Enamelin: Difference between revisions
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* {{cite journal | vauthors = Hart TC, Hart PS, Gorry MC, Michalec MD, Ryu OH, Uygur C, Ozdemir D, Firatli S, Aren G, Firatli E | title = Novel ENAM mutation responsible for autosomal recessive amelogenesis imperfecta and localised enamel defects | journal = Journal of Medical Genetics | volume = 40 | issue = 12 | pages = 900–6 | date = December 2003 | pmid = 14684688 | pmc = 1735344 | doi = 10.1136/jmg.40.12.900 }} |
* {{cite journal | vauthors = Hart TC, Hart PS, Gorry MC, Michalec MD, Ryu OH, Uygur C, Ozdemir D, Firatli S, Aren G, Firatli E | title = Novel ENAM mutation responsible for autosomal recessive amelogenesis imperfecta and localised enamel defects | journal = Journal of Medical Genetics | volume = 40 | issue = 12 | pages = 900–6 | date = December 2003 | pmid = 14684688 | pmc = 1735344 | doi = 10.1136/jmg.40.12.900 }} |
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* {{cite journal | vauthors = Hart PS, Michalec MD, Seow WK, Hart TC, Wright JT | title = Identification of the enamelin (g.8344delG) mutation in a new kindred and presentation of a standardized ENAM nomenclature | journal = Archives of Oral Biology | volume = 48 | issue = 8 | pages = 589–96 | date = August 2003 | pmid = 12828988 | doi = 10.1016/S0003-9969(03)00114-6 }} |
* {{cite journal | vauthors = Hart PS, Michalec MD, Seow WK, Hart TC, Wright JT | title = Identification of the enamelin (g.8344delG) mutation in a new kindred and presentation of a standardized ENAM nomenclature | journal = Archives of Oral Biology | volume = 48 | issue = 8 | pages = 589–96 | date = August 2003 | pmid = 12828988 | doi = 10.1016/S0003-9969(03)00114-6 }} |
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* {{cite journal | vauthors = Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA | title = Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 26 | pages = 16899–903 | date = December 2002 | pmid = 12477932 | pmc = 139241 | doi = 10.1073/pnas.242603899 }} |
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* {{cite journal | vauthors = Kida M, Ariga T, Shirakawa T, Oguchi H, Sakiyama Y | title = Autosomal-dominant hypoplastic form of amelogenesis imperfecta caused by an enamelin gene mutation at the exon-intron boundary | journal = Journal of Dental Research | volume = 81 | issue = 11 | pages = 738–42 | date = November 2002 | pmid = 12407086 | doi = 10.1177/154405910208101103 }} |
* {{cite journal | vauthors = Kida M, Ariga T, Shirakawa T, Oguchi H, Sakiyama Y | title = Autosomal-dominant hypoplastic form of amelogenesis imperfecta caused by an enamelin gene mutation at the exon-intron boundary | journal = Journal of Dental Research | volume = 81 | issue = 11 | pages = 738–42 | date = November 2002 | pmid = 12407086 | doi = 10.1177/154405910208101103 }} |
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* {{cite journal | vauthors = Rajpar MH, Harley K, Laing C, Davies RM, Dixon MJ | title = Mutation of the gene encoding the enamel-specific protein, enamelin, causes autosomal-dominant amelogenesis imperfecta | journal = Human Molecular Genetics | volume = 10 | issue = 16 | pages = 1673–7 | date = August 2001 | pmid = 11487571 | doi = 10.1093/hmg/10.16.1673 }} |
* {{cite journal | vauthors = Rajpar MH, Harley K, Laing C, Davies RM, Dixon MJ | title = Mutation of the gene encoding the enamel-specific protein, enamelin, causes autosomal-dominant amelogenesis imperfecta | journal = Human Molecular Genetics | volume = 10 | issue = 16 | pages = 1673–7 | date = August 2001 | pmid = 11487571 | doi = 10.1093/hmg/10.16.1673 }} |
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Revision as of 22:27, 28 February 2019
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | ENAM, AIH2, AI1C, ADAI, enamelin | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 606585; MGI: 1333772; HomoloGene: 9698; GeneCards: ENAM; OMA:ENAM - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Enamelin | |||||||||
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| Identifiers | |||||||||
| Symbol | Enamelin | ||||||||
| Pfam | PF15362 | ||||||||
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Enamelin is an enamel matrix protein (EMPs), that in humans is encoded by the ENAM gene.[5][6] It is part of the non-amelogenins, which comprise 10% of the total enamel matrix proteins.[7] It is one of the key proteins thought to be involved in amelogenesis (enamel development).
Function
Dental enamel is a highly mineralized tissue with 96% of its volume occupied by unusually large, highly organised, hydroxyapatite crystals. This highly organised and unusual structure is thought to be rigorously controlled in ameloblasts through interactions of various organic matrix protein molecules that include: enamelin, amelogenin (AMELX), ameloblastin (AMBN), tuftelin (TUFT1), dentine sialophosphoprotein (DSPP), and a variety of enzymes. Enamelin is the largest protein (~168kDa) in the enamel matrix of developing teeth and is the least abundant (encompasses approximately 5%) of total enamel matrix proteins. [supplied by OMIM][6] It is present predominantly at the growing enamel surface.
Structure
Enamelin is thought to be the oldest member of the enamel matrix protein (EMP) family, with animal studies showing remarkable conservation of the gene phylogenetically.[8] All other EMPs are derived from enamelin, such as amelogenin.[9] EMPs belong to a larger family of proteins termed 'secretory calcium-binding phosphoproteins' (SCPP);
Similar to other enamel matrix proteins, enamelin undergoes extensive post-translational modifications (mainly phosphorylation), processing, and secretion by proteases. Enamelin has three putative phosphoserines (Ser54, Ser191, and Ser216 in humans) phosphorylated by a Golgi-associated secretory pathway kinase (FAM20C) based on their distinctive Ser-x-Glu (S-x-E) motifs.[10] The major secretory product of the ENAM gene has 1103 amino acids (high in Glycine and Proline), and has an isoelectric point ranging from 4.5 to 6.5 (depending on the fragment).[11]
The protein is involved in the mineralization and structural organization of enamel. Defects in this gene result in amelogenesis imperfect type 1C (2nd tab)
The full-length protein and its largest derivative fragments (to about 89 kDa) created as soon as the protein is secreted are not detected inside forming (secretory stage) enamel; these are present only at the growing enamel surface.
Small fragments from enamelin, however, do linger within enamel (e.g., 32 kDa and 25 kDa); these bind strongly to mineral and are inhibitory to crystal growth.
The EDTA-soluble protein described in older literature as “enamelin” turned out to be enamelin albumin derived from blood contamination - legacy protein (Nanci)
The protein is present in highest concentration at the mineralization front, but a proteolytic fragment of enamelin is located among the enamel crystals throughout the secretory stage enamel matrix. Molecular interactions between enamelin and amelogenin have been shown in in vitro experiments and very likely are important for proper enamel crystal growth. Hand and Frank
Function
Words
Believed to function in part as a modulator for de novo formation of mineral and to promote crystal elongation. Ted Cate's
Concentrated near the cell surface at sites where they are secreted (mineralisation front). At these growth sites, the interface between the membrane and the lengthening extremity of crystals can in fact be regarded as a mineralization front
Critical for enamel mineralization and adhesion of ameloblasts to enamel surface during the secretory stage. Hand and Frank
It is speculated that this protein could interact with amelogenin or other enamel matrix proteins and be important in determining growth of the length of enamel crystallites.
Binds to HAP. It is known to retard seeded growth. Anderson
Murine Studies
Words
Studies using knockout mice (which do not express a given protein), transgenic mice (overexpressing selected protein or ones with point mutations), and mutant mice (expressing altered/defective proteins) are providing us with invaluable information on the function of the various amelo- blast products. Transgenic mice expressing mutated forms of amelogenin and knockout mice exhibit major enamel struc- tural defects that affect overall thickness and enamel rod structure. Consistent with their proposed role in promoting and sustaining mineral formation, no structured enamel layer forms in mice expressing defective ameloblastin or enamelin. This is also the case when expression of enamelin is completely abrogated, attesting to the critical role of non- amelogenins. Nanci
Clinical significance
Words
Loss of function & mutant protein: No defined enamel layer. Nanci
Mutations in ENAM cause a severe form of autosomal-dominant smooth hypoplastic AI that represents 1.5%, and a mild form of autosomal-dominant local hypoplastic AI that accounts for 27% of AI cases in Sweden. (Hu and Yamakoshi)
Autosomal Dominant Hypoplastic AI - ENAM (Hand and Frank)
Mutations in the genes for enamel matrix proteins such as amelogenin (AMELX) and enamelin (ENAM) result in varying degrees of enamel hypoplasia and hypomineralization. These include pit- ting and grooves, as well as generalized thin enamel, and disruption of the normal rod structure.
Three different mutations ENAM gene mutations are associated with different AI types. Anderson
See also
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000132464 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029286 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Mårdh CK, Bäckman B, Holmgren G, Hu JC, Simmer JP, Forsman-Semb K (May 2002). "A nonsense mutation in the enamelin gene causes local hypoplastic autosomal dominant amelogenesis imperfecta (AIH2)". Human Molecular Genetics. 11 (9): 1069–74. doi:10.1093/hmg/11.9.1069. PMID 11978766.
- ^ a b "Entrez Gene: ENAM enamelin".
- ^ ANTONIO., NANCI, (2012). TEN CATE'S ORAL HISTOLOGY, 8E. [Place of publication not identified],: ELSEVIER INDIA. ISBN 813123343X. OCLC 1027350695.
{{cite book}}: CS1 maint: extra punctuation (link) CS1 maint: multiple names: authors list (link) - ^ Al-Hashimi N, Lafont AG, Delgado S, Kawasaki K, Sire JY (September 2010). "The enamelin genes in lizard, crocodile, and frog and the pseudogene in the chicken provide new insights on enamelin evolution in tetrapods". Molecular Biology and Evolution. 27 (9): 2078–94. doi:10.1093/molbev/msq098. PMID 20403965.
- ^ Sire JY, Davit-Béal T, Delgado S, Gu X (2007). "The origin and evolution of enamel mineralization genes". Cells, Tissues, Organs. 186 (1): 25–48. doi:10.1159/000102679. PMID 17627117.
- ^ Yan WJ, Ma P, Tian Y, Wang JY, Qin CL, Feng JQ, Wang XF (November 2017). "The importance of a potential phosphorylation site in enamelin on enamel formation". International Journal of Oral Science. 9 (11): e4. doi:10.1038/ijos.2017.41. PMC 5775333. PMID 29593332.
- ^ Hu JC, Yamakoshi Y (2003). "Enamelin and autosomal-dominant amelogenesis imperfecta". Critical Reviews in Oral Biology and Medicine : an Official Publication of the American Association of Oral Biologists. 14 (6): 387–98. doi:10.1177/154411130301400602. PMID 14656895.
Further reading
- Gutierrez SJ, Chaves M, Torres DM, Briceño I (May 2007). "Identification of a novel mutation in the enamalin gene in a family with autosomal-dominant amelogenesis imperfecta". Archives of Oral Biology. 52 (5): 503–6. doi:10.1016/j.archoralbio.2006.09.014. PMID 17316551.
- Pavlic A, Petelin M, Battelino T (March 2007). "Phenotype and enamel ultrastructure characteristics in patients with ENAM gene mutations g.13185-13186insAG and 8344delG". Archives of Oral Biology. 52 (3): 209–17. doi:10.1016/j.archoralbio.2006.10.010. PMID 17125728.
- Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP (November 2004). "Phosphoproteomic analysis of the developing mouse brain". Molecular & Cellular Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - Hart TC, Hart PS, Gorry MC, Michalec MD, Ryu OH, Uygur C, Ozdemir D, Firatli S, Aren G, Firatli E (December 2003). "Novel ENAM mutation responsible for autosomal recessive amelogenesis imperfecta and localised enamel defects". Journal of Medical Genetics. 40 (12): 900–6. doi:10.1136/jmg.40.12.900. PMC 1735344. PMID 14684688.
- Hart PS, Michalec MD, Seow WK, Hart TC, Wright JT (August 2003). "Identification of the enamelin (g.8344delG) mutation in a new kindred and presentation of a standardized ENAM nomenclature". Archives of Oral Biology. 48 (8): 589–96. doi:10.1016/S0003-9969(03)00114-6. PMID 12828988.
- Kida M, Ariga T, Shirakawa T, Oguchi H, Sakiyama Y (November 2002). "Autosomal-dominant hypoplastic form of amelogenesis imperfecta caused by an enamelin gene mutation at the exon-intron boundary". Journal of Dental Research. 81 (11): 738–42. doi:10.1177/154405910208101103. PMID 12407086.
- Rajpar MH, Harley K, Laing C, Davies RM, Dixon MJ (August 2001). "Mutation of the gene encoding the enamel-specific protein, enamelin, causes autosomal-dominant amelogenesis imperfecta". Human Molecular Genetics. 10 (16): 1673–7. doi:10.1093/hmg/10.16.1673. PMID 11487571.
- Hartley JL, Temple GF, Brasch MA (November 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
- Dong J, Gu TT, Simmons D, MacDougall M (October 2000). "Enamelin maps to human chromosome 4q21 within the autosomal dominant amelogenesis imperfecta locus". European Journal of Oral Sciences. 108 (5): 353–8. doi:10.1034/j.1600-0722.2000.108005353.x. PMID 11037750.
- Hu CC, Hart TC, Dupont BR, Chen JJ, Sun X, Qian Q, Zhang CH, Jiang H, Mattern VL, Wright JT, Simmer JP (April 2000). "Cloning human enamelin cDNA, chromosomal localization, and analysis of expression during tooth development". Journal of Dental Research. 79 (4): 912–9. doi:10.1177/00220345000790040501. PMID 10831092.
- Forsman K, Lind L, Bäckman B, Westermark E, Holmgren G (September 1994). "Localization of a gene for autosomal dominant amelogenesis imperfecta (ADAI) to chromosome 4q". Human Molecular Genetics. 3 (9): 1621–5. doi:10.1093/hmg/3.9.1621. PMID 7833920.
External links
- ENAM human gene location in the UCSC Genome Browser.
- ENAM human gene details in the UCSC Genome Browser.
 | This article on a gene on human chromosome 4 is a stub. You can help Wikipedia by expanding it. |