GLUT1
From Wikipedia, the free encyclopedia
| The introduction to this article provides insufficient context for those unfamiliar with the subject. Please help improve the article with a good introductory style. |
|
Solute carrier family 2 (facilitated glucose transporter), member 1
|
||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | SLC2A1; GLUT; GLUT1; MGC141895; MGC141896 | |||||||||||||
| External IDs | OMIM: 138140 MGI: 95755 HomoloGene: 68520 | |||||||||||||
|
||||||||||||||
| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 6513 | 20525 | ||||||||||||
| Ensembl | ENSG00000117394 | ENSMUSG00000028645 | ||||||||||||
| Uniprot | P11166 | Q3TD17 | ||||||||||||
| Refseq | NM_006516 (mRNA) NP_006507 (protein) |
NM_011400 (mRNA) NP_035530 (protein) |
||||||||||||
| Location | Chr 1: 43.16 - 43.2 Mb | Chr 4: 118.61 - 118.64 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
GLUT1 was the first glucose transporter to be characterized.[1] It is widely distributed in fetal tissues. In the adult it is expressed at highest levels in erythrocytes and also in the endothelial cells of barrier tissues such as the blood-brain barrier. Glut1 is a major receptor for take-up of Vitamin C as well as glucose, especially in non vitamin C producing mammals as part of an adaptation to compensate by participating in a Vitamin C recycling process. In mammals that do produce Vitamin C Glut4 is often expressed instead of Glut1.[2]
Contents |
[edit] Structure
GLUT1 behaves as a Michaelis-Menten enzyme and contains 12 membrane-spanning alpha helices, each containing 20 amino acid residues. A helical wheel analysis shows that the membrane spanning alpha helices are amphipathic, with one side being polar and the other side hydrophobic. Six of these membrane spanning helices are believed to bind together in the membrane to create a polar channel in the center through which glucose can traverse, with the hydrophobic regions on the outside of the channel adjacent to the fatty acid tails of the membrane.
[edit] Pathology
Mutations in the GLUT1 gene are responsible for GLUT1 deficiency or De Vivo disease, which is a rare autosomal dominant disorder.[3] This disease is characterized by a low cerebrospinal fluid glucose concentration (hypoglycorrhachia) which results from impaired glucose transport across the blood-brain barrier.
[edit] References
- ^ Mueckler M, Caruso C, Baldwin SA, et al (1985). "Sequence and structure of a human glucose transporter". Science 229 (4717): 941–5. PMID 3839598.
- ^ Montel-hagen A, Kinet S, Manel N et al (2008). "Erythrocyte Glut1 Triggers Dehydroascorbic Acid Uptake in Mammals Unable to Synthesize Vitamin C". Cell 132 (6): 1039–1048. doi:. Lay summary – ScienceDaily (2008-03-21).
- ^ Seidner G, Alvarez MG, Yeh JI, et al (1998). "GLUT-1 deficiency syndrome caused by haploinsufficiency of the blood-brain barrier hexose carrier". Nat. Genet. 18 (2): 188–91. doi:. PMID 9462754.
[edit] Further reading
- Hruz PW, Mueckler MM (2002). "Structural analysis of the GLUT1 facilitative glucose transporter (review).". Mol. Membr. Biol. 18 (3): 183–93. PMID 11681785.
- Baumann MU, Deborde S, Illsley NP (2003). "Placental glucose transfer and fetal growth.". Endocrine 19 (1): 13–22. PMID 12583599.
- Mobasheri A, Richardson S, Mobasheri R, et al. (2006). "Hypoxia inducible factor-1 and facilitative glucose transporters GLUT1 and GLUT3: putative molecular components of the oxygen and glucose sensing apparatus in articular chondrocytes.". Histol. Histopathol. 20 (4): 1327–38. PMID 16136514.

