Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Magnetic ConA nanoparticles enriched proteins from urine samples of healthy donors and lung cancer patients

ABSTRACT: In this project, we used magnetic ConA nanoparticles to purify glycosylated proteins from urine samples of healthy donors and lung cancer patients to discover potential urinary protein biomarker for lung cancer.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Urine

DISEASE(S): Lung Cancer

SUBMITTER: Honglv Jiang

LAB HEAD: Guoqiang Xu

PROVIDER: PXD025856 | Pride | 2021-10-12

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Publications

Quantitative proteomic analysis of glycosylated proteins enriched from urine samples with magnetic ConA nanoparticles identifies potential biomarkers for small cell lung cancer.

Zhang Zhiyu Z Cheng Xinyu X Jiang Honglv H Gu Jingyu J Yin Yunfei Y Shen Zhijia Z Xu Changgang C Pu Zhongjian Z Li Jia-Bin JB Xu Guoqiang G

Journal of pharmaceutical and biomedical analysis 20210831

Lung cancer has high morbidity and mortality and small cell lung cancer (SCLC) is a highly invasive malignant tumor with a very unfavorable survival rate. Early diagnosis and treatment can result in better prognosis for the SCLC patients but current diagnostic methods are either invasive or incapable for large-scale screen. Therefore, discovering biomarkers for early diagnosis of SCLC is of importance. In this work, we covalently coupled Concanavalin A (ConA) to functionalized magnetic nanoparti ...[more]

PMID: 34509662

Similar Datasets

CUT&RUN of HOXA6 and HOXB6 in neuronal-derived human embryonic stem cells

Project description:CUT&RUN analysis of HOXA6 and HOXB6 binding sites in neuronal-derived human embryonic stem cells

2024-04-30 | E-MTAB-13627 | biostudies-arrayexpress

Characterization of the human urinary proteome and peptidome

Project description:Urine represents an ideal source of clinically relevant biomarkers since it contains a large number of proteins and low molecular weight peptides. Characterization of the normal urinary proteome and peptidome can serve as a reference for disease and can aid in biomarker discovery. Proteomic and peptidomic analysis of urine can also provide insight into normal physiology and disease pathology, especially for urogenital diseases. We developed an integrated proteomic and peptidomic analytical protocol for normal urine. We employed ultrafiltration to separate protein and peptide fractions, which were analyzed separately using liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) on the Q-Exactive mass spectrometer. By analyzing six urines from healthy individuals, we identified 1754 proteins by proteomic analysis and 4543 endogenous peptides, arising from 566 proteins by peptidomic analysis. Overall, we identified 2091 non-redundant proteins by this integrated approach. In silico protease activity analysis indicated that metalloproteases are predominantly involved in the generation of the endogenous peptide signature. In addition, a number of proteins that were detected in normal urine have previously been implicated in various urological malignancies, including bladder cancer and renal cell carcinoma. Thus, this study can provide a reference for assessing alterations in cancer-specific biomarkers.

2016-07-12 | PXD003595 | Pride

Peptidomics analysis of urine from IC/BPS patients and healthy controls

Project description:Interstitial cystitis/bladder pain syndrome (IC/BPS) is a chronic and debilitating pain disorder of the bladder and urinary tract with poorly understood etiology. A definitive diagnosis of IC/BPS can be challenging because many symptoms of IC/BPS are shared with other urological disorders. An analysis of urine presents an attractive and non-invasive resource for monitoring and diagnosing IC/BPS. Here, a non-targeted LC-MS and LC-MS/MS-based peptidomics analysis of urine samples collected from IC/BPS patients were compared to urine samples from asymptomatic controls.

2022-06-06 | PXD031843 | Pride

ChIP-seq for Prep on whole zebrafish embryos at 3.5 and 12hpf

Project description:Prep ChIP-seq on whole zebrafish embryos at 3.5 and 12 hours post fertilisation (hpf)

2018-06-25 | E-MTAB-5967 | biostudies-arrayexpress

Influenza peptide reactivity within a cohort of age-stratified individuals pre and post vaccination with the 2008/2009 trivalent influenza vaccine

Project description:The aim of the study was to test the hypothesis that peptide array reactivity will reveal patterns that can be associated with poor or effective neutralization response to seasonal influenza vaccine We diluted patient sera 1:80 and incubated dilutions on a streptavidin-coated glass surface that was printed with biotinylated peptides derived from seasonal strains of influenza hemagglutinin included in the 2008/2009 trivalent influenza vaccine In this study, serum from 76 study participants, subsetted into young (?30 years old) and elderly (?60 years old) categories were profiled for IgG/IgM antibody reactivity to influenza hemagglutinin peptudes. Using multivariate linear regression and correcting for multiple hypothesis testing by cross-validation, ee found that patterns of peptide reactivity associated with a poor or effective neutralization response to H1N1 and B strains of influenza.

2013-05-01 | E-GEOD-43446 | biostudies-arrayexpress

Secretome Analysis of hippocampal and cortical murine neurons

Project description:To understand how cells communicate with each other, it is essential to define the cellular secretome, a collection of proteins including soluble secreted, unconventionally secreted and proteolytically-shed proteins. Quantitative methodologies to decipher the secretome are challenging, due to the requirement of large cell numbers and abundant serum proteins that interfere with the detection of low-abundant cellular secretome proteins. Here, we have use the highe perfomance secretome-protein-enrichment-with-click-sugars method (hiSPECS) for glyco-secretome analysis. We applied this method to investigate differences of hippocampal and cortical murine neurons. Additionally, we have inhibited the Alzheimer related protease BACE1 to identify potential substrates in the secretome of hippocampal neurons.

2020-09-25 | PXD020503 | Pride

Quantitative secretome analysis using improved secretome-protein-enrichment-with-click-sugars method (iSPECS) establishes the cell type-resolved mouse brain glyco-secretome

Project description:To understand how cells communicate with each other, it is essential to define the cellular secretome, a collection of proteins including soluble secreted, unconventionally secreted and proteolytically-shed proteins. Quantitative methodologies to decipher the secretome are challenging, due to the requirement of large cell numbers and abundant serum proteins that interfere with the detection of low-abundant cellular secretome proteins. Here, we miniaturized secretome analysis by developing the improved secretome-protein-enrichment-with-click-sugars method (iSPECS), which identifies the glyco-secretome. We applied this method to provide a cell type-resolved mouse brain glyco-secretome resource. Our data show that a surprisingly high number of secreted proteins are generated by ectodomain shedding in a cell type-specific manner. Two examples are neuronally secreted ADAM22 and CD200, which we identified as new substrates of the Alzheimer-linked protease BACE1. Taken together, iSPECS and the brain glyco-secretome resource can be exploited for a wide range of applications to study protein secretion and shedding.

2020-09-25 | PXD018171 | Pride

RNA-Seq of Tissue, Plasma and Urinary Extracellular Vesicles of Prostate Cancer patients

Project description:We performed RNA-Seq analysis of plasma and urinary EVs collected before and after radical prostatectomy, and matched tumor and normal prostate tissues of 10 patients with prostate cancer. To identify putative cancer-derived RNA biomarkers, we searched for RNAs that were overexpressed in tumor as compared to normal tissues, present in the pre-operation EVs and decreased in the post-operation EVs in each RNA biotype.

2022-11-16 | E-MTAB-11910 | biostudies-arrayexpress

ChIP-seq for NF-YA and Pbx4 on whole zebrafish embryos at 3.5hpf

Project description:NF-YA and Pbx4 ChIP-seq on pooled whole zebrafish embryos at 3.5 hours post fertilisation (hpf)

2020-04-28 | E-MTAB-8137 | biostudies-arrayexpress

Mass spectrometric analysis of chondroitin sulfate-linked peptides

Project description:Chondroitin sulfate proteoglycans are integral components of the extracellular matrix. These are composed of repeating disaccharide units of glucuronic acid and N-acetylgalactosamine linked to a serine residue on the core protein through an oligosaccharide linker. The functions of chondroitin sulfate proteoglycans are regulated by the disaccharide heteropolymers attached to the core protein. The degree of sulfation and modifications on the oligosaccharide linker differs in different tissues depending upon its function. Here, we characterized the chondroitin sulfate-linked peptides using mass spectrometric-based glycoproteomics approach. We analyzed plasma, urine and fibroblasts from apparently healthy individuals by mass spectrometry. We identified 230 glycopeptides belonging to 25 chondroitin sulfate-linked proteoglycans.

2022-10-13 | PXD029400 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data