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1.
Physiol Mol Biol Plants ; 28(2): 391-409, 2022 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-35400884

RESUMO

Nanotechnology has become one of the several approaches attempting to ameliorate the severe effect of drought on plant's production and to increase the plants tolerance against water deficit for the water economy. In this research, the effect of foliar application of TiO2, nanoparticles or ordinary TiO2, on Helianthus annuus subjected to different levels of water deficit was studied. Cell membrane injury increased by increasing the level of water deficit and TiO2 concentration, and both types of TiO2 affected the leaves in analogous manner. Ord-TiO2 increased H2O2 generation by 67-240% and lipid peroxidation by 4-67% in leaves. These increases were more than that induced by Nano-TiO2 and the effect was concentration dependent. Proline significantly increased in leaves by water deficit stress, reaching at 25% field capacity (FC) to more than fivefold compared to that in plants grown on full FC. Spraying plants with water significantly decreased the activities of enzymes in the water deficit stressed roots. The water deficit stress exerted the highest magnitude of effect on the changes of cell membrane injury, MDA, proline content, and activities of CAT and GPX. Nano-TiO2 was having the highest effect on contents of H2O2 and GPX activity. In roots, the level of water deficit causes highest effect on enzyme activities, but TiO2 influenced more on the changes of MDA and H2O2 contents. GPX activity increased by 283% in leaves of plants treated with 50 and 150 ppm Nano-TiO2, while increased by 170% in those treated with Ord-TiO2, but APX and CAT activities increased by 17-197%, in average, with Ord-TiO2. This study concluded that Nano-TiO2 didn't ameliorate the effects of drought stress on H. annuus but additively increased the stress, so its use in nano-phytotechnology mustn't be expanded without extensive studies. Supplementary Information: The online version contains supplementary material available at 10.1007/s12298-022-01153-z.

2.
ACS Omega ; 5(9): 4424-4432, 2020 Mar 10.
Artigo em Inglês | MEDLINE | ID: mdl-32175490

RESUMO

A spectrophotometric technique has been applied for studying the reduction of chromium(VI) by poly(ethylene glycol) (PEG) as water-soluble and nontoxic synthetic polymer at a constant ionic strength of 4.0 mol dm-3 in the absence and presence of the ruthenium(III) catalyst. In the absence of the catalyst, the reaction orders in [Cr(VI)] and [PEG] were found to be unity and fractional first orders, respectively. The oxidation process was found to be acid-catalyzed with fractional second order in [H+]. The addition of Ru(III) was found to catalyze the oxidation rates with observation of zero-order reaction in [CrO4 2-] and fractional orders in both [PEG] and [Ru(III)], respectively. The PEG reduces the soluble toxic hexavalent Cr(VI) as a model pollutant to the insoluble nontoxic Cr(III) complex, which is known to be eco-friendly and more safer from the environmental points of view. The acid derivative of PEG was found to possess high affinity for the removal of poisonous heavy metal ions from contaminant matters by chelation. Formation of the 1:1 intermediate complex has been kinetically revealed. A consistent reaction mechanism of oxidation was postulated and discussed.

3.
Carbohydr Polym ; 192: 356-363, 2018 Jul 15.
Artigo em Inglês | MEDLINE | ID: mdl-29691031

RESUMO

Corrosion inhibition of aluminum (Al) in hydrochloric acid by anionic polyelectrolyte chondroitin-4-sulfate (CS) polysaccharide has been studied using both gasometrical and weight-loss techniques. The results drawn from these two techniques are comparable and exhibit negligible differences. The inhibition efficiency was found to increase with increasing the inhibitor concentration and decreased with increasing temperature. The inhibition action of CS on Al metal surface was found to obey both of Langmuir and Freundlich isotherms. The factors affecting the corrosion rates such as the concentration and geometrical structure of the inhibitor, concentration of the corrosive medium, and the temperature were examined. The kinetic parameters were evaluated and a suitable corrosion mechanism consistent with the results obtained is discussed.

4.
J Bone Miner Res ; 33(6): 1166-1182, 2018 06.
Artigo em Inglês | MEDLINE | ID: mdl-29461659

RESUMO

Type I collagen is the most abundant extracellular matrix protein in bone and other connective tissues and plays key roles in normal and pathological bone formation as well as in connective tissue disorders and fibrosis. Although much is known about the collagen biosynthetic pathway and its regulatory steps, the mechanisms by which it is assembled extracellularly are less clear. We have generated GFPtpz and mCherry-tagged collagen fusion constructs for live imaging of type I collagen assembly by replacing the α2(I)-procollagen N-terminal propeptide with GFPtpz or mCherry. These novel imaging probes were stably transfected into MLO-A5 osteoblast-like cells and fibronectin-null mouse embryonic fibroblasts (FN-null-MEFs) and used for imaging type I collagen assembly dynamics and its dependence on fibronectin. Both fusion proteins co-precipitated with α1(I)-collagen and remained intracellular without ascorbate but were assembled into α1(I) collagen-containing extracellular fibrils in the presence of ascorbate. Immunogold-EM confirmed their ultrastuctural localization in banded collagen fibrils. Live cell imaging in stably transfected MLO-A5 cells revealed the highly dynamic nature of collagen assembly and showed that during assembly the fibril networks are continually stretched and contracted due to the underlying cell motion. We also observed that cell-generated forces can physically reshape the collagen fibrils. Using co-cultures of mCherry- and GFPtpz-collagen expressing cells, we show that multiple cells contribute collagen to form collagen fiber bundles. Immuno-EM further showed that individual collagen fibrils can receive contributions of collagen from more than one cell. Live cell imaging in FN-null-MEFs expressing GFPtpz-collagen showed that collagen assembly was both dependent upon and dynamically integrated with fibronectin assembly. These GFP-collagen fusion constructs provide a powerful tool for imaging collagen in living cells and have revealed novel and fundamental insights into the dynamic mechanisms for the extracellular assembly of collagen. © 2018 American Society for Bone and Mineral Research.


Assuntos
Colágeno Tipo I/metabolismo , Proteínas de Fluorescência Verde/metabolismo , Proteínas Luminescentes/metabolismo , Imagem Molecular/métodos , Osteoblastos/metabolismo , Proteínas Recombinantes de Fusão/metabolismo , Animais , Linhagem Celular , Colágeno Tipo I/ultraestrutura , Matriz Extracelular/metabolismo , Fibronectinas/metabolismo , Camundongos , Osteoblastos/ultraestrutura , Imagem com Lapso de Tempo , Proteína Vermelha Fluorescente
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