Hemoglobina, alfa 1

Hemoglobina. alfa 1
Estruturas dispoñibles
PDB	Buscar ortólogos: PDBe, RCSB Lista de códigos PDB 1A00 , 1A01, 1A0U, 1A0Z, 1A3N, 1A3O, 1A9W, 1ABW, 1ABY, 1AJ9, 1B86, 1BAB, 1BBB, 1BIJ, 1BUW, 1BZ0, 1BZ1, 1BZZ, 1C7B, 1C7C, 1C7D, 1CLS, 1CMY, 1COH, 1DKE, 1DXT, 1DXU, 1DXV, 1FDH, 1FN3, 1G9V, 1GBU, 1GBV, 1GLI, 1GZX, 1HAB, 1HAC, 1HBA, 1HBB, 1HBS, 1HCO, 1HDB, 1HGA, 1HGB, 1HGC, 1HHO, 1IRD, 1J3Y, 1J3Z, 1J40, 1J41, 1J7S, 1J7W, 1J7Y, 1JY7, 1K0Y, 1K1K, 1KD2, 1LFL, 1LFQ, 1LFT, 1LFV, 1LFY, 1LFZ, 1LJW, 1M9P, 1MKO, 1NEJ, 1NIH, 1NQP, 1O1I, 1O1J, 1O1K, 1O1L, 1O1M, 1O1N, 1O1O, 1O1P, 1QI8, 1QSH, 1QSI, 1QXD, 1QXE, 1R1X, 1R1Y, 1RPS, 1RQ3, 1RQ4, 1RQA, 1RVW, 1SDK, 1SDL, 1SHR, 1SI4, 1THB, 1UIW, 1VWT, 1XXT, 1XY0, 1XYE, 1XZ2, 1XZ4, 1XZ5, 1XZ7, 1XZU, 1XZV, 1Y01, 1Y09, 1Y0A, 1Y0C, 1Y0D, 1Y0T, 1Y0W, 1Y22, 1Y2Z, 1Y31, 1Y35, 1Y45, 1Y46, 1Y4B, 1Y4F, 1Y4G, 1Y4P, 1Y4Q, 1Y4R, 1Y4V, 1Y5F, 1Y5J, 1Y5K, 1Y7C, 1Y7D, 1Y7G, 1Y7Z, 1Y83, 1Y85, 1Y8W, 1YDZ, 1YE0, 1YE1, 1YE2, 1YEN, 1YEO, 1YEQ, 1YEU, 1YEV, 1YFF, 1YG5, 1YGD, 1YGF, 1YH9, 1YHE, 1YHR, 1YIE, 1YIH, 1YVQ, 1YVT, 1YZI, 1Z8U, 2D5Z, 2D60, 2DN1, 2DN2, 2DN3, 2DXM, 2H35, 2HBC, 2HBD, 2HBE, 2HBF, 2HBS, 2HCO, 2HHD, 2HHE, 2M6Z, 2W6V, 2W72, 2YRS, 3B75, 3D17, 3D7O, 3DUT, 3HXN, 3IA3, 3IC0, 3IC2, 3KMF, 3NL7, 3NMM, 3ODQ, 3ONZ, 3OO4, 3OO5, 3OVU, 3P5Q, 3QJB, 3QJC, 3QJD, 3QJE, 3R5I, 3S48, 3S65, 3S66, 3SZK, 3WCP, 3WHM, 4FC3, 4HHB, 4IJ2, 4L7Y, 4M4A, 4M4B, 4MQC, 4MQG, 4MQH, 4MQI, 4MQJ, 4MQK, 4N7N, 4N7O, 4N7P, 4N8T, 4NI0, 4NI1, 4ROL, 4ROM, 4WJG, 4X0L, 4XS0, 6HBW, 5E29, 5E6E, 5EE4, 5HU6, 5JDO, 5KDQ, 5E83,%%s1Y01, 1Z8U, 1BZ1 ;
Identificadores
Nomenclatura	Outros nomes HBA1, HBA-T3, HBH, subunidade alfa 1 da hemoglobina, METHBA, ECYT7 ;
Símbolos	HBA1 (HGNC: 4823) HBA1, HBA-T3, HBH, subunidade alfa 1 da hemoglobina, METHBA, ECYT7
Identificadores; externos	OMIM: 141800 ; MGI: 96015 ; HomoloGene: 469 ; EBI: HBA1; GeneCards: Xene HBA1; UniProt: HBA1;
Locus	Cr. 16 p13.3
Ontoloxía Xénica	Referencias: AmiGO / QuickGO
	Referencias: AmiGO / QuickGO
Ortólogos
Especies
Humano	Rato
Entrez
3039	15122
Ensembl
Véxase HS	Véxase MM
UniProt
P69905	Q91VB8
RefSeq; (ARNm)
NM_000558	NM_008218
RefSeq; (proteína) NCBI
NP_000508	NP_001077424
Localización (UCSC)
Cr. 16:; 0.18 – 0.18 Mb	Cr. 11:; 32.23 – 32.23 Mb
PubMed (Busca)
3039 ;	15122

Hemoglobina, alfa 1^[1] ou HBA1 é un xene situado no cromosoma 16 humano que codifica a subunidade alfa 1 da hemoglobina.^[2]

Xene editar

O cluster de xenes da globina alfa humana localizado no cromosoma 16 abrangue unhas 30 kb e inclúe sete loci: 5'- zeta - pseudozeta - mu - pseudoalfa-1 - alfa-2 - alfa-1 - teta - 3'. O alfa-2 (HBA2) e o alfa-1 (HBA1; o xene deste artigo) teñen secuencias codificantes idénticas. Estes xenes diferéncianse lixeiramente nas rexións non traducidas 5' e nos intróns, pero difiren significativamente nas rexións non traducidas 3'.^[2]

Proteína editar

A hemoglobina A (HbA) é unha proteína tetrámera que está formada por dúas cadeas alfa e dúas cadeas beta, a cal na vida adulta normal constitúe un 97% da hemoglobina total; as cadeas alfa combínanse coas delta para formar a HbA2, a cal, xunto coa hemoglobina fetal (HbF), forma o restante 3% da hemoglobina adulta.^[2]

Importancia clínica editar

A alfa-talasemia orixínase por delecións en calquera dos xenes alfa e tamén delecións de HBA2 e HBA1; tamén se informou de casos de talasemia non debidas a delecións.^[2]

Interaccións editar

Esta proteína presenta interaccións coa subunidade beta da hemoglobina (HBB).^[3]^[4]

Notas editar

↑ "HBA1 gene: MedlinePlus Genetics".
↑ ^2,0 ^2,1 ^2,2 ^2,3 "Entrez Gene: HBA1 hemoglobin, alpha 1".
↑ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (setembro de 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. PMID 16169070. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0.
↑ Shaanan B (novembro de 1983). "Structure of human oxyhaemoglobin at 2.1 A resolution". J. Mol. Biol. 171 (1): 31–59. PMID 6644819. doi:10.1016/S0022-2836(83)80313-1.

Véxase tamén editar

Outros artigos editar

Bibliografía editar

Turbpaiboon C, Svasti S, Sawangareetakul P, et al. (2002). "Hb Siam [alpha15(A13)Gly-->Arg (alpha1) (GGT-->CGT)] is a typical alpha chain hemoglobinopathy without an alpha-thalassemic effect.". Hemoglobin 26 (1): 77–81. PMID 11939517. doi:10.1081/HEM-120002944.
Yalçin A, Avcu F, Beyan C, et al. (1995). "A case of HB J-Meerut (or Hb J-Birmingham) [alpha 120(H3)Ala-->Glu]". Hemoglobin 18 (6): 433–5. PMID 7713747. doi:10.3109/03630269409045775.
Giardina B, Messana I, Scatena R, Castagnola M (1995). "The multiple functions of hemoglobin.". Crit. Rev. Biochem. Mol. Biol. 30 (3): 165–96. PMID 7555018. doi:10.3109/10409239509085142.
Higgs DR, Vickers MA, Wilkie AO, et al. (1989). "A review of the molecular genetics of the human alpha-globin gene cluster.". Blood 73 (5): 1081–104. PMID 2649166. doi:10.1182/blood.V73.5.1081.1081.
Schillirò G, Russo-Mancuso G, Dibenedetto SP, et al. (1992). "Six rare hemoglobin variants found in Sicily.". Hemoglobin 15 (5): 431–7. PMID 1802885. doi:10.3109/03630269108998862.
Vafa M, Troye-Blomberg M, Anchang J, et al. (2008). "Multiplicity of Plasmodium falciparum infection in asymptomatic children in Senegal: relation to transmission, age and erythrocyte variants.". Malar. J. 7: 17. PMC 2267475. PMID 18215251. doi:10.1186/1475-2875-7-17.
Datta P, Chakrabarty S, Chakrabarty A, Chakrabarti A (2008). "Membrane interactions of hemoglobin variants, HbA, HbE, HbF and globin subunits of HbA: effects of aminophospholipids and cholesterol.". Biochim. Biophys. Acta 1778 (1): 1–9. PMID 17916326. doi:10.1016/j.bbamem.2007.08.019.
Taylor JG, Ackah D, Cobb C, et al. (2008). "Mutations and polymorphisms in hemoglobin genes and the risk of pulmonary hypertension and death in sickle cell disease.". Am. J. Hematol. 83 (1): 6–14. PMC 3509176. PMID 17724704. doi:10.1002/ajh.21035.
Sahu SC, Simplaceanu V, Gong Q, et al. (2007). "Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector.". Biochemistry 46 (35): 9973–80. PMC 2532491. PMID 17691822. doi:10.1021/bi700935z.
Sorour Y, Heppinstall S, Porter N, et al. (2007). "Is routine molecular screening for common alpha-thalassaemia deletions necessary as part of an antenatal screening programme?". Journal of Medical Screening 14 (2): 60–1. PMID 17626702. doi:10.1258/096914107781261981.
Hung CC, Lee CN, Chen CP, et al. (2007). "Molecular assay of -alpha(3.7) and -alpha(4.2) deletions causing alpha-thalassemia by denaturing high-performance liquid chromatography.". Clin. Biochem. 40 (11): 817–21. PMID 17512924. doi:10.1016/j.clinbiochem.2007.03.018.
Ye BC, Zhang Z, Lei Z (2007). "Molecular analysis of alpha/beta-thalassemia in a southern Chinese population.". Genet. Test. 11 (1): 75–83. PMID 17394396. doi:10.1089/gte.2006.0502.
Dilley J, Ganesan A, Deepa R, et al. (2007). "Association of A1C with cardiovascular disease and metabolic syndrome in Asian Indians with normal glucose tolerance.". Diabetes Care 30 (6): 1527–32. PMID 17351274. doi:10.2337/dc06-2414.
Fonseka PV, Vasudevan G, Clarizia LJ, McDonald MJ (2007). "Temperature dependent soret spectral band shifts accompany human CN-mesohemoglobin assembly.". Protein J. 26 (4): 257–63. PMID 17191128. doi:10.1007/s10930-006-9067-7.
Sankar VH, Arya V, Tewari D, et al. (2007). "Genotyping of alpha-thalassemia in microcytic hypochromic anemia patients from North India.". J. Appl. Genet. 47 (4): 391–5. PMID 17132905. doi:10.1007/BF03194650.
Origa R, Sollaino MC, Giagu N, et al. (2007). "Clinical and molecular analysis of haemoglobin H disease in Sardinia: haematological, obstetric and cardiac aspects in patients with different genotypes.". Br. J. Haematol. 136 (2): 326–32. PMID 17129226. doi:10.1111/j.1365-2141.2006.06423.x.
Hussein OA, Gefen Y, Zidan JM, et al. (2007). "LDL oxidation is associated with increased blood hemoglobin A1c levels in diabetic patients.". Clin. Chim. Acta 377 (1–2): 114–8. PMID 17070510. doi:10.1016/j.cca.2006.09.002.
Pan W, Galkin O, Filobelo L, et al. (2007). "Metastable mesoscopic clusters in solutions of sickle-cell hemoglobin.". Biophys. J. 92 (1): 267–77. Bibcode:2007BpJ....92..267P. PMC 1697867. PMID 17040989. doi:10.1529/biophysj.106.094854.
Pistrosch F, Koehler C, Wildbrett J, Hanefeld M (2006). "Relationship between diurnal glucose levels and HbA1c in type 2 diabetes.". Horm. Metab. Res. 38 (7): 455–9. PMID 16933182. doi:10.1055/s-2006-947838.
Chong YM, Tan JA, Zubaidah Z, et al. (2006). "Screening of concurrent alpha-thalassaemia 1 in beta-thalassaemia carriers.". Med. J. Malaysia 61 (2): 217–20. PMID 16898315.

Ligazóns externas editar

GeneReviews/NCBI/NIH/UW entrada sobre a alfa-talasemia
Entradas de OMIM sobre a alfa-talasemia
Relación de toda a información estrutural dispoñible en PDB para UniProt: P69905 (Hemoglobin subunit alpha) en PDBe-KB.

[1] "HBA1 gene: MedlinePlus Genetics".

[entrez-2] 2,0 ^2,1 ^2,2 ^2,3 "Entrez Gene: HBA1 hemoglobin, alpha 1".

[pmid16169070-3] Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (setembro de 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. PMID 16169070. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0.

[pmid6644819-4] Shaanan B (novembro de 1983). "Structure of human oxyhaemoglobin at 2.1 A resolution". J. Mol. Biol. 171 (1): 31–59. PMID 6644819. doi:10.1016/S0022-2836(83)80313-1.

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