High-pH reversed-phase fractionated neural retina proteome of normal growing C57BL/6 mouse.

The retina is a key sensory tissue composed of multiple layers of cell populations that work coherently to process and decode visual information. Mass spectrometry-based proteomics approach has allowed high-throughput, untargeted protein identification, demonstrating the presence of these proteins in the retina and their involvement in biological signalling cascades. The comprehensive wild-type mouse retina proteome was prepared using a novel sample preparation approach, the suspension trapping (S-Trap) filter, and further fractionated with high-pH reversed phase chromatography involving a total of 28 injections. This data-dependent acquisition (DDA) approach using a Sciex TripleTOF 6600 mass spectrometer identified a total of 7,122 unique proteins (1% FDR), and generated a spectral library of 5,950 proteins in the normal C57BL/6 mouse retina. Data-independent acquisition (DIA) approach relies on a large and high-quality spectral library to analyse chromatograms, this spectral library would enable access to SWATH-MS acquisition to provide unbiased, multiplexed, and quantification of proteins in the mouse retina, acting as the most extensive reference library to investigate retinal diseases using the C57BL/6 mouse model.

Citation

Ying Hon Sze, Qian Zhao, Jimmy Ka Wai Cheung, King Kit Li, Dennis Yan Yin Tse, Chi Ho To, Thomas Chuen Lam. High-pH reversed-phase fractionated neural retina proteome of normal growing C57BL/6 mouse. Scientific data. 2021 Jan 26;8(1):27

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PMID: 33500412

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