Premium
Role of the NH 2 ‐terminal fragment of dentin sialophosphoprotein in dentinogenesis
Author(s) -
Gibson Monica P.,
Liu Qilin,
Zhu Qinglin,
Lu Yongbo,
Jani Priyam,
Wang Xiaofang,
Liu Ying,
Paine Michael L.,
Snead Malcolm L.,
Feng Jian Q.,
Qin Chunlin
Publication year - 2013
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/eos.12020
Subject(s) - dentin sialophosphoprotein , dentin , dentinogenesis , chemistry , biglycan , dmp1 , odontoblast , microbiology and biotechnology , biochemistry , proteoglycan , extracellular matrix , materials science , biology , gene , composite material , viral matrix protein , decorin
Dentin sialophosphoprotein ( DSPP ) is a large precursor protein that is proteolytically processed into a NH 2 ‐terminal fragment [composed of dentin sialoprotein ( DSP ) and a proteoglycan form ( DSP ‐ PG )] and a COOH ‐terminal fragment [dentin phosphoprotein ( DPP )]. In vitro studies indicate that DPP is a strong initiator and regulator of hydroxyapatite crystal formation and growth, but the role(s) of the NH 2 ‐terminal fragment of DSPP (i.e. DSP and DSP ‐ PG ) in dentinogenesis remain unclear. This study focuses on the function of the NH 2 ‐terminal fragment of DSPP in dentinogenesis. Here, transgenic ( T g) mouse lines expressing the NH 2 ‐terminal fragment of DSPP driven by a 3.6‐kb type I collagen promoter ( C ol 1a1 ) were generated and cross‐bred with Dspp null mice to obtain mice that express the transgene but lack the endogenous Dspp ( Dspp KO / DSP T g). We found that dentin from the Dspp KO / DSP T g mice was much thinner, more poorly mineralized, and remarkably disorganized compared with dentin from the Dspp KO mice. The fact that Dspp KO / DSP T g mice exhibited more severe dentin defects than did the Dspp null mice indicates that the NH 2 ‐terminal fragment of DSPP may inhibit dentin mineralization or may serve as an antagonist against the accelerating action of DPP and serve to prevent predentin from being mineralized too rapidly during dentinogenesis.