Simultaneous preparation of paired, syncytial, microvillous and basal membranes from human placenta

Illsley, Nicholas P.; Wang, Zhi-Qiong; Gray, Andrea; Sellers, M.C.; Jacobs, M.

doi:10.1016/0005-2736(90)90157-j

Cited by 133 publications

(60 citation statements)

References 25 publications

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“…We have previously shown that isolated syncytiotrophoblast plasma membranes show only little or no contamination by markers for intracellular organelles (34). These results confirm that this plasma membrane isolation procedure produces MVMs and BMs with high enrichment and low contamination (24).…”

Section: Resultssupporting

confidence: 78%

Alterations in the Activity of Placental Amino Acid Transporters in Pregnancies Complicated by Diabetes

et al. 2002

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Alterations in placental transport may contribute to accelerated fetal growth in pregnancies complicated by diabetes. We studied the activity of the syncytiotrophoblast amino acid transporter system A and the transport of the essential amino acids leucine, lysine, and taurine. Syncytiotrophoblast microvillous plasma membranes (MVMs) and basal plasma membranes (BMs) were isolated from placentas obtained from normal pregnancies and pregnancies complicated by gestational diabetes mellitus (GDM) and type 1 diabetes, with and without large-for-gestational-age (LGA) fetuses. Amino acid transport was assessed using radio-labeled substrates and rapid filtration techniques. System A activity in MVM was increased (65-80%, P < 0.05) in all groups with diabetes independent of fetal overgrowth. However, MVM system A activity was unaffected in placentas of normal pregnancies with LGA fetuses. MVM leucine transport was increased in the GDM/LGA group. In BMs, amino acid transport was unaffected by diabetes. In conclusion, diabetes in pregnancy is associated with an increased system A activity in MVM, and MVM leucine transport is increased in the GDM/LGA group. We suggest that these changes result in an increased uptake of neutral amino acids across MVM, which may be used in placental metabolism or be delivered to the fetus. The increased MVM leucine uptake in the GDM/LGA group may contribute to accelerated fetal growth in these patients.

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Section: Resultssupporting

confidence: 78%

Alterations in the Activity of Placental Amino Acid Transporters in Pregnancies Complicated by Diabetes

et al. 2002

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“…The ratio of placental alkaline phosphatase activity enrichment of BM compared with that of apical membranes was 0.1 for the placentae used in this study, lower or equivalent to that from several other reports for single or paired apical and basal membrane preparations (Glazier et al, 1990;Illsley et al, 1990) as we demonstrated previously (Jimenez et al, 2004). In addition, for both MVM and BM vesicles, orientation is preferentially right-side out, as reported previously (Illsley et al, 1990). For LMVM vesicles, data about orientation are not available.…”

Section: Introductionsupporting

confidence: 71%

Expression and Distribution of Nucleoside Transporter Proteins in the Human Syncytiotrophoblast

Errasti-Murugarren¹,

Díaz²,

Godoy³

et al. 2011

Mol Pharmacol

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The plasma membrane distribution and related biological activity of nucleoside transporter proteins (NTs) were investigated in human syncytiotrophoblast from term placenta using a variety of approaches, including nucleoside uptake measurements into vesicles from selected plasma membrane domains, NT immunohistochemistry, and subcellular localization (basal, heavy, and light apical membranes as well as raft-enriched membranes from the apical domain). In contrast with other epithelia, in this epithelium, we have identified the high-affinity pyrimidine-preferring human concentrative nucleoside transporter (hCNT) 1 as the only hCNT-type protein expressed at both the basal and apical membranes. hCNT1 localization in lipid rafts is also dependent on its subcellular localization in the apical plasma membrane, suggesting a complex cellular and regional expression. Overall, this result favors the view that the placenta is a pyrimidine-preferring nucleoside sink from both maternal and fetal sides, and hCNT1 plays a major role in promoting pyrimidine salvage and placental growth. This finding may be of pharmacological relevance, because hCNT1 is known to interact with anticancer nucleoside-derived drugs and other molecules, such as nicotine and caffeine, for which a great variety of harmful effects on placental and fetal development, including intrauterine growth retardation, have been reported.

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“…Microvillous membrane vesicles were prepared according to the methods of Illsley et al (1990). The final membrane pellet was resuspended in buffer containing 10 mM Tris-HCl (pH 7.4) and 250 mM sucrose with a 25-gauge needle through which the suspension was passed 10 times.…”

Section: Materials [mentioning

confidence: 99%

Expression and Function of Abcb1 and Abcg2 in Human Placental Tissue

Kolwankar¹,

Glover²,

Ware³

et al. 2005

Drug Metab Dispos

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ABSTRACT:The placenta plays an important role in modulating xenobiotic passage from mother to fetus. Studies in mice have demonstrated that placental ABCB1 and ABCG2 can affect the transfer of drugs across the placental barrier, suggesting a role for these transporters in protecting the fetus from environmental toxicants or drugs ingested by the mother during pregnancy. To assess the role of these transporters in the human placenta, studies were conducted to evaluate the expression and functional activity of placental ABCB1 and ABCG2. The effect of maternal smoking on these placental transporters was also assessed.

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Simultaneous preparation of paired, syncytial, microvillous and basal membranes from human placenta

Cited by 133 publications

References 25 publications

Alterations in the Activity of Placental Amino Acid Transporters in Pregnancies Complicated by Diabetes

Alterations in the Activity of Placental Amino Acid Transporters in Pregnancies Complicated by Diabetes

Expression and Distribution of Nucleoside Transporter Proteins in the Human Syncytiotrophoblast

Expression and Function of Abcb1 and Abcg2 in Human Placental Tissue

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