Document Detail

Distinct proteomic features of two fibrogenic liver cell populations: hepatic stellate cells and portal myofibroblasts.
MedLine Citation:
PMID:  20049859     Owner:  NLM     Status:  MEDLINE    
In chronic liver diseases, the accumulation of extracellular matrix leading to fibrosis is caused by myofibroblasts, the origins of which are debatable. We performed a comparative proteomic study to identify markers and gain insight into distinct functions of myofibroblasts derived either from hepatic stellate cells (HSCs) or from portal mesenchymal cells. After isolation from normal liver and culture in similar conditions, myofibroblastic HSCs (MF-HSCs) presented enlarged cytoplasms whereas portal myofibroblasts (PMFs) were more proliferative, and formed more stress fibers. The two cell types were subjected to comparative analyses by 2-D MS/MS. Six proteins were overexpressed in PMFs, with myofibroblast-related typical functions. Among them, cofilin-1 showed the greatest difference in expression and a lower pI than expected. Immunoblot demonstrated higher levels of phosphorylation, a modification of the protein implicated in stress fiber formation. Eleven proteins, mostly involved in stress response, were overexpressed in MF-HSCs. Cytoglobin had the highest level of overexpression, as confirmed by reverse transcription quantitative real-time PCR, immunoblot and immunocytochemical analyses. These results identify cytoglobin as the best marker for distinguishing MF-HSCs from PMFs and suggest different functions for the two cell populations in the liver wound healing response, with a prominent role for PMFs in scar formation.
Nelly Bosselut; Chantal Housset; Paulo Marcelo; Colette Rey; Thorsten Burmester; J?elle Vinh; Michel Vaubourdolle; Axelle Cadoret; Bruno Baudin
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Proteomics     Volume:  10     ISSN:  1615-9861     ISO Abbreviation:  Proteomics     Publication Date:  2010 Mar 
Date Detail:
Created Date:  2010-03-03     Completed Date:  2010-06-04     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101092707     Medline TA:  Proteomics     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  1017-28     Citation Subset:  IM    
AP-HP, H?pital Saint-Antoine, Biochimie A, Paris, France.
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MeSH Terms
Actin Depolymerizing Factors / chemistry,  metabolism
Amino Acid Sequence
Cells, Cultured
Electrophoresis, Gel, Two-Dimensional
Fibroblasts / metabolism*,  pathology
Gene Expression Profiling
Globins / chemistry,  metabolism
Hepatic Stellate Cells / metabolism*,  pathology
Liver Cirrhosis / metabolism*,  pathology*
Molecular Sequence Data
Peptides / chemistry
Portal System / pathology*
Proteome / chemistry,  metabolism
Proteomics / methods*
Rats, Sprague-Dawley
Reg. No./Substance:
0/Actin Depolymerizing Factors; 0/Peptides; 0/Proteome; 0/cytoglobin; 9004-22-2/Globins

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