NDLI: Recombinant human hemoglobins designed for gene therapy of sickle cell disease.

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Recombinant human hemoglobins designed for gene therapy of sickle cell disease.

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Recombinant human hemoglobins designed for gene therapy of sickle cell disease.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Townes, T. M. Asakura, T. Reilly, M. P. Mccune, S. L. Chomo, M. J.
Description	Author Affiliation: McCune SL ( Department of Biochemistry and Molecular Genetics, School of Medicine, University of Alabama at Birmingham 35294.);
Abstract	Two human hemoglobins designed to inhibit the polymerization of sickle hemoglobin (Hb S; alpha 2 beta S2) have been produced. Mutations that disrupt the ability of Hb S to form polymers were introduced into the normal human beta-globin gene by site-specific mutagenesis. These mutations affect the axial and lateral contacts in the sickle fiber. The recombinant hemoglobin designated anti-sickling hemoglobin 1 (Hb AS1) contains the mutations beta 22 glutamic acid to alanine and beta 80 asparagine to lysine. Hb AS2 has the same beta 22 glutamic acid to alanine mutation combined with beta 87 threonine to glutamine. Human alpha- and beta AS-globin genes were separately fused downstream of beta-globin locus control region sequences and these constructs were coinjected into fertilized mouse eggs. Transgenic mouse lines that synthesize high levels of each anti-sickling hemoglobin were established and anti-sickling hemoglobins were purified from hemolysates and characterized. Both AS hemoglobins bind oxygen cooperatively and the oxygen affinities of these molecules are in the normal range. Delay time experiments demonstrate that Hb AS2 is a potent inhibitor of Hb S polymerization; therefore, locus control region beta AS2-globin gene constructs may be suitable for future gene therapy of sickle cell disease.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Anemia, Sickle Cell Therapy Globins Genetics Hemoglobin, Sickle Antagonists & Inhibitors Hemoglobins Biosynthesis Recombinant Proteins 2,3-Diphosphoglycerate Amino Acid Sequence Blood Animals Diphosphoglyceric Acids Genetic Therapy Isolation & Purification Metabolism Kinetics Mice Mice, Transgenic Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides Oxyhemoglobins Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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