In the kidney, a branched-chain amino acid transferase (BCAAT) activit
y has been localized mainly in the medullary thick ascending limb (MTA
L) of the rat.nephron. BCAAT is the first enzyme involved in the metab
olic pathway of the three branched-chain amino acids (BCAA): leucine,
isoleucine and valine. The present work has been designed to study val
ine catabolism. Valine and leucine oxidation in MTAL were compared by
measuring the rate of (CO2)-C-14 produced when these substrates were i
ncubated as sole substrates at a final concentration of 1 mM. Since gl
ucose is also metabolized in MTAL, valine and leucine oxidation were q
uantified also in the presence of glucose (1 mM). The results show tha
t: (1) valine oxidation was greater than that of leucine (63.0 +/- 4.7
vs 39.7 +/- 5.2 pmol . h-1 . mug-1 protein, respectively; P < 0.001).
As previously shown, leucine oxidation was found to be increased in t
he presence of glucose whereas glucose oxidation decreased. In contras
t, the presence of glucose strongly diminished valine oxidation (19.2
+/- 1.9 vs 63.1 - 4.7 pmol . h-1 . mug 1 protein; P < 0.001) whereas g
lucose oxidation was increased in the presence of valine (268.2 +/- 14
.9 vs 229.6 +/- 16.2 pmol . h-1 . mug-1 protein; P < 0.05). We conclud
e that in rat MTAL, under near physiological conditions (in the presen
ce of glucose, as in vivo), leucine is a preferential respiratory fuel
as compared to valine. However, valine supports energetic salt transp
ort and facilitates glucose oxidation.