Characterization of mutants of the vitamin D-binding protein/group-specific component: molecular evolution of GC*1A2 and GC*1A3, common in some Asian populations |
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Authors: | I. Yuasa A. Kofler A. Braun K. Umetsu R. Bichlmaier S. Kammerer H. Cleve |
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Affiliation: | (1) Institut für Anthropologie und Humangenetik der Universität München, D-80333 München, Germany;(2) Department of Legal Medicine, Tottori University School of Medicine, 683 Yonago, Japan;(3) Dr. von Haunersches Kinderspital der Universität München, D-80337 München, Germany;(4) Department of Forensic Medicine, Yamagata University School of Medicine, 990-23 Yamagata, Japan |
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Abstract: | A well defined polymorphism of vitamin D-binding/ group-specific component (GC) resides in exon 11. To characterize the molecular basis of GC*1A2 and GC*1A3, common in some Asian populations, we analyzed all coding exons amplified by the polymerase chain reaction. GC*1F was divided into GC*1Fc and GC*1FT by a C-T transition in the third nucleotide of the codon (TGC/T) for cysteine283 in exon 8. The sequencing of exons 8 and 11 showed that GC*1A2 and GC*1A3 had occurred on a GC*1Fc genetic background. They also shared a substitution of cysteine (TGC) for arginine (CGC) at position 429 in exon 11. GC*1A2 was characterized by having glycine (GGC) instead of serine (AGC) at position 335 in exon 9. GC*1A2 evolved from GC*1FT by three mutational events, i.e. GC*1FTGC*1FcGC*1A3 GC*1A2. No evidence was obtained for the existence of the duplicated gene GC*1F · 1A2 suggested by isoelectric focusing (IEF) of serum samples. The idea that the characteristic banding pattern of GC*1F · 1A2 after IEF results from partial formation of a disulfide bond in the additional cysteine at position 429 is discussed.Deceased |
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