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1.
J Struct Biol ; 126(1): 27-41, 1999 Jun 01.
Article in English | MEDLINE | ID: mdl-10329486

ABSTRACT

Peritubular dentin (PTD) is a relatively dense mineralized tissue that surrounds the tubules of coronal tooth dentin. It is composed mainly of crystals of carbonated apatite together with a small amount of collagen. Its mode of formation has been investigated by studying the relatively dense particles isolated from a powdered preparation. Electron microscopic examination of the PTD particles, including 3-dimensional image reconstruction and electron diffraction, shows that the organization of the crystals of PTD is very similar to that of the adjacent intertubular dentin (ITD). The latter contains relatively large amounts of collagen and the carbonated apatite crystals are closely associated with the collagen matrix. The proteins present in the PTD particles are soluble after decalcification and stain with Stains All. The principal protein has higher molecular weight and a quite different amino acid composition than the phosphophoryns of the intertubular dentin. The interface between the PTD and the ITD shows structural continuity. These data show how two distinct carbonated apatite-based mineralized tissues can be organized and formed contiguously within the same organ by utilizing different sets of matrix proteins.


Subject(s)
Dentin/ultrastructure , Adult , Chromatography, Ion Exchange , Dentin/chemistry , Electrophoresis, Polyacrylamide Gel , Humans , Image Processing, Computer-Assisted , Indicators and Reagents , Microscopy, Electron , Microscopy, Electron, Scanning , Proteins/isolation & purification
2.
J Biol Chem ; 271(51): 32869-73, 1996 Dec 20.
Article in English | MEDLINE | ID: mdl-8955126

ABSTRACT

Phosphophoryns (PPs), a family of Asp and Ser(P)-rich dentin proteins, are considered to be archetypal regulators of several aspects of extracellular matrix (ECM) biomineralization. We have cloned a rat incisor PP gene, Dmp2, from our odontoblast cDNA library and localized it to mouse chromosome 5q21 within 2 centimorgans of Dmp1, another tooth-specific ECM protein. The carboxyl-terminal region of Dmp2 protein (60 residue % Ser, 31 residue % Asp) is divided into two domains, one with unique repetitive blocks of [DSS]n,3

Subject(s)
Calcification, Physiologic , Extracellular Matrix Proteins/chemistry , Phosphoproteins/chemistry , Amino Acid Sequence , Animals , Chromosome Mapping , Dentin/metabolism , Dentinogenesis Imperfecta/genetics , Extracellular Matrix Proteins/genetics , Extracellular Matrix Proteins/ultrastructure , Gene Expression , Mice , Molecular Sequence Data , Odontoblasts/physiology , Phosphoproteins/genetics , Phosphoproteins/ultrastructure , Protein Conformation , RNA, Messenger/genetics , Rats , Repetitive Sequences, Nucleic Acid , Tissue Distribution
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