Md Arifur Rahman, Ardeshir Amirkhani, Maria Mempin, Seong Beom Ahn, Anand K Deva, Mark S Baker, Karen Vickery, Honghua Hu
{"title":"The Low-Abundance Plasma Proteome Reveals Differentially Abundant Proteins Associated with Breast Implant Capsular Contracture: A Pilot Study.","authors":"Md Arifur Rahman, Ardeshir Amirkhani, Maria Mempin, Seong Beom Ahn, Anand K Deva, Mark S Baker, Karen Vickery, Honghua Hu","doi":"10.3390/proteomes12030022","DOIUrl":null,"url":null,"abstract":"<p><p>Capsular contracture (CC) is one of the most common postoperative complications associated with breast implant-associated infections. The mechanisms that lead to CC remain poorly understood. Plasma is an ideal biospecimen for early proteomics biomarker discovery. However, as high-abundance proteins mask signals from low-abundance proteins, identifying novel or specific proteins as biomarkers for a particular disease has been hampered. Here, we employed depletion of high-abundance plasma proteins followed by Tandem Mass Tag (TMT)-based quantitative proteomics to compare 10 healthy control patients against 10 breast implant CC patients. A total of 450 proteins were identified from these samples. Among them, 16 proteins were significantly differentially expressed in which 5 proteins were upregulated and 11 downregulated in breast implant CC patients compared to healthy controls. Gene Ontology enrichment analysis revealed that proteins related to cell, cellular processes and catalytic activity were highest in the cellular component, biological process, and molecular function categories, respectively. Further, pathway analysis revealed that inflammatory responses, focal adhesion, platelet activation, and complement and coagulation cascades were enriched pathways. The differentially abundant proteins from TMT-based quantitative proteomics have the potential to provide important information for future mechanistic studies and in the development of breast implant CC biomarkers.</p>","PeriodicalId":20877,"journal":{"name":"Proteomes","volume":null,"pages":null},"PeriodicalIF":4.0000,"publicationDate":"2024-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11348101/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Proteomes","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3390/proteomes12030022","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Capsular contracture (CC) is one of the most common postoperative complications associated with breast implant-associated infections. The mechanisms that lead to CC remain poorly understood. Plasma is an ideal biospecimen for early proteomics biomarker discovery. However, as high-abundance proteins mask signals from low-abundance proteins, identifying novel or specific proteins as biomarkers for a particular disease has been hampered. Here, we employed depletion of high-abundance plasma proteins followed by Tandem Mass Tag (TMT)-based quantitative proteomics to compare 10 healthy control patients against 10 breast implant CC patients. A total of 450 proteins were identified from these samples. Among them, 16 proteins were significantly differentially expressed in which 5 proteins were upregulated and 11 downregulated in breast implant CC patients compared to healthy controls. Gene Ontology enrichment analysis revealed that proteins related to cell, cellular processes and catalytic activity were highest in the cellular component, biological process, and molecular function categories, respectively. Further, pathway analysis revealed that inflammatory responses, focal adhesion, platelet activation, and complement and coagulation cascades were enriched pathways. The differentially abundant proteins from TMT-based quantitative proteomics have the potential to provide important information for future mechanistic studies and in the development of breast implant CC biomarkers.
ProteomesBiochemistry, Genetics and Molecular Biology-Clinical Biochemistry
CiteScore
6.50
自引率
3.00%
发文量
37
审稿时长
11 weeks
期刊介绍:
Proteomes (ISSN 2227-7382) is an open access, peer reviewed journal on all aspects of proteome science. Proteomes covers the multi-disciplinary topics of structural and functional biology, protein chemistry, cell biology, methodology used for protein analysis, including mass spectrometry, protein arrays, bioinformatics, HTS assays, etc. Our aim is to encourage scientists to publish their experimental and theoretical results in as much detail as possible. Therefore, there is no restriction on the length of papers. Scope: -whole proteome analysis of any organism -disease/pharmaceutical studies -comparative proteomics -protein-ligand/protein interactions -structure/functional proteomics -gene expression -methodology -bioinformatics -applications of proteomics