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Journal of Dental Research
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Hereditary Dentin Defects

J.-W. Kim1 and J.P. Simmer2,*

1 Seoul National University, School of Dentistry Department of Pediatric Dentistry & Dental Research Institute, 28-2 Yongon-dong, Chongno-gu, Seoul, Korea 110-749; and
2 Department of Biologic and Materials Science, University of Michigan School of Dentistry, Dental Research Lab, 1210 Eisenhower Place, Ann Arbor, MI 48108, USA


Figure 1
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  		Figure 1. SIBLING genes on human chromosome 4. Key: Dentin sialophosphoprotein (DSPP), dentin matrix protein 1 (DMP1), integrin-binding sialoprotein (IBSP), matrix extracellular phosphoglycoprotein (MEPE), secreted phosphoprotein-1 (SPP1).

 

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  		Figure 2. Isolated inherited dentin defects. Primary dentition of a person with DGI-II (top). Bitewing radiographs show pulp obliteration in the molars. Primary dentition of a person with DGI-III (middle). Radiograph shows widened pulp and root canals. Several teeth have abscesses following pulp exposure due to rapid attrition. Permanent dentition of a person with DD-II (bottom). Note the near-normal color of the teeth. The pulp chambers are smaller than normal (becoming obliterated prematurely).

 

Figure 3
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  		Figure 3. Human DSPP gene structure and known disease-causing mutations. The boxes are exons, and the lines are introns. The lines above the gene diagram mark the positions of known disease-causing mutations in DSPP, which are: p.Y6D, p.A15D, p.P17T, Splice IVS2–3C>G, p.V18F, p.Q45X, Splice IVS3+1G>A, p.R68W, and p.del:1160–1171/p.Ins1198–1199. The amino acids corresponding to the porcine DSPP domain structure (Signal peptide-DSP-DGP-DPP) are shown in parentheses. Much of the human DPP coding region in exon 5 is highly redundant and cannot be screened for mutations.

 

Journal of Dental Research, Vol. 86, No. 5, 392-399 (2007)
DOI: 10.1177/154405910708600502
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