ScRNA-seq on C57BL/6J mice retina
Ontology highlight
ABSTRACT:
ORGANISM(S): Mus musculus
PROVIDER: GSE153818 | GEO | 2020/09/29
REPOSITORIES: GEO
Similar Datasets
Project description:Identification of genes expressed in a preferential manner in the developing ciliary body/iris will provide a starting point for future functional analyses. To identify candidate genes expressed in a variety of ocular tissues during development, we have profiled single cells from the developing eye. Post hoc identification of the origin of these cells showed that they included cells from the periphery of the developing optic cup. By comparing the expression profiles of these cells to many retinal cell types, candidate genes for preferential expression in the periphery were identified.
2009-05-01 | GSE15566 | GEO
Project description:The human iris tissue is a thin, circular structure in the eye and it is made up of a pigmented epithelial structure. It is a protected internal organ of the eye, located behind the cornea and the aqueous humour. Iris serves main function to control the diameter, size of the pupil and regulation of light exposure to the internal eye structures. Damage or absent iris always results in allowing excess amount of light into the eye which causes medical problem for the patient and also a psychological problem due to strange eye with black hole. A damaged or congenitally defective iris does not function well which results in poor quality of vision. Although different efforts have been made to elucidate the different parts of the human eye proteome in depth, the protein composition of the human iris tissue remains largely unexplored. We have performed a comprehensive analysis of the human iris tissue employing protein and peptide fractionation methods followed by LC-MS/MS identifying 4918 proteins. Bioinformatics analysis revealed that protein components of the iris tissue participated in a plethora of biological process highlighting cell signal transduction, communication, metabolism, energy pathways protein metabolism cell growth and maintenance, transport and immune response activities. We also compared the proteins of iris tissue with high throughput studies on other parts of eye and plasma proteome, which resulted in identifying proteins unique to iris. To our knowledge, this study is the first attempt to profile the global proteome of the human iris tissue. Taken together, these results increase our knowledge about the molecular composition of the human iris tissue and may be useful to understand the molecular basis of the iris and the baseline proteome described in this study should serve as a resource for future research in iris tissue
2022-02-23 | PXD001299 | Pride
Project description:The iris is a fine structure that controls the amount of light that enters the eye. Iris diseases that result in visual disability and blindness include iritis, primary angle closure glaucoma, and pigment dispersion syndrome. A detailed investigation of the proteome of the normal human iris may provide a foundation for new investigations into the iris biology and pathophysiology. We conducted an in-depth proteomic analysis of five normal irides. Proteins were fractionated using SDS-PAGE. After in-gel digestion, peptides were analyzed using LC-MS/MS on an Orbitrap Elite mass spectrometer. We identified 3,000 non-redundant proteins in the human iris, including 26 unambiguous protein isoforms. The proteins identified in the iris included numerous proteins involved in smooth muscle motility, melanosome development, extracellular matrix, and selenoproteins involved in redox signaling. The MS proteome database of the human iris may serve as a valuable resource for future investigations of the eye in health and disease.
2016-07-18 | PXD001424 | Pride
Project description:The iris is a fine structure that controls the amount of light that enters the eye. The ciliary body controls the shape of the lens and produces aqueous humor. The retinal pigment epithelium and choroid (RPE/choroid) are essential in supporting the retina and absorbing light energy that enters the eye. Proteins were extracted from iris, ciliary body, and RPE/choroid tissues of eyes from five individuals and fractionated using SDS-PAGE. After in-gel digestion, peptides were analyzed using LC-MS/MS on an Orbitrap Elite mass spectrometer. In iris, ciliary body, and RPE/choroid, we identified 2,959, 2,867, and 2,755 non-redundant proteins with protein false positive rate <1%. There were 43 unambiguous protein isoforms identified in iris, ciliary body, and RPE/choroid. Four “missing proteins” were found in ciliary body. The MS proteome database of the human iris, ciliary body, and RPE/choroid may serve as a valuable resource for future investigations of the eye in health and disease. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD001424.
2016-02-04 | PXD002194 | Pride
Project description:Wnt signaling in early eye development, specifically the lens placode shows expression of 12 out of 19 Wnt ligands. We these Wnt activities were suppressed using conditional deletion of Wntless, dramatic phenotypic changes in morphogensis occurred. Microarray analysis of the genes that were changed in response to deletion of Wnt ligands in the developing eye region show direct or indirect responses from the surface ectoderm to the developing RPE and optic cup curvature, creating an overal shape change phenotype in the bilayerd epithelium of the optic cup.
2015-01-22 | GSE65154 | GEO
Project description:The iris is a fine structure that controls the amount of light that enters the eye. Iris diseases that result in visual disability and blindness include iritis, primary angle closure glaucoma, and pigment dispersion syndrome. A detailed investigation of the proteome of the normal human iris may provide a foundation for new investigations into the iris biology and pathophysiology. We conducted an in-depth proteomic analysis of five normal irides. Proteins were fractionated using SDS-PAGE. After in-gel digestion, peptides were analyzed using LC-MS/MS on an Orbitrap Elite mass spectrometer. We identified 3,000 non-redundant proteins in the human iris, including 26 unambiguous protein isoforms. The proteins identified in the iris included numerous proteins involved in smooth muscle motility, melanosome development, extracellular matrix, and selenoproteins involved in redox signaling. The MS proteome database of the human iris may serve as a valuable resource for future investigations of the eye in health and disease.
2017-11-29 | MSV000081765 | MassIVE
Project description:Identification of genes expressed in a preferential manner in the developing ciliary body/iris will provide a starting point for future functional analyses. To identify candidate genes expressed in a variety of ocular tissues during development, we have profiled single cells from the developing eye. Post hoc identification of the origin of these cells showed that they included cells from the periphery of the developing optic cup. By comparing the expression profiles of these cells to many retinal cell types, candidate genes for preferential expression in the periphery were identified. Single retinal cells were isolated in tubes containing lysis buffer, their mRNAs were reverse transcribed, and the resulting cDNAs were PCR amplified for 35 cycles. Labeled cDNA samples were hybridized to Affymetrix 430 2.0 microarrays and the data was normalized using MAS5.0 software. Since the retinal cells isolated during these developmental times had not yet adopted their mature morphologies, a post hoc strategy was employed to classify each cell based upon the expression of clusters of genes (Trimarchi et al., 2008). This classification method allowed for the identification of 21 single cells as developing retinal ganglion (RGC), amacrine (AC) or photoreceptor cells (PR) (Trimarchi et al., 2007) and an additional 42 cells as cycling RPCs (Trimarchi et al., 2008). However, a number of the single cells did not score significantly for any of the retinal cell types. Two cells in particular expressed genes that suggested these cells originated from the developing ciliary body/iris region.
2009-05-01 | E-GEOD-15566 | biostudies-arrayexpress
Project description:High-throughput sequencing of murine retina and RPE/Choroid (eye cup) tissue following mueller-cell mediated expression of either hVEGFA, hTNFa, or hIl6 by adeno-associated viruses (AAV)
2022-11-11 | GSE200191 | GEO
Project description:The iris is a fine structure that controls the amount of light that enters the eye. The ciliary body controls the shape of the lens and produces aqueous humor. The retinal pigment epithelium and choroid (RPE/choroid) are essential in supporting the retina and absorbing light energy that enters the eye. Proteins were extracted from iris, ciliary body, and RPE/choroid tissues of eyes from five individuals and fractionated using SDS-PAGE. After in-gel digestion, peptides were analyzed using LC-MS/MS on an Orbitrap Elite mass spectrometer. In iris, ciliary body, and RPE/choroid, we identified 2,959, 2,867, and 2,755 non-redundant proteins with protein false positive rate <1%. There were 43 unambiguous protein isoforms identified in iris, ciliary body, and RPE/choroid. Four “missing proteins” were found in ciliary body. The MS proteome database of the human iris, ciliary body, and RPE/choroid may serve as a valuable resource for future investigations of the eye in health and disease. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD001424.
2017-11-29 | MSV000081766 | MassIVE
Project description:Wnt signaling in early eye development, specifically the lens placode shows expression of 12 out of 19 Wnt ligands. We these Wnt activities were suppressed using conditional deletion of Wntless, dramatic phenotypic changes in morphogensis occurred. Microarray analysis of the genes that were changed in response to deletion of Wnt ligands in the developing eye region show direct or indirect responses from the surface ectoderm to the developing RPE and optic cup curvature, creating an overal shape change phenotype in the bilayerd epithelium of the optic cup. Mouse embryos at embryonic stage e10.5 were disected into pbs and eye regions were disected and removed for RNA extraction and hybridization to Affymetrix microarrays. We sought to identify the genes that were changed in response to deletion of Wls from the developing surface ectoderm of the eye region. Genes changed could be the direct or indirect result from deleltion of Wls from the surface ectoderm using the LeCre recombinase gene as a tool for analysis.
2015-01-22 | E-GEOD-65154 | biostudies-arrayexpress