Abstract
BackgroundMatrix metalloproteinases‐20 (MMP20) expression is widely regarded as tooth specific, with expression limited to dental hard tissues. Recently, we reported MMP20 expression and interaction with dentin sialophosphoprotein (DSPP), a member of the Small Integrin Binding Ligand N‐linked Glycoproteins (SIBLINGs), in human oral squamous cell carcinoma (OSCC) and dysplastic oral premalignant lesions (OPLs), suggesting a role for MMP20‐DSPP interaction in oral carcinogenesis.MethodsThis study aimed to survey the expression of MMP20 and its cognate DSPP partner in the breast, colon, prostate, thyroid, and cervical neoplasms. Using commercially available tissue microarrays (TMAs) and cell lines, we performed immunohistochemistry, immunofluorescence, proximity ligation assay, and western blot experiments to determine the expressions of MMP20 and DSPP in the breast, colon, prostate, thyroid, cervical neoplasms, and their normal counterparts.ResultsSignificantly high expression levels of MMP20 and DSPP were observed in the malignant breast, colon, prostate, thyroid, and cervical neoplasms compared with their benign and normal counterparts. Furthermore, MMP20 levels increased with advanced stages of colon and thyroid cancers. DSPP expression increased significantly with tumor stage in all cancers examined.ConclusionsThe co‐localization and potential MMP20‐DSPP interaction previously reported in oral cancers are present in other cancers. These results suggest MMP20‐DSPP pairing as a potential marker of disease activity in some epithelial cancers with diagnostic and prognostic implications.
Highlights
Matrix metalloproteinase‐20 (MMP20) is a member of the matrix metalloproteinase family, a group of zinc‐dependent metallopeptidases, involved in extracellular matrix remodeling
dentin sialophosphoprotein (DSPP) is hardly ever isolated as an intact protein because soon after its synthesis it is proteolytically processed into dentin phosphoprotein (DPP), dentin sialoprotein (DSP), and dentin glycoprotein (DGP) in developing teeth by MMP2 and Matrix metalloproteinases‐20 (MMP20).12 DPP, initiates and modulates the formation and growth of hydroxyapatite crystals during dentin formation[13,14] while DSP regulates the initiation of dentin mineralization.[15]
The correlation between expression of MMP20 and DSPP in normal and tumors tissues was tested by regression analysis
Summary
Matrix metalloproteinase‐20 (MMP20) is a member of the matrix metalloproteinase family, a group of zinc‐dependent metallopeptidases, involved in extracellular matrix remodeling. Dentin sialophosphoprotein (DSPP) is a member of the Small Integrin Binding Ligand, N‐linked Glycoprotein (SIBLING) family. We reported MMP20 expression and interaction with dentin sialophosphoprotein (DSPP), a member of the Small Integrin Binding Ligand N‐linked Glycoproteins (SIBLINGs), in human oral squamous cell carcinoma (OSCC) and dysplastic oral premalignant lesions (OPLs), suggesting a role for MMP20‐DSPP interaction in oral carcinogenesis. Using commercially available tissue microarrays (TMAs) and cell lines, we performed immunohistochemistry, immunofluorescence, proximity ligation assay, and western blot experiments to determine the expressions of MMP20 and DSPP in the breast, colon, prostate, thyroid, cervical neoplasms, and their normal counterparts. Results: Significantly high expression levels of MMP20 and DSPP were observed in the malignant breast, colon, prostate, thyroid, and cervical neoplasms compared with their benign and normal counterparts. These results suggest MMP20‐DSPP pairing as a potential marker of disease activity in some epithelial cancers with diagnostic and prognostic implications
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
