Characterization of interleukin-11 receptor and protein tyrosine phosphorylation induced by interleukin-11 in mouse 3T3-L1 cells.

摘要: In this study, we have characterized the biochemical nature of interleukin (IL)-11 receptors (IL-11R) and determined possible signal transduction pathways mediated by IL-11 in 3T3-L1 mouse preadipocytes. The results show that strongly inhibited lipoprotein lipase activity adipogenesis cells, suppression was controlled at post-transcriptional level. ability to inhibit therefore reflected expression functional IL-11R on cell surface. Scatchard plot analysis according specific binding data revealed existence a single class high affinity with Kd 3.49 x 10(-10) M receptor density 5140 sites/cell cells. Affinity cross-linking studies 125I-IL-11 indicated consists polypeptide chain 151 kDa size. Furthermore, studied role protein tyrosine phosphorylation IL-11R-linked pathways. ligation rapidly transiently stimulated 152-, 94-, 47-, 44-kDa proteins. This effect is for since neutralizing antibody abrogated IL-11-induced phosphorylation, other cytokines such as IL-6 IL-1 alpha did not change pattern These suggest closely linked protein-tyrosine kinase pathway, may be key step initiation IL-11R-mediated transmembrane signaling.