Investigation of adipocyte differentiation based on proteomics and intact N-glycopeptide modificationomics

IF 2.5 4区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY

Biochimica et biophysica acta. Proteins and proteomics Pub Date : 2024-10-09 DOI:10.1016/j.bbapap.2024.141052

Xin-Yu Li , Nuerbiye Nuermaimaiti , Xuanyu Meng , Xiaozheng Zhang , Aikedaimu Abudukeremu , Yihuai He , Wenting Ma , Xuelei Chen , Shangkun Li , Jiaxin Sun , Yaqun Guan

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引用次数: 0

Abstract

Objective

To investigate the role of N-glycosylation modification of proteins in adipocyte differentiation during the adipogenic process.

Methods

SVF cells and adipocytes were analyzed for proteomics and intact N-glycopeptide modificationomics.Differential expression of proteins, glycoforms, and sites between the two groups was screened and subjected to Gene Ontology (GO) functional enrichment analysis, KEGG pathway enrichment analysis, and protein-protein interaction (PPI) network analysis. The top 20 most significantly differentially expressed adipogenic differentiation-related proteins were identified, and the most pronouncedly altered proteins were analyzed for glycoforms, glycan chains, and sites.

Results

Proteomics analysis identified 39,392 peptides and 5208 proteins, while intact N-glycopeptide modification profiling identified 3293 intact glycopeptides, 426 proteins, and 161 glycan chains. Proteomics identified 2510 differentially expressed proteins, with CD36 (Cluster of Differentiation 36, CD36) significantly upregulated. In adipocytes, CD36 had 4 N-glycosylation sites: N79, N220, N320, N417, with N320 being a newly identified site. GO enrichment results indicated that CD36 is associated with fatty acid oxidation, lipid oxidation, and fatty acid uptake into cells.

Conclusion

Multiple proteins undergo N-glycosylation modification during adipocyte differentiation, with CD36, a fatty acid translocase, being significantly expressed in adipocytes. This suggests that N-glycosylation modification of CD36 may play a crucial role in adipocyte differentiation, providing a foundation for further investigation into the function of CD36 N-glycosylation in adipocyte differentiation.

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基于蛋白质组学和完整 N-糖肽修饰组学的脂肪细胞分化研究。

目的：研究蛋白质的 N-糖基化修饰在脂肪形成过程中对脂肪细胞分化的作用：方法：对 SVF 细胞和脂肪细胞进行蛋白质组学和完整 N-糖基化肽修饰组学分析：筛选两组间差异表达的蛋白质、糖型和位点，并进行基因本体（GO）功能富集分析、KEGG通路富集分析和蛋白-蛋白相互作用（PPI）网络分析。确定了前 20 个差异表达最明显的脂肪生成分化相关蛋白质，并对变化最明显的蛋白质的糖型、糖链和位点进行了分析：蛋白质组学分析确定了 39392 个肽和 5208 个蛋白质，而完整的 N-糖肽修饰分析确定了 3293 个完整的糖肽、426 个蛋白质和 161 个糖链。蛋白质组学确定了 2510 个差异表达的蛋白质，其中 CD36（分化簇 36，CD36）显著上调。在脂肪细胞中，CD36有4个N-糖基化位点：在脂肪细胞中，CD36有4个N-糖基化位点：N79、N220、N320、N417，其中N320是新发现的位点。GO富集结果表明，CD36与脂肪酸氧化、脂质氧化和脂肪酸摄入细胞有关：结论：在脂肪细胞分化过程中，多种蛋白质都会发生 N-糖基化修饰，其中 CD36（一种脂肪酸转运酶）在脂肪细胞中表达显著。这表明 CD36 的 N-糖基化修饰可能在脂肪细胞分化过程中起着关键作用，为进一步研究 CD36 N-糖基化在脂肪细胞分化中的功能奠定了基础。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Biochimica et biophysica acta. Proteins and proteomics 生物-生化与分子生物学

CiteScore

8.00

自引率

0.00%

发文量

审稿时长

33 days

期刊介绍： BBA Proteins and Proteomics covers protein structure conformation and dynamics; protein folding; protein-ligand interactions; enzyme mechanisms, models and kinetics; protein physical properties and spectroscopy; and proteomics and bioinformatics analyses of protein structure, protein function, or protein regulation.