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1.
Sci Total Environ ; 792: 148295, 2021 Oct 20.
Article in English | MEDLINE | ID: mdl-34147804

ABSTRACT

The N2-fixing shrub Amorpha fruticosa L. is rapidly spreading in the dry riparian natural grasslands of Europe, altering ecosystem functions and depleting plant diversity. Alteration of the N cycle represents the key factor involved in invasions by N2-fixing plants with cascading effects on plant species richness. We hypothesized that A. fruticosa encroachment strongly impacts not only the N but also the C cycle and that the magnitude of such alterations may be modulated by soil characteristics. To test these hypotheses, we selected four river floodplains in North East of Italy and compared natural uninvaded grasslands with half invaded and completely invaded sites, based on A. fruticosa stand characteristic and relevant leaf traits and on soil properties related to soil texture and to C and N cycles. Soil organic matter mineralisation, ammonification and nitrification rates were determined. Soil nitrification increased remarkably with plant invasion while ammonification was significantly higher only in half invaded sites. Soil organic matter mineralisation, microbial biomass C sustained per soil organic C unit and nitrification positively correlated with stand age, regardless to the stage of the encroachment. Mineralisation and nitrification increased with soil organic C and total N in uninvaded and completely invaded sites, but decreased in half invaded sites. At the half invasion stage, trends in nitrification and CO2 mineralisation were transitionally reverted and remediation may be facilitated by less pronounced changes in soil properties compared to completely invaded sites. Direct effects of plant invasion are modulated by the action of soil characteristics such as soil organic C and clay contents, with soils rich in organic C showing larger nitrification and mineralisation rates.


Subject(s)
Fabaceae , Soil , Ecosystem , Grassland , Nitrogen/analysis , Soil Microbiology
2.
Plant Biol (Stuttg) ; 20(2): 346-356, 2018 Mar.
Article in English | MEDLINE | ID: mdl-29181866

ABSTRACT

Knowledge on the metabolism of polysaccharide reserves in wild species is still scarce. In natural sites we collected tubers of Arum italicum Mill. and A. maculatum L. - two geophytes with different apparent phenological timing, ecology and chorology - during five stages of the annual cycle in order to understand patterns of reserve accumulation and degradation. Both the entire tuber and its proximal and distal to shoot portion were utilised. Pools of non-structural carbohydrates (glucose, sucrose and starch), glucose-6-phosphate and ATP were analysed as important markers of carbohydrate metabolism. In both species, starch and glucose content of the whole tuber significantly increased from sprouting to the maturation/senescence stages, whereas sucrose showed an opposite trend; ATP and glucose-6-phosphate were almost stable and dropped only at the end of the annual cycle. Considering the two different portions of the tuber, both ATP and glucose-6-phosphate concentrations were higher in proximity to the shoot in all seasonal stages, except the flowering stage. Our findings suggest that seasonal carbon partitioning in the underground organ is driven by phenology and occurs independently of seasonal climate conditions. Moreover, our results show that starch degradation, sustained by elevated ATP and glucose-6-phosphate pools, starts in the peripheral, proximal-to-shoot portion of the tuber, consuming starch accumulated in the previous season, as a 'Last In-First Out' mechanism of carbohydrate storage.


Subject(s)
Adenosine Triphosphate/physiology , Arum/physiology , Carbohydrates/physiology , Glucose-6-Phosphate/physiology , Plant Tubers/physiology , Adenosine Triphosphate/analysis , Arum/chemistry , Carbohydrates/analysis , Glucose/analysis , Glucose/physiology , Glucose-6-Phosphate/analysis , Plant Shoots/chemistry , Plant Shoots/physiology , Plant Tubers/chemistry , Seasons , Starch/analysis , Starch/physiology , Sucrose/analysis , Sucrose/metabolism
3.
J Bioenerg Biomembr ; 33(2): 107-17, 2001 Apr.
Article in English | MEDLINE | ID: mdl-11456216

ABSTRACT

The immunosuppressive drug, cyclosporin A (CsA), induces the generation of a transmembrane electrical potential difference (deltapsi) in deenergized plant mitochondria incubated in sucrose-based media. Build up of deltapsi is prevented by external monovalent cations in the order K+ > Rb+ = Li+ > Na+, or by the protonophore carbonyl cyanide p-trifluoromethoxyphenylhydrazone, which also collapses the deltapsi generated by CsA. Entry of K+ into mitochondria can be monitored as swelling by incubating the organelles in a medium containing KCl to maintain constant osmolarity. This swelling is inhibited by ATP and stimulated by CsA or valinomycin. In addition, in mitochondria energized by succinate, KCl causes a dissipation of deltapsi, with sigmoidal kinetics, which is favored by CsA. Therefore, plant mitochondria appear to possess a K+ selective, voltage-dependent channel, which is opened by CsA, regulated by the redox state, and inhibited by nucleotides. The hypothetical roles of this new K+ATP channel are discussed in relation to its potential involvement in mitochondrial volume regulation, thermogenesis, apoptosis, and/or prevention of reactive oxygen species formation in plants.


Subject(s)
Cyclosporine/pharmacology , Mitochondria/metabolism , Potassium Channels/drug effects , Potassium Channels/metabolism , Energy Metabolism , Ion Transport/drug effects , Membrane Potentials/drug effects , Mitochondria/drug effects , Mitochondria/ultrastructure , Mitochondrial Swelling/drug effects , Oxidation-Reduction , Pisum sativum/metabolism , Pisum sativum/ultrastructure , Potassium/metabolism
4.
FEBS Lett ; 474(1): 53-7, 2000 May 26.
Article in English | MEDLINE | ID: mdl-10828450

ABSTRACT

The roles of mild uncoupling caused by free fatty acids (mediated by plant uncoupling mitochondrial protein (PUMP) and ATP/ADP carrier (AAC)) and non-coupled respiration (alternative oxidase (AO)) on H(2)O(2) formation by plant mitochondria were examined. Both laurate and oleate prevent H(2)O(2) formation dependent on the oxidation of succinate. Conversely, these free fatty acids (FFA) only slightly affect that dependent on malate plus glutamate oxidation. Carboxyatractylate (CAtr), an inhibitor of AAC, completely inhibits oleate- or laurate-stimulated oxygen consumption linked to succinate oxidation, while GDP, an inhibitor of PUMP, caused only a 30% inhibition. In agreement, CAtr completely restores the oleate-inhibited H(2)O(2) formation, while GDP induces only a 30% restoration. Both oleate and laurate cause a mild uncoupling of the electrical potential (generated by succinate), which is then followed by a complete collapse with a sigmoidal kinetic. FFA also inhibit the succinate-dependent reverse electron transfer. Diamide, an inhibitor of AO, favors the malate plus glutamate-dependent H(2)O(2) formation, while pyruvate (a stimulator of AO) inhibits it. These results show that the succinate-dependent H(2)O(2) formation occurs at the level of Complex I by a reverse electron transport. This generation appears to be prevented by mild uncoupling mediated by FFA. The anionic form of FFA appears to be shuttled by AAC rather than PUMP. The malate plus glutamate-dependent H(2)O(2) formation is, conversely, mainly prevented by non-coupled respiration (AO).


Subject(s)
Hydrogen Peroxide/metabolism , Mitochondria/metabolism , Oxygen Consumption , Pisum sativum/ultrastructure , Atractyloside/analogs & derivatives , Atractyloside/pharmacology , Carrier Proteins/metabolism , Glutamic Acid/pharmacology , Guanosine Diphosphate/pharmacology , Ion Channels , Lauric Acids/pharmacology , Malates/pharmacology , Membrane Proteins/metabolism , Mitochondrial ADP, ATP Translocases/antagonists & inhibitors , Mitochondrial ADP, ATP Translocases/metabolism , Mitochondrial Proteins , Oleic Acid/pharmacology , Oxidation-Reduction , Oxidative Phosphorylation , Succinic Acid/metabolism , Succinic Acid/pharmacology , Uncoupling Agents/metabolism , Uncoupling Protein 1
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