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1 This article was downloaded by:[national Chung Hsing University] On: 8 November 2007 Access Details: [subscription number ] Publisher: Informa Healthcare Informa Ltd Registered in England and Wales Registered Number: Registered office: Mortimer House, Mortimer Street, London W1T 3JH, UK Hemoglobin Publication details, including instructions for authors and subscription information: Hb Hekinan in a ese Subject: A T Substitution at Codon 27 of the α1-globin Gene Abolishes an HaeIII Site Hung-Chang Shih ab ; Mu-Chin Shih a ; Yu-Chang Chang a ; Ching-Tien Peng ac ; Tien-Jye Chang b ; Jan-Gowth Chang d a Department of Laboratory Medicine, China Medical University Hospital, Taichung, b Department of Veterinary Medicine, National Chung Hsing University, Taichung, c Department of Biotechnology and Bioinformatics, Asia University, Taichung, d Department of Laboratory Medicine, Kaohsiung Medical University Hospital, Kaohsiung, Online Publication Date: 01 October 2007 To cite this Article: Shih, Hung-Chang, Shih, Mu-Chin, Chang, Yu-Chang, Peng, Ching-Tien, Chang, Tien-Jye and Chang, Jan-Gowth (2007) 'Hb Hekinan in a ese Subject: A T Substitution at Codon 27 of the α1-globin Gene Abolishes an HaeIII Site', Hemoglobin, 31:4, To link to this article: DOI: / URL: PLEASE SCROLL DOWN FOR ARTICLE Full terms and conditions of use: This article maybe used for research, teaching and private study purposes. Any substantial or systematic reproduction, re-distribution, re-selling, loan or sub-licensing, systematic supply or distribution in any form to anyone is expressly forbidden. The publisher does not give any warranty express or implied or make any representation that the contents will be complete or accurate or up to date. The accuracy of any instructions, formulae and drug doses should be independently verified with primary sources. The publisher shall not be liable for any loss, actions, claims, proceedings, demand or costs or damages whatsoever or howsoever caused arising directly or indirectly in connection with or arising out of the use of this material.
2 Hemoglobin, 31 (4): , (2007) Copyright Informa Healthcare USA, Inc. ISSN: print/ x online DOI: / LHEM X Hemoglobin, Vol. 31, No. 4, August 2007: pp. 1 6 SHORT COMMUNICATION Hb HEKINAN IN A TAIWANESE SUBJECT: A G T SUBSTITUTION AT CODON 27 OF THE a1-globin GENE ABOLISHES AN HaeIII SITE Hb H.-C. Hekinan Shih et in al. the ese Hung-Chang Shih, 1,2 Mu-Chin Shih, 1 Yu-Chang Chang, 1 Ching-Tien Peng, 1,3 Tien-Jye Chang, 2 and Jan-Gowth Chang 4 1 Department of Laboratory Medicine, China Medical University Hospital, Taichung, 2 Department of Veterinary Medicine, National Chung Hsing University, Taichung, 3 Department of Biotechnology and Bioinformatics, Asia University, Taichung, 4 Department of Laboratory Medicine, Kaohsiung Medical University Hospital, Kaohsiung, We recently observed a heterozygote for Hb Hekinan in a ese subject. The molecular lesion of Hb Hekinan is a substitution of G T at codon 27 of the a1-globin gene, which abolishes an HaeIII restriction enzyme site. Hb Hekinan [a27(b8)glu Asp, GAG GAC (a2)] has not been found in. This variant can be detected by high performance liquid chromatography (HPLC) but not by capillary or cellulose electrophoresis. Keywords Hb Hekinan, α1-globin gene, Codon 27, ese Hb Hekinan [α27(b8)glu Asp, GAG GAC (α2)] has been reported in Japanese, Thai, Chinese and Guyanan people (1 4). It is due to a substitution of a glutamic acid by an aspartic acid residue at position 27 of the α1- or α2-globin chain). We recently observed this variant in the heterozygous state in a ese subject. The subject was a 10-years-old boy admitted to the Department of Pediatric Hematology of China Medical University Hospital (Taichung, ) for anemia. The hemogram showed: Hb 9.9 g/dl, RBC Received 28 February 2007; accepted 6 June Address correspondence to Dr. Jan-Gowth Chang, Department of Laboratory Medicine, Kaohsiung Medical University Hospital, 100 Tzyou 1st Road, Kaohsiung 807, ; Tel.: ; Fax: ; jgchang@ms.kmuh.org.tw or Dr. Tien-Jye Chang, Department of Veterinary Medicine, National Chung Hsing University, 250 Kuo Kuang Road, Taichung 404, ; Tel.: , Ext. 54; Fax: ; tjchang@dragon.nchu.edu.tw 495
3 496 H.-C. Shih et al /L, PCV L/L, MCV 72.9 fl, MCH 21.7 pg, MCHC 29.7 g/dl and ferritin 2.58 ng/ml. Electrophoresis of freshly prepared hemolysates in cellulose acetate at ph 8.6 or in capillary electrophoresis showed no remarkable change. On electrophoresis by automated high performance liquid chromatography (HPLC) (PRIMUS CLC 385; Primus Company, Kansas City, MO, USA), an abnormal peak that was distinguished from Hb A in the amount of 14.7% was found (Figure 1A). The abnormal hemoglobin (Hb) could not be detected by capillary electrophoresis (Figure 1B). The α1-, α2- and β-globin gene analyses were performed and DNA was isolated from white blood cells using standard methods. The α1-globin gene was specifically amplified with primers P1 (forward primer, 5 non coding area): 5 -CTC TTC TGG TCC CCA CAG AC-3 and P2 (reverse primer, 3 non coding area): 5 -AGG GGC AAG AAG CAT GGC CA-3, to amplify the whole coding region and two introns. The α2-globin gene was specifically amplified with primers P1 and P3 (reverse primer, 3 non coding area): 5 -CAG GAA GGG CCG GTG CAA GGA G-3, to amplify the whole coding region and two introns. The β-globin genes were amplified with primers P4 (forward primer, 5 non coding area): 5 -GCT TAC CAA GCT GTG ATT CC-3, and P5 (reverse primer, 3 non coding area): 5 -GGA CTT AGG GAA CAA AGG AAC C-3, to amplify the whole coding region and two introns. The polymerase chain reaction (PCR) conditions were as follows: the amplification was performed in 50 μl which consisted of 500 ng genomic DNA, 50 ng each of the primers (P1 + P2 or P1 + P3 or P4 + P5), 0.3% DMSO, 50 μm of each dntp, 1 PCR buffer and 2.5 units of Taq (A) HPLC HBA 82.8% (B) CE HBA 97.7% HBX 14.7% HBA 2 2.5% HBA 2 2.3% FIGURE 1 A) An abnormal peak was distinguished from Hb A by HPLC and amounted to 14.7% of the total Hb. B) The abnormal hemoglobin could not be detected by capillary electrophoresis.
4 Hb Hekinan in the ese 497 polymerase (Perkin Elmer Corporation, Norwalk, CT, USA), using 35 cycles of 2 min. at 94 C for denaturation, 2 min. at 60 C for annealing, and 3 min. at 72 C for extension, and a final extension of 5 min. at 72 C, using a Perkin Elmer Cetus PCR thermocycler. The PCR products were isolated and sequenced as described previously (5,6). In addition to primers P1, P2, P3, P4, and P5, the sequencing primers for the α-globin gene were as follows: P6 (reverse primer, intron 1): 5 -CAG GAC GGT TGA GGG TGG CCT-3, P7 (forward primer, intron 1): 5 -ACC CCA CCC CTC ACT CGC TT-3, P8 (reverse primer, intron 2): 5 -TGC GAG GAA GGC GCC ATC TC- 3 and P9 (forward primer, intron 2): 5 -GCA GAG GAT CAC GCG GGT TG-3. The sequencing primers for the β-globin genes were: P10 (reverse primer, intron 1): 5 -GGC AGA GAG AGT CAG TGC CTA-3, P11 (reverse primer, exon 2, near intron 2): 5 -CCT GAA GTT CTC AGG ATC CA-3 and P12: (forward primer, intron 2): 5 -TGC TAA TCA TGT TCA TAC CT-3. The results showed a G T substitution at the third base of codon 27 of α1-globin gene (GAG GAT) that resulted in the substitution of a glutamic acid for an aspartic acid residue (Figure 2A). This mutation abolishes an HaeIII restriction enzyme site. We further amplified the mutation area using primers (P1 + P6), and the PCR products were digested with HaeIII. The results are shown in Figure 2B. Hb Hekinan co-migrates with Hb A on cellulose acetate electrophoresis and capillary electrophoresis, and is difficult to distinguish from Hb A by (A) Normal (B) Codon bp 73bp 48bp 65bp 200bp 100bp N M HaeIII FIGURE 2 The results of direct sequencing of the α1-globin gene showed a G T substitution at codon 27. Upper case: normal control; lower case: the variant. The results of restriction enzyme HaeIII digestion of PCR products showed that the patient (lane 3) and positive control (lane 1) had fragments of 121 and 65 bp, respectively (the18 bp fragment was not visible), and the normal control (lane 2) had fragments of 73, 65 and 48 bp, respectively (the 18 bp fragment was not visualized). M: 100 bp ladder.
5 498 H.-C. Shih et al. these methods. The HPLC procedure using a weak cation exchange material with polyaspartic acid can differentiate these two Hbs. The Hb variant can be confirmed by either sequencing analysis of the α1-globin gene product or HaeIII digestion of the amplified α1-globin gene product. ACKNOWLEDGMENTS This study was supported by a grant from China Medical University Hospital, (DMR ). REFERENCES 1. Harano T, Harano K, Imai N, Ueda S, Seki M. An electrophoretically silent hemoglobin variant, Hb Hekinan [α27(b8)glu Asp] found in a Japanese. Hemoglobin 1988; 12(1): Merault G, Keclard L, Desfontaines L, Saint-Martin C, Blouquit Y, Rosa J, Galacteros F. Hemoglobin Hekinan [α 2 27(B8)Glu Aspβ 2 ] detected in Guyana. Hemoglobin 1989; 13(4): Zhao W, Wilson JB, Webber BB, Kutlar A, Tamagnini GP, Kuam B, Huisman THJ. Hb Hekinan observed in three Chinese from Macau; identification of the GAG GAT mutation in the α1-globin gene. Hemoglobin 1990; 14(6): Fucharoen S, Changtrakun Y, Ratanasiri T, Fucharoen G, Sanchaisuriya K. Complex interaction of Hb Hekinan [α27(b8)glu Asp] and Hb E [β26(b8)glu Lys] with a deletional α-thalassemia 1 in a Thai family. Eur J Haematol 2003; 70(5): Chang J-G, Yang T-Y, Perng L-I, Wang N-M, Peng C-T, Tsai C-H. Hb Siriraj: a G A substitution at codon 7 of the β-globin chain creates an MboII cutting site. Hemoglobin 1999; 23(2): Chang J-G, Liu H-C, Shih M-C, Liu S-C, Chan W-L, Tsai F-J. Unstable Hb Perth in a ese subject: a T C substitution at codon 32 of the β-globin gene creates an MspI site. Hemoglobin 2002; 26(1):91 94.
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