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  • Title: Chirality differences in amino acid retention and release from acid-extractable pool of cultured mammalian cells.
    Author: Wheatley DN, Slater J, Love EM, Miseta A.
    Journal: Int J Biochem Cell Biol; 1996 Dec; 28(12):1349-64. PubMed ID: 9022293.
    Abstract:
    In previous work, no chiral differences were found between D and L enantiomers of Leu in their ability to displace one another from the acid-extractable pool in mammalian cells. Recent evidence suggested otherwise. Our aim is to examine whether, in physiological range, D-amino acids have an equivalent ability to displace L-amino acids from the acid-extractable pool of HeLa cells, and vice versa. In the Millimolar range, D-Leu and L-Leu have similar uptake and displacement properties with regard to the acid-extractable pool in HeLa cells, despite only the latter isomer being incorporated into protein. Below millimolar concentration however, a distinct difference was found in the displacement of tritium-labelled L-Leu from the pool by unlabelled D-Leu compared with unlabelled L-Leu. Thus, unlabelled L-Leu in the external medium at 10(-4) or 10(-5) M displaced and equivalent amount of label from the pool ad D-Leu introduced at a concentration approx. one order of magnitude higher, respectively. Reciprocal experiments, in which the acid-extractable pool was preloaded with 3H-D-Leu, confirmed this finding. The chirality difference was noted whether pool prelabelling was carried out at 37 or 0 degrees C; but in order to avoid the complications of active transport mechanisms, the competition work reported here was done at 0 degrees C. Similar chirality differences were observed with other hydrophobic amino acids, including His, Ile, and Phe, such as, preferential displacement by the L-Leu racemer compared with the D-Leu racemer below mM levels. This was also true for the D and L forms of the non-utilisable isomer of Leu, norleucine (nLeu). We conclude that D-forms of hydrophobic amino acids have lower affinity for similar or the same intracellular binding sites involved in the acid-extractable pool than in their L-forms. The significance of these findings to amino acid pools in cells, and to the predominance of L-forms of amino acids in the biosphere is considered
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