Author:
Igaz Péter,Bösze Szilvia,Tóth Sára,Falus András,Hudecz Ferenc
Abstract
AbstractInterleukin-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 Cterminal 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 RTPCR 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).
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Cited by
2 articles.
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