Irony Detection in Twitter: The Role of Affective Content

© ACM 2016. This is the author's version of the work. It is posted here for your personal use. Not for redistribution. The definitive Version of Record was published in ACM Transactions on Internet Technology, Vol. 16. http://dx.doi.org/10.1145/2930663.[EN] Irony has been proven to be pervasive in social media, posing a challenge to sentiment analysis systems. It is a creative linguistic phenomenon where affect-related aspects play a key role. In this work, we address the problem of detecting irony in tweets, casting it as a classification problem. We propose a novel model that explores the use of affective features based on a wide range of lexical resources available for English, reflecting different facets of affect. Classification experiments over different corpora show that affective information helps in distinguishing among ironic and nonironic tweets. Our model outperforms the state of the art in almost all cases.The National Council for Science and Technology (CONACyT Mexico) has funded the research work of Delia Irazu Hernandez Farias (Grant No. 218109/313683 CVU-369616). The work of Viviana Patti was partially carried out at the Universitat Politecnica de Valencia within the framework of a fellowship of the University of Turin cofunded by Fondazione CRT (World Wide Style Program 2). The work of Paolo Rosso has been partially funded by the SomEMBED TIN2015-71147-C2-1-P MINECO research project and by the Generalitat Valenciana under the grant ALMAMATER (PrometeoII/2014/030).Hernandez-Farias, DI.; Patti, V.; Rosso, P. (2016). Irony Detection in Twitter: The Role of Affective Content. ACM Transactions on Internet Technology. 16(3):19:1-19:24. https://doi.org/10.1145/2930663S19:119:24163Rob Abbott, Marilyn Walker, Pranav Anand, Jean E. Fox Tree, Robeson Bowmani, and Joseph King. 2011. 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Hepatocyte Growth Factor Increases Osteopontin Expression in Human Osteoblasts through PI3K, Akt, c-Src, and AP-1 Signaling Pathway

BACKGROUND: Hepatocyte growth factor (HGF) has been demonstrated to stimulate osteoblast proliferation and participated bone remodeling. Osteopontin (OPN) is a secreted phosphoglycoprotein that belongs to the SIBLING family and is present during bone mineralization. However, the effects of HGF on OPN expression in human osteoblasts are large unknown. METHODOLOGY/PRINCIPAL FINDINGS: Here we found that HGF induced OPN expression in human osteoblasts dose-dependently. HGF-mediated OPN production was attenuated by c-Met inhibitor and siRNA. Pretreatment of osteoblasts with PI3K inhibitor (Ly294002), Akt inhibitor, c-Src inhibitor (PP2), or AP-1 inhibitor (curcumin) blocked the potentiating action of HGF. Stimulation of osteoblasts with HGF enhanced PI3K, Akt, and c-Src activation. In addition, incubation of cells with HGF also increased c-Jun phosphorylation, AP-1-luciferase activity, and c-Jun binding to the AP-1 element on the OPN promoter. HGF-mediated AP-1-luciferase activity and c-Jun binding to the AP-1 element was reduced by c-Met inhibitor, Ly294002, Akt inhibitor, and PP2. CONCLUSIONS/SIGNIFICANCE: Our results suggest that the interaction between HGF and c-Met increases OPN expression in human osteoblasts via the PI3K, Akt, c-Src, c-Jun, and AP-1 signaling pathway

c-Src is involved in HGF-mediated OPN production in osteoblasts.

<p>Cells were pretreated for 30 min with PP2 or transfected with c-Src mutant and siRNA followed by stimulation with HGF for 24 h. Media and total RNA were collected, and the expression of OPN was analyzed with qPCR and ELISA (n = 5) (A–D). Primary osteoblasts were incubated with HGF for indicated time intervals, and c-Src phosphorylation was examined by Western blotting (E). Primary osteoblasts were incubated with HGF for indicated time intervals, and c-Src kinase activity was examined by c-Src kinase assay kit (F). Primary osteoblasts were pretreated with c-Met inhibitor, Ly294002, and Akt inhibitor for 30 min or transfected with c-Met and Akt siRNA for 24 h followed by stimulation with HGF for 30 min, and c-Src kinase activity was examined by c-Src kinase assay kit (G). *: p<i><</i>0.05 as compared with basal level (F) or HGF-treated group (A-D&G).</p

PI3K is involved in HGF-induced OPN expression.

<p>Cells were pretreated for 30 min with Ly294002 or transfected with p85 mutant and siRNA followed by stimulation with HGF for 24 h. Media and total RNA were collected, and the expression of OPN was analyzed with qPCR and ELISA (n = 4) (A-D). Primary osteoblasts were incubated with HGF for indicated time intervals, and p85 phosphorylation was examined by Western blotting (E). Primary osteoblasts were pretreated with c-Met inhibitor for 30 min or transfected with c-Met siRNA for 24 h followed by stimulation with HGF for 30 min, and p85 phosphorylation was determined by Western blotting (n = 5) (F). *: p<i><</i>0.05 as compared with HGF-treated group.</p

Akt is involved HGF-induced OPN expression.

<p>Cells were pretreated for 30 min with Akt inhibitor or transfected with Akt mutant and siRNA followed by stimulation with HGF for 24 h. Media and total RNA were collected, and the expression of OPN was analyzed with qPCR and ELISA (n = 4) (A–D). Primary osteoblasts were incubated with HGF for indicated time intervals, and Akt phosphorylation was examined by Western blotting (E). Primary osteoblasts cells were pretreated with c-Met inhibitor and Ly294002 for 30 min or transfected with c-Met siRNA for 24 h followed by stimulation with HGF for 30 min, and Akt phosphorylation was determined by Western blotting (F). *: p<i><</i>0.05 as compared with HGF-treated group.</p

The c-Met, PI3K, Akt, and c-Src pathway is involved in HGF-induced AP-1 activation.

<p>(A&B) Primary osteoblasts were transfected with the AP-1-luciferase expression vector and then pretreated with c-Met inhibitor, Ly294002, Akt inhibitor, and PP2 or cotransfected with c-Met and c-Jun siRNA or p85, Akt and c-Src mutant before incubation with HGF for 24 h. Luciferase activity was then assayed (n = 4). *: p<i><</i>0.05 as compared with HGF-treated group. (C) Schematic diagram of the signaling pathways involved in HGF-induced OPN expression in osteoblasts. HGF increases OPN expression by binding to the c-Met receptor and activating PI3K, Akt, and c-Src, which enhances binding of c-Jun to the AP-1 site. This results in the transactivation of OPN expression.</p

HGF increases OPN expression through c-Met receptor.

<p>(A&B) Cells were incubated with HGF for 24 h, and OPN mRNA was examined by qPCR (n = 4). (C-E) Osteoblasts were incubated with HGF for 24 h, and OPN protein was examined by ELISA and Western blotting (n = 4). (F-I) Cells were pretreated for 30 min with c-Met inhibitor or transfected with c-Met siRNA for 24 h followed by stimulation with HGF for 24 h, and OPN expression was examined by qPCR and ELISA (n = 4). *: p<i><</i>0.05 as compared with basal level (A-D) or HGF-treated group (F-I).</p

AP-1 is involved in the potentiation of OPN production by HGF.

<p>Cells were pretreated for 30 min with curcumin or transfected with c-Jun siRNA followed by stimulation with HGF for 24 h. Media and total RNA were collected, and the expression of OPN was analyzed with qPCR and ELISA (n = 5) (A–D). Primary osteoblasts were incubated with HGF for indicated time intervals, and c-Jun phosphorylation was determined by Western blotting (E). Primary osteoblasts were pretreated with c-Met inhibitor, Ly294002, Akt inhibitor, and PP2 or transfected with c-Met and Akt siRNA, and then stimulated with HGF for 120 min. A chromatin immunoprecipitation assay was then performed. The chromatin was immunoprecipitated with anti-c-Jun. One percent of the precipitated chromatin was assayed to verify equal loading (input) (F). MG63 cells were pretreated with c-Met inhibitor, Ly294002, Akt inhibitor, or PP2, and then stimulated with HGF for 120 min, and c-Jun immunofluorescence staining was examined (G). *: p<i><</i>0.05 as compared with HGF-treated group.</p