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1.
Chemosphere ; 286(Pt 2): 131760, 2022 Jan.
Article in English | MEDLINE | ID: mdl-34352536

ABSTRACT

Heavy metal ions (HMI) have attracted worldwide concern due to their serious environmental pollution which led to the risk of health conditions. From Red Malus floribunda fruits, nitrogen-doped carbon dots (N-CDs) were prepared, followed by hybrid-spherical shaped hydrogel particles (CGCDs) were prepared. The prepared CGCDs were utilized as adsorbents for HMI-(Hg(II), Cd(II), Pb(II), and Cr(III)) from water. N-CDs with about 4.0 nm in diameter were characterized by various techniques such as field emission-scanning electron microscopy (FE-SEM) and attenuated total reflection-fourier transform infrared spectroscopy (ATR-FTIR) that confirm the presence of nitrogen, oxygen, and carbon functionalities. The prepared spherical CGCDs were characterized very well before it was used as HMI adsorbents. The sizes of the CGCDs were ranges between 20 and 300 µm and the degree of swelling was calculated as 1320 %. ATR-FTIR and X-ray diffraction analyses reveal the presence of N-CDs in CGCDs. Further, FE-SEM confirms the spherical shape morphology of CGCDs. Three different concentrations of HMI solutions were 500 mg/L, 1000 mg/L, and 1500 mg/L. Hg(II) adsorbed proficiently by CGCDs in single metal ion systems with ~72 % and almost complete removal of Hg(II) ions (99 %) in multiple metal ion systems was observed. Moreover, all metal ions Hg(II), Cd(II), Pb(II), and Cr(III) were efficiently (>70 %) removed in multiple systems by CGCDs. After HMI adsorption experiments, the elemental mapping from FE-SEM and X-ray photoelectron spectroscopy studies conveys the presence of HMI on CGCDs. This suggests that CGCDs would be a suitable adsorbent for the simultaneous removal of multiple HMI from wastewater.


Subject(s)
Metals, Heavy , Water Pollutants, Chemical , Adsorption , Carbon , Hydrogels , Ions , Metals, Heavy/analysis , Wastewater , Water Pollutants, Chemical/analysis
2.
Neurol India ; 59(4): 527-31, 2011.
Article in English | MEDLINE | ID: mdl-21891927

ABSTRACT

BACKGROUND: Familial hypokalemic periodic paralysis is an autosomal-dominant disorder characterized by episodic attacks of muscle weakness with hypokalemia. The combination of sarcolemmal depolarization and hypokalemia has been attributed to abnormalities of the potassium conductance governing the membrane potential; however, the molecular mechanism that causes hypokalemia has not yet been determined. AIM: To test the hypothesis that the expression patterns of delayed rectifier potassium channel genes in the skeletal muscle cells of patients with familial hypokalemic periodic paralysis differ from those in normal cells. MATERIAL AND METHODS: We examined both mRNA and protein levels of two major delayed rectifier potassium channel genes KCNQ3 and KCNQ5 in the skeletal muscle cells from three patients with familial hypokalemic periodic paralysis and three healthy controls. RESULTS: When normal cells were exposed to 50 mM potassium buffer, which was used to induce depolarization, the KCNQ3 protein level significantly increased in the membrane fraction but decreased in the cytosolic fraction, whereas the opposite was true in patient cells. CONCLUSION: Abnormal subcellular distribution of the KCNQ3 protein was observed in patient cells. Our results suggest that the altered expression of KCNQ3 in patient cells exposed to high extracellular potassium levels could possibly hinder normal function of the channel protein. These findings may provide an important clue to understanding the molecular mechanism of familial hypokalemic periodic paralysis.


Subject(s)
Gene Expression Regulation/genetics , Hypokalemic Periodic Paralysis/pathology , KCNQ Potassium Channels/metabolism , KCNQ3 Potassium Channel/metabolism , Muscle Fibers, Skeletal/metabolism , Analysis of Variance , Calcium Channels/genetics , Calcium Channels, L-Type , Cells, Cultured , Gene Expression Regulation/drug effects , Humans , Hypokalemic Periodic Paralysis/genetics , KCNQ Potassium Channels/genetics , KCNQ3 Potassium Channel/genetics , Muscle Fibers, Skeletal/drug effects , Mutation/genetics , Potassium/pharmacology , RNA, Messenger/metabolism
3.
Biochem Biophys Res Commun ; 414(1): 49-52, 2011 Oct 14.
Article in English | MEDLINE | ID: mdl-21945436

ABSTRACT

Batten disease (BD) is the most common form of a group of disorders called neuronal ceroid lipofuscinosis, which are caused by a CLN3 gene mutation. A variety of pathogenic lysosomal storage disorder mechanisms have been suggested such as oxidative stress, endoplasmic reticulum (ER) stress, and altered protein trafficking. Resveratrol, a stilbenoid found in red grape skin, is a potent antioxidant chemical. Recent studies have suggested that resveratrol may have a curative effect in many neurodegenerative diseases. Therefore, we investigated the activities of resveratrol at the levels of oxidative and ER stress and apoptosis factors using normal and BD lymphoblast cells. We report that the BD lymphoblast cells contained low-levels of superoxide dismutase-1 (SOD-1) due to the long-term stress of reactive oxygen species. However, when we treated the cells with resveratrol, SOD-1 increased to levels observed in normal cells. Furthermore, we investigated the expression of glucose-regulated protein 78 as an ER stress marker. BD cells underwent ER stress, but resveratrol treatment resolved the ER stress in a dose-dependent manner. We further demonstrated that the levels of apoptosis markers such as apoptosis induce factor, cytochrome c, and cleavage of poly (ADP)-ribose polymerase decreased following resveratrol treatment. Thus, we propose that resveratrol may have beneficial effects in patients with BD.


Subject(s)
Apoptosis/drug effects , Cytoprotection , Neuronal Ceroid-Lipofuscinoses/pathology , Neuroprotective Agents/pharmacology , Oxidative Stress/drug effects , Stilbenes/pharmacology , Biomarkers/metabolism , Cells, Cultured , Down-Regulation/drug effects , Endoplasmic Reticulum/metabolism , Endoplasmic Reticulum Chaperone BiP , Heat-Shock Proteins/antagonists & inhibitors , Heat-Shock Proteins/metabolism , Humans , Neuronal Ceroid-Lipofuscinoses/metabolism , Resveratrol , Superoxide Dismutase/biosynthesis , Superoxide Dismutase-1
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