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1.
Life Sci ; 323: 121705, 2023 Jun 15.
Article in English | MEDLINE | ID: mdl-37075943

ABSTRACT

The endoplasmic reticulum (ER) is a dynamic organelle and a reliable performer for precisely folded proteins. To maintain its function and integrity, arrays of sensory and quality control systems enhance protein folding fidelity and resolve the highest error-prone areas. Yet numerous internal and external factors disrupt its homeostasis and trigger ER stress responses. Cells try to reduce the number of misfolded proteins via the UPR mechanism, and ER-related garbage disposals systems like ER-associated degradation (ERAD), ER-lysosome-associated degradation (ERLAD), ER-Associated RNA Silencing (ERAS), extracellular chaperoning, and autophagy systems, which activates and increase the cell survival rate by degrading misfolded proteins, prevent the aggregated proteins and remove the dysfunctional organelles. Throughout life, organisms must confront environmental stress to survive and develop. Communication between the ER & other organelles, signaling events mediated by calcium, reactive oxygen species, and inflammation are linked to diverse stress signaling pathways and regulate cell survival or cell death mechanisms. Unresolved cellular damages can cross the threshold limit of their survival, resulting in cell death or driving for various diseases. The multifaceted ability of unfolded protein response facilitates the therapeutic target and a biomarker for various diseases, helping with early diagnosis and detecting the severity of diseases.


Subject(s)
Endoplasmic Reticulum Stress , Unfolded Protein Response , Endoplasmic Reticulum-Associated Degradation , Endoplasmic Reticulum/metabolism , Molecular Chaperones/metabolism
2.
PLoS One ; 15(12): e0243856, 2020.
Article in English | MEDLINE | ID: mdl-33326483

ABSTRACT

Pollen viability is crucial for wheat breeding programs. The unique potential of the protoplasm of live cells to turn brown due to the synthesis of silver nanoparticles (AgNPs) through rapid photoreduction of Ag+, was exploited for testing wheat pollen viability. Ag+-viability test medium (consisting of 0.5 mM AgNO3 and 300 mM KNO3) incubated with wheat pollen turned brown within 2 min under intense light (~600 µmol photon flux density m-2s-1), but not in dark. The brown medium displayed AgNPs-specific surface plasmon resonance band in its absorption spectrum. Light microscopic studies showed the presence of uniformly stained brown protoplasm in viable pollen incubated with Ag+-viability medium in the presence of light. Investigations with transmission electron microscope coupled with energy dispersive X-ray established the presence of distinct 5-35 nm NPs composed of Ag. Powder X-ray diffraction analysis revealed that AgNPs were crystalline and biphasic composed of Ag0 and Ag2O. Conversely, non-viable pollen and heat-killed pollen did not turn brown on incubation with Ag+-medium in light. We believe that the viable wheat pollen turn brown rapidly by bio-transforming Ag+ to AgNPs through photoreduction. Our findings furnish a novel simplest and rapid method for testing wheat pollen viability.


Subject(s)
Cytoplasm/metabolism , Cytoplasm/radiation effects , Light , Pollen/physiology , Silver/metabolism , Staining and Labeling , Tissue Survival/physiology , Triticum/physiology , Pollen/ultrastructure
3.
Protoplasma ; 257(1): 319-330, 2020 Jan.
Article in English | MEDLINE | ID: mdl-31359225

ABSTRACT

Owing to its essentiality for cellular metabolism, phosphate (PO43-) plays a pivotal role in ecosystem dynamics. Frequent testing of phosphate levels is necessary to monitor ecosystem health. Present investigations were aimed to identify the key factors that are essential for proper quantification of PO43-. Primarily, H+ levels played a critical role in the development of molybdenum blue complex by ammonium molybdate and PO43- with ascorbic acid as a reductant. Molybdenum blue complex formed in the presence of 8 to 12 mmol of H+ in 3 ml reaction mixture remained stable even after 72 h. Of different concentrations of ammonium molybdate and ascorbic acid tested, best molybdenum blue complex was formed when their concentrations were 24.3 and 5.68 µmol, respectively. More or less similar intensity of molybdenum blue complex (due to reduction of phosphomolybdic acid and not molybdic acid) was formed in the presence of H+ at levels ranging from 8 to 10 mmol in 3 ml reaction mixture. Our findings unequivocally demonstrated that (i) the reaction mixture containing 3% ammonium molybdate, 0.1% ascorbic acid and 5 M H2SO4 in the ratio of 1:1:1 is ideal for PO43- quantification; (ii) antimony (Sb) significantly curbs the formation of molybdenum blue under these ideal conditions; (iii) this fine-tuned protocol for PO43- quantification could be extended without any problem for determining the level of PO43- both in plant as well as soil samples; and (iv) Azotobacter possesses potential to enhance levels of total PO43- in leaves and grains and soluble/active PO43- in rhizosphere soils of wheat.


Subject(s)
Ascorbic Acid/pharmacology , Phosphates/metabolism , Reducing Agents/pharmacology , Antimony/metabolism , Azotobacter/metabolism , Hydrogen-Ion Concentration , Molybdenum/metabolism , Reproducibility of Results , Soil/chemistry , Triticum/metabolism
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