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Updated: Jul 19, 2026
Identification of Functional Protein Regions Through Chimeric Protein Construction
Published on: January 8, 2019
Molecular and functional characterization of a soluble form of oncostatin M/interleukin-31 shared receptor
Caroline Diveu1, Emilie Venereau, Josy Froger
1Institut National de la Santé et de la Recherche Médicale, U564, F-49033 Angers, France.
Abstract:
Activation of the signaling transduction pathways mediated by oncostatin M (OSM) requires the binding of the cytokine to either type I OSM receptor (leukemia inhibitory factor receptor/gp130) or to type II OSM receptor (OSMR/gp130). In the present work we have developed an enzyme-linked immunosorbent assay detecting a soluble form of OSMR (sOSMR) secreted by glioblastoma, hepatoma, and melanoma tumor cell lines. sOSMR was also present in sera of healthy individuals, with increased levels in multiple myeloma. Molecular cloning of a corresponding cDNA was carried out, and it encoded for a 70-kDa protein consisting of a half cytokine binding domain containing the canonical WSXWS motif, an immunoglobulin-like domain, and the first half of a second cytokine binding domain with cysteines in fixed positions. Analysis of the soluble receptor distribution revealed a preferential expression in lung, liver, pancreas, and placenta. sOSMR was able to bind OSM and interleukin-31 when associated to soluble gp130 or soluble interleukin-31R, respectively, and to neutralize both cytokine properties. We have also shown that OSM could positively regulate the synthesis of its own soluble receptor in tumor cells.
Insights
Researchers developed a new assay to detect soluble Oncostatin M Receptor (sOSMR), finding it in various cell lines and human sera. This soluble receptor can bind and neutralize OSM and IL-31, with its production potentially regulated by OSM.
Area of Science:
- Biochemistry
- Molecular Biology
- Immunology
Background:
- Oncostatin M (OSM) signaling is crucial for cellular processes and is mediated by specific OSM receptors.
- Understanding the role and detection of soluble receptor forms is important for disease biomarker discovery.
Purpose of the Study:
- To develop a method for detecting soluble Oncostatin M Receptor (sOSMR).
- To characterize the properties and distribution of sOSMR.
- To investigate the functional role of sOSMR in cytokine binding and neutralization.
Main Methods:
- Enzyme-linked immunosorbent assay (ELISA) for sOSMR detection.
- Molecular cloning and protein characterization of sOSMR.
- Analysis of sOSMR expression in various cell lines and human sera.
- Functional assays for cytokine binding and neutralization.
Main Results:
- An ELISA was developed to detect sOSMR secreted by glioblastoma, hepatoma, and melanoma cells.
- sOSMR was found in healthy individuals' sera, with elevated levels in multiple myeloma patients.
- The cloned sOSMR cDNA encoded a 70-kDa protein with specific domain structures.
- sOSMR preferentially expressed in lung, liver, pancreas, and placenta, and could bind and neutralize OSM and IL-31.
- OSM was shown to positively regulate sOSMR synthesis in tumor cells.
Conclusions:
- A novel assay effectively detects soluble Oncostatin M Receptor (sOSMR).
- sOSMR is present in human sera and tissues, with altered levels in certain conditions like multiple myeloma.
- Soluble OSMR exhibits functional activity by binding and neutralizing specific cytokines, suggesting a regulatory role in OSM and IL-31 signaling pathways.
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