Mapping the cell-membrane proteome of the SKBR3/HER2+ cell line to the cancer hallmarks

The hallmarks of biological processes that underlie the development of cancer have been long recognized, yet, existing therapeutic treatments cannot prevent cancer from continuing to be one of the leading causes of death worldwide. This work was aimed at exploring the extent to which the cell-membra...

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Bibliographic Details
Published in:PloS one 2022-08, Vol.17 (8), p.e0272384-e0272384
Main Authors: Lazar, Iulia M, Karcini, Arba, Haueis, Joshua R. S
Format: Article
Language:English
Subjects:
Adhesion
Analysis
Annotations
Antigens
Biological activity
Biology and Life Sciences
Breast cancer
Cancer
Cancer immunotherapy
CD44 antigen
Cell cycle
Cell membranes
Chemical compounds
Computer and Information Sciences
Cytokines
Data processing
Diagnosis
Epigenetics
ErbB-2 protein
Fibroblast growth factor receptors
Gene expression
Gene mapping
Genetic aspects
Genomes
Growth factors
Kinases
Mass spectrometry
Mass spectroscopy
Medicine and Health Sciences
Membrane proteins
Membranes
Metabolism
Metastasis
Motility
Multiagent systems
Mutation
Peptides
Pharmacology
Precision medicine
Protein interaction
Protein transport
Protein-protein interactions
Proteins
Proteomes
Receptors
Scientific imaging
Signaling
Suppressors
Therapeutic applications
Therapeutic targets
TOR protein
Tumor suppressor genes
Tumors
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Summary:The hallmarks of biological processes that underlie the development of cancer have been long recognized, yet, existing therapeutic treatments cannot prevent cancer from continuing to be one of the leading causes of death worldwide. This work was aimed at exploring the extent to which the cell-membrane proteins are implicated in triggering cancer hallmark processes, and assessing the ability to pinpoint tumor-specific therapeutic targets through a combined membrane proteome/cancer hallmark perspective. By using GO annotations, a database of human proteins associated broadly with ten cancer hallmarks was created. Cell-membrane cellular subfractions of SKBR3/HER2+ breast cancer cells, used as a model system, were analyzed by high resolution mass spectrometry, and high-quality proteins (FDR
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0272384