Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

See all formats and pricing
More options …
Volume 384, Issue 3


Interleukin-6 N-Terminal Peptides Modulate the Expression of junB Protooncogene and the Production of Fibrinogen in HepG2 Cells

S. Bősze / F. Hudecz / P. Igaz / Z. Ortutay / G. Csík / A. Falus / S. Tóth
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2003.047


Interleukin-6 (IL-6) is a helical cytokine exerting pleiotropic activities including the regulation of hematopoiesis, B cell activation and acute-phase reaction. The structure-function relationship of the molecule is the subject of intensive investigation using point and deletion mutants. Our objective was to analyse the role of the N-terminal 18–46 region in IL-6-mediated expression of junB protooncogene and fibrinogen production, reflecting the acute phase response, with synthetic overlapping peptides. mRNA expression of junB was monitored by competitive RT-PCR, while sandwich ELISA was used for the detection of fibrinogen in the supernatant of HepG2 human hepatoma cells. We found that even short synthetic octapeptides can be stimulatory (in the absence of IL-6) or inhibitory (in the presence of IL-6) in both assays. To establish the molecular mechanism by which synthetic peptides exert their biological effects electromobility shift assay was carried out using HepG2 nuclear extracts. Peptides inducing junB expression initiate gel shifts of STAT3/DNA complexes, which may indicate the involvement of this signal transduction pathway. Circular dicroism spectroscopy data suggest that 8-11-mer peptides representing different parts of the 18–46 region have a marked tendency to adopt ordered conformations in a water/trifluoroethanol (1:1 v/v) mixture. Competition studies with rhIL-6 and selected fluorophorelabelled peptides indicate the presence of more than one binding site on soluble IL-6 receptor. Considering the possible multiple etiologic role of IL-6 in the pathogenesis of various diseases, these peptides could be useful for dissection of IL-6 related biological effects.

About the article

Published Online: 2005-06-01

Published in Print: 2003-03-14

Citation Information: Biological Chemistry, Volume 384, Issue 3, Pages 409–421, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2003.047.

Export Citation

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

Mirjana Liovic, Brian Lee, Marjana Tomic-Canic, Mariella D'Alessandro, Viacheslav N. Bolshakov, and E. Birgitte Lane
Experimental Cell Research, 2008, Volume 314, Number 10, Page 2066

Comments (0)

Please log in or register to comment.
Log in