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Ten new silent KEL alleles were identified in Japanese individuals with the Ko phenotype.
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description of four new KEL*01M alleles
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The expression of Kell glycoprotein on RBCs is not critical to the erythrocyte function
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Through molecular genotyping we also identified polymorphisms in RhCE, Kell, Duffy, Colton, Lutheran and Scianna loci in donors and patients.
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A relatively increased KEL1 antigen expression in KEL:1,2null and KEL:1,2mod individuals suggest that the expression of Kell-XK complexes depends on the availability of the XK protein.
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High-throughput Kell, Kidd, and Duffy matrix-assisted laser desorption/ionization, time-of-flight mass spectrometry-based blood group genotyping of 4000 donors shows close to full concordance with serotyping and detects new alleles.
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After sequencing the whole KEL gene, we found three new missense mutations: c.455A>G (p.Tyr152Cys) at Exon 5, c.2111A>C (p.Pro704His) at Exon 19, and c.1726G>C (p.Gly576Arg) at Exon 16.
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A new allele, KEL(Thr193Met, Pro326Leu), has a drastic effect on the Kell glycoprotein probably due to defects in protein trafficking or reduced membrane integration.
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Sequence analysis of genomic DNA from 2 Caucasian Brazilian women revealed a new homozygous change in KEL Exon 2, a guanine to an adenine substitution at Position 71 (c.71G>A, NCBI_ss#: 831878329) leading to a premature stop codon.
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A compensatory mechanism of the KELmod allele deficient expression in heterozygote patients may exist. Retrospective analysis of 80,000 subjects showed a local KEL:1,-2 frequency 4 times lower than expected.
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A rare allele in this family has been numbered KEL*02M.04 and contains a Gly703Arg substitution that appears to cause weakened expression of Kell antigens and a Kmod phenotype when in trans with a null allele in the propositus.
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Systematic DNA analysis showed that the number of discordant phenotype/genotype results, related to silent KEL*02 alleles was higher than expected in France.
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These findings identify the translational start site and define the full cytoplasmic tail of the human Kell glycoprotein.
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Novel IVS6-13C>T mutation recognized as a cause of discrepancy between phenotyping and genotyping in KEL*3,4 polymorphism identification.
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x-ray analysis of Kell blood group protein
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Kell K2 antigen is a catalytically active metalloprotease, but the rare Kell K1 antigen is inactive
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KEL6 red blood cells have endothelin-3-converting enzyme activity
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Results demonstrate the lack of Kell expression in rodent neuronal cells and strongly suggest the same for human cerebral tissue, in which the Kellprotein was exclusively observed on RBCs in cerebral blood vessels.
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This is the first description of the KEL*1,3 allele encoding KEL1 and KEL3 on the same molecule.
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In screening 87665 unrelated healthy blood donors in China, two K(0) probands were detected; in exon 3, 185insT (Ser62Phe and a premature stop codon in exon 4
