Authentizität von Milch und Fisch – Erkennung von Bioprodukten im Labor

Die Nachfrage nach Bio-Lebensmitteln ist in Deutschland in den letzten Jahren stetig gestiegen. So erhöhte sich der Absatz von Bio-Trinkmilch in 2007 im Vergleich zum Vorjahr erneut um 34 %. Aufgrund sporadisch resultierender Lieferengpässe bei Bio-Milch aber auch der erheblichen Handelspreisdifferenz – wie z. B. insbesondere bei Bio-Lachs – besteht ein potenzielles Risiko der Falschdeklaration konventioneller Produkte als Bio-Ware. Zum Schutz von Verbrauchern wie auch Erzeugern werden daher Verfahren zur Überprüfung der Kennzeichnung benötigt, die – in Ergänzung der betrieblichen Kontrollen – im Zweifelsfall eine Unterscheidung ökologisch und konventionell erzeugter Lebensmittel auf Ebene des Einzelhandels erlauben

Pressemitteilung des MRI: Bio-Milch – neues Verfahren unterstützt Echtheitsprüfung

Der Absatz von Bio-Trinkmilch ist in den letzten Jahren deutlich gestiegen. Aufgrund der erheblichen Handelspreisdifferenz sowie des begrenzten Rohstoffangebots erhöht der boomende Markt allerdings die Gefahr der Falschdeklaration konventionell erzeugter Milch. Deshalb wurde im Institut für Sicherheit und Qualität bei Milch und Fisch am Standort Kiel des Max Rubner-Instituts an Verfahren zum Nachweis der Echtheit von Bio-Milch gearbeitet. Ein Nachweis¬verfahren, das im Zweifelsfall eine Unterscheidung ökologisch und konventionell erzeugter Milch auf Ebene des Einzelhandels erlaubt, stellt eine sinnvolle Ergänzung der betrieblichen Kontrollen dar und dient gleichermaßen dem Schutz der Verbraucher wie auch der gewissenhaften Erzeuger

Ist die Unterscheidung ökologisch und konventionell erzeugter Milch mittels Nahinfrarotspektroskopie möglich?

The aim of the investigations was to evaluate the ability of NIRS to differentiate between organically and conventionally produced milk. Milk from organic and conventional production systems was analysed for milk fat fatty acid content by gas chromatography, and NIRS calibrations were developed with these reference data by partial least square regression. As a result, a standard error of prediction of 0.099 % for C18:3ω3 and a regression coefficient of 0.9 were obtained. For the prediction of C20:5ω3 the standard error was 0.014 %, and the regression coefficient 0.84. The contents of ω3-fatty acids predicted by NIRS show seasonable differences with a higher level in organic milk samples. The mean value of C18:3ω3 content in organic milk was 0.73 ± 0.16 % and in conventional milk 0.42 ± 0.1%. The mean value of C20:5ω3 content in organic milk was 0.12 ± 0.02 % and in conventional milk 0.08 ± 0.01 %. The results indicated that NIRS had the potential to predict ω3-fatty acids in milk samples and could be used as fast method to monitor the milk production system

Periostin as a Heterofunctional Regulator of Cardiac Development and Disease

Periostin (Postn) is a heterofunctional secreted extracellular matrix (ECM) protein comprised of four fasciclin domains that promotes cellular adhesion and movement, as well as collagen fibrillogenesis. Postn is expressed in unique growth centers during embryonic development where it facilitates epithelial-mesenchymal transition (EMT) of select cell populations undergoing reorganization. In the heart, Postn is expressed in the developing valves, cardiac fibroblasts and in regions of the outflow track. In the adult, Postn expression is specifically induced in areas of tissue injury or areas with ongoing cellular re-organization. In the adult heart Postn is induced in the ventricles following myocardial infarction, pressure overload stimulation, or generalized cardiomyopathy. Here we will review the functional consequences associated with Postn induction in both the developing and adult heart. The majority of data collected to date suggest a common function for Postn in both development and disease as a potent inducible regulator of cellular reorganization and extracellular matrix homeostasis, although some alternate and controversial functions have also been ascribed to Postn, the validity of which will be discussed here

Molecular monitoring of minimal residual disease in two patients with MLL-rearranged acute myeloid leukemia and haploidentical transplantation after relapse

This report describes the clinical courses of two acute myeloid leukemia patients. Both had MLL translocations, the first a t(10;11)(p11.2;q23) with MLL-AF10 and the second a t(11;19)(q23;p13.1) with MLL-ELL fusion. They achieved a clinical remission under conventional chemotherapy but relapsed shortly after end of therapy. Both had a history of invasive mycoses (one had possible pulmonary mycosis, one systemic candidiasis). Because no HLA-identical donor was available, a haploidentical transplantation was performed in both cases. Using a specially designed PCR method for the assessment of minimal residual disease (MRD), based on the quantitative detection of the individual chromosomal breakpoint in the MLL gene, all patients achieved complete and persistent molecular remission after transplantation. The immune reconstitution after transplantation is described in terms of total CD3+/CD4+, CD3+/CD8+, CD19+, and CD16+/CD56+ cell numbers over time. The KIR and HLA genotypes of donors and recipients are reported and the possibility of a KIR-mediated alloreactivity is discussed. This report illustrates that haploidentical transplantation may offer a chance of cure without chronic graft-versus-host disease in situations where no suitable HLA-identical donor is available even in a high-risk setting and shows the value of MRD monitoring in the pre- and posttransplant setting

Nuclear Dbf2-related protein kinases (NDRs) in isolated cardiac myocytes and the myocardium: activation by cellular stresses and by phosphoprotein serine-/threonine-phosphatase inhibitors

The nuclear Dbf2-related protein kinases 1 and 2 (NDR1/2) are closely-related AGC family kinases that are strongly conserved through evolution. In mammals, they are activated inter alia by phosphorylation of an hydrophobic domain threonine-residue [NDR1(Thr-444)/NDR2(Thr-442)] by an extrinsic protein kinase followed by autophosphorylation of a catalytic domain serine-residue [NDR1(Ser-281)/NDR2(Ser-282)]. We examined NDR1/2 expression and regulation in primary cultures of neonatal rat cardiac myocytes and in perfused adult rat hearts. In myocytes, transcripts for NDR2, but not NDR1, were induced by the hypertrophic agonist, endothelin-1. NDR1(Thr-444) and NDR2(Thr-442) were rapidly phosphorylated (maximal in 15-30 min) in myocytes exposed to some phosphoprotein Ser-/Thr-phosphatase 1/2 inhibitors (calyculin A, okadaic acid) and, to a lesser extent, by hyperosmotic shock, low concentrations of H(2)O(2), or chelerythrine. In myocytes adenovirally-transduced to express FLAG-NDR2 (which exhibited a mainly-cytoplasmic localisation), the same agents increased FLAG-NDR2 activity as assessed by in vitro protein kinase assays, indicative of FLAG-NDR2(Ser-282/Thr-442) phosphorylation. Calyculin A-induced phosphorylation of NDR1(Thr-444)/NDR2(Thr-442) and activation of FLAG-NDR2 were inhibited by staurosporine, but not by other protein kinase inhibitors tested. In ex vivo rat hearts, NDR1(Thr-444)/NDR2(Thr-442) were phosphorylated in response to ischaemia-reperfusion or calyculin A. From a pathological viewpoint, we conclude that activities of NDR1 and NDR2 are responsive to cytotoxic stresses in heart preparations and this may represent a previously-unidentified response to myocardial ischaemia in vivo

Thrombospondin-3 augments injury-induced cardiomyopathy by intracellular integrin inhibition and sarcolemmal instability.

Thrombospondins (Thbs) are a family of five secreted matricellular glycoproteins in vertebrates that broadly affect cell-matrix interaction. While Thbs4 is known to protect striated muscle from disease by enhancing sarcolemmal stability through increased integrin and dystroglycan attachment complexes, here we show that Thbs3 antithetically promotes sarcolemmal destabilization by reducing integrin function, augmenting disease-induced decompensation. Deletion of Thbs3 in mice enhances integrin membrane expression and membrane stability, protecting the heart from disease stimuli. Transgene-mediated overexpression of α7β1D integrin in the heart ameliorates the disease predisposing effects of Thbs3 by augmenting sarcolemmal stability. Mechanistically, we show that mutating Thbs3 to contain the conserved RGD integrin binding domain normally found in Thbs4 and Thbs5 now rescues the defective expression of integrins on the sarcolemma. Thus, Thbs proteins mediate the intracellular processing of integrin plasma membrane attachment complexes to regulate the dynamics of cellular remodeling and membrane stability

Mechanisms Underlying Heterogeneous Ca2+ Sparklet Activity in Arterial Smooth Muscle

In arterial smooth muscle, single or small clusters of Ca2+ channels operate in a high probability mode, creating sites of nearly continual Ca2+ influx (called “persistent Ca2+ sparklet” sites). Persistent Ca2+ sparklet activity varies regionally within any given cell. At present, the molecular identity of the Ca2+ channels underlying Ca2+ sparklets and the mechanisms that give rise to their spatial heterogeneity remain unclear. Here, we used total internal reflection fluorescence (TIRF) microscopy to directly investigate these issues. We found that tsA-201 cells expressing L-type Cavα1.2 channels recapitulated the general features of Ca2+ sparklets in cerebral arterial myocytes, including amplitude of quantal event, voltage dependencies, gating modalities, and pharmacology. Furthermore, PKCα activity was required for basal persistent Ca2+ sparklet activity in arterial myocytes and tsA-201 cells. In arterial myocytes, inhibition of protein phosphatase 2A (PP2A) and 2B (PP2B; calcineurin) increased Ca2+ influx by evoking new persistent Ca2+ sparklet sites and by increasing the activity of previously active sites. The actions of PP2A and PP2B inhibition on Ca2+ sparklets required PKC activity, indicating that these phosphatases opposed PKC-mediated phosphorylation. Together, these data unequivocally demonstrate that persistent Ca2+ sparklet activity is a fundamental property of L-type Ca2+ channels when associated with PKC. Our findings support a novel model in which the gating modality of L-type Ca2+ channels vary regionally within a cell depending on the relative activities of nearby PKCα, PP2A, and PP2B