Linked Life Data

9541227

Source:http://linkedlifedata.com/resource/pubmed/id/9541227

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-5-29
pubmed:abstractText
Dentinogenesis consists of highly controlled events occurring a short distance from the periphery of odontoblasts: it involves formation of extracellular collagen fibrils that act as an undergirding for deposition of plate-like carbonate apatite crystals. Odontoblasts also form a set of matrix proteins that are probably secreted at the mineralization front. Although most of these proteins are similar to those of bone, and differ from soft tissue proteins, dentin contains two unique proteins. Dentin phosphoprotein (DPP) is rich in aspartic acid (D) and phosphoserine (S*) and binds large amounts of calcium. DPP contains repeating sequences of DS*S* and S*D in discrete areas of the protein. DS*S* repeats form ridges of phosphates and carboxyllates while the S*D sequences give rise to ridges with phosphates and carboxyllates on opposing sides of the peptide chain. These structures undoubtedly have functional significance since DPP is involved in promotion of mineral initiation and in control of mineral size and shape. Dentin sialoprotein (DSP), found only in dentin, is a 53 kDa glycoprotein rich in aspartic acid, serine, glutamic acid and glycine. DSP is made by odontoblasts and also by pre-ameloblasts, but not by osteoblasts or other cell types. The gene for DSP is now known to be continuous with that of DPP. Thus, DSP and DPP must be secreted as a single protein which is then proteolytically processed to form the individual components found in the dentin matrix. Significantly, the DSP/DPP gene has been localized to human chromosome 4q21 at a site implicated in dentinogenesis imperfecta type II.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0909-8836
pubmed:author
pubmed:issnType
Print
pubmed:volume
106 Suppl 1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
204-10
pubmed:dateRevised
2010-2-5
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Dentin matrix proteins.
pubmed:affiliation
Department of Basic Sciences, The University of Texas-Houston Health Science Center, Dental Branch, 77030, USA. wbutler@mail.db.uth.tmc.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review