| First Author | Yang J | Year | 2010 |
| Journal | Immunology | Volume | 131 |
| Issue | 2 | Pages | 174-82 |
| PubMed ID | 20465571 | Mgi Jnum | J:166403 |
| Mgi Id | MGI:4844237 | Doi | 10.1111/j.1365-2567.2010.03286.x |
| Citation | Yang J, et al. (2010) Proviral integration site 2 is required for interleukin-6 expression induced by interleukin-1, tumour necrosis factor-alpha and lipopolysaccharide. Immunology 131(2):174-82 |
| abstractText | PIM (proviral integration site) kinases are a distinct class of serine/threonine-specific kinases consisting of PIM1, PIM2 and PIM3. PIM2 is known to function in apoptosis pathways. Expression of PIM2 is highly induced by pro-inflammatory stimuli but the role of PIM2 in the expression of pro-inflammatory cytokines is unclear. In this study, we showed that over-expression of PIM2 in HeLa cells as well as in human umbilical vein endothelial cells enhanced interleukin-1beta (IL-1beta) -induced and tumour necrosis factor-alpha-induced IL-6 expression, whereas over-expression of a kinase-dead PIM2 mutant had the opposite effect. Studies with small interfering RNA specific to PIM2 further confirmed that IL-6 expression in HeLa cells requires PIM2. To investigate the function of PIM2 further, we generated PIM2-deficient mice. It was found that IL-6 production was significantly decreased from PIM2-deficient spleen cells after stimulation with lipopolysaccharide. Taken together, we demonstrated an important function of PIM2 in controlling the expression of the pro-inflammatory cytokine IL-6. PIM2 inhibitors may be beneficial for IL-6-mediated diseases such as rheumatoid arthritis. |
