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Mannan-binding protein levels in human amniotic fluid during gestation and its interaction with collectin receptor from amnion cells.

Collectins are a group of soluble proteins, each of which has collagenous and non-collagenous globular domains, and may be complement associated and/or have lectin activity. The complement protein C1q is structurally and functionally related to the collectins. Members of the collectin family are mannan-binding protein (MBP), lung surfactant protein A, CL-43, conglutinin and lung surfactant protein D. All except the last of these proteins have been shown to interact with a single, widely distributed receptor, named collectin receptor (also called C1q receptor). It has been proposed that collectins play an important role as opsonins in innate immunity. MBP is a serum protein and has been shown to activate the classical complement pathway. MBP has also been shown to opsonize bacteria and enhance clearance of bacteria by phagocytosis. In this article we demonstrate the presence of MBP in amniotic fluid and the localization of collectin receptor on the surface of amniotic epithelium. MBP levels in amniotic fluid were found to increase sharply from about 32 weeks of gestation. Collectin receptor was purified from a cell line, FL, derived from amniotic epithelium and was shown to interact with MBP. These results suggest that MBP may play a role in the antibody-independent recognition and clearance of pathogens in the amniotic cavity, towards term.

Amino Acid Sequence↗

Ethanol effect on the ionic transfer through isolated human amnion. II. Cellular targets of the in vitro acute ethanol action and of the antagonism between magnesium, taurine and ethanol.

The ultrastructure of the human amniotic membrane from normal pregnancies at term, was studied by transmission electron microscopy. The results were analysed by a stereological method which indicates the ratio between the area of intercellular spaces (R1), microvilli (R2) and podocytes (R3) versus the cell area. Addition of ethanol (0.4 g/l) in the external medium decreased R1 and R3 and had no significant effect on R2. Ethanol reduced intercellular space and podocyte exchange surface. Two mM MgCl2 or 2 mM taurine restored R1 and R3 to normal values. The cellular targets of the antagonism between Mg, taurine and ethanol are particularly intercellular spaces and podocytes.

Amnion↗

[Subcellular distribution of adenosine-, adenosine-5-monophosphate- and cytidine-5-monophosphate desaminase activity in the humna placenta and amnion tissue].

With the method of pH-Stat the adenosinedeaminase-, adenosine-5'-monophosphate deaminase-, cytidine-5'-monophosphate deaminase activities are determined in the nucleus-, mitochondrial-, microsomalfractions and in the cytoplasmatic fractions of the human termplacental and amniotic tissues. The desaminase activities were higher in the amniotic fractions. The possible importance of the adenosinedesaminase and adenosine-5'-monophosphate desaminase for the fetal-placental blood circulation is discussed.

AMP Deaminase↗

Nuclear microanalysis of the monovalent ion distribution in the human amnion. I. Effect of magnesium.

The effect of the addition of MgCl2 on the Na+, K+, and Cl- concentration and distribution in epithelial and compact layers of the human amniotic membrane was investigated using the Bordeaux nuclear microprobe. Particle-induced X-ray emission and Rutherford backscattering spectrometry techniques were used to provide quantitative measurements. In physiological medium (Hanks' solution), the monovalent ion concentrations were identical in both layers. The addition of Mg2+ ions in Hanks' solution induced a decrease of, K+, and Cl- concentration in both layers and, Na+ concentration in the compact layer. The results obtained from nuclear microanalysis might be explained from electrophysiological data which indicate that the addition of Mg2+ ions results in an increase in the cellular, paracellular and exchanger ion pathways.

Amnion↗