Bildung für Nachhaltige Entwicklung: eine lernende Strategie für Österreich. Empfehlungen zu Reformen im Kontext der UNO-Dekade Bildung für Nachhaltige Entwicklung (2005-2014)

Heinrich M, Rauch F, Minsch J, Schmidt E, Vielhaber C. Bildung für Nachhaltige Entwicklung: eine lernende Strategie für Österreich. Empfehlungen zu Reformen im Kontext der UNO-Dekade Bildung für Nachhaltige Entwicklung (2005-2014). Schriftenreihe Bildung & nachhaltige Entwicklung. Vol 4. Münster: Monsenstein und Vannerdat; 2007

„… es läuft viel in Richtung BNE …“ Die Autoren der österreichischen Dekadenstrategie blicken zurück

Heinrich M, Minsch J, Rauch F, Vielhaber C. „… es läuft viel in Richtung BNE …“ Die Autoren der österreichischen Dekadenstrategie blicken zurück. In: Sorgo W, FORUM Umweltbildung im Umweltdachverband, eds. Krisen- und Transformationsszenarios. Frühkindpädagogik, Resilienz & Weltaktionsprogramm . Bildung für nachhaltige Entwicklung : Jahrbuch. Vol 2014. Wien: FORUM Umweltbildung; 2014: 143-151

72161-10 57..62

Abstract: Objectives: To investigate the relationship between an insertion/deletion (4G/5G) polymorphism of the plasminogen activator inhibitor (PAI)-1 gene and childhood patients with a past history of ischemic stroke. Methods: The PAI-1 4G/4G genotype and the coinheritance with lipoprotein (Lp) (a) levels, the factor V (FV) G1691A mutation, the prothrombin (PT) G20210A variant, and the methylenetetrahydrofolate reductase (MTHFR) T677T genotype were studied in 198 Caucasian children with stroke and 951 controls (same age, sex and ethnical distribution). In a randomly selected subgroup of patients/ controls (n=60) PAI-1 activities have been investigated. Results: The distribution of the 4G/5G genotypes was no different in childhood stroke patients and controls, with a 4G allele frequency of 55.8% in patients compared with 53.8% in control subjects (P=0.49). The 4G/4G genotype compared with the remaining genotypes was present in 43 cases and 167 (17.6% vs. 21.7%; OR/CI: 1.30/0.89±1.98; P=0.3). PAI-1 activity was signi®cantly elevated (P<0.001) in the patient group. Conclusions: Data presented here suggest that the 4G/4G genotype is not a major risk factor in the aetiology of childhood ischemic stroke

Purified recombinant human prosaposin forms oligomers that bind procathepsin D and affect its autoactivation

Before delivery to endosomes, portions of proCD (procathepsin D) and proSAP (prosaposin) are assembled into complexes. We demonstrate that such complexes are also present in secretions of cultured cells. To study the formation and properties of the complexes, we purified proCD and proSAP from culture media of Spodoptera frugiperda cells that were infected with baculoviruses bearing the respective cDNAs. The biological activity of proCD was demonstrated by its pH-dependent autoactivation to pseudocathepsin D and that of proSAP was demonstrated by feeding to saposin-deficient cultured cells that corrected the storage of radioactive glycolipids. In gel filtration, proSAP behaved as an oligomer and proCD as a monomer. ProSAP altered the elution of proCD such that the latter was shifted into proSAP-containing fractions. ProSAP did not change the elution of mature cathepsin D. Using surface plasmon resonance and an immobilized biotinylated proCD, binding of proSAP was demonstrated under neutral and weakly acidic conditions. At pH 6.8, specific binding appeared to involve more than one binding site on a proSAP oligomer. The dissociation of the first site was characterized by a K(D1) of 5.8±2.9×10(−8) M(−1) (calculated for the monomer). ProSAP stimulated the autoactivation of proCD and also the activity of pseudocathepsin D. Concomitant with the activation, proSAP behaved as a substrate yielding tri- and disaposins and smaller fragments. Our results demonstrate that proSAP forms oligomers that are capable of binding proCD spontaneously and independent of the mammalian type N-glycosylation but not capable of binding mature cathepsin D. In addition to binding proSAP, proCD behaves as an autoactivable and processing enzyme and its binding partner as an activator and substrate