title: Novel distribution of junctional adhesion molecule-C in the neural retina and retinal pigment epithelium.
abstract: Junction adhesion molecules-A, -B, and -C (Jams) are cell surface glycoproteins that have been shown to play an important role in the assembly and maintenance of tight junctions and in the establishment of epithelial cell polarity. Recent studies reported that Jam-C mRNA was increased threefold in the all-cone retina of the Nrl(-/-) mouse, suggesting that Jam-C is required for maturation and polarization of cone photoreceptors cells. We examined the expression of Jams in the mouse retina by using confocal immunofluorescence localization. Jam-C was detected in tight junctions of retinal pigment epithelium (RPE) and at the outer limiting membrane (OLM) in the specialized adherens junctions between Müller and photoreceptor cells. Additionally, Jam-C labeling was observed in the long apical processes of Müller and RPE cells that extend between the inner segments and outer segments of photoreceptors, respectively. Jam-B was also detected at the OLM. In the developing retina, Jam-B and -C were detected at the apical junctions of embryonic retinal neuroepithelia, suggesting a role for Jams in retinogenesis. In eyes from Jam-C(-/-) mice, retinal lamination, polarity, and photoreceptor morphology appeared normal. Although Jam-A was not detected at the OLM in wild-type retinas, it was present at the OLM in retinas of Jam-C(-/-) mice. These findings indicate that up-regulation of Jam-A in the retina compensates for the loss of Jam-C. The nonclassical distribution of Jam-C in the apical membranes of Müller cells and RPE suggests that Jam-C has a novel function in the retina.
authors.affiliation: F.M. Kirby Center for Molecular Ophthalmology, Department of Ophthalmology, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Lauren L
authors.initials: LL
authors.lastname: Daniele
authors.forename: Ralf H
authors.initials: RH
authors.lastname: Adams
authors.forename: Diane E
authors.initials: DE
authors.lastname: Durante
authors.forename: Edward N
authors.initials: EN
authors.lastname: Pugh
authors.forename: Nancy J
authors.initials: NJ
authors.lastname: Philp
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D050976:Basic-Leucine Zipper Transcription Factors / Q000172:deficiency; D015815:Cell Adhesion Molecules / Q000172:deficiency / Q000378:metabolism*; D004622:Embryo, Mammalian; D005136:Eye Proteins; D018507:Gene Expression Regulation, Developmental / Q000502:physiology*; D007136:Immunoglobulins / Q000172:deficiency / Q000378:metabolism*; D008565:Membrane Proteins / Q000172:deficiency / Q000378:metabolism*; D051379:Mice; D018345:Mice, Knockout; D010750:Phosphoproteins / Q000378:metabolism; D010857:Pigment Epithelium of Eye / Q000378:metabolism*; D012160:Retina / Q000166:cytology / Q000378:metabolism*; D062826:Zonula Occludens-1 Protein; D062765:Junctional Adhesion Molecule B
chemical_list: D000199:Actins; D050976:Basic-Leucine Zipper Transcription Factors; D015815:Cell Adhesion Molecules; D005136:Eye Proteins; D007136:Immunoglobulins; D008565:Membrane Proteins; D010750:Phosphoproteins; D062826:Zonula Occludens-1 Protein; C498781:Jam2 protein, mouse; D062765:Junctional Adhesion Molecule B; C486723:Jam3 protein, mouse; C084884:Nrl protein, mouse; C569043:Tjp1 protein, mouse