Intracellular signaling prevents effective blockade of oncogenic gp130 mutants by neutralizing antibodies.

ABSTRACT:

Background

Short in-frame deletions in the second extracellular domain of the cytokine receptor gp130 are the leading cause of inflammatory hepatocellular adenomas (IHCAs). The deletions render gp130 constitutively active. In this study we investigate the intracellular signaling potential of one of the most potent constitutively active gp130 mutants (CAgp130) found in IHCAs.

Results

Trafficking and signaling of CAgp130 were studied in stably transfected cell lines that allowed the inducible expression of CAgp130 fused to fluorescent proteins such as YFP and mCherry. In contrast to the predominantly highly glycosylated gp130 wild type (WTgp130), CAgp130 is preferentially found in the less glycosylated high-mannose form. Accordingly, the mutated receptor is retained intracellu

SUBMITTER: Rinis N 

PROVIDER: S-EPMC4007646 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature