Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Hs_platelets_Phospho_Thrombin

ABSTRACT: Human platelets Phospho proteome, treated with thrombin

REANALYSIS of: PXD000451

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Platelet

SUBMITTER: Bjoern Titz

PROVIDER: PAe005291 | PeptideAtlas | 2014-12-31

REPOSITORIES: PeptideAtlas

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	PAe005291_10330_tandem.params	Other
	PAe005291_README	Other
	PAe005291_Search_Results_10330_201601041427.properties	Other
	PAe005291_Search_Results_10330_201601041427.tar.gz	Other
	PAe005291_mzXML_201601041426.properties	Other

Items per page:

1 - 5 of 8

Publications

Phosphoproteomic analysis of platelets activated by pro-thrombotic oxidized phospholipids and thrombin.

Zimman Alejandro A Titz Bjoern B Komisopoulou Evangelia E Biswas Sudipta S Graeber Thomas G TG Podrez Eugene A EA

PloS one 20140106 1

Specific oxidized phospholipids (oxPCCD36) promote platelet hyper-reactivity and thrombosis in hyperlipidemia via the scavenger receptor CD36, however the signaling pathway(s) induced in platelets by oxPCCD36 are not well defined. We have employed mass spectrometry-based tyrosine, serine, and threonine phosphoproteomics for the unbiased analysis of platelet signaling pathways induced by oxPCCD36 as well as by the strong physiological agonist thrombin. oxPCCD36 and thrombin induced differential p ...[more]

PMID: 24400094

Similar Datasets

Phospho-antibody microarray anayses for control and DG-LRG1 treated HUVEC cells.

Project description:Deglycosylated-leucine-rich α-2-glycoprotein1 (DG-LRG1) as well as LRG1 was discovered to promote angiogenesis under diabetes mellitus condition through TGF-β independent binding to endoglin. To examine the signaling pathways triggered by DG-LRG1, we subjected whole-cell protein lysates of control and DG-LRG1 treated HUVECs to a Phospho Explorer antibody array analysis using commercial antibody array assay kit (Full Moon Biosystems, Inc.). Samples were probed against 1318 site-specific and phospho-specific antibodies with two replicates per antibody printed on a coated glass microscope slide. Phospho Explorer antibody array experiments and analyses were performed as a custom service by E-Biogen (Ebiogen Inc., Seoul, Republic of Korea).

2020-10-25 | GSE160005 | GEO

Comparison of phosphorylation status of Wnt proteins in control and Fto deficient cells upon Wnt 3a stimulation

Project description:Wnt Phospho protein profiling comparing control and Fto deficient cell after Wnt3a stimulation Control vs Fto deficient MEFs treated with Wnt 3a condioned medium for 40 minutes. 6 replicates per array

2013-11-21 | E-GEOD-52572 | biostudies-arrayexpress

Hs_platelets_Phospho_PLPC

Project description:Human platelets Phospho proteome, treated with PLPC

2014-12-31 | PAe005239 | PeptideAtlas

Phospho-antibody microarray analyses for islets of control and IFT88 knockout mice [PEX100]

Project description:β-cell specific IFT88 knock-out mice recapitulate human diabetes with impaired insulin secretion and altered islet hormone paracrine regulation. To examine the signaling pathways regulating islet cell function, we subjected protein lysates of whole islets from control and IFT88 knockout mice to a commercial phospho-antibody array analysis (Full Moon Bio, Inc). Samples were probed against 1318 site-specific and phospho-specific antibodies with 2 replicates per antibody on 76 x 25 x 1mm glass slides.

2019-10-30 | GSE138856 | GEO

PI3K/mTOR specific phospho-antibody microarray to study the effect of rapamycin to the innate immune respsonse

Project description:To comprehensively analyze the effects of mTORC1 inhibition on GSK3, we employed the use of a PI3K/mTOR-specific phospho-antibody microarray that analyzed the site-specific phosphorylation of over 130 kinases within the PI3K/mTOR pathway. The phosphorylation levels of different kinases in monocytes were measured when stimulated with LPS in the presence or absence of a kind of mTORC1 inhibitor, rapamycin More than 130 highly specific and characterized phospho-antibodies for the human mTOR signaling pathway were immobilized and replicated six times on glass slides. The same non-phosphorylated target antibodies were included to allow the determination of the relative level of phosphorylatioin

2010-11-25 | E-GEOD-25520 | biostudies-arrayexpress

Functionally-relevant splicing of resident pre-mRNAs in anucleate platelets upon activation by physiological stimuli

Project description:Platelet activation is the key event triggering thrombus formation in physiological and pathological conditions, such as acute coronary syndromes. Current therapies using antiaggregants still fail to prevent thrombotic coronary events in a significant number of patients, indicating that the mechanisms modulating platelet response during activation need to be clarified. The evidence that platelets are capable of de novo protein synthesis in response to stimuli raised the issue of how the activity of megakaryocyte-derived mRNAs is regulated in these anucleate cell fragments. We applied a combined multi-omics approach to investigate this phenomenon in platelets from healthy donors activated in vitro with Collagen or Thrombin Receptor Activating Peptide. Combining HiRIEF LC-MS to transcriptome analysis by RNA-Seq allowed platelet proteome characterization at deep coverage, revealing a significant effect of either stimulus on proteome composition. In silico intron retention analysis was then applied to search for splicing events induced by platelet activation, coupled to unbiased proteogenomics, to correlate intron retention in resting platelets to intron removal by RNA splicing during activation. This allowed identification of a set of transcripts, specifically involved in platelet shape changes, showing reduced intron retention and high peptide representation at exon-exon junctions in activated vs resting platelets. These results indicate that RNA splicing events takes place in platelets during activation and that pre-mRNA maturation of specific transcripts is part of the activation cascade and could therefore provide novel molecular markers of platelet activation status in acute coronary syndromes and other pathological conditions.

2018-01-15 | E-MTAB-6148 | biostudies-arrayexpress

Hs_platelets_Phospho_KODA-PC

Project description:Human platelets Phospho proteome, treated with KODA-PC

2014-12-31 | PAe005256 | PeptideAtlas

Phlpp1 regulates endochondral ossification via the chondrocyte phospho-proteome

Project description:Phlpp1 regulates endochondral ossification via the chondrocyte phospho-proteome

| PRJNA1104178 | ENA

Water-soluble tomato extract Fruitflow alters the phosphoproteomic profile of collagen-stimulated platelets

Project description:The present study used proteomics to quantitatively analyze the effect of FF on the inhibition of collagen-stimulated platelets and validated the involvement of several signaling molecules.Fruitflow significantly inhibited human platelet aggregation and P-selectin expression that were induced by collagen. Proteomics analysis revealed that 60 proteins were upregulated in FF-treated collagen-stimulated platelets, and 10 proteins were downregulated in collagen-stimulated platelets alone. Additionally, 66 phosphorylated peptides were upregulated in FF-treated collagen-stimulated platelets, whereas 37 phosphorylated peptides were downregulated in collagen-stimulated platelets alone.

2021-08-10 | PXD027834 |

YBX1 integration of oncogenic PI3K/mTOR signalling regulates the fitness of malignant epithelial cells [RPPA]

Project description:In heterogeneous head and neck cancer (HNC), subtype-specific treatment regimens are currently missing. An integrated analysis of patient HNC subtypes using single-cell sequencing and proteome profiles revealed an epithelial-mesenchymal transition (EMT) signature within the epithelial cancer-cell population. The EMT signature coincided with PI3K/mTOR inactivation in the mesenchymal subtype. Conversely, the signature was suppressed in epithelial cells of the basal subtype which exhibits hyperactive PI3K/mTOR signalling. We further identified YBX1 phosphorylation, downstream of the PI3K/mTOR pathway, restrains basal-like cancer cell proliferation. In contrast, YBX1 acts as a safeguard against the proliferation-to-invasion switch in mesenchymal-like epithelial cancer cells, and its loss accentuates partial-EMT and in vivo invasion. Interestingly, phospho-YBX1 that is mutually exclusive to partial-EMT, emerged as a prognostic marker for overall patient outcomes. Expression profiling by reverse-phase protein array were performed to explore the underlying molecular mechanisms.

2023-03-03 | GSE226356 | GEO