File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Expression of phosphoproteins and amelotin in teeth

TitleExpression of phosphoproteins and amelotin in teeth
Authors
KeywordsAmelotin
Dentin
Enamel
Phosphoproteins
Rat Incisors
Sibling
Tooth Formation
Issue Date2007
PublisherDemetrios A Spandidos Ed & Pub. The Journal's web site is located at http://147.52.72.117/IJMM/ijmm.htm
Citation
International Journal Of Molecular Medicine, 2007, v. 19 n. 1, p. 49-54 How to Cite?
AbstractThe organic material of our teeth consists of collagens and a number of calcium-binding phosphoproteins. Six of these phosphoproteins have recently been grouped in the family of the SIBLINGs (small integrin-binding ligand, N-linked glycoproteins), namely osteopontin, bone sialo-protein, dentin matrix protein (DMP1), dentin sialophosphoprotein (DSPP), matrix extracellular phosphoglycoprotein (MEPE) and enamelin. We prepared a cDNA library from rat incisors in order to identify the genes involved in tooth formation. The library was screened by subtractive hybridization with two probes; one specific for teeth, the other for bone. We found that the vast majority of the clones from our library were expressed at similar levels in bone and teeth, demonstrating the close relationship of the two tissues. Only 7% of all the clones were expressed in a tooth-specific fashion. These included clones for the enamel proteins; amelotin, amelogenin, ameloblastin and enamelin; for the dentin proteins DSPP and DMP1; and for the intermediate filament protein cytokeratin 13. Several typical bone proteins, including collagen I, osteocalcin, alkaline phosphatase and FATSO, were also expressed at significantly higher levels in teeth than in bone, probably due to the extreme growth rate of rat incisors. The amino acid sequence of rat amelotin showed 62% identity with the sequence from humans. It was expressed considerably later than the other enamel proteins, suggesting that amelotin may serve a function different from those of amelogenin, ameloblastin and enamelin.
Persistent Identifierhttp://hdl.handle.net/10722/154481
ISSN
2015 Impact Factor: 2.348
2015 SCImago Journal Rankings: 0.868
References

 

DC FieldValueLanguage
dc.contributor.authorTrueb, Ben_US
dc.contributor.authorTaeschler, Sen_US
dc.contributor.authorSchild, Cen_US
dc.contributor.authorLang, NPen_US
dc.date.accessioned2012-08-08T08:25:34Z-
dc.date.available2012-08-08T08:25:34Z-
dc.date.issued2007en_US
dc.identifier.citationInternational Journal Of Molecular Medicine, 2007, v. 19 n. 1, p. 49-54en_US
dc.identifier.issn1107-3756en_US
dc.identifier.urihttp://hdl.handle.net/10722/154481-
dc.description.abstractThe organic material of our teeth consists of collagens and a number of calcium-binding phosphoproteins. Six of these phosphoproteins have recently been grouped in the family of the SIBLINGs (small integrin-binding ligand, N-linked glycoproteins), namely osteopontin, bone sialo-protein, dentin matrix protein (DMP1), dentin sialophosphoprotein (DSPP), matrix extracellular phosphoglycoprotein (MEPE) and enamelin. We prepared a cDNA library from rat incisors in order to identify the genes involved in tooth formation. The library was screened by subtractive hybridization with two probes; one specific for teeth, the other for bone. We found that the vast majority of the clones from our library were expressed at similar levels in bone and teeth, demonstrating the close relationship of the two tissues. Only 7% of all the clones were expressed in a tooth-specific fashion. These included clones for the enamel proteins; amelotin, amelogenin, ameloblastin and enamelin; for the dentin proteins DSPP and DMP1; and for the intermediate filament protein cytokeratin 13. Several typical bone proteins, including collagen I, osteocalcin, alkaline phosphatase and FATSO, were also expressed at significantly higher levels in teeth than in bone, probably due to the extreme growth rate of rat incisors. The amino acid sequence of rat amelotin showed 62% identity with the sequence from humans. It was expressed considerably later than the other enamel proteins, suggesting that amelotin may serve a function different from those of amelogenin, ameloblastin and enamelin.en_US
dc.languageengen_US
dc.publisherDemetrios A Spandidos Ed & Pub. The Journal's web site is located at http://147.52.72.117/IJMM/ijmm.htmen_US
dc.relation.ispartofInternational Journal of Molecular Medicineen_US
dc.subjectAmelotinen_US
dc.subjectDentinen_US
dc.subjectEnamelen_US
dc.subjectPhosphoproteinsen_US
dc.subjectRat Incisorsen_US
dc.subjectSiblingen_US
dc.subjectTooth Formationen_US
dc.titleExpression of phosphoproteins and amelotin in teethen_US
dc.typeArticleen_US
dc.identifier.emailLang, NP:nplang@hkucc.hku.hken_US
dc.identifier.authorityLang, NP=rp00031en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-34548101555en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34548101555&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume19en_US
dc.identifier.issue1en_US
dc.identifier.spage49en_US
dc.identifier.epage54en_US
dc.publisher.placeGreeceen_US
dc.identifier.scopusauthoridTrueb, B=7006783821en_US
dc.identifier.scopusauthoridTaeschler, S=6506302775en_US
dc.identifier.scopusauthoridSchild, C=36878498900en_US
dc.identifier.scopusauthoridLang, NP=7201577367en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats