File Download
There are no files associated with this item.
Supplementary
-
Citations:
- Scopus: 0
- Appears in Collections:
Article: Expression of phosphoproteins and amelotin in teeth
Title | Expression of phosphoproteins and amelotin in teeth |
---|---|
Authors | |
Keywords | Amelotin Dentin Enamel Phosphoproteins Rat Incisors Sibling Tooth Formation |
Issue Date | 2007 |
Publisher | Demetrios 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? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/154481 |
ISSN | 2023 Impact Factor: 5.7 2023 SCImago Journal Rankings: 1.167 |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Trueb, B | en_US |
dc.contributor.author | Taeschler, S | en_US |
dc.contributor.author | Schild, C | en_US |
dc.contributor.author | Lang, NP | en_US |
dc.date.accessioned | 2012-08-08T08:25:34Z | - |
dc.date.available | 2012-08-08T08:25:34Z | - |
dc.date.issued | 2007 | en_US |
dc.identifier.citation | International Journal Of Molecular Medicine, 2007, v. 19 n. 1, p. 49-54 | en_US |
dc.identifier.issn | 1107-3756 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/154481 | - |
dc.description.abstract | The 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.language | eng | en_US |
dc.publisher | Demetrios A Spandidos Ed & Pub. The Journal's web site is located at http://147.52.72.117/IJMM/ijmm.htm | en_US |
dc.relation.ispartof | International Journal of Molecular Medicine | en_US |
dc.subject | Amelotin | en_US |
dc.subject | Dentin | en_US |
dc.subject | Enamel | en_US |
dc.subject | Phosphoproteins | en_US |
dc.subject | Rat Incisors | en_US |
dc.subject | Sibling | en_US |
dc.subject | Tooth Formation | en_US |
dc.title | Expression of phosphoproteins and amelotin in teeth | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lang, NP:nplang@hkucc.hku.hk | en_US |
dc.identifier.authority | Lang, NP=rp00031 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.scopus | eid_2-s2.0-34548101555 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-34548101555&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 19 | en_US |
dc.identifier.issue | 1 | en_US |
dc.identifier.spage | 49 | en_US |
dc.identifier.epage | 54 | en_US |
dc.publisher.place | Greece | en_US |
dc.identifier.scopusauthorid | Trueb, B=7006783821 | en_US |
dc.identifier.scopusauthorid | Taeschler, S=6506302775 | en_US |
dc.identifier.scopusauthorid | Schild, C=36878498900 | en_US |
dc.identifier.scopusauthorid | Lang, NP=7201577367 | en_US |
dc.identifier.issnl | 1107-3756 | - |