A Novel Hemoglobin Variant Found on the α1 Chain: Hb KSVGH (HBA1: p.Lys57_Gly58insSerHisGlySerAlaGlnValLys)

References

• Carta M, Dall’Olio G, Soffiati G. Determination of Hb A1C in the presence of haemoglobin variants: Comparison of three HPLC techniques. Eur J Clin Chem Clin Biochem. 1997;35(12):923–925
   PubMedGoogle Scholar
• Caruso D, Da Riva L, Giavarini F, et al. A hemoglobin variant found during glycohemoglobin measurement, identified as Hb Toulon [α77(EF6)Pro→His] by tandem mass spectrometry. Hemoglobin. 2002;26(2):197–199
   PubMed Web of Science ®Google Scholar
• Musil M. Serological differences between some isolates of bean yellow mosaic virus. Acta Virol. 1975;19(6):473–480
   PubMedGoogle Scholar
• Chu CH, Lam HC, Lee JK, et al. Common hemoglobin variants in southern Taiwan and their effect on the determination of Hb A1C by ion-exchange high-performance liquid chromatography. J Chin Med Assoc. 2009;72(7):362–367
   PubMedGoogle Scholar
• Lin HJ, Shih MC, Peng CT, et al. Hematological features and molecular lesions of hemoglobin gene disorders in Taiwanese patients. Int J Lab Hematol. 2010;32(1 Pt 2):1–7
   PubMedGoogle Scholar
• Liu SC, Peng CT, Lin TH, et al. Molecular lesion frequency of hemoglobin gene disorders in Taiwan. Hemoglobin. 2011;35(3):228–236
   PubMed Web of Science ®Google Scholar
• Patrinos GP, Giardine B, Riemer C, et al. Improvements in the HbVar database of human hemoglobin variants and thalassemia mutations for population and sequence variation studies. Nucleic Acids Res. 2004;32(Database issue):D537–D541 (http://globin.cse.psu.edu)
   PubMed Web of Science ®Google Scholar
• Little RR, Roberts WL. A review of variant hemoglobins interfering with Hemoglobin A1c measurement. J Diabetes Sci Technol. 2009;3(3):446–451
   PubMedGoogle Scholar
• Tefferi A, Vardiman JW. Classification and diagnosis of myeloproliferative neoplasms: The 2008 World Health Organization criteria and point-of-care diagnostic algorithms. Leukemia. 2008;22(1):14–22
   PubMed Web of Science ®Google Scholar
• Baxter EJ, Scott LM, Campbell PJ, et al. Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders. Lancet. 2005;365(9464):1054–1061
   PubMed Web of Science ®Google Scholar
• Kralovics R, Passamonti F, Buser AS, et al. A gain-of-function mutation of JAK2 in myeloproliferative disorders. N Engl J Med. 2005;352(17):1779–1790
   PubMed Web of Science ®Google Scholar
• James C, Delhommeau F, Marzac C, et al. Detection of JAK2 V617F as a first intention diagnostic test for erythrocytosis. Leukemia. 2006;20(2):350–353
   PubMed Web of Science ®Google Scholar
• McMullin MF. The classification and diagnosis of erythrocytosis. Int J Lab Hematol. 2008;30(6):447–459
   PubMedGoogle Scholar
• Charache S, Weatherall DJ, Clegg JB. Polycythemia associated with a hemoglobinopathy. J Clin Invest. 1966;45(6):813–822
   PubMed Web of Science ®Google Scholar
• Bromberg PA, Alben JO, Bare GH, et al. High oxygen affinity variant of Haemoglobin Little Rock with unique properties. Nat New Biol. 1973;243(127):177–179
   PubMedGoogle Scholar
• Wajcman H, Galacteros F. Abnormal hemoglobins with high oxygen affinity and erythrocytosis. Hematol Cell Ther. 1996;38(4):305–312
   PubMedGoogle Scholar
• Imai K. Oxygen-equilibrium characteristics of abnormal Hemoglobin Hiroshima (α-2 β-2 143 Asp). Arch Biochem Biophys. 1968;127(1):543–547
   PubMedGoogle Scholar
• Poyart C, Krishnamoorthy R, Bursaux E, et al. Structural and functional studies of Haemoglobin Suresnes or α2141(HC3)Arg→Hisβ2, a new high oxygen affinity mutant. FEBS Lett. 1976;69(1):103–107
   PubMedGoogle Scholar
• Reed CS, Hampson R, Gordon S, et al. Erythrocytosis secondary to increased oxygen affinity of a mutant hemoglobin, Hemoglobin Kempsey. Blood. 1968;31(5):623–632
   PubMedGoogle Scholar
• Stamatoyannopoulos G, Nute PE, Adamson JW, et al. Hemoglobin Olympia (β20 Valine→Methionine): An electrophoretically silent variant associated with high oxygen affinity and erythrocytosis. J Clin Invest. 1973;52(2):342–349
   PubMedGoogle Scholar
• Wajcman H, Girodon E, Prome D, et al. Germline mosaicism for an alanine to valine substitution at residue β140 in Hemoglobin Puttelange, a new variant with high oxygen affinity. Hum Genet. 1995;96(6):711–716
   PubMedGoogle Scholar
• Wajcman H, Kister J, Marden M, et al. Hemoglobin Calais [β76(E20)Ala→Pro]: A hemoglobin variant with decreased intrinsic oxygen affinity. Biochim Biophys Acta. 1990;1096(1):60–66
   PubMedGoogle Scholar
• Wajcman H, Kister J, M’Rad A, et al. Hb Saint Nazaire (β103[G5]Phe→Ile): A new example of polycythemia due to a hemoglobin variant with increased oxygen affinity. Am J Hematol. 1993;44(1):16–21
   PubMed Web of Science ®Google Scholar
• Li S, Kralovics R, De Libero G, et al. Clonal heterogeneity in polycythemia vera patients with JAK2 exon 12 and JAK2-V617F mutations. Blood. 2008;111(7):3863–3866
   PubMed Web of Science ®Google Scholar
• Wajcman H, Blouquit Y, Vasseur C, et al. Two new hemoglobin variants caused by unusual mutational events: Hb Zaire contains a five residue repetition within the α-chain and Hb Duino has two residues substituted in the β-chain. Hum Genet. 1992;89(6):676–680
   PubMed Web of Science ®Google Scholar
• Huisman THJ, Wilson JB, Gravely M, et al. Hemoglobin Grady: The first example of a variant with elongated chains due to an insertion of residues. Proc Natl Acad Sci USA. 1974;71(8):3270–3273
   PubMed Web of Science ®Google Scholar
• Wajcman H, Dahmane M, Prehu C, et al. Haemoglobin J-Biskra: A new mildly unstable α1 gene variant with a deletion of eight residues (α50–57, α51–58 or α52–59) including the distal histidine. Br J Haematol. 1998;100(2):401–406
   PubMed Web of Science ®Google Scholar
• Carver MFH, Huisman THJ. International Hemoglobin Information Center variant list. Hemoglobin. 1996;20(3):213–312
   PubMed Web of Science ®Google Scholar