Placenta has a wide range of functions. Some are supported by novel genes that have evolved following gene duplication events while others require acquisition of gene expression by the trophoblast. Although not expressed in the placenta, high-affinity fetal hemoglobins play a key role in placental gas exchange. They evolved following duplications within the beta-globin gene family with convergent evolution occurring in ruminants and primates. In primates there was also an interesting rearrangement of a cassette of genes in relation to an upstream locus control region. Substrate transfer from mother to fetus is maintained by expression of classic sugar and amino acid transporters at the trophoblast microvillous and basal membranes. In contrast, placental peptide hormones have arisen largely by gene duplication, yielding for example chorionic gonadotropins from the luteinizing hormone gene and placental lactogens from the growth hormone and prolactin genes. There has been a remarkable degree of convergent evolution with placental lactogens emerging separately in the ruminant, rodent, and primate lineages and chorionic gonadotropins evolving separately in equids and higher primates. Finally, coevolution in the primate lineage of killer immunoglobulin-like receptors and human leukocyte antigens can be linked to the deep invasion of the uterus by trophoblast that is a characteristic feature of human placentation.

Evolution of Placental Function in Mammals: The Molecular Basis of Gas and Nutrient Transfer, Hormone Secretion, and Immune Responses

Placental transport and metabolism of amino acids.

Transport of amino acids in the placenta.

Placental transport produces concentrations of amino acids in fetal blood greater than those of maternal blood. Competitive inhibition studies of zwitterionic amino acid transport in isolated vesicles from the microvillous (maternal facing) plasma membranes of syncytiotrophoblast defined three transport systems: 1) a sodium-dependent system that supports methylaminoisobutyric acid (MeAIB) transport and has the characteristics of an A system; 2) a sodium-independent system with a high affinity for leucine and other amino acids with branched or aromatic side chains; and 3) a sodium-independent system with a preference for alanine as a substrate. The two sodium-independent systems could be further discriminated by marked specificity for trans stimulation with alanine or with leucine. System ASC, known to be present in whole placenta, and the neutral brush-border or imino systems of other polarized epithelia were apparently absent. Kinetic characteristics of the A system make it the probable primary driving force for concentrative transfer of its substrate amino acids to the fetus. Characteristics of the high-affinity leucine system demonstrated that it is saturated by normal serum leucine concentrations. Regulation of either system has the potential to alter placental amino acid uptake and transfer to the fetus.

Neutral amino acid transport systems of microvillous membrane of human placenta

Normal fetal growth and development depend on a continuous supply of amino acids from the mother to the fetus. The placenta is responsible for the transfer of amino acids between the two circulatio...

Placental amino acid transport

1. The unidirectional influx of amino acids into the guinea-pig syncytiotrophoblast was measured using a single circulation paired-tracer dilution technique which allows separate characterization of both fetal and maternal interfaces. An in situ preparation perfused through the fetal circulation was used to examine the fetal side, while an isolated preparation perfused through both the fetal and maternal circulations was used to study both interfaces simultaneously.



2. On the fetal side the maximal uptake (Umax) determined at tracer concentrations was high for the short-chain neutral amino acid alanine (76%) and the long-chain neutrals, leucine (75%), phenylalanine (90%) and tyrosine (82%) and for the basic amino acid lysine (65%). In contrast, Umax was negligible for α-methylaminoisobutyric acid and taurine, a β-amino acid.



3. The uptake of alanine and phenylalanine on the fetal side was inhibited by both short-chain (alanine, serine, cysteine) and long-chain (phenylalanine, methionine, leucine) neutral amino acids. d-alanine had no effect on l-alanine uptake whereas d-phenylalanine significantly inhibited that of l-phenylalanine. Diaminobutyric acid, lysine and arginine were effective inhibitors of alanine uptake but had no effect on phenylalanine uptake.



4. On the maternal side uptake of alanine, phenylalanine and lysine was measured. Over a wide range of concentrations self-inhibition of alanine influx was similar to the cross-inhibition observed with phenylalanine. In contrast, the influx of phenylalanine, which was strongly self-inhibited, was only partially cross-inhibited by alanine.



5. Influx of alanine and phenylalanine was measured at various perfusate concentrations and was found to be saturable on both maternal and fetal sides. The data were fitted to a single hyperbola and, on the maternal side, the Km for alanine (10.3±2.7 m m, mean± s.e., n = 3) was three-fold higher than the value measured for phenylalanine (3·1±0·8 m m). On the fetal side the Km values for alanine (8·4±1·4 m m, n = 4) and phenylalanine (11·9±1·9 m m, n = 3) were similar.



6. The uptake of alanine, phenylalanine and lysine appeared to be highly sodium-dependent accounting for 40-70% of the total influx. However, the inhibited fractions were found to be different on the two sides of the placenta.



7. The results of uptake, cross-inhibition and Na+-dependency experiments suggest the presence of an alanine-serine-cysteine (ASC) type system and a leucine (L) type system with markedly overlapping specificities at both the fetal and maternal interfaces. Separate kinetic characterization of a two carrier system was not possible under the conditions of these experiments. However, kinetic parameters for the over-all transport of alanine and phenylalanine were measured.

Transport specificity for neutral and basic amino acids at maternal and fetal interfaces of the guinea‐pig placenta

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Transport specificity for neutral and basic amino acids at maternal and fetal interfaces of the guinea‐pig placenta