The ontogeny of amino acid transport in rat kidney II. Kinetics of uptake and effect of anoxia

1971 ◽  
Vol 249 (2) ◽  
pp. 364-372 ◽  
Author(s):  
Kurt E. Baerlocher ◽  
Charles R. Scriver ◽  
Fazl Mohyuddin
1962 ◽  
Vol 237 (7) ◽  
pp. 2265-2270
Author(s):  
Leon E. Rosenberg ◽  
Sylvia J. Downing ◽  
Stanton Segal

1975 ◽  
Vol 19 (1) ◽  
pp. 127-139
Author(s):  
M. Frank ◽  
S.B. Horowitz

Ultra-low temperature techniques (microdissection and autoradiography) were used to study the nucleocytoplasmic distribution and transport of alpha-aminoisobutyric acid (AIB) in an amino acid-accumulating cell. In amphibiam oocytes incubated in AIB, the nuclear concentration of this non-metabolizable amino acid exceeds the cytoplasmic concentration by 45%, remaining constant both over time and variation in substrate concentration. The kinetics of uptake suggest that this nucleo-cytoplasmic asymmetry arises from solubility differences between the 2 compartments, and that the nuclear envelope plays a negligible role in amino acid transport. A solute exclusion model is offered to explain the nucleocytoplasmic asymmetry.


1987 ◽  
Vol 49 (5) ◽  
pp. 1651-1658 ◽  
Author(s):  
Quentin R. Smith ◽  
Seiji Momma ◽  
Masaki Aoyagi ◽  
Stanley I. Rapoport

1992 ◽  
Vol 263 (6) ◽  
pp. F1087-F1092 ◽  
Author(s):  
Y. Kanai ◽  
M. G. Stelzner ◽  
W. S. Lee ◽  
R. G. Wells ◽  
D. Brown ◽  
...  

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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