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The Odontogenic Ameloblast-Associated Protein (ODAM) Cooperates With RUNX2 and Modulates Enamel Mineralization Via Regulation of MMP-20

Cited 46 time in Web of Science Cited 47 time in Scopus
Authors

Lee, Hye-Kyung; Lee, Dong-Seol; Ryoo, Hyun-Mo; Park, Jong-Tae; Park, Su-Jin; Bae, Hyun-Sook; Cho, Moon-Il; Park, Joo-Cheol

Issue Date
2010-09
Publisher
WILEY-LISS
Citation
JOURNAL OF CELLULAR BIOCHEMISTRY Vol.111 No.111, pp. 755-767
Keywords
복합학ENAMELODAMMMP-20REGULATIONMINERALIZATION
Abstract
We have previously reported that the odontogenic ameloblast-associated protein (ODAM) plays important roles in enamel mineralization
through the regulation of matrix metalloproteinase-20 (MMP-20). However, the precise function of ODAM in MMP-20 regulation remains
largely unknown. The aim of the present study was to uncover the molecular mechanisms responsible for MMP-20 regulation. The subcellular
localization of ODAM varies in a stage-specific fashion during ameloblast differentiation. During the secretory stage of amelogenesis ODAM
was localized to both the nucleus and cytoplasm of ameloblasts. However, during the maturation stage of amelogenesis, ODAM was observed
in the cytoplasm and at the interface between ameloblasts and the enamel layer, but not in the nucleus. Secreted ODAM was detected in the
conditioned medium of ameloblast-lineage cell line (ALC) from days 14 to 21, which coincided with the maturation stage of amelogenesis.
Interestingly, the expression of Runx2 and nuclear ODAM correlated with MMP-20 expression in ALC. We therefore examined whether ODAM
cooperates with Runx2 to regulate MMP-20 and modulate enamel mineralization. Increased expression of ODAM and Runx2 augmented
MMP-20 expression, and Runx2 expression enhanced expression of ODAM, although overexpression of ODAM did not influence Runx2
expression. Conversely, loss of Runx2 in ALC decreased ODAM expression, resulting in down-regulation of MMP-20 expression. Increased
MMP-20 expression accelerated amelogenin processing during enamel mineralization. Our data suggest that Runx2 regulates the expression
of ODAM and that nuclear ODAM serves an important regulatory function in the mineralization of enamel through the regulation of MMP-20
apart from a different, currently unidentified, function of extracellular ODAM
We have previously reported that the odontogenic ameloblast-associated protein (ODAM) plays important roles in enamel mineralization
through the regulation of matrix metalloproteinase-20 (MMP-20). However, the precise function of ODAM in MMP-20 regulation remains
largely unknown. The aim of the present study was to uncover the molecular mechanisms responsible for MMP-20 regulation. The subcellular
localization of ODAM varies in a stage-specific fashion during ameloblast differentiation. During the secretory stage of amelogenesis ODAM
was localized to both the nucleus and cytoplasm of ameloblasts. However, during the maturation stage of amelogenesis, ODAM was observed
in the cytoplasm and at the interface between ameloblasts and the enamel layer, but not in the nucleus. Secreted ODAM was detected in the
conditioned medium of ameloblast-lineage cell line (ALC) from days 14 to 21, which coincided with the maturation stage of amelogenesis.
Interestingly, the expression of Runx2 and nuclear ODAM correlated with MMP-20 expression in ALC. We therefore examined whether ODAM
cooperates with Runx2 to regulate MMP-20 and modulate enamel mineralization. Increased expression of ODAM and Runx2 augmented
MMP-20 expression, and Runx2 expression enhanced expression of ODAM, although overexpression of ODAM did not influence Runx2
expression. Conversely, loss of Runx2 in ALC decreased ODAM expression, resulting in down-regulation of MMP-20 expression. Increased
MMP-20 expression accelerated amelogenin processing during enamel mineralization. Our data suggest that Runx2 regulates the expression
of ODAM and that nuclear ODAM serves an important regulatory function in the mineralization of enamel through the regulation of MMP-20
apart from a different, currently unidentified, function of extracellular ODAM
ISSN
0730-2312
Language
English
URI
https://hdl.handle.net/10371/81390
DOI
https://doi.org/10.1002/jcb.22766
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