ALAS2
| ALAS2 | |||
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| Estruturas dispoñibles | |||
| PDB | Buscar ortólogos: PDBe, RCSB | ||
| Identificadores | |||
| Nomenclatura | Outros nomes
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| Símbolo | ALAS2 (HGNC: 397) | ||
| Identificadores externos | |||
| Locus | Cr. X p11.21 | ||
| Ortólogos | |||
| Especies |
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| Entrez |
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| Ensembl |
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| UniProt |
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| RefSeq (ARNm) |
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| RefSeq (proteína) NCBI |
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| Localización (UCSC) |
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| PubMed (Busca) |
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A delta-aminolevulinato sintase 2, tamén coñecida como 5'-aminolevulinato sintase 2 ou ALAS2, é un encima que nos humanos está codificado polo xene ALAS2 do cromosoma X.[1][2][3] ALAS2 é un tipo de ácido aminolevulínico sintase; outro tipo é o ALAS1.
O produto deste xene é un encima específico de tecido eritroide de localización mitocondrial. A proteína codificada cataliza o primeiro paso da biosíntese do grupo hemo na que se sintetiza ácido 5-aminolevulínico a partir de glicina e succinil-CoA, para o cal utiliza o piridoxal 5-fosfato (PLP) como cofactor. Defectos neste xene causan a anemia sideroblástica que responde á piridoxina ligada ao X. Identificáronse variantes de transcrición de empalme alternativo que codifican diferentes isoformas.[3]
O seu xene contén un elemento de resposta ao ferro (IRE) na súa rexión 5'-UTR ao cal se une unha proteína que se une ao elemento de resposta ao ferro (IRP) se o nivel de ferro é demasiado baixo, inhibindo así a tradución.
Notas[editar | editar a fonte]
- ↑ Bishop DF, Henderson AS, Astrin KH (xuño de 1990). "Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome". Genomics 7 (2): 207–14. PMID 2347585. doi:10.1016/0888-7543(90)90542-3.
- ↑ Cotter PD, Willard HF, Gorski JL, Bishop DF (maio de 1992). "Assignment of human erythroid delta-aminolevulinate synthase (ALAS2) to a distal subregion of band Xp11.21 by PCR analysis of somatic cell hybrids containing X; autosome translocations" (PDF). Genomics 13 (1): 211–2. PMID 1577484. doi:10.1016/0888-7543(92)90223-F. hdl:2027.42/30074.
- ↑ 3,0 3,1 "Entrez Gene: Delta-aminolevulinate synthase 2".
Véxase tamén[editar | editar a fonte]
Bibliografía[editar | editar a fonte]
- Han L, Zhong Y, Huang B, Han L, Pan L, Xu X, Wang X, Huang B, Lu J (2008). "Sodium butyrate activates erythroid-specific 5-aminolevulinate synthase gene through Sp1 elements at its promoter". Blood Cells, Molecules & Diseases 41 (2): 148–53. PMID 18555711. doi:10.1016/j.bcmd.2008.04.002.
- Kaneko K, Furuyama K, Aburatani H, Shibahara S (Mar 2009). "Hypoxia induces erythroid-specific 5-aminolevulinate synthase expression in human erythroid cells through transforming growth factor-beta signaling". The FEBS Journal 276 (5): 1370–82. PMID 19187226. doi:10.1111/j.1742-4658.2009.06878.x.
- Cox TC, Sadlon TJ, Schwarz QP, Matthews CS, Wise PD, Cox LL, Bottomley SS, May BK (Feb 2004). "The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis". The International Journal of Biochemistry & Cell Biology 36 (2): 281–95. PMID 14643893. doi:10.1016/S1357-2725(03)00246-2.
- Harigae H, Furuyama K, Kudo K, Hayashi N, Yamamoto M, Sassa S, Sasaki T (Oct 1999). "A novel mutation of the erythroid-specific gamma-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia". American Journal of Hematology 62 (2): 112–4. PMID 10577279. doi:10.1002/(SICI)1096-8652(199910)62:2<112::AID-AJH9>3.0.CO;2-L.
- Hurford MT, Marshall-Taylor C, Vicki SL, Zhou JZ, Silverman LM, Rezuke WN, Altman A, Tsongalis GJ (Jul 2002). "A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia". Clinica Chimica Acta; International Journal of Clinical Chemistry 321 (1–2): 49–53. PMID 12031592. doi:10.1016/S0009-8981(02)00095-5.
- Bekri S, May A, Cotter PD, Al-Sabah AI, Guo X, Masters GS, Bishop DF (Jul 2003). "A promoter mutation in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causes X-linked sideroblastic anemia". Blood 102 (2): 698–704. PMID 12663458. doi:10.1182/blood-2002-06-1623.
- Astner I, Schulze JO, van den Heuvel J, Jahn D, Schubert WD, Heinz DW (Sep 2005). "Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans". The EMBO Journal 24 (18): 3166–77. PMC 1224682. PMID 16121195. doi:10.1038/sj.emboj.7600792.
- Cazzola M, May A, Bergamaschi G, Cerani P, Ferrillo S, Bishop DF (Dec 2002). "Absent phenotypic expression of X-linked sideroblastic anemia in one of 2 brothers with a novel ALAS2 mutation". Blood 100 (12): 4236–8. PMID 12393718. doi:10.1182/blood-2002-03-0685.
- Sussman NL, Lee PL, Dries AM, Schwartz MR, Barton JC (2008). "Multi-organ iron overload in an African-American man with ALAS2 R452S and SLC40A1 R561G". Acta Haematologica 120 (3): 168–73. PMID 19066423. doi:10.1159/000181183.
- Whatley SD, Ducamp S, Gouya L, Grandchamp B, Beaumont C, Badminton MN, Elder GH, Holme SA, Anstey AV, Parker M, Corrigall AV, Meissner PN, Hift RJ, Marsden JT, Ma Y, Mieli-Vergani G, Deybach JC, Puy H (Sep 2008). "C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload". American Journal of Human Genetics 83 (3): 408–14. PMC 2556430. PMID 18760763. doi:10.1016/j.ajhg.2008.08.003.
- Furuyama K, Sassa S (Mar 2000). "Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia". The Journal of Clinical Investigation 105 (6): 757–64. PMC 377455. PMID 10727444. doi:10.1172/JCI6816.
- Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (Sep 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research 14 (9): 1711–8. PMC 515316. PMID 15342556. doi:10.1101/gr.2435604.
- Lee PL, Barton JC, Rao SV, Acton RT, Adler BK, Beutler E (2006). "Three kinships with ALAS2 P520L (c. 1559 C --> T) mutation, two in association with severe iron overload, and one with sideroblastic anemia and severe iron overload". Blood Cells, Molecules & Diseases 36 (2): 292–7. PMID 16446107. doi:10.1016/j.bcmd.2005.12.004.
- Bergmann AK, Campagna DR, McLoughlin EM, Agarwal S, Fleming MD, Bottomley SS, Neufeld EJ (Feb 2010). "Systematic molecular genetic analysis of congenital sideroblastic anemia: evidence for genetic heterogeneity and identification of novel mutations". Pediatric Blood & Cancer 54 (2): 273–8. PMC 2843911. PMID 19731322. doi:10.1002/pbc.22244.
- Rabstein S, Unfried K, Ranft U, Illig T, Kolz M, Mambetova C, Vlad M, Roman C, Weiss T, Becker D, Brüning T, Pesch B (2008). "Lack of association of delta-aminolevulinate dehydratase polymorphisms with blood lead levels and hemoglobin in Romanian women from a lead-contaminated region". Journal of Toxicology and Environmental Health. Part A 71 (11–12): 716–24. Bibcode:2008JTEHA..71..716R. PMID 18569569. doi:10.1080/15287390801985190.
- Abu-Farha M, Niles J, Willmore WG (Oct 2005). "Erythroid-specific 5-aminolevulinate synthase protein is stabilized by low oxygen and proteasomal inhibition". Biochemistry and Cell Biology 83 (5): 620–30. PMID 16234850. doi:10.1139/o05-045.
- Nachman MW, D'Agostino SL, Tillquist CR, Mobasher Z, Hammer MF (maio de 2004). "Nucleotide variation at Msn and Alas2, two genes flanking the centromere of the X chromosome in humans". Genetics 167 (1): 423–37. PMC 1470878. PMID 15166166. doi:10.1534/genetics.167.1.423.
Ligazóns externas[editar | editar a fonte]
- Localización no xenoma humano de ALAS2 e páxina con detalles sobre o xene ALAS2 no UCSC Genome Browser.
- GeneReviews/NCBI/NIH/UW entrada sobre a anemia sideroblástica e ataxia ligada ao X
Este artigo incorpora textos da Biblioteca Nacional de Medicina dos Estados Unidos, que están en dominio público.
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