| http://purl.uniprot.org/citations/19681047 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19681047 | http://www.w3.org/2000/01/rdf-schema#comment | "Metabolic control analysis of tumor glycolysis has indicated that hexokinase (HK) and glucose transporter (GLUT) exert the main flux control (71%). To understand why they are the main controlling steps, the GLUT and HK kinetics and the contents of GLUT1, GLUT2, GLUT3, GLUT4, HKI, and HKII were analyzed in rat hepatocarcinoma AS-30D and HeLa human cervix cancer. An improved protocol to determine the kinetic parameters of GLUT was developed with D-[2-(3)H-glucose] as physiological substrate. Kinetic analysis revealed two components at low- and high-glucose concentrations in both tumor cells. At low glucose and 37 degrees C, the V(max) was 55 +/- 20 and 17.2 +/-6 nmol (min x mg protein)(-1), whereas the K(m) was 0.52 +/- 0.7 and 9.3 +/-3 mM for hepatoma and HeLa cells, respectively. GLUT activity was partially inhibited by cytochalasin B (IC(50) = 0.44 +/- 0.1; K(i) = 0.3 +/-0.1 microM) and phloretin (IC(50) = 8.7 microM) in AS-30D hepatocarcinoma. At physiological glucose, GLUT1 and GLUT3 were the predominant active isoforms in HeLa cells and AS-30D cells, respectively. HK activity in HeLa cells was much lower (60 mU/mg protein) than that in AS-30D cells (700 mU/mg protein), but both HKs were strongly inhibited by G6P. HKII was the predominant isoform in AS-30D carcinoma and HeLa cells. The much lower GLUT V(max) and catalytic efficiency (V(max)/K(m)) values in comparison to those of G6P-sensitive HK suggested the transporter exerts higher control on the glycolytic flux than HK in cancer cells. Thus, GLUT seems a more adequate therapeutic target."xsd:string |
| http://purl.uniprot.org/citations/19681047 | http://purl.org/dc/terms/identifier | "doi:10.1002/jcp.21885"xsd:string |
| http://purl.uniprot.org/citations/19681047 | http://purl.uniprot.org/core/author | "Moreno-Sanchez R."xsd:string |
| http://purl.uniprot.org/citations/19681047 | http://purl.uniprot.org/core/author | "Rodriguez-Enriquez S."xsd:string |
| http://purl.uniprot.org/citations/19681047 | http://purl.uniprot.org/core/author | "Marin-Hernandez A."xsd:string |
| http://purl.uniprot.org/citations/19681047 | http://purl.uniprot.org/core/author | "Gallardo-Perez J.C."xsd:string |
| http://purl.uniprot.org/citations/19681047 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19681047 | http://purl.uniprot.org/core/name | "J Cell Physiol"xsd:string |
| http://purl.uniprot.org/citations/19681047 | http://purl.uniprot.org/core/pages | "552-559"xsd:string |
| http://purl.uniprot.org/citations/19681047 | http://purl.uniprot.org/core/title | "Kinetics of transport and phosphorylation of glucose in cancer cells."xsd:string |
| http://purl.uniprot.org/citations/19681047 | http://purl.uniprot.org/core/volume | "221"xsd:string |
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