Dataset Information

Comprehensive Proteomic Analysis of Exosomes Derived from Human Bone Marrow-, Adipose Tissue-, and Human Umbilical Cord- Mesenchymal Stem Cells

ABSTRACT: Mesenchymal stem cells (MSCs)-derived exosomes (exo) have shown comprehensive application prospects over the years. Despite similar functions, exomes from different origins present heterogeneous characteristics and components; however, there are no relevant proteomic analyses. In this study, we isolated exosomes from MSCs, derived from different tissues, by ultracentrifugation. A total of 1014 proteins were detected using a label-free method and analyzed with bioinformatics tools. The results revealed their shared function in the extracellular matrix receptor. Bone marrow-MSCs-derived exosomes showed superior regeneration ability. Likewise, adipose tissue-MSCs-derived exosomes played a significant role in immune regulation. Whereas, umbilical cord-MSCs-derived exosomes were more prominent in tissue damage repair.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Zhenggang Wang

LAB HEAD: Zheng-gang Wang

PROVIDER: PXD020948 | Pride | 2021-04-14

REPOSITORIES: Pride

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Publications

Comprehensive proteomic analysis of exosomes derived from human bone marrow, adipose tissue, and umbilical cord mesenchymal stem cells.

Wang Zheng-Gang ZG He Zhi-Yi ZY Liang Shuang S Yang Qing Q Cheng Peng P Chen An-Min AM

Stem cell research & therapy 20201127 1

<h4>Background</h4>Mesenchymal stem cell (MSC)-derived exosomes have shown comprehensive application prospects over the years. Despite performing similar functions, exosomes from different origins present heterogeneous characteristics and components; however, the relative study remains scarce. Lacking of a valuable reference, researchers select source cells for exosome studies mainly based on accessibility and personal preference.<h4>Methods</h4>In this study, exosomes secreted by MSCs derived f ...[more]

PMID: 33246507

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Project description:N-glycosylation is an important posttranslational modification in all eukaryotes, but little is known about the N-glycoproteomes in microalgal systems. Here, N-glycoproteome of the model diatom Phaeodactylum tricornutum was unveiled. Totally, 893 different N-glycosylated sites from 649 proteins were identified from P. tricornutum. The new synthesized N-glycans were principally transferred to asparagine residues within the conserved N-X-S/T (where X is a residue other than proline) sequence of nascent polypeptide chains. Functional annotation of N-glycosylated proteins showed that 70% N-glycoproteins were involved in vesicular transport and posttranslational modification, protein turnover, chaperones, indicating the N-glycosylation was important for these functions. Of the all identified N-glycoproteins 45.3% were predicted to localize on chloroplast, which implied the widespread regulatory role of N-glycosylation in chloroplast. Furthermore, the enrichment results of N-glycoproteins indicated that compared to ‘Cellular component’ and ‘Biological process’ categories proteins related with the ‘Molecular function’ category were more prone to be N-glycosylated. And it was speculated that N-glycosylation played a vital regulatory role in catalytic activity of enzymes and metabolism processes of many small molecules. 47% of all enriched proteins were related with metabolic pathways. The functional annotation and enrichment of N-glycoproteins suggested that N-glycoproteins participated in a variety of important metabolic pathways and perform different functions in P. tricornutum. 12 proteins involved in the ER quality control mechanism and ER- associated degradation pathway were identified as N-glycosylated proteins, indicating that the N-glycosylated modification was important for their functions in the protein N-glycosylation pathway. Additionally, some interacted glycoproteins were classified from this study, which provided valuable information for studying the functions of these glycoproteins. In the study, the identification of N-glycosylation on nascent proteins expands our understanding of this PTM at a proteomics scale and may facilitate the elucidation of the precise function of proteins in this model diatom.

Dataset Information

Comprehensive Proteomic Analysis of Exosomes Derived from Human Bone Marrow-, Adipose Tissue-, and Human Umbilical Cord- Mesenchymal Stem Cells

Publications

Comprehensive proteomic analysis of exosomes derived from human bone marrow, adipose tissue, and umbilical cord mesenchymal stem cells.

Similar Datasets

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