Document Detail


Vigilin is a cytoplasmic protein. A study on its expression in primary cells and in established cell lines of different species.
MedLine Citation:
PMID:  8477745     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A fusion protein composed of about two vigilin domains and beta-galactosidase was used to raise polyclonal antibodies which were affinity-purified and employed for immunoblotting and immunohistochemistry. A protein of an apparent molecular mass of 155 kDa could be stained in extracts of a variety of cells from different species and organs. Immunohistological studies on single cells showed that vigilin is accumulated in the cytoplasm. During in vitro maintenance of primary cell cultures, as well as of a growth-factor-dependent cell line, vigilin expression decreases and ceases in senescent cells. In contrast, vigilin is constitutively expressed in all other transformed cell lines of various origin studies so far. Vigilin expression can be induced in peripheral blood lymphocytes by mitogen stimulation. These observations suggest an involvement of vigilin in processes of cell activation. Immunoblot experiments demonstrating the presence of vigilin in a broad range of eukaryotes, indicate a high degree of evolutionary conservation.
Authors:
G Neu-Yilik; H Zorbas; T R Gloe; H M Raabe; T A Hopp-Christensen; P K Müller
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  213     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1993 Apr 
Date Detail:
Created Date:  1993-05-25     Completed Date:  1993-05-25     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  727-36     Citation Subset:  IM    
Affiliation:
Medizinische Universität zu Lübeck, Institut für Med. Molekularbiologie, Germany.
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MeSH Terms
Descriptor/Qualifier:
Animals
Carrier Proteins*
Cartilage / metabolism*
Cell Line
Cell Line, Transformed
Cells, Cultured
Chickens
Cytoplasm / metabolism
Electrophoresis, Polyacrylamide Gel
Humans
Immunoblotting
Lymphocyte Activation
Lymphocytes / metabolism
Protein Biosynthesis*
Proteins / chemistry,  isolation & purification
RNA, Messenger / analysis,  metabolism
RNA-Binding Proteins*
Tumor Cells, Cultured
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Proteins; 0/RNA, Messenger; 0/RNA-Binding Proteins; 147605-06-9/high density lipoprotein binding protein

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


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