In vitro Perfusion Studies of the Human Placenta Angioradiographic Study of the Maternal Circulation (With Colour Plate I)

1973 ◽  
Vol 4 (1) ◽  
pp. 50-60 ◽  
Author(s):  
J.E. Rourke ◽  
L.V. Gould ◽  
P.A. Rice ◽  
R.E.L. Nesbitt, Jr.
Keyword(s):  
Human Placenta ◽  
Maternal Circulation ◽  
Perfusion Studies ◽  
Colour Plate

In vitro Perfusion Studies of the Human Placenta

1976 ◽  
Vol 7 (4) ◽  
pp. 213-221 ◽  
Author(s):  
Philip A. Rice ◽  
James E. Rourke ◽  
Robert E.L. Nesbitt, Jr.
Keyword(s):  
Human Placenta ◽  
Perfusion Studies

In vitro Perfusion Studies of the Human Placenta

1976 ◽  
Vol 7 (6) ◽  
pp. 344-357 ◽  
Author(s):  
Philip A. Rice ◽  
Robert E.L. Nesbitt, Jr. ◽  
James E. Rourke
Keyword(s):  
Human Placenta ◽  
In Vitro Perfusion ◽  
Perfusion Studies

In vitro Perfusion Studies of the Human Placenta

1973 ◽  
Vol 4 (5-6) ◽  
pp. 243-253 ◽  
Author(s):  
Robert E.L. Nesbitt, jr. ◽  
Philip A. Rice ◽  
James E. Rourke
Keyword(s):  
Human Placenta ◽  
Perfusion Studies

In vitro Perfusion Studies of the Human Placenta

1970 ◽  
Vol 1 (4) ◽  
pp. 185-203 ◽  
Author(s):  
R.E.L. Nesbitt, Jr. ◽  
P.A. Rice ◽  
J.E. Rourke ◽  
V.F. Torresi ◽  
A.M. Souchay
Keyword(s):  
Human Placenta ◽  
Perfusion Studies

In vitro perfusion studies of the human placenta

1979 ◽  
Vol 133 (6) ◽  
pp. 649-655 ◽  
Author(s):  
Philip A. Rice ◽  
James E. Rourke ◽  
Robert E.L. Nesbitt
Keyword(s):  
Human Placenta ◽  
In Vitro Perfusion ◽  
Perfusion Studies

PERFUSION STUDIES OF THE HUMAN PLACENTA

1968 ◽  
Vol 57 (3) ◽  
pp. 379-385 ◽  
Author(s):  
Montserrat de Miquel ◽  
Philip Troen
Keyword(s):  
Human Placenta ◽  
Conversion Product ◽  
Perfusion Studies ◽  
17 Hydroxyprogesterone

ABSTRACT Mid-pregnancy human placentas were perfused in vitro with 14C-17α-hydroxyprogesterone. The major conversion product was 14C-17α,20α-dihydroxy-pregn-4-en-3-one in an uncorrected yield of 24% from the starting 17-hydroxyprogesterone. Traces of 14C-androstenedione, 14C-oestrone and 14C-17β-oestradiol detected suggest 17–20 desmolase activity in mid-pregnancy placentas.

scholarly journals In vitro function and in situ localization of Multidrug Resistance-associated Protein (MRP)1 (ABCC1) suggest a protective role against methyl mercury-induced oxidative stress in the human placenta

2020 ◽  
Vol 94 (11) ◽  
pp. 3799-3817
Author(s):  
Sebastian Granitzer ◽  
Isabella Ellinger ◽  
Rumsha Khan ◽  
Katharina Gelles ◽  
Raimund Widhalm ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Multidrug Resistance ◽  
Human Placenta ◽  
Methyl Mercury ◽  
Amino Acid Transporters ◽  
Maternal Circulation ◽  
Mercury Transport ◽  
Placental Cells

Abstract Methyl mercury (MeHg) is an organic highly toxic compound that is transported efficiently via the human placenta. Our previous data suggest that MeHg is taken up into placental cells by amino acid transporters while mercury export from placental cells mainly involves ATP binding cassette (ABC) transporters. We hypothesized that the ABC transporter multidrug resistance-associated protein (MRP)1 (ABCC1) plays an essential role in mercury export from the human placenta. Transwell transport studies with MRP1-overexpressing Madin-Darby Canine Kidney (MDCK)II cells confirmed the function of MRP1 in polarized mercury efflux. Consistent with this, siRNA-mediated MRP1 gene knockdown in the human placental cell line HTR-8/SVneo resulted in intracellular mercury accumulation, which was associated with reduced cell viability, accompanied by increased cytotoxicity, apoptosis, and oxidative stress as determined via the glutathione (GSH) status. In addition, the many sources claiming different localization of MRP1 in the placenta required a re-evaluation of its localization in placental tissue sections by immunofluorescence microscopy using an MRP1-specific antibody that was validated in-house. Taken together, our results show that (1) MRP1 preferentially mediates apical-to-basolateral mercury transport in epithelial cells, (2) MRP1 regulates the GSH status of placental cells, (3) MRP1 function has a decisive influence on the viability of placental cells exposed to low MeHg concentrations, and (4) the in situ localization of MRP1 corresponds to mercury transport from maternal circulation to the placenta and fetus. We conclude that MRP1 protects placental cells from MeHg-induced oxidative stress by exporting the toxic metal and by maintaining the placental cells' GSH status in equilibrium.

Prorenin secretion from human placenta perfused in vitro

1991 ◽  
Vol 260 (6) ◽  
pp. E876-E882 ◽  
Author(s):  
T. Lenz ◽  
G. D. James ◽  
J. H. Laragh ◽  
J. E. Sealey
Keyword(s):  
Chorionic Gonadotropin ◽  
Human Placenta ◽  
Human Chorionic Gonadotropin ◽  
Maternal Circulation ◽  
Fetal Circulation ◽  
Active Renin ◽  
Tissue Extracts ◽  
No Activation

We examined whether renin (prorenin plus renin) is secreted from the human placenta into the maternal or fetal circulation and compared the secretion rate to that of human chorionic gonadotropin (hCG), progesterone, and estradiol. While estradiol and progesterone passed into both circulations, renin (mostly prorenin) and hCG were secreted predominantly into the maternal circulation. To examine if prorenin passed from the maternal to the fetal circulation and vice versa, we perfused both circuits separately with exogenous recombinant human prorenin. No prorenin passed from maternal to fetal circulations, but a small amount (less than 10%) slowly passed from fetal to maternal, beginning 15 min after the addition of prorenin. Exogenous prorenin was not converted to renin in either circulation. Perfusate total renin had close to 10% active renin, whereas that of tissue extracts was closer to 50%. In conclusion, the results are consistent with some tissue activation of prorenin, either in vitro or in vivo, but no activation in the maternal or fetal circulations. The human placenta may secrete prorenin into the maternal but not into the fetal circulation. The possibility that the placenta may secrete a small amount of active renin into the maternal circulation was not ruled out.

scholarly journals Transfer of Insulin Lispro Across the Human Placenta: In vitro perfusion studies

Diabetes Care ◽  
2003 ◽  
Vol 26 (5) ◽  
pp. 1390-1394 ◽  
Author(s):  
R. Boskovic ◽  
D. S. Feig ◽  
L. Derewlany ◽  
B. Knie ◽  
G. Portnoi ◽  
...  
Keyword(s):  
Human Placenta ◽  
Insulin Lispro ◽  
In Vitro Perfusion ◽  
Perfusion Studies

Transport and metabolism of ascorbic acid in human placenta

1989 ◽  
Vol 257 (1) ◽  
pp. C110-C113 ◽  
Author(s):  
J. L. Choi ◽  
R. C. Rose
Keyword(s):  
Ascorbic Acid ◽  
Cellular Uptake ◽  
Human Placenta ◽  
Placental Tissue ◽  
Reduced Form ◽  
Cellular Transport ◽  
Maternal Circulation ◽  
Uptake Mechanism ◽  
Acid Metabolites

The role of human placenta in cellular transport and metabolism of the potentially toxic oxidized form and the useful reduced form of ascorbic acid was examined in surviving tissue fragments in vitro. At the end of a 60-min incubation with the 14C label nominally present in the reduced form, a tissue-to-medium ratio in excess of unity was reached. The importance of evaluating uptake of the ascorbic acid metabolites is evident from a careful assay of 14C label present in the bathing media. Significant spontaneous oxidation occurs, which is slowed or reversed to a limited extent by the presence of placental tissue. Uptake of the oxidized substrate, dehydro-L-ascorbic acid, proceeds much more rapidly than uptake of ascorbic acid. At the end of a 15-min incubation, most of the substrate taken up was in the reduced form. From an additional evaluation of 14C label in the bath it is calculated that 25% of ascorbic acid formed by the tissue is released within 15 min. The cellular uptake mechanism for dehydro-L-ascorbic acid is not shared by glucose and is not dependent on the presence of Na+ but is dependent on intact cellular metabolism. The finding of avid cellular uptake and reduction of the oxidized form of ascorbic acid supports the concept that the placenta helps to clear the toxic molecule from the maternal circulation, metabolizes it, and delivers the useful reduced form to the fetus.

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