Abstract:
:Interleukin-6 (IL-6) is a 185 amino acid residue helical cytokine with various biological activities (e. g. B cell development, acute phase reaction). We have investigated the role of the 168-185 C-terminal region of IL-6 in the induction of fibrinogen synthesis and expression of junB mRNA using synthetic peptides corresponding to this region. Circular dichroism spectroscopy data suggest that even truncated peptides have a strong tendency to adopt an ordered conformation. Peptides were tested alone or in combination with recombinant hIL-6 on an IL-6 responsive human hepatoma HepG2 cell line. The expression of the protooncogene junB monitored by competitive RT-PCR represents an early, while the fibrinogen production detected by sandwich ELISA a late, marker of IL-6 initiated events. We found that peptides--depending on their structure--modulate spontaneous as well as IL-6 induced fibrinogen production and/or mRNA expression of junB by exhibiting inhibition (in the presence of IL-6) or stimulation (in the absence of IL-6).
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Igaz P,Bösze S,Tóth S,Falus A,Hudecz Fdoi
10.1515/BC.2001.079keywords:
subject
Has Abstractpub_date
2001-04-01 00:00:00pages
669-76issue
4eissn
1431-6730issn
1437-4315journal_volume
382pub_type
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