scholarly journals Functional expression of two glucose transporter isoforms from the parasitic protozoan Leishmania enriettii.

1994 ◽  
Vol 269 (27) ◽  
pp. 17939-17943
Author(s):  
C.K. Langford ◽  
B.M. Little ◽  
M.P. Kavanaugh ◽  
S.M. Landfear
Endocrinology ◽  
1993 ◽  
Vol 133 (2) ◽  
pp. 600-607 ◽  
Author(s):  
G J Mantych ◽  
G S Hageman ◽  
S U Devaskar

1990 ◽  
Vol 259 (1) ◽  
pp. 1-1 ◽  
Author(s):  
B. Thorens ◽  
Z. -Q. Cheng ◽  
D. Brown ◽  
H. F. Lodish

Pages C279–C294: B. Thorens, Z.-Q. Cheng, D. Brown, and H. F. Lodish. “Liver glucose transporter: a basolateral protein in hepatocytes and intestine and kidney cells.” B. Thorens, H. F. Lodish, and D. Brown. “Differential localization of two glucose transporter isoforms in rat kidney.” Because of the disappointing reproduction of the halftones, these articles are reprinted at the end of the December issue.


Physiology ◽  
1995 ◽  
Vol 10 (1) ◽  
pp. 22-29 ◽  
Author(s):  
MM Mueckler

Experiments with transgenic mice overexpressing glucose transporter isoforms demonstrate the preeminence of the transport step with respect to muscle glucose disposal and whole body glucose homeostasis. These studies suggest the feasibility of controlling diabetic hyperglycemia by pharmacological or genetic enhancement of muscle glucose transport.


1990 ◽  
Vol 259 (2) ◽  
pp. C286-C294 ◽  
Author(s):  
B. Thorens ◽  
H. F. Lodish ◽  
D. Brown

The localization of two glucose transporter isoforms was mapped in the rat kidney: the high-Michaelis constant (Km; 15-20 mM) low-affinity "liver" transporter and the low-Km (1-2 mM) high-affinity "erythroid/brain" transporter. Both are basolateral membrane proteins, but the liver transporter was present exclusively in the S1 part of the proximal tubule, whereas the erythroid/brain transporter was expressed at variable levels in different nephron segments. Staining intensity was low in the straight proximal tubule (S3), intermediate in the medullary thin and thick ascending limbs, and highest in connecting segments and collecting ducts. In the collecting duct, the erythroid/brain glucose transporter was expressed at the highest level in intercalated cells; less was present in principal cells. In the papilla, only intercalated cells expressed this transporter isoform. These results suggest specific involvements of each transporter isoform in transepithelial glucose reabsorption by different segments of the proximal tubule. They also indicate that while the liver glucose transporter is present in gluconeogenic cells, there is a good correlation between the level of expression of the erythroid/brain glucose transporter and the glycolytic activity of the different nephron segments.


1989 ◽  
Vol 9 (10) ◽  
pp. 4187-4195 ◽  
Author(s):  
J C Vera ◽  
O M Rosen

We report the functional expression of two different mammalian facilitative glucose transporters in Xenopus oocytes. The RNAs encoding the rat brain and liver glucose transporters were transcribed in vitro and microinjected into Xenopus oocytes. Microinjected cells showed a marked increase in 2-deoxy-D-glucose uptake as compared with controls injected with water. 2-Deoxy-D-glucose uptake increased during the 5 days after microinjection of the RNAs, and the microinjected RNAs were stable for at least 3 days. The expression of functional glucose transporters was dependent on the amount of RNA injected. The oocyte-expressed transporters could be immunoprecipitated with anti-brain and anti-liver glucose transporter-specific antibodies. Uninjected oocytes expressed an endogenous transporter that appeared to be stereospecific and inhibitable by cytochalasin B. This transporter was kinetically and immunologically distinguishable from both rat brain and liver glucose transporters. The uniqueness of this transporter was confirmed by Northern (RNA) blot analysis. The endogenous oocyte transporter was responsive to insulin and to insulinlike growth factor I. Most interestingly, both the rat brain and liver glucose transporters, which were not insulin sensitive in the tissues from which they were cloned, responded to insulin in the oocyte similarly to the endogenous oocyte transporter. These data suggest that the insulin responsiveness of a given glucose transporter depends on the type of cell in which the protein is expressed. The expression of hexose transporters in the microinjected oocytes may help to identify tissue-specific molecules involved in hormonal alterations in hexose transport activity.


1990 ◽  
Vol 259 (6) ◽  
pp. 1-1 ◽  
Author(s):  
B. Thorens ◽  
Z. -Q. Cheng ◽  
D. Brown ◽  
H. F. Lodish

Pages C279–C294: B. Thorens, Z.-Q. Cheng, D. Brown, and H. F. Lodish. “Liver glucose transporter: a basolateral protein in hepatocytes and intestine and kidney cells.” B. Thorens, H. F. Lodish, and D. Brown. “Differential localization of two glucose transporter isoforms in rat kidney.” Because of the disappointing reproduction of the halftones, these articles are reprinted at the end of the December issue.


Sign in / Sign up

Export Citation Format

Share Document