title: Maturation of the blood-retina barrier in the developing pecten oculi of the chicken.
abstract: The major interest in the development of the blood-brain barrier and its underlying induction mechanisms is given by the crucial role they play in the maturation of the central nervous system in general. Whilst it is believed that it is the microenvironment in the brain that destines the endothelial cells to become committed to barrier properties, the analysis of the multitude of factors probably responsible for this commitment is extremely difficult. Therefore, in a previous study, we inaugurated the pecten oculi of the avian eye as a relatively simple in vivo model of the blood-brain barrier [Gerhardt, S. et al, Cell Tissue Res., 285 (1996) 91-100]. In the present study, we demonstrate data on the development of the pecten which allow us to understand better the commitment of barrier properties in endothelial cells in an environment which is considerably less complex than that realized in the brain. The pecten is built up by mainly two cell types, the pigmented glial cells and the endothelial cells. The pigmented cells, which are believed to originate from the retinal pigment epithelium, lose their tight junctions in the microenvironment of the vitreous body, whereas the endothelial cells, which originate from the permeable choroidal vessels, gain tight junctions and other barrier properties in the microenvironment of the vitreous body. On embryonic day 7 (E7), tight and gap junctions between epithelial-like glial cells line the vitreal border of the developing pecten. By E16, these junctions disappear, and the endothelial cells gradually acquire barrier characteristics (continuous and P-face associated tight junctions, no extravasation of lanthanum nitrate, and the exclusive expression of the glucose transporter isoform 1 and the barrier specific antigen HT7 in their luminal and abluminal membranes). The results are discussed considering the switch from an epithelial (glial) to an endothelial barrier.
authors.affiliation: Institute of Pathology, University of Tübingen, Germany.
authors.forename: S
authors.initials: S
authors.lastname: Liebner
authors.forename: H
authors.initials: H
authors.lastname: Gerhardt
authors.forename: H
authors.initials: H
authors.lastname: Wolburg
mesh_terms: D000818:Animals; D015703:Antigens, CD; D000951:Antigens, Neoplasm; D000954:Antigens, Surface; D030161:Avian Proteins; D051926:Basigin; D001798:Blood Proteins; D001813:Blood-Retinal Barrier / Q000502:physiology*; D002642:Chick Embryo; D004396:Coloring Agents; D004730:Endothelium, Vascular / Q000166:cytology / Q000196:embryology / Q000648:ultrastructure; D005614:Freeze Fracturing; D051272:Glucose Transporter Type 1; D007150:Immunohistochemistry; D007811:Lanthanum; D008562:Membrane Glycoproteins / Q000096:biosynthesis; D008854:Microscopy, Electron; D009004:Monosaccharide Transport Proteins / Q000096:biosynthesis; D012160:Retina / Q000196:embryology* / Q000648:ultrastructure; D012171:Retinal Vessels / Q000166:cytology / Q000196:embryology* / Q000648:ultrastructure; D019108:Tight Junctions / Q000502:physiology
chemical_list: D015703:Antigens, CD; D000951:Antigens, Neoplasm; D000954:Antigens, Surface; D030161:Avian Proteins; D001798:Blood Proteins; C102624:Bsg protein, Gallus gallus; C079432:Bsg protein, rat; D004396:Coloring Agents; D051272:Glucose Transporter Type 1; D008562:Membrane Glycoproteins; D009004:Monosaccharide Transport Proteins; D051926:Basigin; C016534:lanthanide nitrate; D007811:Lanthanum