PXD006703

PXD006703 is an original dataset announced via ProteomeXchange.

Title	Large-Scale Analysis of Breast Cancer-Related Conformational Changes in Proteins using SILAC-SPROX
Description	Proteomic methods for disease state characterization and biomarker discovery have traditionally utilized quantitative mass spectrometry methods to identify proteins with altered expression levels in disease states. Here we report on the large-scale use of protein folding stability measurements to characterize different subtypes of breast cancer using the Stable Isotope Labeling with Amino Acids in Cell Culture and Stability of Proteins from Rates of Oxidation (SILAC-SPROX) technique. Protein folding stability differences were studied in a comparison of two luminal breast cancer subtypes, luminal-A and -B (i.e., MCF-7 and BT-474 cells, respectively), and in a comparison of a luminal-A and basal subtype of the disease (i.e., MCF-7 and MDA-MB-468 cells, respectively). The 242 and 445 protein hits identified with altered stabilities in these comparative analyses, included a large fraction with no significant expression level changes. This suggests thermodynamic stability measurements create a new avenue for protein biomarker discovery. A number of the identified protein hits are known from other biochemical studies to play a role in tumorigenesis and cancer progression. This not only substantiates the biological significance of the protein hits identified using the SILAC-SPROX approach, but it also helps elucidate the molecular basis for their dysregulation and/or dysfunction in cancer.
HostingRepository	PRIDE
AnnounceDate	2017-07-10
AnnouncementXML	Submission_2017-07-10_00:43:36.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Fang Liu
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	methylthiolated residue; acetylated residue; monohydroxylated residue; deamidated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-06-13 01:34:42	ID requested
⏵ 1	2017-07-10 00:43:37	announced

Liu F, Meng H, Fitzgerald MC, Large-Scale Analysis of Breast Cancer-Related Conformational Changes in Proteins Using SILAC-SPROX. J Proteome Res, 16(9):3277-3286(2017) [pubmed]

curator keyword: Biomedical

submitter keyword: MCF-7, BT-474, MDA-MB-468, protein folding, chemical denaturation

Michael C. Fitzgerald
contact affiliation	Departments of Chemistry and Biochemistry, Duke University, United States
contact email	michael.c.fitzgerald@duke.edu
lab head
Fang Liu
contact affiliation	Duke university
contact email	fang.liu@duke.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD006703
     1. Label: PRIDE project
     2. Name: Large-Scale Analysis of Breast Cancer-Related Conformational Changes in Proteins using SILAC-SPROX