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HBA  -  hemoglobin, alpha 2

Bos taurus

Synonyms: HBA2, alpha globin
 
 
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Disease relevance of alpha globin

  • It is shown that neokyotorphin (the alpha-globin fragment 137-141) stimulates proliferation of normal cells (murine embryonic fibroblasts, red bone marrow and spleen cells) and tumor cells (murine melanoma and transformed fibroblasts L929) in the absence or in the presence of fetal bovine serum [1].
 

High impact information on alpha globin

 

Biological context of alpha globin

  • The stable globin mRNAs provide an ideal system for studying the mechanism governing mammalian mRNA turnover. alpha-Globin mRNA stability is dictated by sequences in the 3' untranslated region (3'UTR) which form a specific ribonucleoprotein complex (alpha-complex) whose presence correlates with mRNA stability [2].
  • However, a high concentration (up to 2.7 times over random sequences) of hexanucleotide factor sites is observed on small stretches of the alpha-globin gene MAR. (2) Some regulatory protein binding sites are underrepresented whereas others are overrepresented, giving to an MAR a particular transcription factor flavor [6].
  • The B haplotype encodes two alpha-globin chains, Ialpha2 and IIalpha4, which differ at positions 10 and 11: Ialpha2 has 10 I1e, 11 Gln, 64 Asn; IIalpha4 has 10 Val, 11 Lys, 64 Asn [7].
  • Apart from the Ala/Asn polymorphism at position 64, amino acid substitutions in allelic and nonallelic alpha-globin chains seem to have arisen by single point mutations [7].
 

Anatomical context of alpha globin

  • IOVs from membranes incubated with alpha-globin chains or haemoglobin A were nearly normal (79 +/- 3% and 86 +/- 5% of controls, respectively) [8].
  • These studies show that isolated beta-globin chains (but not alpha-globin chains) can produce a spectrin-binding defect in normal red cell membranes similar to that seen in alpha thalassaemia [8].
 

Associations of alpha globin with chemical compounds

References

  1. Endogenous fragment of hemoglobin, neokyotorphin, as cell growth factor. Blishchenko, E.Y., Kalinina, O.A., Sazonova, O.V., Khaidukov, S.V., Egorova, N.S., Surovoy, A.Y., Philippova, M.M., Vass, A.A., Karelin, A.A., Ivanov, V.T. Peptides (2001) [Pubmed]
  2. An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro. Wang, Z., Day, N., Trifillis, P., Kiledjian, M. Mol. Cell. Biol. (1999) [Pubmed]
  3. Polarity of DNA replication through the avian alpha-globin locus. James, C.D., Leffak, M. Mol. Cell. Biol. (1986) [Pubmed]
  4. Inositol monophosphatase is a highly conserved enzyme having localized structural similarity to both glycerol 3-phosphate dehydrogenase and haemoglobin. Wreggett, K.A. Biochem. J. (1992) [Pubmed]
  5. The mammalian alphaD-globin gene lineage and a new model for the molecular evolution of alpha-globin gene clusters at the stem of the mammalian radiation. Cooper, S.J., Wheeler, D., De Leo, A., Cheng, J.F., Holland, R.A., Marshall Graves, J.A., Hope, R.M. Mol. Phylogenet. Evol. (2006) [Pubmed]
  6. Transcription factor binding sites in the matrix attachment region (MAR) of the chicken alpha-globin gene. Boulikas, T. J. Cell. Biochem. (1994) [Pubmed]
  7. Primary structure of alpha-globin chains from river buffalo (Bubalus bubalis L.) hemoglobins. Ferranti, P., Facchiano, A., Zappacosta, F., Vincenti, D., Rullo, R., Masala, B., Di Luccia, A. J. Protein Chem. (2001) [Pubmed]
  8. Isolated beta-globin chains reproduce, in normal red cell membranes, the defective binding of spectrin to alpha-thalassaemic membranes. Shalev, O., Shinar, E., Lux, S.E. Br. J. Haematol. (1996) [Pubmed]
  9. Effects of nutrient source and time of feeding on changes in blood metabolites in young calves. Quigley, J.D., Bernard, J.K. J. Anim. Sci. (1992) [Pubmed]
 
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