Title : Caffeine inhibits glucose transport by binding at the GLUT1 nucleotide-binding site.

Pub. Date : 2015 May 15

PMID : 25715702






6 Functional Relationships(s)
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1 Intracellular ATP is also an uncompetitive GLUT1 inhibitor and shares structural similarities with caffeine, suggesting that caffeine acts at the previously characterized endofacial GLUT1 nucleotide-binding site. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
2 Intracellular ATP is also an uncompetitive GLUT1 inhibitor and shares structural similarities with caffeine, suggesting that caffeine acts at the previously characterized endofacial GLUT1 nucleotide-binding site. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
3 Caffeine and ATP displace the fluorescent ATP derivative, trinitrophenyl-ATP, from the GLUT1 nucleotide-binding site, but d-glucose and the transport inhibitor cytochalasin B do not. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
4 Caffeine and ATP displace the fluorescent ATP derivative, trinitrophenyl-ATP, from the GLUT1 nucleotide-binding site, but d-glucose and the transport inhibitor cytochalasin B do not. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
5 Like ATP, caffeine renders the GLUT1 carboxy-terminus less accessible to peptide-directed antibodies, but cytochalasin B and d-glucose do not. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
6 Caffeine binding to GLUT1 mimics the action of ATP but not cytochalasin B on sugar transport. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens