Document Detail


Membrane glycoproteins associated with breast tumor cell progression identified by a lectin affinity approach.
MedLine Citation:
PMID:  18729497     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The membrane glycoprotein component of the cellular proteome represents a promising source for potential disease biomarkers and therapeutic targets. Here we describe the development of a method that facilitates the analysis of membrane glycoproteins and apply it to the differential analysis of breast tumor cells with distinct malignant phenotypes. The approach combines two membrane extraction procedures, and enrichment using ConA and WGA lectin affinity columns, prior to digestion and analysis by LC-MS/MS. The glycoproteins are identified and quantified by spectral counting. Although the distribution of glycoprotein expression as a function of MW and p I was very similar between the two related cell lines tested, the approach enabled the identification of several distinct membrane glycoproteins with an expression index correlated with either a precancerous (MCF10AT1), or a malignant, metastatic cellular phenotype (MCF10CA1a). Among the proteins associated with the malignant phenotype, Gamma-glutamyl hydrolase, CD44, Galectin-3-binding protein, and Syndecan-1 protein have been reported as potential biomarkers of breast cancer.
Authors:
Yanfei Wang; Xiaoping Ao; Huy Vuong; Meghana Konanur; Fred R Miller; Steve Goodison; David M Lubman
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2008-08-27
Journal Detail:
Title:  Journal of proteome research     Volume:  7     ISSN:  1535-3893     ISO Abbreviation:  J. Proteome Res.     Publication Date:  2008 Oct 
Date Detail:
Created Date:  2008-10-06     Completed Date:  2008-11-13     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  101128775     Medline TA:  J Proteome Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4313-25     Citation Subset:  IM    
Affiliation:
Department of Chemistry, The University of Michigan, 930 North University Avenue, Ann Arbor, Michigan 48109-1055, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Breast Neoplasms* / metabolism,  pathology
Cell Line, Tumor
Chromatography, Affinity / methods*
Female
Humans
Lectins / metabolism*
Mass Spectrometry
Membrane Glycoproteins / chemistry,  genetics,  metabolism*
Molecular Sequence Data
Peptides / chemistry,  genetics,  metabolism
Grant Support
ID/Acronym/Agency:
R01 CA090503-04/CA/NCI NIH HHS; R01 CA100104-05/CA/NCI NIH HHS; R01 CA108597/CA/NCI NIH HHS; R01 CA108597-05/CA/NCI NIH HHS; R01 GM049500-12/GM/NIGMS NIH HHS; R01CA100104/CA/NCI NIH HHS; R01CA108597/CA/NCI NIH HHS; R01CA90503/CA/NCI NIH HHS; R01GM49500/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Lectins; 0/Membrane Glycoproteins; 0/Peptides
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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