GLUT1

'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.

Contents

Structure

Pathology

References

External links

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.

Pathology

Mutations in the GLUT1 gene are responsible for GLUT1 deficiency or De Vivo disease, which is a rare autosomal dominant disorder.^[2] This disease is characterized by a low cerebrospinal fluid glucose concentration (hypoglycorrhachia) which results from impaired glucose transport across the blood-brain barrier.

References

1. Sequence and structure of a human glucose transporter, Mueckler M, Caruso C, Baldwin SA, ''et al'', , , Science, 1985
2. GLUT-1 deficiency syndrome caused by haploinsufficiency of the blood-brain barrier hexose carrier, Seidner G, Alvarez MG, Yeh JI, ''et al'', , , Nat. Genet., 1998

External links

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