PMID: 9189620Jan 1, 1997Paper

Extracellular matrix proteins of dentine

Ciba Foundation Symposium
W T ButlerA L Bronckers

Abstract

Bone and dentine extracellular matrix proteins are similar, consisting primarily of type I collagen, acidic proteins and proteoglycans. Although collagen forms the lattice for deposition of calcium and phosphate for formation of carbonate apatite, the non-collagenous proteins are believed to control initiation and growth of the crystals. Despite this similarity, dentine contains three unique proteins apparently absent from bone and other tissue: dentine phosphophoryn (DPP), dentine matrix protein 1 (DMP1) and dentine sialoprotein (DSP). DPP and DMP1 are acidic phosphoproteins probably involved in the control of mineralization processes. DPP may localize in gap regions of collagen and initiate apatite crystal formation by binding large quantities of calcium in a conformation that promotes this process. Extensive studies have been conducted in our laboratory on the nature, biosynthesis, localization and gene structure of DSP. Immunolocalization studies showed that rat DSP, a 53 kDa sialic acid-rich glycoprotein, was synthesized by young and mature odontoblasts, and by dental pulp cells and pre-ameloblasts, but not by ameloblasts, osteoblasts, chondrocytes or other cell types. The cDNA sequence indicated that DSP was a 366-residue...Continue Reading

Citations

Jul 31, 2002·Journal of Dental Research·S GronthosS Shi
Jul 27, 2010·Indian Journal of Dental Research : Official Publication of Indian Society for Dental Research·B KavithaT R Saraswathi
May 4, 2005·Acta histochemica·Rajeswari M H Ravindranath, Rajam M Basilrose

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