Faculty Opinions recommendation of 'Fetal side' of the placenta: anatomical mis-annotation of carbon particle 'transfer' across the human placenta.

Author(s):  
Anthony Michael Carter
2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Eva Bongaerts ◽  
Hannelore Bové ◽  
Ivo Lambrichts ◽  
Nelly D. Saenen ◽  
Wilfried Gyselaers ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Beth Holder ◽  
John D. Aplin ◽  
Nardhy Gomez-Lopez ◽  
Alexander E. P. Heazell ◽  
Joanna L. James ◽  
...  

2017 ◽  
Vol 77 (04) ◽  
pp. 379-395
Author(s):  
K Mayer-Pickel ◽  
M Gruber ◽  
B Hirschmugl ◽  
U Lang ◽  
M Cervar-Zivkovic ◽  
...  

1985 ◽  
Vol 54 (02) ◽  
pp. 431-437 ◽  
Author(s):  
M J Dembélé-Duchesne ◽  
A Laghchim Lahlou ◽  
H Thaler-Dao ◽  
A Crastes de Paulet

SummaryHuman placental cytosol inhibits platelet aggregation induced by high doses of collagen. The aim of this study was to investigate whether this anti-aggregating activity was caused only by the presence of various activities already described in the placenta (an ADP-consuming enzyme, a fatty acid cyclooxygenase inhibitor, and a thromboxane synthetase inhibitor) or whether another factor was present.Heating the cytosol at 50° C for 6 min destroyed the inhibitor of collagen-induced aggregation. ADPase and the AA pathway inhibitors were not modified by this treatment. We therefore show the presence of an additional anti-aggregating factor: it is destroyed by heating at 50° C.We also tested for the presence of an inhibitor of AA release in the placental cytosol using three different methods (rabbit platelets in PRP, washed rabbit platelets, and NRK fibroblasts) but no inhibition could be evidenced.We conclude that this new anti-aggregating factor, which is probably a protein, acts neither through AA release inhibition nor AA cascade inhibition.


1961 ◽  
Vol 36 (4) ◽  
pp. 511-519 ◽  
Author(s):  
Margaret Wiener ◽  
Charles I. Lupa ◽  
E. Jürgen Plotz

ABSTRACT 17α-hydroxyprogesterone-4-14C-17α-caproate (HPC), a long-acting progestational agent, was incubated with homogenates of rat liver and human placenta. The rat liver was found to reduce Ring A of HPC under anaerobic conditions to form allopregnane-3β,17α-diol-20-one-17α-caproate and pregnane-3β,17α-diol-20-one-17α-caproate, the allopregnane isomer being the major product. The caproic acid ester was neither removed nor altered during the incubation. Placental tissue did not attack HPC under conditions where the 20-ketone of progesterone was reduced. It is postulated that this absence of attack on the side chain is due to steric hindrance from the caproate ester, and that this may account for the prolonged action of HPC.


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