Document Detail


Distinct primary translation products from human liver mRNA give rise to secreted and cell-associated forms of complement protein C2.
MedLine Citation:
PMID:  6088497     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The second component of complement (C2), is a class III major histocompatibility complex gene product and a glycoprotein in the classical complement activating system. Synthesis in the human hepatoma-derived cell line HepG2 results in three intracellular forms: an 84-kDa form secreted in 1-2 h; 79-kDa and 70-kDa forms that remain cell-associated for intervals up to 12 h. All three forms are C2 polypeptides as demonstrated by inhibition of immunoprecipitation with unlabeled C2 and the presence of common major peptide fragments following chymotryptic digestion. The cell-associated forms of C2 are not products of proteolysis as demonstrated by experiments with multiple proteinase inhibitors and by observations of the kinetics of synthesis. Inhibition of core glycosylation by tunicamycin and deglycosylation by acid hydrolysis indicate that the three intracellular C2 polypeptides are glycosylated to a similar extent. Although the 84-kDa form of C2 is susceptible to C1s cleavage, the two cell-associated forms are not. Cell-free biosynthesis by mRNA from HepG2 or human liver results in three primary translation products corresponding to the three unglycosylated forms of C2. These results indicate that HepG2 cells synthesize C2 protein in both secreted and cell-associated forms and that each form is derived from a separate primary translation product.
Authors:
D H Perlmutter; F S Cole; G Goldberger; H R Colten
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  259     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1984 Aug 
Date Detail:
Created Date:  1984-09-28     Completed Date:  1984-09-28     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  10380-5     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Carcinoma, Hepatocellular
Cell Line
Complement C2 / biosynthesis,  genetics*,  secretion
Humans
Kinetics
Liver / metabolism
Liver Neoplasms
Major Histocompatibility Complex
Peptide Fragments / analysis
Protein Biosynthesis*
RNA, Messenger / genetics*
Tunicamycin / pharmacology
Grant Support
ID/Acronym/Agency:
1F32AM07114/AM/NIADDK NIH HHS; HD17461/HD/NICHD NIH HHS; KO8 HD00584/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/Complement C2; 0/Peptide Fragments; 0/RNA, Messenger; 11089-65-9/Tunicamycin

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


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