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Role of the NH2 -terminal fragment of dentin sialophosphoprotein in dentinogenesis.
Eur J Oral Sci. 2013 Apr; 121(2):76-85.EJ

Abstract

Dentin sialophosphoprotein (DSPP) is a large precursor protein that is proteolytically processed into a NH2 -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 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 NH2 -terminal fragment of DSPP driven by a 3.6-kb type I collagen promoter (Col 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 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 NH2 -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.

Authors+Show Affiliations

Texas A&M Health Science Center Baylor College of Dentistry, Dallas, TX 75246, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural

Language

eng

PubMed ID

23489896

Citation

Gibson, Monica P., et al. "Role of the NH2 -terminal Fragment of Dentin Sialophosphoprotein in Dentinogenesis." European Journal of Oral Sciences, vol. 121, no. 2, 2013, pp. 76-85.
Gibson MP, Liu Q, Zhu Q, et al. Role of the NH2 -terminal fragment of dentin sialophosphoprotein in dentinogenesis. Eur J Oral Sci. 2013;121(2):76-85.
Gibson, M. P., Liu, Q., Zhu, Q., Lu, Y., Jani, P., Wang, X., Liu, Y., Paine, M. L., Snead, M. L., Feng, J. Q., & Qin, C. (2013). Role of the NH2 -terminal fragment of dentin sialophosphoprotein in dentinogenesis. European Journal of Oral Sciences, 121(2), 76-85. https://doi.org/10.1111/eos.12020
Gibson MP, et al. Role of the NH2 -terminal Fragment of Dentin Sialophosphoprotein in Dentinogenesis. Eur J Oral Sci. 2013;121(2):76-85. PubMed PMID: 23489896.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Role of the NH2 -terminal fragment of dentin sialophosphoprotein in dentinogenesis. AU - Gibson,Monica P, AU - Liu,Qilin, AU - Zhu,Qinglin, AU - Lu,Yongbo, AU - Jani,Priyam, AU - Wang,Xiaofang, AU - Liu,Ying, AU - Paine,Michael L, AU - Snead,Malcolm L, AU - Feng,Jian Q, AU - Qin,Chunlin, Y1 - 2013/02/07/ PY - 2012/12/03/accepted PY - 2013/3/16/entrez PY - 2013/3/16/pubmed PY - 2013/9/6/medline SP - 76 EP - 85 JF - European journal of oral sciences JO - Eur J Oral Sci VL - 121 IS - 2 N2 - Dentin sialophosphoprotein (DSPP) is a large precursor protein that is proteolytically processed into a NH2 -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 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 NH2 -terminal fragment of DSPP driven by a 3.6-kb type I collagen promoter (Col 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 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 NH2 -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. SN - 1600-0722 UR - https://www.unboundmedicine.com/medline/citation/23489896/Role_of_the_NH2__terminal_fragment_of_dentin_sialophosphoprotein_in_dentinogenesis_ L2 - https://doi.org/10.1111/eos.12020 DB - PRIME DP - Unbound Medicine ER -