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Rat amnion: a novel site of oxytocin production.

Fetal membranes, in addition to serving as passive barriers, possess secretory capacities and have a role in amniotic fluid production. In the present study, we demonstrate that rat amniotic/chorionic membranes have the capacity to synthesize oxytocin (OT). Analysis of RNA extracted from rat amnion/chorion membranes by RNA blotting and polymerase chain reaction (PCR) revealed the presence of a single species of OT mRNA. The transcript was smaller than the hypothalamic OT transcript and equaled the size of uterine and placental OT mRNA. The abundance of amniotic OT mRNA decreased by 37% from Day 14 to Day 21 of pregnancy. Over the same time, amniotic/chorionic OT immunoreactivity, as assessed by RIA, increased from 0.17 +/- 0.03 to 1.36 +/- 0.18 ng/g tissue weight. HPLC analysis of amniotic/chorionic membrane extracts revealed two peaks of immunoreactive OT (ir-OT). The first peak (36% of total ir-OT) co-eluted with synthetic OT, while the second peak (64%) corresponded to a noncovalent complex, most likely between OT and neurophysin-I. Using the selective OT receptor ligand, 125I-d(CH2)5 [Tyr(Me)2,Thr4,Tyr-NH2(9)]OVT, we detected high numbers of OT binding sites in rat uterine tissues, but no OT binding sites in amniotic/chorionic or placental membranes. We conclude that the rat amniotic/chorionic membranes represent an extra-hypothalamic site of OT gene expression in the rat during pregnancy and thus represent a possible source of OT present in amniotic fluid.

Amnion↗

Amnionitis with intact amniotic membranes involving Streptobacillus moniliformis.

A 23-year-old black woman was admitted to the hospital in premature labor with intact amniotic membranes. The patient was afebrile and did not have any obvious signs of infection. Gram stain of the amniotic fluid, obtained via transabdominal amniocentesis, revealed the presence of gram-negative rods. The bacterium was identified as Streptobacillus moniliformis, the agent of rat-bite fever.

Adult↗

Identification of a 37 kilodalton protein at the epidermal basement membrane by an antiserum to human amnion.

A protein which is recognized by an antibody to human amniotic epithelial basement membrane was identified at the basal lamina of human epidermis by immunohistology. This protein was localized at the lamina lucida of human epidermal basement membrane by immunoelectron microscopy. Studies of normal human keratinocyte cultures and epidermal wound healing suggested that the protein was probably produced by keratinocytes. By immunoblotting, a basic apparent isoelectric pH (pHiapp = 7.3) protein band of 37 kD was seen. These data indicate that this 37 kD protein, clearly different from other known basement membrane components, is present in simple and stratified epithelia of ectodermal origin, and is associated with hemidesmosomes.

Amnion↗

Dipalmitoylphosphatidylcholine (L-alpha-lecithin) stimulates prostaglandin E production in human amnion.

The effect of dipalmitoylphosphatidylcholine (DPPC, L-alpha-lecithin), a substance not containing arachidonic acid, on prostaglandin E (PGE) production of amniotic membrane was studied. DPPC (3.125-800 micrograms/ml) stimulated PGE production of amniotic membrane (150-200%), suggesting that lecithin, the major surfactant component, is directly involved in the mechanism of human parturition as a stimulator of PGE production.

1,2-Dipalmitoylphosphatidylcholine↗

The number of muscarinic receptors in chick amnion muscle.

1. [(3)H]-Propyl benzilylcholine mustard ([(3)H]-PrBCM) an irreversible specific antagonist of muscarinic acetylcholine receptors, has been used to label the muscarinic receptors in the aneuronal muscle of isolated 11 day amniotic membranes of chick embryos.2. This muscle was found to have about 9 fmol/mg dry weight of receptor material. This is only 1-2% of the amount found in intestinal muscle.3. Pharmacological studies with isolated amniotic membranes using PrBCM show that labelling is to functional receptors and that the receptor reserve is small.4. The significance of the difference in receptor reserve in innervated and aneuronal plain muscle is discussed.

Acetylcholine↗