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The Hidden Culprit of Visceral Fat: Dysfunctional Subcutaneous Adipose Tissue – Serum proteomics

ABSTRACT: To investigate the proteomic profiles of paired subcutaneous adipose tissue (SAT) and visceral adipose tissue (VAT) samples, as well as their correlations with clinical traits in severely obese patients, and to identify potential serum protein markers associated with tissue expression or metabolic states.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Serum

DISEASE(S): Obesity

SUBMITTER: David Potesil

LAB HEAD: Zbynek Zdrahal

PROVIDER: PXD041750 | Pride | 2024-05-24

REPOSITORIES: Pride

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			Action	DRS
	4734_TIMS1_2col-74m_01_01_Slot1-10_1_4924.d.zip	Other
	4734_TIMS1_2col-74m_02_01_Slot1-11_1_4963.d.zip	Other
	4734_TIMS1_2col-74m_03_01_Slot1-12_1_4899.d.zip	Other
	4734_TIMS1_2col-74m_04_01_Slot1-13_1_4969.d.zip	Other
	4734_TIMS1_2col-74m_05_01_Slot1-14_1_4948.d.zip	Other

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Publications

Unraveling adipose tissue proteomic landscapes in severe obesity: insights into metabolic complications and potential biomarkers.

Hruska Pavel P Kucera Jan J Kuruczova Daniela D Buzga Marek M Pekar Matej M Holeczy Pavol P Potesil David D Zdrahal Zbynek Z Bienertova-Vasku Julie J

American journal of physiology. Endocrinology and metabolism 20231004 5

In this study, we aimed to comprehensively characterize the proteomic landscapes of subcutaneous adipose tissue (SAT) and visceral adipose tissue (VAT) in patients with severe obesity, to establish their associations with clinical characteristics, and to identify potential serum protein biomarkers indicative of tissue-specific alterations or metabolic states. We conducted a cross-sectional analysis of 32 patients with severe obesity (16 males and 16 females) of Central European descent who under ...[more]

PMID: 37792298

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The Hidden Culprit of Visceral Fat: Dysfunctional Subcutaneous Adipose Tissue – Adipose tissue proteomics

Project description:To investigate the proteomic profiles of paired subcutaneous adipose tissue (SAT) and visceral adipose tissue (VAT) samples, as well as their correlations with clinical traits in severely obese patients, and to identify potential serum protein markers associated with tissue expression or metabolic states.

2023-10-16 | PXD041721 | Pride

Enhancement of Tryptic Peptide Signals from Tissue Sections using MALDI IMS Post-ionization (MALDI-2)

Project description:Matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) allows for highly multiplexed, unlabeled mapping of analytes from tissue sections. However, further work is needed to improve sensitivity and depth of coverage for protein and peptide IMS. Laser-based post-ionization MALDI-2 has been shown to increase sensitivity for several molecular classes but has not yet been reported for peptides. We demonstrate signal enhancement of proteolytic peptides from thin tissue sections of human kidney by conventional MALDI (termed MALDI-1), and conventional MALDI augmented using a second ionizing laser (termed MALDI-2). Proteins were digested in situ using trypsin prior to IMS analysis. For tentative identification of peptides and proteins, a tissue homogenate from the same tissue analyzed by IMS was analyzed by LC-MS/MS. These proteins were digested in silico to generate a database of theoretical peptides to then match to MALDI IMS datasets. Peptides were tentatively identified by matching the MALDI peak list to the database peptide list employing a 5 ppm error window. This resulted in 314 ± 45 (n=3) peptides and 1 112 ± 84 (n=3) peptides for MALDI-1 and MALDI-2, respectively. Protein identifications requiring two or more peptides per protein resulted in 55 ± 13 proteins identifications with MALDI-1 and 205 ± 10 with MALDI-2. These results demonstrate that MALDI-2 provides enhanced sensitivity for the spatial mapping of tryptic peptides and significantly increases the number of proteins identified in IMS experiments.

2021-12-30 | PXD023877 | Pride

Microarray for transcript expression comparison of normal and Sox18 dominant negative dermal spheres.

Project description:The experiment was designed to identify differential gene expression due to dominant negative mutation of the Sox18 gene in the ragged Opossum spontaneous mouse mutant. Gene expression was analysed after whole RNA isolation in dermal spheres as hair follicle inductive mesenchyme tissue, and was intended to identify gene expression patterns associated with alteration of hair induction post Sox18 mutation.

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microRNA-dependent regulation of biomechanical genes establishes tissue stiffness homeostasis

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MOI analysis of purslane responses to salinity stress - leaf

Project description:This project constructed a multiomics (proteome, metabolome, and transcriptome) database on the response of purslane (Portulaca oleracea L.) plants to salt stress and subsequently started to employ Single-omics (SOA) and Multi-omics Integration (MOI) strategies to characterize the molecular basis of the resistance to salinity stress found in this halophyte species. After evaluating the morpho-physiological responses of purslane plants to salinity stress using a robust salinity stress protocol developed in-house, leaves, and roots were used to generate the database. The proteome data from five plants (control and salt-stressed - leaf and root) was generated and then submitted to the MaxQuant software version 2.1.3.0 for protein identification and abundance, generating a .txt file named “proteinsgroups” that underwent statistical analysis in Perseus software version 2.0.5.0. Here the data and results of the proteome part of the project are presented. For additional information, please read: Silva, V. N. B., da Silva, T. L. C., Ferreira, T. M. M., Neto, J. C. R., Leão, A. P., de Aquino Ribeiro, J. A., Abdelnur, P. V., Valadares, L. F., de Sousa, C. A. F., & Júnior, M. T. S. (2022). Multi-omics Analysis of Young Portulaca oleracea L. Plants' Responses to High NaCl Doses Reveals Insights into Pathways and Genes Responsive to Salinity Stress in this Halophyte Species. Phenomics (Cham, Switzerland), 3(1), 1–21. https://doi.org/10.1007/s43657-022-00061-2

2023-06-01 | PXD041627 | Pride

Identification of RNAs associated with the Caenorhabditis elegans spliced-leader trans-splicing proteins SNA-2, SNA-3, SNR-2 and SUT-1 proteins by RIP-Seq.

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2024-04-24 | E-MTAB-13193 | biostudies-arrayexpress

Comparative proteomics of human visceral and subcutaneous adipocytes

Project description:Adipose tissue (AT) distribution is an important determinant of cardiometabolic health. Increased visceral adiposity has been associated with a higher risk of obesity-related diseases. An important step in deciphering the molecular complexity of subcutaneous AT (SAT) and visceral AT (VAT) is to elucidate the molecular composition of the principal AT cell type, adipocytes. We present a comprehensive protein expression profile of abdominal subcutaneous (SA) and omental visceral adipocytes (VA). We isolated adipocytes from paired AT biopsies obtained during bariatric surgery of 19 morbidly obese women (BMI > 30 kg/m2) and performed state-of-the-art mass spectrometry to investigate their proteome profiles. We identified 3,686 proteins groups and found 1,140 differentially expressed proteins (adj. p-value < 0.05), of which 576 proteins were upregulated in SA and 564 in VA samples. In addition to providing a global protein profile of abdominal SA and omental VA, we also present the most differentially expressed pathways and processes distinguishing SA from VA. We show that SA are significantly more active in processes linked to vesicular transport and secretion, and also to increased lipid metabolism activity. Conversely, the expression of proteins involved in the mitochondrial energy metabolism and translational or biosynthetic activity is higher in VA. We also performed prediction analyses of differentially expressed putative secreted proteins, which revealed a significantly higher number of potentially secreted proteins in SA compared to VA. Our analysis represents a valuable resource of protein expression profiles in abdominal SA and omental VA, highlighting key differences in their role in obesity. Additionally, we predict possible protein targets among secreted proteins, which may be utilized for the further investigation of the role of different AT depots in obesity using peripheral blood.

2021-11-04 | PXD024734 | Pride

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Examination of the role of BMP signaling in patterning of human pluripotent stem cell derived mid/hindgut spheroids and maintenance of this patterning in organoids transplanted under mouse kidney capsules.

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