The impact of maternal obesity on iron status, placental transferrin receptor expression and hepcidin expression in human pregnancy

2015 ◽  
Vol 39 (4) ◽  
pp. 571-578 ◽  
Author(s):  
L Garcia-Valdes ◽  
C Campoy ◽  
H Hayes ◽  
J Florido ◽  
I Rusanova ◽  
...  
Keyword(s):  
Transferrin Receptor ◽  
Maternal Obesity ◽  
Iron Status ◽  
Receptor Expression ◽  
Hepcidin Expression ◽  
Human Pregnancy ◽  
Transferrin Receptor Expression ◽  
The Impact

Effect of iron on transferrin receptor expression by human placental syncytiotrophoblast cells

1997 ◽  
Vol 9 (6) ◽  
pp. 609 ◽  
Author(s):  
Martha L. Kennedy ◽  
Gordon C. Douglas ◽  
Barry F. King
Keyword(s):  
Transferrin Receptor ◽  
Iron Status ◽  
Primary Cultures ◽  
Receptor Expression ◽  
Transferrin Receptors ◽  
Iron Salts ◽  
Intracellular Receptor ◽  
Cytotrophoblast Cells ◽  
Diferric Transferrin ◽  
Transferrin Receptor Expression

Transferrin receptor expression has been examined in primary cultures of morphologically differentiated placental syncytiotrophoblast cells. More than 90% of the cells were multinucleated. Incubation of syncytiotrophoblast for 4 days in the presence of iron salts had no effect on receptor expression assessed by measuring the binding of 125I-labelled transferrin. However, incubation of cells in the presence of human diferric transferrin (10-100 µM) led to a 50% decrease in surface and intracellular receptor expression. This down-regulation was not accompanied by a signicant decrease in receptor synthesis. In contrast to syncytiotrophoblast, expression of intracellular transferrin receptors in non-differentiated cytotrophoblast cells decreased when cells were cultured with iron salts; this was accompanied by decreased receptor synthesis. Addition of diferric transferrin to cytotrophoblast cells led to a 50% reduction in surface and intracellular receptor expression, similar to that seen in the syncytiotrophoblast. This reduction was accompanied by a decrease in receptor synthesis. In contrast to that of most cell types, the expression and distribution of trophoblast transferrin receptors were not altered by insulin, epidermal growth factor or hydrocortisone. These characteristics of syncytiotrophoblast transferrin receptor expression may assist in ensuring a supply of iron to the fetus regardless of the maternal iron status.

Impact of maternal and neonatal iron status on placental transferrin receptor expression in pregnant adolescents

Placenta ◽  
2010 ◽  
Vol 31 (11) ◽  
pp. 1010-1014 ◽  
Author(s):  
M.F. Young ◽  
E. Pressman ◽  
M.L. Foehr ◽  
T. McNanley ◽  
E. Cooper ◽  
...  
Keyword(s):  
Transferrin Receptor ◽  
Iron Status ◽  
Receptor Expression ◽  
Pregnant Adolescents ◽  
Transferrin Receptor Expression

scholarly journals Ferritin uptake by human erythroid precursors is a regulated iron uptake pathway

Blood ◽  
1996 ◽  
Vol 88 (8) ◽  
pp. 3200-3207 ◽  
Author(s):  
D Gelvan ◽  
E Fibach ◽  
EG Meyron-Holtz ◽  
AM Konijn
Keyword(s):  
Transferrin Receptor ◽  
Iron Uptake ◽  
Iron Status ◽  
Receptor Expression ◽  
Erythroid Precursor ◽  
Cellular Iron ◽  
Uptake Pathway ◽  
Iron Assimilation ◽  
Ferritin Iron ◽  
Transferrin Receptor Expression

Iron delivery to mammalian cells is traditionally ascribed to diferric transferrin (Tf). We recently reported that human erythroid precursor cells possess specific membranes receptors that bind and internalize acid isoferritin. Here we show that ferritin uptake by these cells is highly regulated and that the internalized ferritin-iron is used for home synthesis and thus, this process could constitute a physiological pathway for iron assimilation. Ferritin was internalized by a specific, saturable process, distinct from the uptake of iron associated with albumin. Ferritin uptake downregulated transferrin-receptor expression, indicating that internalized ferritin-iron was recognized as an integral part of the cellular iron content. Ferritin receptor expression was coordinated to cell development and was tightly regulated by cellular iron status. Receptor abundance was increased by iron-depletion and decreased by iron-loading, while the affinity of the ferritin receptor for acid isoferritin remained nearly constant (kd = 4.1 +/- 0.5 x 10(-6) mol/L). Under all experimental conditions, ferritin- and transferrin-receptor expression was closely coordinated, suggesting that these pathways possess a common regulatory element. It is concluded that ferritin uptake by erythroid cells constitutes an iron uptake pathway in addition to the classical transferrin uptake pathway.

scholarly journals Role of Maternal/Fetal Iron Status on Placental Transferrin Receptor Expression

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Melissa Fox Young ◽  
Marisa Foehr ◽  
Thomas McNanley ◽  
Elizabeth Cooper ◽  
Eva Pressman ◽  
...  
Keyword(s):  
Transferrin Receptor ◽  
Iron Status ◽  
Receptor Expression ◽  
Transferrin Receptor Expression

Diltiazem inhibits transferrin receptor expression and causes G1 arrest in normal and neoplastic T cells

1986 ◽  
Vol 6 (12) ◽  
pp. 4244-4250
Author(s):  
L M Neckers ◽  
S Bauer ◽  
R C McGlennen ◽  
J B Trepel ◽  
K Rao ◽  
...  
Keyword(s):  
T Cells ◽  
Transferrin Receptor ◽  
Interleukin 2 ◽  
Receptor Expression ◽  
Calcium Flux ◽  
G1 Arrest ◽  
Receptor Mrna ◽  
Interleukin 2 Receptor ◽  
Transferrin Receptor Expression ◽  
Malignant T Cells

Transferrin receptor expression is essential for the proliferation of both normal and malignant T cells. While transferrin receptor expression in normal T cells is tightly coupled to interleukin-2 receptor expression, transferrin receptor expression in malignant cells is usually constitutive and is released from this constraint. Temporally, the appearance of these membrane receptors is preceded by changes in the expression of the proto-oncogenes c-myc and c-myb. In addition, although an increase in the level of intracellular free calcium occurs early in the sequence of T-cell activation, the activation events dependent on this calcium flux have not been resolved. In the present study we report that diltiazem, an ion channel-blocking agent that inhibits calcium influx, arrested the growth in vitro of both normal and malignant human T cells in the G1 phase of the cell cycle. However, diltiazem did not inhibit the expression of c-myc or interleukin-2 receptor mRNA and protein in normal mitogen-activated T cells or the constitutive expression of c-myc and c-myb mRNA in malignant T cells (T acute lymphoblastic leukemia cells). In contrast, diltiazem prevented the induction of transferrin receptor (mRNA and protein) in normal T cells and caused a progressive loss of transferrin receptor (mRNA and protein) in malignant T cells. These data demonstrate that diltiazem can dissociate several growth-related processes normally occurring in G1 and thereby disrupt the biochemical cascade leading to cell proliferation.

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