Resistance to change in Greek higher education

This thesis is a study of resistance to the changes in Greek higher education that were implemented within the framework of the 1999 Bologna Agreement of the European Union in the period 2007-2008. The changes that occurred were of great significance for Greece’s education system as they introduced important changes in the structure and function of Greek higher education. This thesis argues that the organisational culture that had been created throughout the history of Greek higher education was a powerful factor that provoked resistance to the new policies. Methodologically, the thesis argues that discourse, change and institutional culture are closely tied together, and that this is of crucial importance in creating, modifying, and sustaining change within higher education institutions. The process of resistance is examined through the theoretical framework of Critical Discourse Analysis (CDA) (Fairclough, 1995, 2000, 2001, 2003, 2009; Chouliaraki and Fairclough, 1999), and within this framework by applying the empirical-analytical method of the Discourse Historical Approach (Wodak and Meyer, 2009; Reisigl and Wodak, 2009). The framework and method for the study are also complemented by the discourse theory of Laclau and Mouffe (1985). The narrative of the thesis includes a critical examination of the hegemonic struggles that occurred in the 2007-2008 period, the perceptions and ideologies of the key stakeholders (politicians, university faculty, and student groups), and the ways in which the discourses about Greek higher education have been influenced by social, political, and institutional factors. Finally, the implications of the findings for adding to the existing knowledge about management and change in higher education institutions are discussed

Initial screening results of the compounds in the LOPAC and NINDS chemical libraries using the cystine-induced glutamate release assay.

<p>CCF-STTG-1 cells were seeded and grown to confluence. On Day 3, cells were washed with pre-warmed EBSS and transport initiated upon the addition of cystine (80 μM). Cystine-induced glutamate released over 2h at 37°C, in the presence and absence of inhibitors, was measured directly using glutamate oxidase, horse radish peroxidase and Amplex UltraRed and the rate of change of fluorescence monitored at ex 530, em 590. Results were normalized to totals and blanks and the IC₅₀ values determined as a function of the normalized values.</p

xCT/<i>SLC7A11</i> mRNA and cystine-induced glutamate release activity in various cell lines.

<p>xCT/<i>SLC7A11</i> mRNA and cystine-induced glutamate release activity in various cell lines.</p

Dependence of cystine-induced glutamate release in CCF-STTG-1 cells at 37°C on A. cystine concentration, B. cystine concentration represented via Lineweaver-Burk transformation C. protein concentration (mg/ml) and D. time of incubation.

<p>Unless otherwise specified, CCF-STTG-1 cells were seeded at 0.04 x 10⁶ cells per 96-well, grown to confluence (Day 3), washed with pre-warmed EBSS and transport initiated upon the addition of cystine. Substrate dependence experiments were carried out with 0–400 μM cystine while protein- and time-dependence experiments were carried out with 80 μM cystine. Cells were maintained for 2h at 37°C in an incubator with 5% CO₂. At the end of the incubation period, glutamate release was measured directly using glutamate oxidase (0.04 U/mL), HRP (0.125 U/mL) and Amplex UltraRed (50 μM), in Tris buffer (100 mM, pH 7.4), at ex 530, em 590. Data are an average of 3 independent experiments with 16–24 determinations per experiment.</p

Dose responses of A. sulfasalazine (SAS), B. (<i>S</i>)-4-carboxyphenylglycine ((<i>S</i>)-4CPG) and C. (<i>R</i>)-4-carboxyphenylglycine ((<i>R</i>)-4CPG) using [¹⁴C]-cystine uptake and cystine-induced glutamate release assays in CCF-STTG-1 cells.

<p>Cystine uptake was conducted at 37°C for 15 min using 80μM cystine, and at a specific activity of 5.631 μCi/μmol, in the presence and absence of inhibitors. At the end of the experiment, cells were lysed and the radioactivity in the cells measured using a scintillation counter and normalized to the protein contents. Cystine-induced glutamate released over 2h at 37°C upon the addition of 80 μM cystine, in the presence and absence of inhibitors, was measured directly using glutamate oxidase, horse radish peroxidase and Amplex UltraRed and the rate of change of fluorescence monitored at ex 530, em 590. For both assays, results were normalized to totals and blanks and the IC₅₀ values determined as a function of the normalized values. Data are an average of 2–6 independent experiments.</p

IC₅₀ values (μM) of (<i>S</i>)-, (<i>R</i>)-4CPG, glutamate and sulfasalazine (SAS) in [¹⁴C]-cystine uptake and cystine-induced glutamate release assays using different cell sources of the antiporter and under different buffering conditions.

<p>Cystine uptake and glutamate release assays were carried out within the linear range for both processes; 15 min and 2 h, respectively.</p