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N‐Terminal and C‐terminal fragments of dentin matrix protein 1(DMP1) are distributed differently in bone, dentin and cells.
Author(s) -
Maciejewska Izabela,
Svoboda Kathy,
Butler William,
Qin Chunlin
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.233.6
Subject(s) - dmp1 , terminal (telecommunication) , chemistry , dentin , cleavage (geology) , biomineralization , fragment (logic) , extracellular matrix , microbiology and biotechnology , biophysics , mineralization (soil science) , crystallography , biochemistry , biology , pathology , viral matrix protein , gene , medicine , telecommunications , paleontology , fracture (geology) , computer science , programming language , organic chemistry , nitrogen
DMP1 is critical for biomineralization. In the extracellular matrix of bone and dentin, DMP1 shows as N‐terminal and C‐terminal fragments derived from proteolitic cleavage. In vitro study showed that the C‐terminal fragment promotes mineralization. Information about the N‐terminal fragment function is lacking. Aim of this study was to examine if DMP1 N‐terminal and C‐terminal fragments were localized differently in bone or dentin. Rat bones and teeth were stained immunohistochemically with antibodies that specifically recognized DMP1 N‐terminal and C‐terminal fragments and subsequently assessed with a confocal microscope. Different distribution of both fragments was observed. In the growth plate of bone only N‐terminal fragment was present in a proliferation and hypertrophic zone, while the C‐terminal fragment occupied ossification zone. In tooth, predentin reacted stronger with anti‐N‐terminal fragment antibody, while dentin reacted stronger with the anti‐C‐terminal fragment antibody. Different localization of the N‐terminal and C‐terminal fragments suggests that they have diverse roles in biomineralization. We believe that the C‐terminal fragment promotes mineralization, while the N‐terminal fragment serves as an inhibitor. Supported by NIH grant DE005092 (CQ).