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1.
Vet Pathol ; 48(2): 361-8, 2011 Mar.
Article in English | MEDLINE | ID: mdl-20634409

ABSTRACT

Junctional adhesion molecule A (JAM-A) is an immunoglobulin superfamily protein that plays an important role in the assembly and maintenance of tight junctions and the establishment of epithelial cell polarity. The feline JAM-A (fJAM-A) is a functional receptor for feline calicivirus (FCV). Among natural diseases associated with FCV infection, isolates that cause oral vesicular disease are detected in epithelial cells; however, isolates that cause systemic disease are detected in multiple cell types. The distribution of an FCV receptor or receptors in feline tissues is relevant to viral pathogenesis in that it should reflect the wide latitude of clinical sequelae associated with FCV infection. The authors examined the expression of feline JAM-A in the cat by using confocal immunofluorescence localization on normal tissues, with special regard to tissue targets of naturally occurring FCV. As described in the human and the mouse, fJAM-A was widely distributed in feline tissues, where it localized at cell-cell junctions of epithelial and endothelial cells. fJAM-A was highly expressed on feline platelets, with lower levels of expression on feline peripheral blood leukocytes. Additionally, FCV infection of a feline epithelial cell monolayer causes redistribution of fJAM-A to the cytosol of infected cells. It is reasonable to propose that the spectrum of lesions caused by FCV reflects disruption of intercellular junctions that rely on fJAM-A function and tight junctional integrity.


Subject(s)
Calicivirus, Feline/metabolism , Cell Adhesion Molecules/metabolism , Epithelial Cells/metabolism , Intercellular Junctions/metabolism , Animals , Blood Platelets/metabolism , Cats , Flow Cytometry , Fluorescent Antibody Technique , Junctional Adhesion Molecules , Microscopy, Confocal
2.
Neuroscience ; 140(1): 123-36, 2006 Jun 19.
Article in English | MEDLINE | ID: mdl-16626866

ABSTRACT

The mouse retina offers an increasingly valuable model for vision research given the possibilities for genetic manipulation. Here we assess how the structural properties of mouse retinal ganglion cells relate to the stratification pattern of the dendrites of these neurons within the inner plexiform layer. For this purpose, we used 14 morphological measures to classify mouse retinal ganglion cells parametrically into different clusters. Retinal ganglion cells were labeled in one of three ways: Lucifer Yellow injection, 'DiOlistics' or transgenic expression of yellow fluorescent protein. The resulting analysis of 182 cells revealed 10 clusters of monostratified cells, with dendrites confined to either On or Off sublaminae of the inner plexiform layer, and four clusters of bistratified cells, dendrites spanning the On and Off sublaminae. We also sought to establish how these parametrically identified retinal ganglion cell clusters relate to cell types identified previously on the basis of immunocytochemical staining and the expression of yellow fluorescent protein. Cells labeled with an antibody against melanopsin were found to be located within a single cluster, while those labeled with the SMI-32 antibody were in four different clusters. Yellow fluorescent protein expressing cells were distributed within 13 of the 14 clusters identified here, which demonstrates that yellow fluorescent protein expression is a useful method for labeling virtually the entire population of mouse retinal ganglion cells. Collectively, these findings provide a valuable baseline for future studies dealing with the effects of genetic mutations on the morphological development of these neurons.


Subject(s)
Retinal Ganglion Cells/classification , Retinal Ganglion Cells/cytology , Animals , Cell Count/methods , Cell Size , Dendrites/metabolism , Diagnostic Imaging/methods , Immunohistochemistry/methods , Isoquinolines/metabolism , Luminescent Proteins/biosynthesis , Mice , Mice, Inbred C57BL , Mice, Transgenic , Neurofilament Proteins/metabolism , Retinal Ganglion Cells/metabolism , Rod Opsins/metabolism , Staining and Labeling/methods
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