Linked Life Data

6851336

Source:http://linkedlifedata.com/resource/pubmed/id/6851336

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
176
pubmed:dateCreated
1983-7-15
pubmed:abstractText
Hydroxyapatite crystal deposition and stabilization within the collagen matrix of bone and dentin have been linked to the presence of noncollagenous proteins (NCP). Dentinogenesis imperfecta (DI), a genetic disorder of dentin mineralization, is being studied as a model for the analysis of mineralization mechanisms. A comparative study of the NCP in normal human dentin and dentinogenesis imperfecta Type II (hereditary opalescent dentin) dentin has been performed. The proteins of each tissue were extracted and separated using a variety of techniques. The calcium-binding, highly phosphorylated protein phosphophoryn was one of the principal NCP in normal human teeth dentin, whereas there was no evidence for the presence of such a component in the DI teeth. These data imply that dentin phosphophoryn may be related in function to the mineralization process. A similar calcium-binding protein defect should be sought in the various types of osteogenesis imperfecta.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0009-921X
pubmed:author
pubmed:issnType
Print
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
282-90
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Relation of mineralization defects in collagen matrices to noncollagenous protein components. Identification of a molecular defect in dentinogenesis imperfecta.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Case Reports