Search

Vor rund zweieinhalb Jahren starteten die Spitzenverbände der Freien Wohlfahrtspflege und die Arbeitsgemeinschaft für Kinder- und Jugendhilfe - AGJ ein Projekt, um Demokratie und Vielfalt in der Kindertagesbetreuung zu stärken. Zum Ende der ersten Förderphase fassen die Beteiligten ihre Erkenntnisse zusammen.

Im Folgenden werde ich in das Thema Demokratiebildung in Kindertageseinrichtungen einfuhren. Dazu werfe ich zunachst einen Blick zuruck auf die Verknupfung von Kindertagesbetreuung und Demokratie, um herauszuarbeiten, welche demokratischen Potentiale der Kita als Institution fur die Betreuung junger Kinder historisch zugeschrieben wurden. Anschliesend werde ich auf das Konzept „Die Kinderstube der Demokratie“ sowie Kritik an diesem Konzept eingehen.

Im empirischen Teil dieser Arbeit stelle ich die Ergebnisse meiner Forschungsarbeit vor. Meine Beobachtungen in der Kita Seitenstrase uber den Zeitraum eines halben Jahres machen deutlich, dass der Morgenkreis, ein bereits bestehendes Ritual, dessen Ablauf Kindern und padagogischen Fachkraften gut bekannt ist, an Donnerstagen zu einer Vollversammlung abgewandelt wurde. Da ich diesen Transformationsprozess uber ein halbes Jahr begleiten konnte, hat sich meine Fragestellung leicht verandert.

Ausgangspunkt der vorliegenden Arbeit ist die Frage nach dem Verhaltnis von Ritualen und Demokratiebildung in Kindertageseinrichtungen. Die Fragestellung war zunachst, wie in Kita-Gremien demokratische Partizipation umgesetzt wird. Im Zuge der Auseinandersetzung mit Theorie und Empirie habe ich das Thema dahingehend verschoben und konkretisiert, wie ein etabliertes Versammlungsritual zu einem Ritual der demokratischen Partizipation von Kindern transformiert wird.

Rituale sind aus dem padagogischen Alltag in Kindertageseinrichtungen nicht wegzudenken. „Kinder brauchen Rituale“ ist eine Alltagsweisheit, die bei einer Internet-Recherche mehr als hunderttausend Treffer bringt. Eltern und Padagog*innen erhalten in Publikationen Anregungen dafur, wie sie „stressfrei durch den Familien-Alltag“ (Graser und Hovermann 2015) kommen oder ihre Kinder „im Alltag mit Ritualen unterstutzen“ (Langlotz und Paulzen 2008) konnen.

The levels of polyamines (PAs), proline (Pro), and γ-aminobutyric acid (GABA) as well as the activity of diamine oxidase (DAO; EC 1.4.3.6) were studied in the roots of 2-day-old lupine (Lupinus luteus L. ‘Juno’) seedlings treated with 200 mM NaCl for 24 h. The effect of adding 1 mM aminoguanidine (AG), an inhibitor of DAO activity, was also analyzed. It was found that in roots of lupine seedlings growing under salt stress, a negative correlation between Pro accumulation and putrescine (Put) content takes place. Pro level increased in roots by about 160% and, at the same time, Put content decreased by about 60%, as a result of ca. twofold increase of DAO activity. The AG added to the seedlings almost totally inhibited the activity of DAO, increased Put accumulation to control level, decreased Pro content by about 25%, and reduced GABA level by about 22%. Addition of 50 mM GABA to the lupine seedlings growing in the presence of AG and NaCl restored Pro content in roots to its level in NaCl-treated plants. In this research, the clear correlation between Put degradation and GABA and Pro accumulation was shown for the first time in the roots of seedlings growing under salt stress. This could be considered as a short-term response of a plant to high salt concentration. Our findings indicate that during intensive Pro accumulation in roots induced by salt stress, the pool of this amino acid is indirectly supported by GABA production as a result of Put degradation.

Mit Blick auf die zunehmend komplexeren Therapien entwickelte die eHealth-Projektgruppe des Universitatsklinikums Dresden ein innovatives computerbasiertes Patientenmanagementsystem MSDS3D im Bereich der Multiplen Sklerose (MS), das multidimensional und interaktiv Daten von Arzt, Schwester und Patienten integriert. Das System kann nicht nur Daten des Patienten erfassen und interpretieren, sondern auch interaktiv Informationen an den Patienten vermitteln. Im Rahmen von MSDS3D konnen die fur die Anwendung komplexer Therapien innerhalb eines definierten klinischen Pfads notwendigen Vor- und Begleituntersuchungen abgebildet werden, wie auch Befragungen der Patienten zu verschiedenen Aspekten ihrer Erkrankung.

The modifying effect of sucrose on glutamate dehydrogenase (GDH) activity and isoenzyme pattern was investigated in isolated embryos of lupine (Lupinus luteus L.), cultured in vitro in a medium with sucrose (+S) or without sucrose (-S) and exposed to cadmium (Cd) and lead (Pb) stress. Sucrose starvation of lupine embryos led to a rapid increase in the specific activity of GDH, immunoreactive beta-polypeptide and it was accompanied by appearance of new cathodal isoforms of enzyme. This suggests that isoenzymes induced in lupine embryos by sucrose starvation combine into GDH hexamers with the predominance of beta-GDH subunits synthetized under GDH1 gene control. The addition of sucrose to the medium caused an opposite effect. Along with upregulation of catabolic activity of GDH by sucrose starvation, activity of proteolytic enzymes was also induced. These data can point to regulatory mechanism implying a sucrose dependent repression of the GDH1 gene according to the mechanism of catabolic repression. Treatment of embryos with Cd(2+) or Pb(2+) resulted in ammonium accumulation in the tissues, accompanied by an increase in anabolic activity of GDH and activity of anodal isoenzymes, in both (+S) and (-S) embryos without new de novo synthesis of alpha subunit proteins. Thus, GDH isoenzyme profiles may reflect the physiological function of GDH, which appears to be an important link of metabolic adaptation in cells, aimed at using carbon sources other than sugar during carbohydrate starvation (catabolic activity of GDH) and protecting plant tissues against ammonium accumulated because of heavy metal stress (anabolic activity of GDH).

In germinating seeds of legumes, amino acids liberated during mobilization of storage proteins are partially used for synthesis of storage proteins of the developing axis, but some of them are respired. The amino acids are catabolized by both glutamate dehydrogenase (GDH) and transaminases. Ammonium is reassimilated by glutamine synthetase (GS) and, through the action of asparagine synthetase (AS), is stored in asparagine (Asn). This review presents the ways in which amino acids are converted into Asn and their regulation, mostly in germinating seeds of yellow lupine, where Asn can make up to 30% of dry matter. The energy balance of the synthesis of Asn from glutamate, the most common amino acid in lupine storage proteins, also shows an adaptation of lupine for oxidation of amino acids in early stages of germination. Regulation of the pathway of Asn synthesis is described with regard to the role of GDH and AS, as well as compartmentation of particular metabolites. The regulatory effect of sugar on major links of the pathway (mobilization of storage proteins, induction of genes and activity of GDH and AS) is discussed with respect to recent genetic and molecular studies. Moreover, the effect of glutamate and phytohormones is presented at various stages of Asn biosynthesis.

The modifying effect of sucrose on GDH activity and isoenzyme pattern in isolated embryos of lupine subjected to treatments with inhibitors of RNA synthesis (transcription inhibitors: actinomycin D and cordycepin) and protein synthesis (cycloheximide and chloramphenicol) was investigated. Sucrose starvation of embryos caused the increase of total activity of GDH(NADH-GDH and NAD-GDH) more than twice. Supply of sucrose to sucrose starved embryos caused a reduction of enzyme activity by 40 %. Electrophoretic analysis showed the presence of ca 17 isoenzymes of glutamate dehydrogenase in embryos grown for 72 h in medium with sucrose, while sucrose starvation increased the number of isoenzymes up to 22 forms. Addition of sucrose to sucrose starved embryos after 24 h of cultivation caused the inhibition of synthesis of new isoenzymes. This down-regulation by sucrose was blocked when sucrose was added together with cycloheximide, CHX, (0.025 mM). Treatment of sucrose fed and sucrose starved embryos with cycloheximide (0.020 mM) inhibited protein synthesis by 58 % and 24 %, respectively. The addition of cycloheximide (0.025 mM) to sucrose starved embryos decreased by 60 % NADH-GDH and by 30 % NAD-GDH activity and reduced the spectrum of isoenzymes. CHX treatment did not lead to a significant reduction of enzyme activity and isoenzyme pattern in sucrose fed embryos. The chloramphenicol (CMP) treatment (1 mM) stimulated the total GDH activity, 2.5 fold and 1.5 fold, in sucrose fed and sucrose starved embryos, respectively. Addition of CMP (10 mM) to the media did not affect GDH activity. Both concentrations of CMP caused no significant changes in the isoenzymatic pattern of enzyme in sucrose starved embryos, but induction of new isoenzymes was observed in sucrose fed embryos treated with CMP. In the case of using RNA synthesis inhibitors only cordycepin inhibited the total GDH activity (by ca 25 %) but neither actinomycin D or cordycepin caused any changes in isoenzyme pattern of GDH. The possible mechanism of sugar-mediated regulation of GDH activity is discussed.

Thermal decomposition (TD) of proteins is being investigated as a rapid digestion step for bottom-up proteomics. Mass spectrometry (MS) analyses of the TD products of simple peptides and intact proteins have revealed several nonvolatile products at masses lower than the precursor biomolecule (M). In addition to products stemming from site-specific cleavages, many signals are also observed at a corresponding M-18, most likely because of dehydration (M-H2O) during the heating process. Understanding the structural nature of the water loss product is important in establishing the utility of their tandem mass spectra (collision-induced dissociation) in determining the precursor ion amino acid sequence in a bottom-up proteomic workflow. Dehydration of a peptide can take place from a variety of sources including side chain groups, C-terminus, and/or intramolecular cyclization (C to N-terminus cyclization). In this work, liquid chromatography-tandem MS (LC-MS/MS) and a series of standard peptides (angiotensin II, DRVYIHPF and its cyclic analog) are implemented to decipher the structure of the TD dehydration product. In addition, a derivatization strategy incorporating N-terminus acetylation was developed that allowed the direct comparison of tandem mass spectra of standard cyclic peptides with those resulting from the TD process, thus eliminating any ambiguity from the direct comparison of their mass spectra (due to gas-phase cyclization of b-ions, which can result in sequence scrambling of the precursor ion). Results from these investigations indicated that peptide dehydrated TD products were mostly linear in nature, and water loss was favored from the C-terminus carboxyl group or, when present, the aspartic acid side chain. Given the predictable nature of the formation of TD dehydration products, their MS/MS analysis can be of utility in providing complementary and confirmatory sequence information of the precursor peptide.

4-trans-(N,N-dimethylamino)cinnamaldehyde (DACA) is a chromophoric and fluorogenic substrate of aldehyde dehydrogenase. Fluorescence of DACA is enhanced by binding to aldehyde dehydrogenase in the absence of catalysis both in the presence and absence of the coenzyme analogue 5'AMP. DACA binds to aldehyde dehydrogenase with a dissociation constant of 1-3 microM and stoichiometry of 2 mol mol(-1) enzyme. Incorporation of DACA during catalysis was also investigated and found to be 2 mol DACA mol(-1) enzyme. Effect of pH on the stoichiometry of DACA incorporation during catalysis has shown that DACA incorporation remained constant at 2 mol DACA mol(-1) enzyme, despite a 74-fold velocity enhancement between pH 5.0 and 9.0. Increase of pH increased decomposition of enzyme-acyl intermediate without affecting the rate-limiting step of the reaction. At pH 7.0 the pH stimulated velocity enhancement was 10-fold over that at pH 5.0; further velocity enhancement (11.5-fold that of pH 7.0) was achieved by 150 microM Mg(2+) ions. The velocity at pH 7.0 with Mg(2+) exceeded that of pH 9.0, and that at maximal pH stimulation at pH 9.5. It was observed that level of intermediate decreased to about 1 mol mol(-1) enzyme, indicating that Mg(2+) ions increased the rate of decomposition of the enzyme-acyl intermediate and shifted the rate-limiting step of the reaction to another step in the reaction sequence.

Embryos of pea (Pisum sativum L. cv Sol) deprived of cotyledons were cultured for 3 days in medium with or without sucrose. Respiratory activity of embryos (intact) as well as the ability to oxidize glutamate by mitochondria isolated from embryos were studied. Respiration of intact embryos grown in sucrose supplemented medium was more intensive than in the starved ones. Transfer of the starved embryos to the sucrose-containing medium induced the increase in the intensity of O2 consumption. Mitochondria isolated from both starved and control embryos exhibited respiratory control. Mitochondria isolated from embryos cultured in the absence of sucrose showed higher (about 60 %) ability to oxidize glutamate and α-ketoglutarate than mitochondria from embryos grown in sucrose containing medium. The absence of sucrose in the medium led to a rapid increase in the specific activity of glutamate dehydrogenase (NADH-GDH and NAD-GDH) and it was accompanied by changes in izoenzymatic pattern of enzyme. These results suggest that in the conditions of sucrose starvation glutamate dehydrogenase may be responsible for the increase of glutamate oxidation by mitochondria of pea embryos. Electrophoretic separation of glutamate dehydrogenase isolated from embryos cultured in medium without sucrose showed the presence of ca. 17 isoenzymes while in non-starved embryos only 7 isoenzymes were identified. However, the addition of sucrose to starved embryos after 24 hours of cultivation led to a decrease in glutamate dehydrogenase activity (up to 40 %) but it did not cause the changes in isoenzymatic pattern. These results suggest that in the conditions of sucrose starvation glutamate dehydrogenase maybe responsible for the increase of glutamate oxidation by mitochondria of pea embryos. The posibility of glutamate dehydrogenase regulation by sucrose is discussed.

The rate of phosphoenolpyruvate carboxylation by extracts from germinating lupin seeds was measured through the H14CO3 fixation. PEP carboxylation in seed axes increased during their imbibition, mainly as a result of the increase in the activity of PEP carboxylase [EC 4.1.1.31]. However, the activity of PEP carboxykinase [EC 4.1.1.38], present during the first 3 hours of imbibition, as well as the activity of PEP-carboxykinase [EC 4.1.1.49], after 24 hours of imbibition, have also been shown. Possible physiological role of the changes in the activity of PEP carboxylases during lupin seeds germination is discussed.

Glutamate dehydrogenase (GDH, EC 1.4.2-4) is present in yellow lupine (Lupinus luteus cv. Juno) in many isoforms. The number and banding pattern of isoenzymes varies with respect to plant organ and developmental stage. To better understand the complex nature of GDH regulation in plants, the levels of GDH transcripts, enzyme activity and isoenzyme patterns in germinating seeds and roots of yellow lupine were examined. The analysis of GDH cDNA sequences in lupine revealed three mRNA types, of which two encoded the β-GDH subunit and one encoded the α-GDH subunit (corresponding to the GDH1(GDH3) and GDH2 genes, respectively). The relative expression of GDH1 and GDH2 genes was analyzed in various lupine organs by using quantitative real-time PCR. Our results indicate that different mRNA types were differently regulated depending on organ type. Although both genes appeared to be ubiquitously expressed in all lupine tissues, the GDH1 transcripts evidently predominated over those of GDH2. Immunochemical analyses confirmed that, during embryo development, varied expression of two GDH subunits takes place. The α-GDH subunit (43kDa) predominated in the early stages of germinating seeds, while the β-GDH subunit (44kDa) was the only GDH polypeptide present in lupine roots. These results firmly support the hypothesis that isoenzyme variability of GDH in yellow lupine is associated with the varied expression of α and β subunits into the complexes of hexameric GDH forms. The presence of several isogenes of GDH in yellow lupine may explain the high number (over 20) of its molecular forms in germinating lupine.

Nitrate esters are used clinically as the smooth muscle relaxants (Needleman, 1975) in the treatment of angina pectoris. Guanine cyclase-mediated relaxation of aortic strips is dependent on the conversion of nitrate esters to nitric oxide by tissue sulfhydryl groups (Needleman and Johnson, 1973).

The incorporation of 14C-aspartate during the imbibition of yellow lupin seeds resulted in the production of 14C-alanine and 14CO2. On the basis of tracer and enzymatic assays, conducted in vitro on the extract obtained from lupin seeds, it is postulated that aspartate can be converted to oxaloacetate, then, by phosphoenolopyruvate and pyruvate to alanine. This pathway can be catalyzed by the following enzymes: aspartate aminotransferase, phosphoenolpyruvate carboxykinase, pyruvate kinase and alanine aminotransferase.