Cited 1 time in webofscience Cited 2 time in scopus

Integrated Transcriptomic and Proteomic Analysis of Primary Human Umbilical Vein Endothelial Cells

Title
Integrated Transcriptomic and Proteomic Analysis of Primary Human Umbilical Vein Endothelial Cells
Authors
Madugundu, Anil K.Na, Chan HyunNirujogi, Raja SekharRenuse, SantoshKim, Kwang PyoBurns, Kathleen H.Wilks, ChristopherLangmead, BenEllis, Shannon E.Collado-Torres, LeonardoHalushka, Marc K.Kim, Min-SikPandey, Akhilesh
DGIST Authors
Kim, Min-Sik
Issue Date
2019-08
Citation
Proteomics, 19(15), 1800315
Type
Article
Article Type
Article
Author Keywords
allelic expressioncoding SNPmass-spectrometryproteoformproteogenomicsRNA-seqsplice variantstranscriptome
Keywords
ADHESION MOLECULESGENOME ANNOTATIONQUALITY-CONTROLNONCODING RNASIDENTIFICATIONTRANSLATIONEXPRESSIONPROTEINSDRAFTQUANTIFICATION
ISSN
1615-9853
Abstract
Understanding the molecular profile of every human cell type is essential for understanding its role in normal physiology and disease. Technological advancements in DNA sequencing, mass spectrometry, and computational methods allow us to carry out multiomics analyses although such approaches are not routine yet. Human umbilical vein endothelial cells (HUVECs) are a widely used model system to study pathological and physiological processes associated with the cardiovascular system. In this study, next-generation sequencing and high-resolution mass spectrometry to profile the transcriptome and proteome of primary HUVECs is employed. Analysis of 145 million paired-end reads from next-generation sequencing confirmed expression of 12 186 protein-coding genes (FPKM ≥0.1), 439 novel long non-coding RNAs, and revealed 6089 novel isoforms that were not annotated in GENCODE. Proteomics analysis identifies 6477 proteins including confirmation of N-termini for 1091 proteins, isoforms for 149 proteins, and 1034 phosphosites. A database search to specifically identify other post-translational modifications provide evidence for a number of modification sites on 117 proteins which include ubiquitylation, lysine acetylation, and mono-, di- and tri-methylation events. Evidence for 11 “missing proteins,” which are proteins for which there was insufficient or no protein level evidence, is provided. Peptides supporting missing protein and novel events are validated by comparison of MS/MS fragmentation patterns with synthetic peptides. Finally, 245 variant peptides derived from 207 expressed proteins in addition to alternate translational start sites for seven proteins and evidence for novel proteoforms for five proteins resulting from alternative splicing are identified. Overall, it is believed that the integrated approach employed in this study is widely applicable to study any primary cell type for deeper molecular characterization. © 2019 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
URI
http://hdl.handle.net/20.500.11750/10384
DOI
10.1002/pmic.201800315
Publisher
Wiley-VCH Verlag
Related Researcher
  • Author Kim, Min-Sik Laboratory for QBIO and Precision Medicine
  • Research Interests Cancer Proteogenomics, Biomarker Discovery, Integrative Multi-Omics
Files:
There are no files associated with this item.
Collection:
Department of New BiologyLaboratory for QBIO and Precision Medicine1. Journal Articles


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