Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Vaspin-induced effects in brown adipocytes – Phosphoproteome

ABSTRACT: To gain insights into the cellular response of brown and white adipocytes to vaspin, a phosphoproteomic analysis was conducted. Murine brown (imBA) and white (3T3L1) cells were treated with 500 ng/ml vaspin for 30 min, followed by lysis in RIPA buffer.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: Kristin Schubert

LAB HEAD: Kristin Schubert

PROVIDER: PXD068908 | Pride | 2025-12-12

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	3T3L1_Co1_PP.raw	Raw
	3T3L1_Co2_PP.raw	Raw
	3T3L1_Co3_PP.raw	Raw
	3T3L1_Co4_PP.raw	Raw
	3T3L1_Co5_PP.raw	Raw

Items per page:

1 - 5 of 26

Publications

Inhibition of adipocyte lipolysis by vaspin impairs thermoregulation in vivo.

Rapöhn Inka I Broghammer Helen H Hoffmann Anne A Möhlis Kevin K Moormann Anna A Kaczmarek Isabell I Thor Doreen D Großkopf Henning H Krieg Laura L Karkossa Isabel I Schubert Kristin K von Bergen Martin M Krause Kerstin K Breitfeld Jana J Kovacs Peter P Klöting Nora N Nuwayhid Rima R Langer Stefan S Ghosh Adhideb A Wolfrum Christian C Stumvoll Michael M Blüher Matthias M Heiker John T JT Weiner Juliane J

Nature communications 20251210 1

Altered activity of brown adipose tissue (BAT) contributes to obesity, insulin resistance, and cardiovascular disease. BAT secretes endocrine factors ("batokines") that regulate thermogenesis. We identify the serpin vaspin as a batokine that modulates adrenergic control of lipolysis and thermogenesis. Adipocyte-specific vaspin overexpression in mice reduces BAT activation and impairs thermoregulation during cold exposure or fasting. Mechanistically, vaspin binds low-density lipoprotein receptors ...[more]

PMID: 41372246

Similar Datasets

An Internal Standard for Assessing Phosphopeptide Recovery from Metal Ion/Oxide Enrichment Strategies

Project description:Phosphorylation-mediated signaling pathways have major implications in cellular regulation and disease. Mass spectrometry-based proteomics is a well-established approach for quantifying thousands of phosphorylation events in a single experiment. However, proteins with roles in signaling pathways are frequently less abundant and phosphorylation is often sub-stoichiometric. As such, the efficient enrichment and subsequent recovery of phosphorylated peptides is vital. To understand better phosphopeptide recovery from enrichment strategies, we designed a peptide internal standard-based assay directed toward sample preparation strategies for mass spectrometry analysis. We coupled mass-differential tandem mass tag (mTMT) reagents (specifically, TMTzero and TMTsuper-heavy), nine mass spectrometry-amenable phosphopeptides (phos9), and peak area measurements from extracted ion chromatograms to determine phosphopeptide recovery. We showcase this mTMT/phos9 recovery assay by evaluating three commercial phosphopeptide enrichment workflows. Our assay provides data on the recovery of phosphopeptides, which complement other metrics, namely the number of identified phosphopeptides and enrichment specificity. Our mTMT/phos9 assay is applicable to any enrichment protocol in a typical experimental workflow irrespective of sample origin or labeling strategy.

2018-12-04 | PXD008966 | Pride

Phosphopeptide-analysis in ALS muscle

Project description:Phosphoproteomics of muscle biopsies from ALS-patients and healthy controls.

2025-02-07 | PXD055632 | Pride

Vaspin-induced effects in brown adipocytes – Proteome

Project description:To gain insights into cellular responses of brown and white adipoctes to vaspin a proteomic analysis was concucted. Murine brown (imBA) and white (3T3L1) cells were treated with 500 ng/ml vaspin for 6h, 12h and 24h, followed by lysis in RIPA buffer.

2025-12-12 | PXD069112 | Pride

Quantitative phosphoproteomics study for assessing rodent thyroid toxicity

Project description:Here, we aimed to apply a TMT based quantitative phosphoproteomics approach to investigate rodent thyroid toxicity. For this purpose, male Wistar rats have been exposed to a direct (6-propyl-2-thiouracil, PTU) and an indirect (phenytoin) thyroid toxicant, respectively. Thereby, two doses (low:5ppm for PTU and 300ppm for phenytoin , high: 50ppm for PTU and 2400ppm for phenytoin) and three exposure time phase (short: 2 weeks, long:4 weeks, and long+recovery: 4weeks+2weeks) were investigated, allowing insights into the modes of action during thyroid toxicity. Phosphoproteomics were applied to liver.

2024-10-25 | PXD030254 | Pride

Phosphoproteome enrichment strategy using complementary chemistries of Fe-NTA and TiO2 followed by LC-MS/MS

Project description:The global phosphoproteome analysis by liquid chromatography-mass spectrometry (LC-MS) has emerged as an important tool to study cell signalling. However, the coverage of phosphoproteome by LC-MS is limited despite various approaches for phosphoprotein enrichment. Studies in literature have exploited the complementary chemistries of affinity materials like metal (immobilized metal ion affinity chromatography- IMAC) and metal oxides (metal oxide affinity chromatography- MOAC) independently and in a sequential elution approach to improve coverage of phosphoproteins. We demonstrate that further improvement in the enrichment of phosphoproteins can be achieved by using these metals and metal oxides independently and pooling the data.

2025-05-06 | PXD050933 | Pride

Phosphoproteome enrichment strategy using complementary chemistries of Fe-NTA and TiO2 followed by LC-MS/MS

2025-10-30 | PXD057032 | Pride

Phosphoproteome dynamics during differentiation of 3T3-L1 adipocytes

Project description:Here, we identified temporal dynamics of the phosphoproteome during adipocyte differentiation in the murine 3T3-L1 cells, applying untargeted proteomics in combination with enrichment strategies for phosphorylated peptides. Samples were taken at initiation of differentiation, at an intermediate and terminal time point.

2024-06-13 | PXD045778 | Pride

Phosphoproteome dynamics during differentiation of SGBS adipocytes

Project description:Here, we identified temporal dynamics of the phosphoproteome during adipocyte differentiation in the human SGBS cells, applying untargeted proteomics in combination with enrichment strategies for phosphorylated peptides. Samples were taken at initiation of differentiation, at an intermediate and terminal time point.

2024-06-13 | PXD045770 | Pride

Effects of high molecular weight phthalates on LPS-stimulated THP-1 macrophages - phosphoproteome

Project description:In this study, the effects of three high molecular weight phthalates (DINP, DIDP, DPHP) and their metabolites (MHINP, MCINP, OHMPHP) were investigated in THP-1 macrophages. For this purpose, the phosphoproteome was evaluated.

2023-09-13 | PXD042912 | Pride

MBOAT7-Driven Lysophosphatidylinositol Acylation in Adipocytes Contributes to Systemic Glucose Homeostasis

Project description:We previously demonstrated that antisense oligonucleotide (ASO)-mediated knockdown of Mboat7, the gene encoding Membrane Bound O-Acyltransferase 7, in the liver and adipose tissue of mice promoted high fat diet-induced hepatic steatosis, hyperinsulinemia, and systemic insulin resistance. Thereafter, other groups showed that hepatocyte-specific genetic deletion of Mboat7 promoted striking fatty liver and NAFLD progression in mice but does not alter insulin sensitivity, suggesting the potential for cell autonomous roles. Here, we show that MBOAT7 function in adipocytes contributes to diet-induced metabolic disturbances including hyperinsulinemia and systemic insulin resistance. We generated floxed Mboat7 mice and created hepatocyte- and adipocyte-specific knockout mice using Cre-recombinase mice under the control of the albumin and adiponectin promoter, respectively. After chow and high fat diet feeding (60% kCal fat), mice were subjected to metabolic phenotyping and tissues to molecular workup and analysis. Here, we show that MBOAT7 function in adipocytes contributes to diet-induced metabolic disturbances including hyperinsulinemia and systemic insulin resistance. The expression of Mboat7 in white adipose tissue closely correlates with diet-induced obesity across a panel of ~100 inbred strains of mice fed a high fat/high sucrose diet. Moreover, we found that adipocyte-specific genetic deletion of Mboat7 is sufficient to promote hyperinsulinemia, systemic insulin resistance, and mild fatty liver. Unlike in the liver, where Mboat7 plays a relatively minor role in maintaining arachidonic acid (AA)-containing PI pools, Mboat7 is the major source of AA-containing PI pools in adipose tissue. Our data demonstrate that MBOAT7 is a critical regulator of adipose tissue PI homeostasis, and adipocyte MBOAT7-driven PI biosynthesis is closely linked to hyperinsulinemia and insulin resistance in mice.

2023-05-10 | PXD039894 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

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