| First Author | Elson GC | Year | 1998 |
| Journal | J Immunol | Volume | 161 |
| Issue | 3 | Pages | 1371-9 |
| PubMed ID | 9686600 | Mgi Jnum | J:61516 |
| Mgi Id | MGI:1355114 | Doi | 10.4049/jimmunol.161.3.1371 |
| Citation | Elson GC, et al. (1998) Cytokine-like factor-1, a novel soluble protein, shares homology with members of the cytokine type I receptor family. J Immunol 161(3):1371-9 |
| abstractText | In this report we describe the identification, cloning, and expression pattern of human cytokine-like factor 1 (hCLF-1) and the identification and cloning of its murine homologue. They were identified from expressed sequence tags using amino acid sequences from conserved regions of the cytokine type I receptor family. Human CLF-1 and murine CLF-1 shared 96% amino acid identity and significant homology with many cytokine type I receptors. CLF-1 is a secreted protein, suggesting that it is either a soluble subunit within a cytokine receptor complex, like the soluble form of the IL-6R alpha-chain, or a subunit of a multimeric cytokine, e.g., IL-12 p40. The highest levels of hCLF-1 mRNA were observed in lymph node, spleen, thymus, appendix, placenta, stomach, bone marrow, and fetal lung, with constitutive expression of CLF-1 mRNA detected in a human kidney fibroblastic cell line. In fibroblast primary cell cultures, CLF-1 mRNA was up-regulated by TNF-alpha, IL-6, and IFN-gamma. Western blot analysis of recombinant forms of hCLF-1 showed that the protein has the tendency to form covalently linked di- and tetramers. These results suggest that CLF-1 is a novel soluble cytokine receptor subunit or part of a novel cytokine complex, possibly playing a regulatory role in the immune system and during fetal development. |
