Evidence map›Paper›PMID 35406736›Full record

ArticleCells2022

Multi-Omics Approach Reveals Dysregulation of Protein Phosphorylation Correlated with Lipid Metabolism in Mouse Non-Alcoholic Fatty Liver.

Sora Q Kim, Rodrigo Mohallem, Jackeline Franco, Kimberly K Buhman, Kee-Hong Kim, Uma K Aryal

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
6.2field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.

  1. Pooled it
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  11. Proteomic analysis of unicellular cyanobacteriumbioRxiv : the preprint server for biology · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Sora Q KimDepartment of Nutrition Science, Purdue University, West Lafayette, IN 47907, USA.ORCID 0000-0003-3151-0970
Rodrigo MohallemBindley Bioscience Center, Purdue Proteomics Facility, Purdue University, West Lafayette, IN 47907, USA.ORCID 0000-0003-3680-1291
Jackeline FrancoBindley Bioscience Center, Purdue Proteomics Facility, Purdue University, West Lafayette, IN 47907, USA.ORCID 0000-0002-0737-4764
Kimberly K BuhmanDepartment of Nutrition Science, Purdue University, West Lafayette, IN 47907, USA.
Kee-Hong KimDepartment of Food Science, Purdue University, West Lafayette, IN 47907, USA.
Uma K AryalBindley Bioscience Center, Purdue Proteomics Facility, Purdue University, West Lafayette, IN 47907, USA.ORCID 0000-0003-4543-1536
Purdue University West Lafayette · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Obesity caused by overnutrition is a major risk factor for non-alcoholic fatty liver disease (NAFLD). Several lipid intermediates such as fatty acids, glycerophospholipids and sphingolipids are implicated in NAFLD, but detailed characterization of lipids and their functional links to proteome and phosphoproteome remain to be elucidated. To characterize this complex molecular relationship, we used a multi-omics approach by conducting comparative proteomic, phoshoproteomic and lipidomic analyses of high fat (HFD) and low fat (LFD) diet fed mice livers. We quantified 2447 proteins and 1339 phosphoproteins containing 1650 class I phosphosites, of which 669 phosphosites were significantly different between HFD and LFD mice livers. We detected alterations of proteins associated with cellular metabolic processes such as small molecule catabolic process, monocarboxylic acid, long- and medium-chain fatty acid, and ketone body metabolic processes, and peroxisome organization. We observed a significant downregulation of protein phosphorylation in HFD fed mice liver in general. Untargeted lipidomics identified upregulation of triacylglycerols, glycerolipids and ether glycerophosphocholines and downregulation of glycerophospholipids, such as lysoglycerophospholipids, as well as ceramides and acylcarnitines. Analysis of differentially regulated phosphosites revealed phosphorylation dependent deregulation of insulin signaling as well as lipogenic and lipolytic pathways during HFD induced obesity. Thus, this study reveals a molecular connection between decreased protein phosphorylation and lipolysis, as well as lipid-mediated signaling in diet-induced obesity.

Indexed as

Non-alcoholic Fatty Liver DiseaseAnimalsDiet, High-FatFatty AcidsGlycerophospholipidsLipid MetabolismMiceObesityPhosphorylationProteomicsTriglyceridesFatty AcidsGlycerophospholipidsTriglyceridesfatty liverHFDlipidomicsmass spectrometryNAFLDproteomics

Identifiers

PMID35406736
PMCPMC8997945
OpenAlexW4220782779

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.