L-serine uptake by human placental microvillous membrane vesicles
L-serine uptake by human placental microvillous membrane vesicles
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DOI:
10.1016/j.placenta.2006.06.014
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发表时间:
2007-05-01
期刊:
影响因子:
3.8
通讯作者:
Hanson, M. A.
中科院分区:
文献类型:
--
作者:
Lewis, R. M.;Glazier, J.;Hanson, M. A.
The human fetus requires more glycine than any other amino acid but placental glycine transfer to the fetus is insufficient to meet fetal demand. L-Serine could represent a major metabolic source of glycine for the human fetus but little is known about the kinetics and physiology of L-serine uptake by the human placenta. We have characterised the amino acid transport systems involved in the uptake of L-serine by the microvillous membrane of the human placental syncytiotrophoblast and compared the uptake rates to those of glycine.L-Serine uptake into microvillous membrane (MVM) vesicles was primarily mediated by system A (MeAIB inhibitable) and system L (BCH inhibitable). Further characterisation using specific substrates of LAT1 and LAT2 found the pattern of L-serine uptake was consistent with that expected for uptake mediated by LAT2. Uptakes were performed with tracer levels of C-14-L-serine, physiological levels of L-serine, or with physiological levels of amino acids. As amino acid concentrations rose, the proportion of uptake by System L decreased while uptake by uncharacterised Na+-independent systems increased.Uptake of L-serine into MVM vesicles had a V-max of 2.1 +/- 0.4 nmol/mg protein/min, which was significantly higher than for glycine (V-max 1.0 +/- 0.2 nmol/mg protein/min). This indicates that MVM vesicles have a higher uptake capacity for L-serine than glycine, despite a greater demand for glycine over serine for fetal protein synthesis. Further studies are now required to define the fate of L-serine taken up by the placenta and its importance for the fetus. (c) 2006 Elsevier Ltd. All rights reserved.