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Dentin sialophosphoprotein (DSPP) is a large precursor protein that is proteolyti-cally processed into a NH2-terminal fragment [composed of dentin sialoprolein (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 NH2-terminal fragment of DSPP (i.e. DSP and DSP-PG) in dentinogenesis remain unclear. This study focuses on the function of the NH2-terminal fragment of DSPP in dentinogenesis. Here, transgenic (Tg) mouse lines expressing the NHi-lerminal fragment of DSPP driven by a 3.6-kb type I collagen promoter (Col lal) were generated and cross-bred with Dspp null mice to obtain mice that express the transgene but.lack the endogenous Dspp (Dspp KO/DSP Tg). We found that dentin from the Dspp KO/DSP Tg mice was much thinner, more poorly mineralized, and remarkably disorganized compared with dentin from the Dspp KO mice. The fact that Dspp KO/DSP Tg mice exhibited more severe dentin defects than did the Dspp null mice indicates that the NHi-lerminal 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 [ABSTRACT FROM AUTHOR]