Linked Life Data

21031560

Source:http://linkedlifedata.com/resource/pubmed/id/21031560

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2010-10-29
pubmed:abstractText
Although synaptogenesis within the retina is obviously essential for vision, mechanisms responsible for the initiation and maintenance of retinal synapses are poorly understood. In addition to its scientific interest, understanding retinal synapse formation is becoming clinically relevant with ongoing efforts to develop transplantation-based approaches for the treatment of retinal degenerative disease. To extend our understanding, we have focused on the chick model system and have studied the neuroligin family of neuronal adhesion factors that has been shown to participate in synapse assembly in the brain. We identified chicken orthologs of neuroligins 1, -3, and -4, but could find no evidence of neuroligin 2. We investigated temporal and spatial patterns of mRNA and protein expression during development using standard polymerase chain reaction (RT-PCR), quantitative PCR (QPCR), laser-capture microdissection (LCM), and confocal microscopy. At the mRNA level, neuroligins were detected at the earliest period tested, embryonic day (ED)5, which precedes the period of inner retina synaptogenesis. Significant alternative splicing was observed through development. While neuroligin gene products were generally detected in the inner retina, low levels of neuroligin 1 mRNA were also detected in the photoreceptor layer. Neuroligin 3 and -4 transcripts, on the other hand, were only detected in the inner retina. At retinal synapses neuroligin 1 protein was detected in the inner plexiform layer, but its highest levels were detected in the outer plexiform layer on the tips of horizontal cell dendrites. This work lays the groundwork for future studies on the functional roles of the neuroligins within the retina.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1096-9861
pubmed:author
pubmed:copyrightInfo
© 2010 Wiley-Liss, Inc.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
518
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4938-62
pubmed:meshHeading
pubmed-meshheading:21031560-Alternative Splicing, pubmed-meshheading:21031560-Animals, pubmed-meshheading:21031560-Avian Proteins, pubmed-meshheading:21031560-Cell Adhesion Molecules, Neuronal, pubmed-meshheading:21031560-Cell Differentiation, pubmed-meshheading:21031560-Chick Embryo, pubmed-meshheading:21031560-Chickens, pubmed-meshheading:21031560-Dendrites, pubmed-meshheading:21031560-Eye Proteins, pubmed-meshheading:21031560-Gene Expression Regulation, Developmental, pubmed-meshheading:21031560-Membrane Glycoproteins, pubmed-meshheading:21031560-Membrane Proteins, pubmed-meshheading:21031560-Nerve Tissue Proteins, pubmed-meshheading:21031560-Neurons, pubmed-meshheading:21031560-Protein Isoforms, pubmed-meshheading:21031560-Retina, pubmed-meshheading:21031560-Synapses, pubmed-meshheading:21031560-Transcription, Genetic
pubmed:year
2010
pubmed:articleTitle
Alternative splicing of neuroligin and its protein distribution in the outer plexiform layer of the chicken retina.
pubmed:affiliation
Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21287, USA. kwahlin1@jhmi.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural