Dataset Information

Quantitative iTRAQ LC-MS/MS reveals muscular proteome profiles of deep pressure ulcers.

ABSTRACT: Pressure ulcers (PUs) are a common clinical issue lacking effective treatment and validated pharmacological therapy in hospital settings. Ischemia-reperfusion injury of deep tissue, especially muscle, plays a vital role in the formation and development of the overwhelming majority of PUs. However, muscular protein expression study in PUs has not been reported. Herein, we aimed to investigate the muscular proteins profiles in PUs and to explore the pathological mechanism of PUs. The iTRAQ LC-MS/MS was conducted to detect the protein profiles in clinical muscle samples of PUs. The GO and KEGG pathways analyses were performed for annotation of differentially expressed proteins. Protein-protein interaction (PPI) network was constructed by STRING online database, and hub proteins were validated by the immunoblotting. Based on proteomics results, we found a number of proteins that were differentially expressed in PU muscle samples compared with the normal and identified unique proteins expression patterns between these two groups, suggesting that they might involve in pathological process of the disease. Importantly, cathepsin B and D, as well as other autophagy-lysosome and apoptosis associated proteins were identified. Further experiments characterize the expression of these proteins and their regulation in the process of apoptosis and autophagy. These findings may provide novel insights into the mechanisms of lysosome-associated pathways involved in the initiation of PUs. This is the first study linking proteomics to PUs muscle tissues, which indicated cathepsin B and D might be key drug target for PUs.

SUBMITTER: Liu Z

PROVIDER: S-EPMC7295623 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature

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Quantitative iTRAQ LC-MS/MS reveals muscular proteome profiles of deep pressure ulcers.

Liu Zan Z Cui Xu X Hu Yanke Y Zhang Pihong P

Bioscience reports 20200601 6

Pressure ulcers (PUs) are a common clinical issue lacking effective treatment and validated pharmacological therapy in hospital settings. Ischemia-reperfusion injury of deep tissue, especially muscle, plays a vital role in the formation and development of the overwhelming majority of PUs. However, muscular protein expression study in PUs has not been reported. Herein, we aimed to investigate the muscular proteins profiles in PUs and to explore the pathological mechanism of PUs. The iTRAQ LC-MS/M ...[more]

PMID: 32458987

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Project description:BackgroundThe observed molecular weight of a protein on a 1D polyacrylamide gel can provide meaningful insight into its biological function. Differences between a protein's observed molecular weight and that predicted by its full length amino acid sequence can be the result of different types of post-translational events, such as alternative splicing (AS), endoproteolytic processing (EPP), and post-translational modifications (PTMs). The characterization of these events is one of the important goals of total proteome profiling (TPP). LC/MS/MS has emerged as one of the primary tools for TPP, but since this method identifies tryptic fragments of proteins, it has not generally been used for large-scale determination of the molecular weight of intact proteins in complex mixtures.ResultsWe have developed a set of computational tools for extracting molecular weight information of intact proteins from total proteome profiles in a high throughput manner using 1D-PAGE and LC/MS/MS. We have applied this technology to the proteome profile of a human lymphoblastoid cell line under standard culture conditions. From a total of 1 x 10(7) cells, we identified 821 proteins by at least two tryptic peptides. Additionally, these 821 proteins are well-localized on the 1D-SDS gel. 656 proteins (80%) occur in gel slices in which the observed molecular weight of the protein is consistent with its predicted full-length sequence. A total of 165 proteins (20%) are observed to have molecular weights that differ from their predicted full-length sequence. We explore these molecular-weight differences based on existing protein annotation.ConclusionWe demonstrate that the determination of intact protein molecular weight can be achieved in a high-throughput manner using 1D-PAGE and LC/MS/MS. The ability to determine the molecular weight of intact proteins represents a further step in our ability to characterize gene expression at the protein level. The identification of 165 proteins whose observed molecular weight differs from the molecular weight of the predicted full-length sequence provides another entry point into the high-throughput characterization of protein modification.

Dataset Information

Quantitative iTRAQ LC-MS/MS reveals muscular proteome profiles of deep pressure ulcers.

Publications

Quantitative iTRAQ LC-MS/MS reveals muscular proteome profiles of deep pressure ulcers.

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