Source:http://linkedlifedata.com/resource/pubmed/id/10765957
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2000-4-17
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pubmed:abstractText |
Dentinogenesis Imperfecta type II (DGI-II) is a localized form of mesodermal dysplasia of the dentin affecting both the primary and permanent dentitions. This is an autosomal-dominant disease in which there is a disorder in dentin mineralization. Several studies have localized DGI-II to human chromosome 4 in the region 4q 12-21. Many ECM genes-such as OPN, DMP1, DMP2, DMP3 (DSPP), and BSP-have been mapped to the same locus. Biochemical studies indicated that dentin phosphophoryn (DMP2) might be a candidate gene in DGI-II. In this study, we have used histological and RFLP analyses of tissues from a DGI-II-affected patient, as compared with two normal controls, to determine if DMP1, 2, or 3 was linked to DGI-II. The histology of the affected tooth was very different in the DGI-II patient as compared with the normals. In particular, the dentinal tubules in the DGI-II patient were very irregular, which could be the result of perturbations in the process of dentin formation. Patient and control DNA samples were digested with EcoRI or PstI and Southern-hybridized with the DMP1, DMP2, and DMP3 cDNAs. Few differences in the restriction pattern were observed between affected and normal samples for DMP1 and DMP3-3' region (phosphophoryn-like sequences) probes. On the other hand, DMP2 showed a dramatic shift in the restriction pattern in DGI-II. This study suggests that the different restriction enzyme digestion profiles of the DNA from the DGI-II patient, as probed by DMP2, might be related to the defective mineralization of dentin in DGI-II.
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pubmed:grant | |
pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
D
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sialoglycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/dentin sialophosphoprotein,
http://linkedlifedata.com/resource/pubmed/chemical/phosphophoryn
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-0345
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
79
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
835-9
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pubmed:dateRevised |
2010-2-5
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pubmed:meshHeading |
pubmed-meshheading:10765957-Chromosomes, Human, Pair 4,
pubmed-meshheading:10765957-Dentinogenesis Imperfecta,
pubmed-meshheading:10765957-Extracellular Matrix Proteins,
pubmed-meshheading:10765957-Female,
pubmed-meshheading:10765957-Genes, Dominant,
pubmed-meshheading:10765957-Humans,
pubmed-meshheading:10765957-Male,
pubmed-meshheading:10765957-Nucleic Acid Hybridization,
pubmed-meshheading:10765957-Pedigree,
pubmed-meshheading:10765957-Phosphoproteins,
pubmed-meshheading:10765957-Polymorphism, Restriction Fragment Length,
pubmed-meshheading:10765957-Sequence Analysis, DNA,
pubmed-meshheading:10765957-Sialoglycoproteins,
pubmed-meshheading:10765957-Tooth Calcification
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pubmed:year |
2000
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pubmed:articleTitle |
The non-collagenous dentin matrix proteins are involved in dentinogenesis imperfecta type II (DGI-II).
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pubmed:affiliation |
Department of Oral Biology, School of Dentistry, University of Illinois at Chicago, 60612, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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