Document Detail


Acidic stress facilitates tyrosine phosphorylation of HLJ1 to associate with actin cytoskeleton in lung cancer cells.
MedLine Citation:
PMID:  20615403     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Acidosis is a common stress in solid tumours and is also a major determinant of tumour growth, metabolism, and metastasis. During cellular stress, heat shock proteins play an important role in actin cytoskeleton stability. HLJ1, a member of the DnaJ-like heat shock protein 40, has been characterised as a tumour suppressor gene; however, the effect of acidic stress on HLJ1 is unknown. In this study, we found that the migration ability of human lung adenocarcinoma cells was significantly impaired following the increased protein level of HLJ1 under acidic culture conditions. However, HLJ1 transcriptional activity was no different in the normal and acidic culture medium. Incubation of the cells in an acidic extracellular pH (pHe 6.4) caused up-regulated tyrosine phosphorylation of HLJ1 within 2h. We further identified the sub-cellular distribution of tyrosine phospho-HLJ1 and its tyrosine-phosphorylated sites. Most importantly, acidic stress was observed to remarkably enhance the interaction between HLJ1 and β-actin, which was a tyrosine phosphorylation-dependent association. In conclusion, our results not only validate that HLJ1 is a tyrosine phosphoprotein, but also suggest that the increased level of tyrosine phospho-HLJ1 is crucial for binding with the actin cytoskeleton, especially in acidic pHe. We propose that acidic stress increases the association between HLJ1 and β-actin to modulate migration of human lung cancer cells.
Authors:
Ching-Hsien Chen; Ho Lin; Show-Mei Chuang; Sheng-Yi Lin; Jeremy J W Chen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-07-13
Journal Detail:
Title:  Experimental cell research     Volume:  316     ISSN:  1090-2422     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2010 Oct 
Date Detail:
Created Date:  2010-09-24     Completed Date:  2010-11-10     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2910-21     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier Inc. All rights reserved.
Affiliation:
Department of Life Science, National Chung Hsing University, Taichung, Taiwan.
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MeSH Terms
Descriptor/Qualifier:
Acidosis / metabolism*
Actins / metabolism*
Cell Movement
Cytoskeleton / pathology*
HSP40 Heat-Shock Proteins / metabolism*
Humans
Lung Neoplasms / pathology*
Phosphoproteins / metabolism
Phosphorylation
Protein Binding
Tumor Cells, Cultured
Tyrosine / metabolism
Chemical
Reg. No./Substance:
0/Actins; 0/DNAJB4 protein, human; 0/HSP40 Heat-Shock Proteins; 0/Phosphoproteins; 55520-40-6/Tyrosine

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