Analytical developments in the assay of intra- and extracellular GSH homeostasis: Specific protein S-glutathionylation, cellular GSH and mixed disulphide compartmentalisation and interstitial GSH redox balance

BioFactors ◽  
2003 ◽  
Vol 17 (1-4) ◽  
pp. 269-277 ◽  
Author(s):  
Ian A. Cotgreave
Keyword(s):  
Protein S ◽  
Redox Balance ◽  
Specific Protein

Deep learning based prediction of species-specific protein S-glutathionylation sites

2020 ◽  
Vol 1868 (7) ◽  
pp. 140422 ◽  
Author(s):  
Shihua Li ◽  
Kai Yu ◽  
Dawei Wang ◽  
Qingfeng Zhang ◽  
Ze-Xian Liu ◽  
...  
Keyword(s):  
Deep Learning ◽  
Protein S ◽  
Specific Protein ◽  
Species Specific

scholarly journals First evidence showing that Pepper vein yellows virus P4 protein is a movement protein

2020 ◽  
Author(s):  
Sangsang Li ◽  
Xianyang Su ◽  
Xiangwen Luo ◽  
Yu Zhang ◽  
Deyong Zhang ◽  
...  
Keyword(s):  
Transmembrane Domain ◽  
Movement Protein ◽  
Protein S ◽  
Bioinformatic Analysis ◽  
Plant Viruses ◽  
Specific Protein ◽  
Virus Movement ◽  
Genomic Rnas ◽  
Pepper Vein Yellows Virus ◽  
Substitution Mutant

Abstract Background Plant viruses move through plasmodesmata (PD) to infect new cells. To overcome the PD barrier, plant viruses have developed specific protein(s) to guide their genomic RNAs or DNAs to path through the PD. Results In the present study, we analyzed the function of Pepper vein yellows virus P4 protein. Our bioinformatic analysis showed that the P4 protein contains an transmembrane domain, encompassing the amino acid residue 117-138. The P4 protein was found to target PD and form small punctates near walls. The P4 deletion mutant or the substitution mutant lost their function to produce punctates near the walls inside the fluorescent loci. The P4-YFP fusion was found to move from cell to cell in infiltrated leaves, and P4 could complement Cucumber mosaic virus movement protein deficiency mutant to move between cells. Conclustion Taking together, we consider that the P4 protein is a movement protein of Pepper vein yellows virus.

Effect of albumin on net copper accumulation by fibroblasts and hepatocytes

1990 ◽  
Vol 259 (2) ◽  
pp. G219-G225 ◽  
Author(s):  
G. L. Waldrop ◽  
F. A. Palida ◽  
M. Hadi ◽  
P. A. Lonergan ◽  
M. J. Ettinger
Keyword(s):  
Protein S ◽  
Cell Types ◽  
Specific Protein ◽  
Copper Accumulation ◽  
Copper Binding ◽  
Copper Binding Protein ◽  
Albumin Receptor ◽  
Preferential Uptake ◽  
Free Media ◽  
High Binding Affinity

The liver accumulates copper rapidly and preferentially from plasma. The effects of albumin on net copper accumulation by fibroblasts and hepatocytes were compared to determine whether preferential uptake involves hepatocyte-specific sequestering of copper. Although albumin inhibits the initial rates (30 s) of copper transport by fibroblasts and hepatocytes similarly, the effects of albumin on net copper accumulation (4 h) by these cell types were strikingly different. Fibroblasts accumulate only approximately 15% as much copper when equimolar albumin is present as from albumin-free media; hepatocytes accumulate about the same amount of copper with or without extracellular albumin present. Copper efflux data show that the special capacity of hepatocytes to accumulate copper in the presence of extracellular albumin is due to greater copper retention by hepatocytes than fibroblasts. The ability of hepatocytes to accumulate copper does not seem to be due to albumin-receptor-mediated uptake, since albumin was not co-transported with copper. The data are consistent with an equilibrium model of copper accumulation in which intracellular and extracellular copper are in equilibrium with intracellular and extracellular ligands. A high-affinity, copper-binding fraction that was previously identified in cytosols from hepatocytes was low or absent in fibroblasts. This may contain a liver-specific protein(s) that helps hepatocytes sequester and retain copper from albumin or serum-containing media. Irrespective of the exact species involved, the data are consistent with rapid, preferential copper uptake by the liver being due in part to a liver-specific, intracellular copper-binding protein(s) with a high binding affinity for copper.

ROLE OF SPECIFIC PROTEIN S-THIOLATION UNDER OXIDATIVE STRESS

1991 ◽  
pp. 476-480
Author(s):  
Kazuhito Rokutan ◽  
Keiya Nakamura ◽  
Nobuyuki Marui ◽  
Hiroshi Kutsumi ◽  
Syuji Niki ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Protein S ◽  
Specific Protein
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