Functional consequences of an in vivo mutation in exon 10 of the human GLUT1 gene
| Autor: | Elena Gertsen, Peter E. Lange, Konrad Keller, Ingrid Monden, Jörg Klepper |
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| Rok vydání: | 2003 |
| Předmět: |
Gene isoform
Erythrocytes Monosaccharide Transport Proteins Transport kinetics Cytochalasin B Blotting Western Molecular Sequence Data Mutant Biophysics Deoxyglucose Tritium Biochemistry Frameshift mutation Xenopus laevis Exon chemistry.chemical_compound Structural Biology Genetics Animals Humans Amino Acid Sequence Insertion Frameshift Mutation Molecular Biology Facilitated glucose transporter isoform 1 Glucose Transporter Type 1 Microscopy Confocal Guanosine biology Glucose transporter Biological Transport Exons Cell Biology Molecular biology carbohydrates (lipids) Kinetics chemistry Oocytes biology.protein GLUT1 Xenopus oocyte Facilitated glucose transporter isoform 1 deficiency syndrome |
| Zdroj: | FEBS Letters. 555:274-278 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(03)01247-x |
| Popis: | The functional consequences of an in vivo heterozygous insertion mutation in the human facilitated glucose transporter isoform 1 (GLUT1) gene were investigated. The resulting frameshift in exon 10 changed the primary structure of the C-terminus from 42 in native GLUT1 to 61 amino acid residues in the mutant. Kinetic studies on a patient’s erythrocytes were substantiated by expressing the mutant cDNA in Xenopus laevis oocytes. Km and Vmax values were clearly decreased explaining pathogenicity. Targeting to the plasma membrane was comparable between mutant and wild-type GLUT1. Transport inhibition by cytochalasin B was more effective in the mutant than in the wild-type transporter. The substrate specificity of GLUT1 remained unchanged. |
| Databáze: | OpenAIRE |
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