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{{Infobox_gene}}'''Tuftelin''' is an acidic [[Phosphorylation|phosphorylated]] [[glycoprotein]] found in [[tooth]] [[tooth enamel|enamel]].  In humans, the Tuftelin protein is encoded by the ''TUFT1'' gene.<ref name="entrez">{{cite web | title = Entrez Gene: TUFT1 tuftelin 1| url =https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7286| accessdate = }}</ref><ref name="pmid7919663">{{cite journal |vauthors=Deutsch D, Palmon A, Young MF, Selig S, Kearns WG, Fisher LW | title = Mapping of the human tuftelin (TUFT1) gene to chromosome 1 by fluorescence in situ hybridization | journal = Mamm. Genome | volume = 5 | issue = 7 | pages = 461–2 |date=July 1994 | pmid = 7919663 | doi = 10.1007/BF00357011| url =  }}</ref> It is an acidic protein that is thought to play a role in dental enamel mineralization and is implicated in caries susceptibility. It is also thought to be involved with adaptation to hypoxia, mesenchymal stem cell function, and neurotrophin nerve growth factor mediated neuronal differentiation.<ref>{{Cite web|url=https://www.ncbi.nlm.nih.gov/gene/7286|title=TUFT1 tuftelin 1 [Homo sapiens (human)] - Gene - NCBI|website=www.ncbi.nlm.nih.gov|access-date=2018-03-05}}</ref>


== Classification ==
There are two kinds of enamel proteins: [[Amelogenin|Amelogenins]] & Nonamelogenins. Tuftelin falls under nonamelogenins.<ref>{{Cite book|url=https://books.google.co.in/books?hl=en&lr=&id=XR0xDwAAQBAJ&oi=fnd&pg=PP1&dq=ten+cate's+oral+histology&ots=b9qhZ1f2iN&sig=31lbRhe9AxSrTFHwh5h9NNPSGQk#v=onepage&q=ten%20cate's%20oral%20histology&f=false|title=Ten Cate's Oral Histology - E-Book: Development, Structure, and Function|last=Nanci|first=Antonio|date=2017-08-15|publisher=Elsevier Health Sciences|isbn=9780323485180|language=en}}</ref>


==Overview==
== Function ==
{{SI}}
'''Tuftelin''' is an acidic [[Phosphorylation|phosphorylated]] [[glycoprotein]] found in [[tooth]] [[tooth enamel|enamel]].  This protein is formed for a short time during [[amelogenesis]].  The function of tuftelins is under contention, but it is proposed that it acts to start the mineralization process of enamel during [[tooth development]].


Other significant proteins in enamel are [[amelogenin|amelogenins]], [[enamelin|enamelins]], and [[ameloblastin|ameloblastins]].
This protein is formed for a short time during [[amelogenesis]].  The function of tuftelins is under contention, but it is proposed that it acts to start the mineralization process of enamel during [[tooth development]].<ref name="pmid2672884">{{cite journal | author = Deutsch D | title = Structure and function of enamel gene products | journal = Anat. Rec. | volume = 224 | issue = 2 | pages = 189–210 |date=June 1989 | pmid = 2672884 | doi = 10.1002/ar.1092240209 | url =  }}</ref><ref name="pmid1874744">{{cite journal |vauthors=Deutsch D, Palmon A, Fisher LW, Kolodny N, Termine JD, Young MF | title = Sequencing of bovine enamelin ("tuftelin") a novel acidic enamel protein | journal = J. Biol. Chem. | volume = 266 | issue = 24 | pages = 16021–8 |date=August 1991 | pmid = 1874744 | doi = | url = http://www.jbc.org/cgi/content/abstract/266/24/16021 }}</ref>


Other significant proteins in enamel are [[amelogenin]]s, [[enamelin]]s, and [[ameloblastin]]s.


== Research ==
The human encoding [[gene]] for tuftelin (TUFT1) was cloned by Profs. Dany Deutsch and Aharon Palmon from the [[Hebrew University]]-[[Hadassah]] [[List of dental schools in Israel|School of Dental Medicine]] in [[Jerusalem]].<ref name="pmid7919663"/>


==Interactions==
Tuftelin has been shown to [[Protein-protein interaction|interact]] with [[TFIP11]].<ref name=pmid10806191>{{cite journal |last=Paine |first=C T |authorlink= |author2=Paine M L |author3=Luo W |author4=Okamoto C T |author5=Lyngstadaas S P |author6=Snead M L  |date=July 2000  |title=A tuftelin-interacting protein (TIP39) localizes to the apical secretory pole of mouse ameloblasts |journal=J. Biol. Chem. |volume=275 |issue=29 |pages=22284–92 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10806191 |doi = 10.1074/jbc.M000118200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>
== References ==
{{Reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  |vauthors=Deutsch D, Leiser Y, Shay B, etal |title=The human tuftelin gene and the expression of tuftelin in mineralizing and nonmineralizing tissues.|journal=Connect. Tissue Res. |volume=43 |issue= 2–3 |pages= 425–34 |year= 2003 |pmid= 12489194 |doi=  10.1080/03008200290001186}}
*{{cite journal  |vauthors=Deutsch D, Palmon A, Young MF, etal |title=Mapping of the human tuftelin (TUFT1) gene to chromosome 1 by fluorescence in situ hybridization|journal=Mamm. Genome |volume=5 |issue= 7 |pages= 461–2 |year= 1994 |pmid= 7919663 |doi=10.1007/BF00357011  }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene|volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  }}
*{{cite journal  |vauthors=Paine CT, Paine ML, Luo W, etal |title=A tuftelin-interacting protein (TIP39) localizes to the apical secretory pole of mouse ameloblasts|journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22284–92 |year= 2000 |pmid= 10806191 |doi= 10.1074/jbc.M000118200 }}
*{{cite journal  |vauthors=Bashir MM, Abrams WR, Tucker T, etal |title=Molecular cloning and characterization of the bovine and human tuftelin genes |journal=Connect. Tissue Res. |volume=39 |issue= 1–3 |pages= 13–24; discussion 63–7 |year= 2000 |pmid= 11062985 |doi=10.3109/03008209809023908  }}
*{{cite journal  |vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA Cloning Using In Vitro Site-Specific Recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948  }}
*{{cite journal  |vauthors=Wiemann S, Weil B, Wellenreuther R, etal |title=Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R  | pmc=311072 }}
*{{cite journal  |vauthors=Simpson JC, Wellenreuther R, Poustka A, etal |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058  | pmc=1083732 }}
*{{cite journal  |vauthors=Mao Z, Shay B, Hekmati M, etal |title=The human tuftelin gene: cloning and characterization |journal=Gene |volume=279 |issue= 2 |pages= 181–96|year= 2002 |pmid= 11733143 |doi=10.1016/S0378-1119(01)00749-1  }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M }}
*{{cite journal  |vauthors=Clark HF, Gurney AL, Abaya E, etal |title=The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003  | pmc=403697 }}
*{{cite journal  |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet.|volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal  |vauthors=Wiemann S, Arlt D, Huber W, etal |title=From ORFeome to Biology: A Functional Genomics Pipeline |journal=Genome Res. |volume=14 |issue= 10B|pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704  | pmc=528930 }}
*{{cite journal  |vauthors=Mehrle A, Rosenfelder H, Schupp I, etal |title=The LIFEdb database in 2006 |journal=Nucleic Acids Res. |volume=34 |issue= Database issue|pages= D415–8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139  | pmc=1347501 }}
*{{cite journal  |vauthors=Gregory SG, Barlow KF, McLay KE, etal |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441|issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |bibcode=2006Natur.441..315G }}
}}
{{refend}}
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[[Category:Teeth]]
[[Category:Teeth]]
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Latest revision as of 22:34, 26 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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View/Edit Human

Tuftelin is an acidic phosphorylated glycoprotein found in tooth enamel. In humans, the Tuftelin protein is encoded by the TUFT1 gene.[1][2] It is an acidic protein that is thought to play a role in dental enamel mineralization and is implicated in caries susceptibility. It is also thought to be involved with adaptation to hypoxia, mesenchymal stem cell function, and neurotrophin nerve growth factor mediated neuronal differentiation.[3]

Classification

There are two kinds of enamel proteins: Amelogenins & Nonamelogenins. Tuftelin falls under nonamelogenins.[4]

Function

This protein is formed for a short time during amelogenesis. The function of tuftelins is under contention, but it is proposed that it acts to start the mineralization process of enamel during tooth development.[5][6]

Other significant proteins in enamel are amelogenins, enamelins, and ameloblastins.

Research

The human encoding gene for tuftelin (TUFT1) was cloned by Profs. Dany Deutsch and Aharon Palmon from the Hebrew University-Hadassah School of Dental Medicine in Jerusalem.[2]

Interactions

Tuftelin has been shown to interact with TFIP11.[7]

References

  1. "Entrez Gene: TUFT1 tuftelin 1".
  2. 2.0 2.1 Deutsch D, Palmon A, Young MF, Selig S, Kearns WG, Fisher LW (July 1994). "Mapping of the human tuftelin (TUFT1) gene to chromosome 1 by fluorescence in situ hybridization". Mamm. Genome. 5 (7): 461–2. doi:10.1007/BF00357011. PMID 7919663.
  3. "TUFT1 tuftelin 1 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2018-03-05.
  4. Nanci, Antonio (2017-08-15). Ten Cate's Oral Histology - E-Book: Development, Structure, and Function. Elsevier Health Sciences. ISBN 9780323485180.
  5. Deutsch D (June 1989). "Structure and function of enamel gene products". Anat. Rec. 224 (2): 189–210. doi:10.1002/ar.1092240209. PMID 2672884.
  6. Deutsch D, Palmon A, Fisher LW, Kolodny N, Termine JD, Young MF (August 1991). "Sequencing of bovine enamelin ("tuftelin") a novel acidic enamel protein". J. Biol. Chem. 266 (24): 16021–8. PMID 1874744.
  7. Paine, C T; Paine M L; Luo W; Okamoto C T; Lyngstadaas S P; Snead M L (July 2000). "A tuftelin-interacting protein (TIP39) localizes to the apical secretory pole of mouse ameloblasts". J. Biol. Chem. UNITED STATES. 275 (29): 22284–92. doi:10.1074/jbc.M000118200. ISSN 0021-9258. PMID 10806191.

Further reading