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Quantitative proteomics profiling revealed serum exosomes inhibited the differentiation of osteoclast in SAPHO patients during the active period

ABSTRACT: The serum samples from patients and normal volunteers were pooled together, respectively, to perform isolation of exosomes by ultracentrifugation.TMT-labeled quantitative proteomics were performed to find out the differently expressed proteins.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Serum

SUBMITTER: Wei Ge

LAB HEAD: Wei Ge

PROVIDER: PXD012125 | Pride | 2021-09-08

REPOSITORIES: Pride

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			Action	DRS
	MS180145SAPHOserumucexosome.xlsx	Xlsx
	MS180145_S_.msf	Msf
	MS180145_S_.pdResult	Other
	MS180145_S_.pep.xml	Pepxml
	MS180145_S_1.raw	Raw

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Publications

Serum-derived extracellular vesicles inhibit osteoclastogenesis in active-phase patients with SAPHO syndrome.

Gao Yanpan Y Chen Yanyu Y Wang Lun L Li Chen C Ge Wei W

Therapeutic advances in musculoskeletal disease 20210416

<h4>Objective</h4>Synovitis, acne, pustulosis, hyperostosis, and osteitis (SAPHO) syndrome is a rare chronic inflammatory disorder and the underlying pathogenesis is unclear. In this study, 88 SAPHO patients and 118 healthy controls were recruited to investigate the role of serum-derived extracellular vesicles (SEVs) in SAPHO syndrome.<h4>Methods</h4>Quantitative proteomics was applied for SEVs proteome identification, and ELISA and Western blotting was performed to verify the results of mass sp ...[more]

PMID: 33948126

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Human osteoclast derived from SAPHO PBMC

Project description:Inducing the PBMCs from SAPHO patients differentiation into osteoclasts while stimulating with serum exosomes. Compared with exosomes from normal volunteer, we found that about 2/3 of patients’ osteoclast differentiation were inhibited in response to exosomes from SAPHO patients. We present a TMT-labeled quantitative proteomics analysis of the osteoclasts which respond differently to different exosomes.

2021-09-08 | PXD012218 | Pride

Quantitative proteomics analysis of exosomes purified from serum of patients with colorectal cancer

Project description:Tumor cells of colorectal cancer (CRC), release exosomes into peripheral blood. These exosomes can mediate communication between cells and affect various tumor-related processes in their target cells. We present a quantitative proteomics analysis on the exosomes purified from serum of patients with CRC and normal volunteers. 918 proteins were identified with an overlap of 725 Gene IDs in Exocarta proteins list. Comparing with the serum-purified exosomes of normal volunteers, we found 36 proteins upregulated and 22 proteins downregulated in the serum-purified exosomes of CRC patients, of which over 50% were involved in protein metabolism and immune response. Pathway and interaction network analysis results revealed that most of the exosome-enriched differentially expressed proteins (DEPs) were associated with complement and coagulation cascades and cancer pathways, suggesting their potential roles in tumor carcinogenesis. Our study demonstrates that serum-purified exosomes of CRC patients can play a pivotal role in invasiveness and pre-metastatic niche establishment of CRC, but not sustain the tumor survival and proliferation. The content selection of exosomes might be associated with the functions of proteins in the development of CRC. This information will be helpful in elucidating the pathophysiological functions of tumor-derived exosomes, and aid in the development of colorectal cancer diagnostics and therapeutics.

2016-12-12 | PXD003875 | Pride

Inhibition of DOT1L increases osteoclast fusion and resorption and aggravates bone loss

Project description:Osteoclasts are absorptive cells and play a critical role in homeostatic bone remodeling and pathological bone resorption. Emerging evidence suggests an important role for epigenetic regulation of osteoclastogenesis. In this study, we investigated the role of DOT1L, which regulates gene expression epigenetically by histone H3K79 methylation during osteoclast formation. DOT1L and H3K79me2 levels were upregulated during osteoclast differentiation. Small molecule inhibitor- (EPZ5676 or EPZ004777) or short hairpin RNA-mediated reduction in DOT1L expression promoted osteoclast differentiation and resorption. DOT1L inhibition also increased osteoclast area and accelerated bone mass reduction in a mouse ovariectomy (OVX) model of osteoporosis. DOT1L inhibitors did not alter osteoblast differentiation in vitro and in vivo. Proteomics data, together with bioinformatics analysis, revealed that DOT1L inhibition altered reactive oxygen species (ROS) generation, autophagy activation, and cell fusion-related protein expression. ROS generation increased, and autophagy activation and cell migration ability enhancement were verified subsequently by flow cytometry and transwell migration assays. DOT1L inhibition increased NFATc1 nuclear translocation and NF-κB activation and strengthend osteoclast fusion and expression of resorption-related protein CD9, and MMP9 in osteoclasts derived from RAW264.7. Our findings support a new mechanism of DOT1L-mediated H3K79me2 epigenetic regulation of osteoclast differentiation, implicating DOT1L as a new therapeutic target for osteoclast dysregulation-induced disease.

2018-01-24 | PXD006448 | Pride

Quantitative proteomic characterization of hippocampus during ageing from APP/PS1 mice brain

Project description:Ageing is the most important non-genetic risk factor of late-onset AD. However, the relationship between AD and aging process is still unclear. Here, by comparative analysis, we demonstrated the low correlation between AD and aging process during ageing.

2022-03-20 | PXD005875 | Pride

Quantitative proteomic characterization of temporal lobe during ageing from APP/PS1 mice brain

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Migrasomes provide regional cues for organ morphogenesis during zebrafish gastrulation

Project description:Migrasomes are recently identified vesicular organelles that form on retraction fibers behind migrating cells, cellular contents are released from migrasome by a process named migracytosis. The function of migrasomes in living organisms is unknown. Here we show that migrasomes are formed during zebrafish gastrulation, signaling molecules such as chemokines are enriched in migrasomes. Migrasomes are clustered on spatially restricted area in embryo where they provide regional cues for organ morphogenesis. Our study shown migrasome is signaling organelles which integrate spatial and specific biochemical information to coordinate migrating cells in complex biological processes such as morphogenesis.

2019-06-03 | PXD013835 | Pride

Quantitative proteomic characterization of senile plaques from Alzheimer's disease and non-demented brain

Project description:The deposition of amyloid senile plaques (SPs) play a central role in Alzheimer’s disease (AD), but the mechanisms by which SPs induce neural toxicity are disputed. Genetically engineered mouse models emphasising SPs have had limited success in reproducing the neuropathology of AD, and have also failed to be good indicators of successful amyloid-targeting therapies. Moreover, elderly people with a heavy plaque burden can show normal cognition. Therefore, it is fundamentally important to fully characterize and distinguish the pathological changes elicited by SPs in human and mouse brains. Using laser capture microdissection (LCM) combined with high-throughput mass spectrometry, we quantified ~5000 proteins with high confidence in SPs and non-plaque regions from AD and non-AD human postmortem brain. We found proteomic alteration in SPs is more evident than in non-plaque regions, and identified more than 30 human that are significantly enriched in SPs. We found that AD SPs elicited much more extensive proteomic alterations compared to non-AD SPs. Together, our findings represent the most systematic analysis of sub-proteome of senile plaques and provide a framework for future studies on plaque pathology and AD progression.

2019-02-18 | PXD005824 | Pride

Quantitative proteomic characterization of senile plaques from APP/PS1 mice brain

Project description:The deposition of amyloid senile plaques (SPs) plays a central role in Alzheimer’s disease (AD), but the mechanisms by which SPs induce neural toxicity are disputed. Genetically engineered mouse models emphasizing SPs have had limited success in reproducing the neuropathology of AD, and have also failed to be good indicators of successful amyloid-targeting therapies. Therefore, it is fundamentally important to fully characterize and distinguish the pathological changes elicited by SPs in human and mouse brains. Using laser capture microdissection (LCM) combined with high-throughput mass spectrometry, we quantified ~5000 proteins with high confidence in SPs and non-plaque regions from APP/PS1 mouse model brain. We found more proteomic alteration in SPs than in non-plaque regions, and identified more than 200 mouse proteins that were significantly enriched in SPs. Together, our findings represent the most systematic analysis of the sub-proteome of SPs and provide a framework for future studies on plaque pathology and AD progression.

2022-03-20 | PXD005876 | Pride

Comprehensive proteome analysis reveals the central role of macrophage lysosomes in regulating immune responses

Project description:Phagocytosis and autophagy in macrophages have been shown to be essential to both innate and adaptive immunity. Lysosomes are the main catabolic subcellular organelles responsible for degradation and recycling of both extracellular and intracellular material, which are the final steps in phagocytosis and autophagy. Lysosomes are critical for the correct function of macrophages; however, the molecular mechanisms underlying lysosomal functions after infection remain to be fully clarified. In this study, we conducted a quantitative proteomics analysis of the changes in constitution and glycosylation of proteins in lysosomes derived from murine RAW 264.7 macrophage cells treated with different types of pathogens comprising examples of bacteria (Listeria monocytogenes, L. m), DNA viruses (Herpes simplex virus type-1, HSV-1) and RNA viruses (vesicular stomatitis virus, VSV). In total, 3,704 lysosome-related proteins and 264 glycosylated proteins were identified. Bioinformatic analysis showed lysosomes initiated distinct pathways according to the type of pathogens and function via integrated signaling of the innate and adaptive immune systems. Fluctuations in the glycosylation of several lysosomal proteins were also determined. Immunofluorescence assays showed that autophagy was increased following infection with all three types of pathogens, while only L. m infection stimulated lysosomal biosynthesis. Combined with more detailed immunoblotting and immunofluorescence analyses, these results suggest that macrophage lysosomes function as a signaling center in regulating immune responses to microbial infection.

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Project description:Fracture healing, in which osteoclasts and osteoblasts play important roles, has drawn much clinical attention. Osteoclast deficiency or decreased osteoblast activity will impair fracture healing. TRPV1 is a member of the Ca2+ permeable cation channel subfamily, and pharmacological inhibition of TRPV1 prevents ovariectomy-induced bone loss, which makes TRPV1 a potential target for osteoporosis. However, whether long term TRPV1 inhibition or TRPV1 deletion will affect the fracture healing process is unclear. In this study, we found that the wild-type mice showed a well-remodeled fracture callus, whereas TRPV1 knockout mice still had an obvious fracture gap with unresorbed soft-callus 4 weeks post-fracture. The number of osteoclasts was reduced in the TRPV1 knockout fracture callus, and osteoclast formation and resorption activity were also impaired in vitro. TRPV1 deletion decreased the calcium oscillation frequency and peak cytoplasmic concentration in osteoclast precursors, subsequently reducing the expression and nuclear translocation of NFATc1 and downregulating DC-stamp, cathepsin K, and ATP6V. In addition, TRPV1 deletion caused reduced mRNA and protein expression of Runx2 and ALP in bone marrow stromal cells (BMSCs) and reduced calcium deposition in vitro. Our results suggest that TRPV1 deletion impairs fracture healing, and inhibited osteoclastogenesis and osteogenesis.

| S-EPMC5320507 | biostudies-literature