CD130, also known as gp130, is a type I transmembrane signaling molecule of 130-140 kDa that is found on cell surfaces usually associated with the specific receptor chains for the following cytokines: IL-6, IL-11, leukemia inhibitory factor (LIF), Oncostatin M, ciliary neurotrophic factor (CNTF) and cardiotrophin-1 (CT-1) (1). The overlap of biological activity of these cytokines is proof of the common role that gp130/CD130 plays in the signaling cascade for these molecules. The extracellular structure of gp130/CD130 is composed of six fibronectin type III modules. A soluble form of gp130/CD130 exists in serum and can act as an antagonist for molecules that interact with gp130/CD130. CD130 has no intrinsic kinase activity, however, it does appear to possess some important biological properties that require its presence during the early stages ontogeny. Mice that have a mutated gp130 gene survive only a few weeks largely due to myocardial malformations (2). The CD130 molecule forms homodimers in the presence of IL-6 and IL-11 receptors (3,4). In contrast, CD130 forms heterodimers when present with LIF R, OSM R, CNTF R and CT-1 R (5). Although CD130 does not appear to directly bind these cytokines (OSM being the only exception), its presence in conjunction with the cytokine specific receptor chain imparts high affinity binding characteristics to the receptors. Most cells express CD130, however, the ligand specific receptors associated with CD130 display a much more restricted cellular expression pattern ultimately determining the cytokine-specific response.
1. Taga, T. and Kishimoto, T. (1997) Ann. Rev. Immnuol. 15:797.
2. Yoshida, K. et al. (1996) Proc. Natl. Acad. Sci. USA 93:407.
3. Marakami, M. et al. (1993) Science 260:1808.
4. Yin, T. et al. (1993) J. Immunol. 151:25550
5. Gearing, D.P. et al. (1992) Science 255:1434.
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