leukemia inhibitory factor lif  (R&D Systems)

Journal: Journal of neurochemistry

Article Title: Recapitulation of cell signaling events associated with astrogliosis using the brain slice preparation.

doi: 10.1111/j.1471-4159.2006.04321.x

Figure Lengend Snippet: Fig. 2 Relative mRNA expression levels for various cytokines and chemokines in the striatal slice preparation. Striatal mRNA expression of monocyte chemoattractive protein-1 (MCP-1), leukemia inhibitory factor (LIF), oncostatin M (OSM), interleukin-6 (IL-6), ciliary neuro- trophic factor (CNTF), and glial fibrillary acidic protein (GFAP) was examined by reverse transcriptase-polymerase chain reaction using template specific primers with GAPDH serving as an internal control. Agarose gel analysis shows a band of expected size in each case (LIF 388 bp, MCP-1 303 bp, OSM 266 bp, IL-6 154 bp, CNTF 243 bp, GFAP 462 bp, GAPDH 276 bp). Lanes were loaded with RNA pre- pared from slices as follows: 0 m (frozen immediately), 30, 45, 60, and 75 m post-preparation. Representative gels from at least three inde- pendent experiments are displayed. mRNA expression levels for MCP-1, OSM, and IL-6 at 60 min were significantly increased over 0 min control (p < 0.05–0.01, one-way ANOVA). mRNA expression for LIF at 75 min was significantly increased over 0 min control (p < 0.01; one-way ANOVA). CNTF and GFAP did not differ significantly from 0 min control at any time point. These images were prepared in accordance with the Provisional Guide for Digital images (http:// www.nature.com/nature/authors/submissions/images/index.html).

Article Snippet: Recombinant mouse oncostatin M (OSM), anti-mouse leukemia inhibitory factor (LIF), and antimouse OSM antibody were purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Expressing, Slice Preparation, Reverse Transcription, Polymerase Chain Reaction, Control, Agarose Gel Electrophoresis

Journal: Journal of neurochemistry

Article Title: Recapitulation of cell signaling events associated with astrogliosis using the brain slice preparation.

doi: 10.1111/j.1471-4159.2006.04321.x

Figure Lengend Snippet: Fig. 4 Phosphorylation of STAT3(tyr705) is increased by addition of the gp130 cytokines, leukemia inhibitory factor (LIF) and oncostatin M (OSM), to the striatal slice preparation. These effects are antagonized by addition of neutralizing antibodies directed against these cytokines. Immunoblot analysis of P-STAT3(tyr705) in striatal slices following incubation in buffer alone, 100 lmol/L leukemia inhibitory factor (LIF), 100 lmol/L OSM, or co-incubation with 50 lg a-LIF or 50 lg a-OSM for 45 min. These images were prepared in accordance with the Provisional Guide for Digital images (http://www.nature.com/nature/ authors/submissions/images/index.html).

Article Snippet: Recombinant mouse oncostatin M (OSM), anti-mouse leukemia inhibitory factor (LIF), and antimouse OSM antibody were purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Phospho-proteomics, Slice Preparation, Western Blot, Incubation

Journal: Journal of neurochemistry

Article Title: Recapitulation of cell signaling events associated with astrogliosis using the brain slice preparation.

doi: 10.1111/j.1471-4159.2006.04321.x

Figure Lengend Snippet: Fig. 5 Mechanical damage associated with preparation of striatal brain slices results in recapitulation of cell signaling events associated with astrogliosis. For example, slice-induced or exogenously applied leukemia inhibitory factor (LIF) or oncostatin M (OSM) results in the enhanced phosphorylation of STAT3(tyr705), an event known to be associated with activation of astrocytes. LIF, OSM and other mediat- iors may emanate from the damaged cells, activated microglia or even the astrocyte itself. The effects of LIF and OSM on phosphorylation of STAT3(tyr705) can be blocked by addition of neutralizing antibodies (a- LIF or a-OSM) to the slice.

Article Snippet: Recombinant mouse oncostatin M (OSM), anti-mouse leukemia inhibitory factor (LIF), and antimouse OSM antibody were purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Phospho-proteomics, Activation Assay