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Proteome profiling of embryo chick retina.

Mizukami M, Kanamoto T, Souchelnytskyi N, Kiuchi Y - Proteome Sci (2008)

Bottom Line: Some of identified proteins were known to regulate cell proliferation, cell death, transport, metabolism, organization and extracellular matrix, and others also included novel proteins.We identified thirteen proteins which differentially expressed in embryonal retina of chicken at day 7, as compared to the retina of embryo of day 11.They were various regulatory proteins for cellular signaling.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Ophthalmology and Visual Science, Hiroshima University, Japan. suzumi-na@hiroshima-u.ac.jp

ABSTRACT

Background: Little is known regarding the molecular pathways that underlie the process of retinal development. The purpose of this study was to identify proteins which may be involved in development of retina. We used a proteomics-based approach to identify proteins that are up- or down-regulated during the development of the embryo chick retina.

Results: Two-dimensional gel electrophoresis was performed with the retina of embryo chicken, which was obtained from embryos of day 7 (ED7) and of day 11 (ED11). The protein spots showing significant differences were selected for identification by MALDI mass spectrometry. Thirteen proteins were differentially expressed; seven proteins were up-regulated in embryo retina of chicken at ED 11 and six proteins were down-regulated. Significant proteins were also evaluated in embryo day 15 (ED15). Some of identified proteins were known to regulate cell proliferation, cell death, transport, metabolism, organization and extracellular matrix, and others also included novel proteins.

Conclusion: We identified thirteen proteins which differentially expressed in embryonal retina of chicken at day 7, as compared to the retina of embryo of day 11. They were various regulatory proteins for cellular signaling.

No MeSH data available.


Related in: MedlinePlus

Photographs of two-dimensional electrophoresis gels with annotation of the spots of identified proteins. The left image shows a silver-stained gel of embryo chick retina at ED7 and the right image is that of embryo chick retina at ED11. The proteins spots that increased or decreased in embryo days ED7 to ED11, and that were identified by PMF are shown. Spots S1 through S13 represent the annotated spots. The pI gradient of the first dimension electrophoresis is shown on the top of the gels, and the migration of molecular mass markers for SDS-PAGE in the second dimension is shown on the side of the gel. Representative gel images are shown.
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Figure 1: Photographs of two-dimensional electrophoresis gels with annotation of the spots of identified proteins. The left image shows a silver-stained gel of embryo chick retina at ED7 and the right image is that of embryo chick retina at ED11. The proteins spots that increased or decreased in embryo days ED7 to ED11, and that were identified by PMF are shown. Spots S1 through S13 represent the annotated spots. The pI gradient of the first dimension electrophoresis is shown on the top of the gels, and the migration of molecular mass markers for SDS-PAGE in the second dimension is shown on the side of the gel. Representative gel images are shown.

Mentions: To identify the development-dependent proteins in the retina, we compared the proteome of ED7 chick retina with that of ED11. Total lysates of retina samples were resolved by two-dimensional gel electrophoresis. We detected an average one thousand protein spots on the two-dimensional gels after silver staining (Figure 1). We generated three gels for each experimental condition to ensure the reliability of the selection of spots with significant changes of expression. [See Additional file 1]


Proteome profiling of embryo chick retina.

Mizukami M, Kanamoto T, Souchelnytskyi N, Kiuchi Y - Proteome Sci (2008)

Photographs of two-dimensional electrophoresis gels with annotation of the spots of identified proteins. The left image shows a silver-stained gel of embryo chick retina at ED7 and the right image is that of embryo chick retina at ED11. The proteins spots that increased or decreased in embryo days ED7 to ED11, and that were identified by PMF are shown. Spots S1 through S13 represent the annotated spots. The pI gradient of the first dimension electrophoresis is shown on the top of the gels, and the migration of molecular mass markers for SDS-PAGE in the second dimension is shown on the side of the gel. Representative gel images are shown.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2267454&req=5

Figure 1: Photographs of two-dimensional electrophoresis gels with annotation of the spots of identified proteins. The left image shows a silver-stained gel of embryo chick retina at ED7 and the right image is that of embryo chick retina at ED11. The proteins spots that increased or decreased in embryo days ED7 to ED11, and that were identified by PMF are shown. Spots S1 through S13 represent the annotated spots. The pI gradient of the first dimension electrophoresis is shown on the top of the gels, and the migration of molecular mass markers for SDS-PAGE in the second dimension is shown on the side of the gel. Representative gel images are shown.
Mentions: To identify the development-dependent proteins in the retina, we compared the proteome of ED7 chick retina with that of ED11. Total lysates of retina samples were resolved by two-dimensional gel electrophoresis. We detected an average one thousand protein spots on the two-dimensional gels after silver staining (Figure 1). We generated three gels for each experimental condition to ensure the reliability of the selection of spots with significant changes of expression. [See Additional file 1]

Bottom Line: Some of identified proteins were known to regulate cell proliferation, cell death, transport, metabolism, organization and extracellular matrix, and others also included novel proteins.We identified thirteen proteins which differentially expressed in embryonal retina of chicken at day 7, as compared to the retina of embryo of day 11.They were various regulatory proteins for cellular signaling.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Ophthalmology and Visual Science, Hiroshima University, Japan. suzumi-na@hiroshima-u.ac.jp

ABSTRACT

Background: Little is known regarding the molecular pathways that underlie the process of retinal development. The purpose of this study was to identify proteins which may be involved in development of retina. We used a proteomics-based approach to identify proteins that are up- or down-regulated during the development of the embryo chick retina.

Results: Two-dimensional gel electrophoresis was performed with the retina of embryo chicken, which was obtained from embryos of day 7 (ED7) and of day 11 (ED11). The protein spots showing significant differences were selected for identification by MALDI mass spectrometry. Thirteen proteins were differentially expressed; seven proteins were up-regulated in embryo retina of chicken at ED 11 and six proteins were down-regulated. Significant proteins were also evaluated in embryo day 15 (ED15). Some of identified proteins were known to regulate cell proliferation, cell death, transport, metabolism, organization and extracellular matrix, and others also included novel proteins.

Conclusion: We identified thirteen proteins which differentially expressed in embryonal retina of chicken at day 7, as compared to the retina of embryo of day 11. They were various regulatory proteins for cellular signaling.

No MeSH data available.


Related in: MedlinePlus