Document Detail

MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro.
MedLine Citation:
PMID:  24014025     Owner:  NLM     Status:  MEDLINE    
LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells. In this study, we selected MCF-7 cells that stably express forms of recombinant LOXL2 differing in their subcellular localizations and catalytic competencies. This enabled us to dissect the molecular functions of intracellular and extracellular LOXL2s and examine their contributions to breast cancer metastasis/invasion. We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus. Both forms of LOXL2 can oxidize lysine in solution. However, we found that expression of intracellular LOXL2 is more strongly associated with EMT and invasiveness than secreted LOXL2 in vitro. The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
Hee-Jung Moon; Joel Finney; Li Xu; David Moore; Danny R Welch; Minae Mure
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2013-09-06
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  288     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2013 Oct 
Date Detail:
Created Date:  2013-10-21     Completed Date:  2013-12-31     Revised Date:  2014-10-21    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  30000-8     Citation Subset:  IM    
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MeSH Terms
Amino Acid Oxidoreductases / biosynthesis*,  genetics
Breast Neoplasms / enzymology*,  genetics,  pathology
Cell Line, Tumor
Cell Nucleus / enzymology*,  genetics,  pathology
Epithelial-Mesenchymal Transition*
Gene Expression Regulation, Enzymologic*
Gene Expression Regulation, Neoplastic*
Neoplasm Invasiveness
Neoplasm Metastasis
Neoplasm Proteins / biosynthesis*,  genetics
Grant Support
Reg. No./Substance:
0/Neoplasm Proteins; EC 1.4.-/Amino Acid Oxidoreductases; EC 1.4.3.-/LOXL2 protein, human

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