Differential transferrin expression in placentae from normal and abnormal pregnancies: a pilot study

Abstract Background The placenta is an important site for iron metabolism in humans. It transfers iron from the mother to the fetus. One of the major iron transport proteins is transferrin, which is a blood plasma protein crucial for iron uptake. Its localization and expression may be one of the markers to distinguish placental dysfunction. Methods In the experimental study we used antibody preparation, mass spectrometric analysis, biochemical and immunocytochemical methods for characterization of transferrin expression on the human choriocarcinoma cell line JAR (JAR cells), placental lysates, and cryostat sections. Newly designed monoclonal antibody TRO-tf-01 to human transferrin was applied on human placentae from normal (n = 3) and abnormal (n = 9) pregnancies. Results Variations of transferrin expression were detected in villous syncytiotrophoblast, which is in direct contact with maternal blood. In placentae from normal pregnancies, the expression of transferrin in the syncytium was significantly lower (p \u3c 0.001) when compared to placentae from abnormal ones (gestational diabetes, pregnancy induced hypertension, drug abuse). Conclusion These observations suggest that in the case of abnormal pregnancies, the fetus may require higher levels of transferrin in order to prevent iron depletion due to the stress from the placental dysfunction

Differential transferrin expression in placentae from normal and abnormal pregnancies: a pilot study

Abstract Background The placenta is an important site for iron metabolism in humans. It transfers iron from the mother to the fetus. One of the major iron transport proteins is transferrin, which is a blood plasma protein crucial for iron uptake. Its localization and expression may be one of the markers to distinguish placental dysfunction. Methods In the experimental study we used antibody preparation, mass spectrometric analysis, biochemical and immunocytochemical methods for characterization of transferrin expression on the human choriocarcinoma cell line JAR (JAR cells), placental lysates, and cryostat sections. Newly designed monoclonal antibody TRO-tf-01 to human transferrin was applied on human placentae from normal (n = 3) and abnormal (n = 9) pregnancies. Results Variations of transferrin expression were detected in villous syncytiotrophoblast, which is in direct contact with maternal blood. In placentae from normal pregnancies, the expression of transferrin in the syncytium was significantly lower (p Conclusion These observations suggest that in the case of abnormal pregnancies, the fetus may require higher levels of transferrin in order to prevent iron depletion due to the stress from the placental dysfunction.</p

Differential transferrin expression in placentae from normal and abnormal pregnancies: a pilot study-0

according to pI, in the second dimension, 10% polyacrylamide slab gel (SDS) was used. After immunoblotting with MoAb TRO-tf-01, only one isoform (arrow) of transferrins (underlined) was labeled (B). Detected antigen was identified by MALDI-TOF analysis as human transferrin (TF, sequence coverage of 31%, Z-score of 2.31). Molecular weight is shown on the left.<p><b>Copyright information:</b></p><p>Taken from "Differential transferrin expression in placentae from normal and abnormal pregnancies: a pilot study"</p><p>http://www.rbej.com/content/6/1/27</p><p>Reproductive biology and endocrinology : RB&E 2008;6():27-27.</p><p>Published online 2 Jul 2008</p><p>PMCID:PMC2459177.</p><p></p

Differential transferrin expression in placentae from normal and abnormal pregnancies: a pilot study-2

and on extravillous cytotrophoblast cells (arrowhead). B) Control experiment without primary antibody shows no transferrin staining in the syncytium of normal term placenta. C) Very low expression of transferrin in the syncytium of normal term placenta. D) Placenta of mother with gestational diabetes shows strong villous expression of transferrin. E) Placenta of mother with pregnancy-induced hypertension shows strong expression of transferrin in villous syncytium. F) Placenta of drug-abuse mother during pregnancy; the transferrin expression is very strong. Hematoxylin counterstained the nuclei.<p><b>Copyright information:</b></p><p>Taken from "Differential transferrin expression in placentae from normal and abnormal pregnancies: a pilot study"</p><p>http://www.rbej.com/content/6/1/27</p><p>Reproductive biology and endocrinology : RB&E 2008;6():27-27.</p><p>Published online 2 Jul 2008</p><p>PMCID:PMC2459177.</p><p></p

Differential transferrin expression in placentae from normal and abnormal pregnancies: a pilot study-3

Ifferent placentae. NP, normal pregnancies; GD, gestational diabetes during pregnancy; PIH, pregnancy-induced hypertension during pregnancy; DrA, drug-abusing mothers during pregnancy. Statistical analysis has shown highly significant differences (p < 0.001) between normal (a) and each of the selected abnormal pregnancy types (b).<p><b>Copyright information:</b></p><p>Taken from "Differential transferrin expression in placentae from normal and abnormal pregnancies: a pilot study"</p><p>http://www.rbej.com/content/6/1/27</p><p>Reproductive biology and endocrinology : RB&E 2008;6():27-27.</p><p>Published online 2 Jul 2008</p><p>PMCID:PMC2459177.</p><p></p

Differential transferrin expression in placentae from normal and abnormal pregnancies: a pilot study-4

according to pI, in the second dimension, 10% polyacrylamide slab gel (SDS) was used. After immunoblotting with MoAb TRO-tf-01, only one isoform (arrow) of transferrins (underlined) was labeled (B). Detected antigen was identified by MALDI-TOF analysis as human transferrin (TF, sequence coverage of 31%, Z-score of 2.31). Molecular weight is shown on the left.<p><b>Copyright information:</b></p><p>Taken from "Differential transferrin expression in placentae from normal and abnormal pregnancies: a pilot study"</p><p>http://www.rbej.com/content/6/1/27</p><p>Reproductive biology and endocrinology : RB&E 2008;6():27-27.</p><p>Published online 2 Jul 2008</p><p>PMCID:PMC2459177.</p><p></p