Placenta polymorphism

Tanabe M, Ieiri I, Nagata N, Inoue K, Ito S, Kanamori Y et al. Expression of P-glycoprotein in human placenta relation to genetic polymorphism of the multidrug resistance (MDR)-l gene. J Pharmacol Exp Ther 2001 297(3) 1137-1143. 

Kobayashi, D., leiri, I., Hirota, T., et al. (2005) Eunctional assessment of ABCG2 (BCRP) gene polymorphisms to protein expression in human placenta. Drug Metab. Dispos. 33, 94-101. 

Myatt, L., Brockman, D. E., Eis, A. L., and Pollock, J. S. (1993). Immunohistochemical localization of nitric oxide synthase in the human placenta. Placenta 14, 487-495. Nadaud, S., Bonnardeaux, A., Lathrop, M., and Soubrier, F. (1994). Gene structure, polymorphism and mapping of the human endothelial nitric oxide synthase gene. Biochem. Bio-phys. Res. Commun. 198, 1027-1033. 

Human cells contain an intracellular protein whose properties resemble those of the Ah receptor in animals. Binding studies and hydrodynamic analyses have identified an Ah receptor-like protein(s) in a variety of human tissues. Functional Ah receptors have been found in many human tissues, including lymphocytes, liver, lung, and placenta. By analogy with the existence of multiple receptor forms in mice, it is reasonable to anticipate that the human population will also be polymorphic with respect to Ah receptor structure and function [170]. Therefore, it is also reasonable to expect that humans may differ from one another in their susceptibilities to TCDD. The binding and hydrodynamic properties of the Ah receptor differ relatively little across species and tissues yet responses vary widely it is impossible, therefore, to account for the diversity of TCDD s biological effects by characteristics of the receptor alone. 

---