Gene/Protein
Disease
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Enzyme
Compound
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Target Concepts:
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Query: UMLS:C0028961 (
oliguria
)
1,847
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The structural requirements for aromatic amino acid reabsorption and secretion in the dog were investigated using a series of tyrosine analogs. In clearance experiments, l-tyrosine and l-phenylalanine underwent net reabsorption at rates 5 to 6 times greater than those of the corresponding d-enantiomers and about 1.5 time those of o- and m-dl-tyrosine. 3-(p-hydroxyphenyl)Propionic acid underwent net secretion under conditions of polyuria and high urinary pH and net reabsorption under conditions of
oliguria
and low pH. In stop-flow experiments, (U/Pl-amino acid)/(U/Pln) ratios, where U/P = concentration in urine and plasma and In = inulin, of proximal tubular samples were 1.5 to 5-fold greater than the control (free-flow) values of 0.1 to 0.3, indicating tubular secretion. Secretion was inhibited, and net reabsorption enhanced, by probenecid, p-aminohippuric acid and 2,4-dinitrophenol. (U/Pd-amino acid)/(U/
PIN
) ratios of proximal tubular samples were below the control values of 0.6 to 0.8, indicating tubular reabsorption. Probenecid had no effect on the overall pattern but caused a slight decrease in the relative clearance values. The stop-flow pattern of 3-(p-hydroxyphenyl)propionic acid excretion was similar to that of the I-amino acids. It was concluded that the I-amino acids undergo bidirectional transport and that the I-configuration and amino group are required for optimal active reabsorption, whereas ring hydroxylation has little effect on reabsorption transport. No absolute structural requirements for active secretion were elucidated.
...
PMID:Structural specificity in the renal tubular transport of tyrosine. 728 17