Membrane ultrastructure at mammalian intercellular junctions.
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Two PDZ-domain-containing adapter-like proteins, PAR-3 and PAR-6, and a protein kinase, atypical protein kinase C (PKC), cooperate together to establish cell polarity in a variety of biological contexts. These include asymmetric cell division in early Caenorhabditis elegans embryo and Drosophila neuroblasts, as well as the establishment and maintenance of apical-basal polarity in Drosophila and mammalian epithelial cells. Recent studies on the role of this PAR-aPKC complex in epithelial cell polarization provide new insights into the molecular basis of epithelial junctional formation and cell polarity.
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The distribution of lanthanum chloride and horseradish peroxidase within the full-term chorioallantoic placenta of the rat was investigated 1 to 20 min after administration of these tracers into the maternal blood circulation. Both tracers rapidly penetrate trophoblastic layer I and diffuse into the interspace between layers I and II. They are localized in extensive infoldings and caveolae of the outer surface of layer II. The syncytial character of layer II is confirmed at this development stage of the placenta. There is no vesicular uptake or penetration beyond layer II until 20 min after tracer administration. Our results indicate that trophoblastic layer II is the main barrier in the chorioallantoic rat placenta preventing the permeation of macromolecules from maternal to fetal compartments. With freeze-fracturing, particulate strutures of variable arrangement and size are found between adjacent cells of layer I. With goniometric analysis small gaps between the appositions of the membrane are observed. These structures are interpreted as tight and/or gap junctions during stages of assembly or disassembly.
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