A monoclonal antibody (203-lC7) was generated against synthesized human enamelysin oligopeptide and was used to assess the immunolocalization of enamelysin in healthy developing tooth germs and various types of odontogenic lesions. In tooth germs, enamelysin expression was detected only in the secretory enamel. Thus, 203-1C7 may serve as an enamel-specific marker in the late stage of enamel matrix development and calcification. In odontogenic lesions, strong enamelysin staining was demonstrated in the immature enamel matrix of ameloblastic fibro-odontomas and odontomas. Furthermore, enamelysin was also detected in globular amyloid masses and calcified foci in calcifying epithelial odontogenic tumors, hyaline droplets, small and large mineralized areas in adenomatoid odontogenic tumors, and a portion of ghost cells in calcifying odontogenic cysts. Positive reactivity was also observed in selected tumor cells in some of these tumors. No intracellular staining for enamelysin was detected in ameloblastomas or the ameloblastic portion of ameloblastic fibro-odontomas. Also, enamelysin was not detected in dentin, dysplastic dentinoid hyaline matrices, and cementum that were present within the tumors examined. Thus, taken together, our results suggest that the enamelysin-specific monoclonal antibody (203-1C7) may be utilized as a marker of early enamel development and that enamelysin may be involved in the pathogenesis of specific odontogenic tumors.