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The proteolytic processing of amelogenin by enamel matrix metalloproteinase (MMP-20) is controlled by mineral ions
- Source :
-
BBA - General Subjects . Mar2013, Vol. 1830 Issue 3, p2600-2607. 8p. - Publication Year :
- 2013
-
Abstract
- Abstract: Background: Enamel synthesis is a highly dynamic process characterized by simultaneity of matrix secretion, assembly and processing during apatite mineralization. MMP-20 is the first protease to hydrolyze amelogenin, resulting in specific cleavage products that self-assemble into nanostructures at specific mineral compositions and pH. In this investigation, enzyme kinetics of MMP-20 proteolysis of recombinant full-length human amelogenin (rH174) under different mineral compositions is elucidated. Methods: Recombinant amelogenin was cleaved by MMP-20 under various physicochemical conditions and the products were analyzed by SDS-PAGE and MALDI-TOF MS. Results: It was observed that mineral ions largely affect cleavage pattern, and enzyme kinetics of rH174 hydrolysis. Out of the five selected mineral ion compositions, MMP-20 was most efficient at high calcium concentration, whereas it was slowest at high phosphate, and at high calcium and phosphate concentrations. In most of the compositions, N- and C-termini were cleaved rapidly at several places but the central region of amelogenin was protected up to some extent in solutions with high calcium and phosphate contents. Conclusion: These in vitro studies showed that the chemistry of the protein solutions can significantly alter the processing of amelogenin by MMP-20, which may have significant effects in vivo matrix assembly and subsequent calcium phosphate mineralization. General significance: This study elaborates the possibilities of the processing of the organic matrix into mineralized tissue during enamel development. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 03044165
- Volume :
- 1830
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- BBA - General Subjects
- Publication Type :
- Academic Journal
- Accession number :
- 85396309
- Full Text :
- https://doi.org/10.1016/j.bbagen.2012.11.021