scholarly journals Discrete structural domains determine differential endoplasmic reticulum to Golgi transit times for glucose transporter isoforms.

1994 ◽  
Vol 269 (51) ◽  
pp. 32110-32119 ◽  
Author(s):  
R C Hresko ◽  
H Murata ◽  
B A Marshall ◽  
M Mueckler
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.


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.


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