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Heparanase expression in periapical granulomas and radicular cysts
Authors:S. Elad  Y. Sherman  A. Palmon  I. Vlodavsky  R. Or
Affiliation:1. Department of Oral Medicine, Hebrew University-Hadassah School of Dental Medicine, POB 12272, Jerusalem, 91120, Israel
2. Eastman Institute for Oral Health, University of Rochester, Rochester, NY, USA
3. Department of Pathology, Hadassah University Medical Center, Jerusalem, Israel
4. Institute of Dental Sciences, Hebrew University-Hadassah School of Dental Medicine, Jerusalem, Israel
5. Cancer and Vascular Biology Research Center, The Bruce Rappaport Faculty of Medicine, Technion, Haifa, Israel
6. Department of Bone Marrow Transplantation and Cancer Immunobiology Research Laboratory, Hadassah University Medical Center, Jerusalem, Israel
Abstract:Heparanase is an endo-β-d-glucuronidase enzyme which degrades heparan sulfate glycosaminoglycan side chains of proteoglycans in the extracellular matrix and in basement membranes. The aim of this study was to evaluate the expression of heparanase in periapical granulomas (PGs) and radicular cysts (RCs). Immunohistochemistry was used to assess heparanase expression in PGs and RCs. Parameters including stain intensity, location and cell type were used to characterize heparanase expression in the periapical lesions. Ordered categories (from weak to strong) were used to compare the level of heparanase staining in the PG and RC groups. Both epithelial cells and inflammatory cells were positive for heparanase. The relative staining of the epithelial cells was strong, whereas the relative staining of the inflammatory cells was weak. Significant differences in immunohistochemical staining of epithelial cells were observed between RCs and PGs (p = 0.002). The relative expression of heparanase in epithelial cells in RCs was strong. In PGs, lesions with few or no epithelial cells, heparanase was predominantly expressed weakly by inflammatory cells. PGs and RCs have the same infectious origin. Therefore, the different cellular sources of heparanase in these periapical lesions may imply that this enzyme has specific pathogenetic functions in RCs and PGs.
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