The ontogeny of amino acid transport in rat kidney I. Effect on distribution ratios and intracellular metabolism of proline and glycine

1971 ◽  
Vol 249 (2) ◽  
pp. 353-363 ◽  
Author(s):  
Kurt E. Baerlocher ◽  
Charles R. Scriver ◽  
Fazl Mohyuddin
Keyword(s):  
Amino Acid ◽  
Amino Acid Transport ◽  
Rat Kidney ◽  
Acid Transport ◽  
Intracellular Metabolism

scholarly journals Competitive Inhibition of Dibasic Amino Acid Transport in Rat Kidney

1962 ◽  
Vol 237 (7) ◽  
pp. 2265-2270
Author(s):  
Leon E. Rosenberg ◽  
Sylvia J. Downing ◽  
Stanton Segal
Keyword(s):  
Amino Acid ◽  
Amino Acid Transport ◽  
Competitive Inhibition ◽  
Rat Kidney ◽  
Acid Transport ◽  
Dibasic Amino Acid

Expression of mRNA (D2) encoding a protein involved in amino acid transport in S3 proximal tubule

1992 ◽  
Vol 263 (6) ◽  
pp. F1087-F1092 ◽  
Author(s):  
Y. Kanai ◽  
M. G. Stelzner ◽  
W. S. Lee ◽  
R. G. Wells ◽  
D. Brown ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Proximal Tubule ◽  
Amino Acid Transport ◽  
Glucose Transporter ◽  
Rat Kidney ◽  
Expression Cloning ◽  
Acid Transport ◽  
Specific Expression ◽  
High Affinity

A rat kidney- and intestine-specific cDNA (D2) that induces high-affinity, Na(+)-independent uptake of cystine and dibasic and neutral amino acids into cRNA-injected Xenopus oocytes was recently isolated by expression cloning in our laboratory (R. G. Wells and M. A. Hediger. Proc. Natl. Acad. Sci. USA 89: 5596-5600, 1992). At present it is not known whether the D2-encoded protein functions as a transporter or as a transporter activator. To gain more insight into the role of D2 in renal amino acid transport, we studied the site of its expression in the kidney. This was determined by Northern blot analysis and by using a combination of in situ hybridization and immunocytochemistry with antibodies that recognize specific proximal tubule segments. D2 antisense RNA hybridized to the same tubular segments that were strongly positive for anti-ecto-adenosinetriphosphatase but negative for carbonic anhydrase type IV and the facilitated glucose transporter GLUT2. We conclude that D2 mRNA is strongly expressed in the rat kidney proximal tubule S3 segment, although there is weak hybridization to the S1 and S2 segments. The signal is absent in all other parts of the kidney. The S3 specific expression of D2 mRNA coincides with the site of high-affinity transport of cystine and other amino acids, consistent with the proposed involvement of D2 in these processes.

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