16 research outputs found

    Environmental heterogeneity affects input, storage, and transformation of coarse particulate organic matter in a floodplain mosaic

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    Quantifying spatial and temporal dynamics of organic matter (OM) is critical both for understanding ecosystem functioning and for predicting impacts of landscape change. To determine the influence of different habitats and coarse particulate OM (CPOM) types upon floodplain OM dynamics, we quantified aerial input, lateral surface transfer, and surface storage of CPOM over an annual cycle on the near-natural floodplain of the River Tagliamento in NE-Italy. Using these data, we modelled floodplain leaf dynamics, taking account of the spatial distribution and hydrologic connectivity of habitats, and using leaf storage as a response variable. Mean aerial CPOM input to the floodplain was similar from riparian forest and islands, but surface transfer was greater from islands, supporting the suggestion that these habitats act as "islands of fertility” along braided rivers. Leaves were the lateral conveyor of energy to more open parts of the floodplain, whereas CPOM was mainly stored as small wood in vegetated islands and riparian forest. Simulating the loss of habitat diversity (islands, ponds) decreased leaf storage on the whole floodplain, on exposed gravel and in large wood accumulations. In contrast, damming (loss of islands, ponds and floods plus floodplain overgrowth) greatly increased storage on exposed gravel. A random shuffle of habitats led to a storage increase on exposed gravel, while that in large wood accumulations and ponds declined. These results disentangle some of the complexities of CPOM dynamics in floodplain ecosystems, illustrate the value of models in understanding ecosystem functioning at a landscape level, and directly inform river management practic

    Volle Feldstärke erreicht

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    The biggest magnet in the world, in Cern near Geneva, has reached at mid-september its field strength: 4 Tesla. (1/2 page

    CPCCOEt, a noncompetitive metabotropic glutamate receptor antagonist, inhibits receptor signaling without affecting glutamate binding. Mol Pharmacol 55:453–461.

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    ABSTRACT Metabotropic glutamate receptors (mGluRs) are a family of G protein-coupled receptors characterized by a large, extracellular N-terminal domain comprising the glutamate-binding site. In the current study, we examined the pharmacological profile and site of action of the non-amino-acid antagonist 7-hydroxyiminocyclopropan[b]chromen-1a-carboxylic acid ethyl ester (CPCCOEt). CPCCOEt selectively inhibited glutamate-induced increases in intracellular calcium at human mGluR1b (hmGluR1b) with an apparent IC 50 of 6.5 M while having no agonist or antagonist activity at hmGluR2, -4a, -5a, -7b, and -8a up to 100 M. Schild analysis indicated that CPCCOEt acts in a noncompetitive manner by decreasing the efficacy of glutamate-stimulated phosphoinositide hydrolysis without affecting the EC 50 value or Hill coefficient of glutamate. Similarly, CPCCOEt did not displace [ 3 H]glutamate binding to membranes prepared from mGluR1a-expressing cells. To elucidate the site of action, we systematically exchanged segments and single amino acids between hmGluR1b and the related subtype, hmGluR5a. Substitution of Thr815 and Ala818, located at the extracellular surface of transmembrane segment VII, with the homologous amino acids of hmGluR5a eliminated CPCCOEt inhibition of hmGluR1b. In contrast, introduction of Thr815 and Ala818 at the homologous positions of hmGluR5a conferred complete inhibition by CPCCOEt (IC 50 Ď­ 6.6 M), i.e., a gain of function. These data suggest that CPCCOEt represents a novel class of G protein-coupled receptor antagonists inhibiting receptor signaling without affecting ligand binding. We propose that the interaction of CPCCOEt with Thr815 and Ala818 of mGluR1 disrupts receptor activation by inhibiting an intramolecular interaction between the agonistbound extracellular domain and the transmembrane domain. Metabotropic glutamate receptors (mGluRs) are coupled to heterotrimeric G proteins, and through this interaction they modulate intracellular concentrations of second messengers and ion channel functions (see reviews b
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