Repair activity and crystal adhesion inhibition of polysaccharides with different molecular weights from red algae Porphyra yezoensis against oxalate-induced oxidative damage in renal epithelial cells

2019 ◽  
Vol 10 (7) ◽  
pp. 3851-3867 ◽  
Author(s):  
Xin-Yuan Sun ◽  
Hui Zhang ◽  
Jie Liu ◽  
Jian-Ming Ouyang
Keyword(s):  
Epithelial Cells ◽  
Cell Surface ◽  
Oxidative Damage ◽  
Red Algae ◽  
Porphyra Yezoensis ◽  
Renal Epithelial Cells ◽  
Molecular Weights ◽  
Repair Activity ◽  
Crystal Adhesion ◽  
Adhesion Inhibition

Porphyra yezoensis polysaccharide repaired oxalate-injured renal epithelial cells and decreased COM crystal adhesion on the cell surface.

scholarly journals Protective Effect of Degraded Porphyra yezoensis Polysaccharides on the Oxidative Damage of Renal Epithelial Cells and on the Adhesion and Endocytosis of Nanocalcium Oxalate Crystals

2021 ◽  
Vol 2021 ◽  
pp. 1-15
Author(s):  
Qian-Long Peng ◽  
Chuang-Ye Li ◽  
Yao-Wang Zhao ◽  
Xin-Yuan Sun ◽  
Hong Liu ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Epithelial Cells ◽  
Oxidative Damage ◽  
Protective Effect ◽  
Calcium Oxalate ◽  
Kidney Stone ◽  
Stone Formation ◽  
Porphyra Yezoensis ◽  
Renal Epithelial Cells ◽  
Kidney Stone Formation

The protective effects of Porphyra yezoensis polysaccharides (PYPs) with molecular weights of 576.2 (PYP1), 105.4 (PYP2), 22.47 (PYP3), and 3.89 kDa (PYP4) on the oxidative damage of human kidney proximal tubular epithelial (HK-2) cells and the differences in adherence and endocytosis of HK-2 cells to calcium oxalate monohydrate crystals before and after protection were investigated. Results showed that PYPs can effectively reduce the oxidative damage of oxalic acid to HK-2 cells. Under the preprotection of PYPs, cell viability increased, cell morphology improved, reactive oxygen species levels decreased, mitochondrial membrane potential increased, S phase cell arrest was inhibited, the cell apoptosis rate decreased, phosphatidylserine exposure reduced, the number of crystals adhered to the cell surface reduced, but the ability of cells to endocytose crystals enhanced. The lower the molecular weight, the better the protective effect of PYP. The results in this article indicated that PYPs can reduce the risk of kidney stone formation by protecting renal epithelial cells from oxidative damage and reducing calcium oxalate crystal adhesion, and PYP4 with the lowest molecular weight may be a potential drug for preventing kidney stone formation.

Protective Effects of Degraded Soybean Polysaccharides on Renal Epithelial Cells Exposed to Oxidative Damage

2016 ◽  
Vol 64 (42) ◽  
pp. 7911-7920 ◽  
Author(s):  
Xin-Yuan Sun ◽  
Jian-Ming Ouyang ◽  
Poonam Bhadja ◽  
Qin Gui ◽  
Hua Peng ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Oxidative Damage ◽  
Protective Effects ◽  
Renal Epithelial Cells

scholarly journals Preprotection of Tea Polysaccharides with Different Molecular Weights Can Reduce the Adhesion between Renal Epithelial Cells and Nano-Calcium Oxalate Crystals

2020 ◽  
Vol 2020 ◽  
pp. 1-13
Author(s):  
Yao-Wang Zhao ◽  
Li Liu ◽  
Chuang-Ye Li ◽  
Hui Zhang ◽  
Xin-Yuan Sun ◽  
...  
Keyword(s):  
Calcium Oxalate ◽  
Cell Activity ◽  
Calcium Oxalate Monohydrate ◽  
Oxygen Species ◽  
Calcium Oxalate Crystals ◽  
Renal Epithelial Cells ◽  
Molecular Weights ◽  
Before And After ◽  
Tea Polysaccharides ◽  
Crystal Adhesion

Crystal adhesion is an important link in the formation of kidney stones. This study investigated and compared the adhesion differences between nano-calcium oxalate monohydrate (COM) and human renal proximal tubule epithelial (HK-2) cells before and after treatment with tea polysaccharides (TPSs) TPS0, TPS1, TPS2, and TPS3 with molecular weights of 10.88, 8.16, 4.82, and 2.31 kDa, respectively. TPS treatment effectively reduced the damage of COM to HK-2 cells, thereby resulting in increased cell activity, decreased release of lactate dehydrogenase, cell morphology recovery, decreased level of reactive oxygen species, increased mitochondrial membrane potential, increased lysosomal integrity, decreased expression of adhesion molecule osteopontin and eversion of phosphatidylserine, and decreased crystal adhesion. Among the TPSs, TPS2 with moderate molecular weight had the best protective effect on cells and the strongest effect on the inhibition of crystal adhesion. Thus, TPS2 may be a potential anticalculus drug.

Adhesion of calcium oxalate monohydrate crystals to renal epithelial cells is inhibited by specific anions

1995 ◽  
Vol 268 (4) ◽  
pp. F604-F612 ◽  
Author(s):  
J. C. Lieske ◽  
R. Leonard ◽  
F. G. Toback
Keyword(s):  
Epithelial Cells ◽  
Cell Surface ◽  
Calcium Oxalate ◽  
Chondroitin Sulfate ◽  
Kidney Stones ◽  
Calcium Oxalate Monohydrate ◽  
Apical Surface ◽  
Dependent Manner ◽  
Renal Epithelial Cells ◽  
Renal Tubular Cells

Adhesion of urinary crystals to the apical surface of renal tubular cells could be a critical step in the formation of kidney stones. The interaction between renal epithelial cells (BSC-1 line) and the most common crystal in kidney stones, calcium oxalate monohydrate (COM), was studied in a tissue culture model system. COM crystals bound to the cell surface within seconds in a concentration-dependent manner to a far greater extent than did brushite, another calcium-containing crystal found in urine. Adhesion of COM crystals to cells was blocked by the polyanion, heparin. Other glycosaminoglycans including chondroitin sulfate A or B, heparan sulfate, and hyaluronic acid, but not chondroitin sulfate C, prevented binding of COM crystals. Two nonsulfated polyanions, polyglutamic acid and polyaspartic acid, also blocked adherence of COM crystals. Three molecules found in urine, nephrocalcin, uropontin, and citrate, each inhibited binding of COM crystals, whereas Tamm-Horsfall glycoprotein (THP) did not. Prior exposure of crystals but not cells to inhibitory molecules blocked adhesion, suggesting that these agents exert their effect at the crystal surface. Inhibition of crystal binding followed a linear Langmuir adsorption isotherm for each inhibitor identified, suggesting that these molecules bind to a single class of sites on the crystal that are important for adhesion to the cell surface. Inhibition of crystal adhesion by heparin was rapidly overcome by the polycation protamine, suggesting that the glycosaminoglycan regulates cell-crystal interactions in a potentially reversible manner.(ABSTRACT TRUNCATED AT 250 WORDS)

An apical expression signal of the renal type IIc Na+-dependent phosphate cotransporter in renal epithelial cells

2010 ◽  
Vol 299 (1) ◽  
pp. F243-F254 ◽  
Author(s):  
Mikiko Ito ◽  
Aya Sakurai ◽  
Keiji Hayashi ◽  
Akiko Ohi ◽  
Natsumi Kangawa ◽  
...  
Keyword(s):  
Amino Acids ◽  
Epithelial Cells ◽  
Cell Surface ◽  
Cellular Localization ◽  
Mutational Analysis ◽  
Apical Membrane ◽  
Apical Cell ◽  
Terminal Deletion ◽  
Deletion Mutants ◽  
Renal Epithelial Cells

The type IIc Na+-dependent phosphate cotransporter (NaPi-IIc) is specifically targeted to, and expressed on, the apical membrane of renal proximal tubular cells and mediates phosphate transport. In the present study, we investigated the signals that determine apical expression of NaPi-IIc with a focus on the role of the N- and the C-terminal tails of mouse NaPi-IIc in renal epithelial cells [opossum kidney (OK) and Madin-Darby canine kidney cells]. Wild-type NaPi-IIc, the cotransporter NaPi-IIa, as well as several IIa-IIc chimeras and deletion mutants, were fused to enhanced green fluorescent protein (EGFP), and their cellular localization was analyzed in polarized renal epithelial cells by confocal microscopy and by cell-surface biotinylation. Fluorescent EGFP-fused NaPi-IIc transporter proteins are correctly expressed in the apical membrane of OK cells. The apical expression of N-terminal deletion mutants (deletion of N-terminal 25, 50, or 69 amino acids) was not affected by truncation. In contrast, C-terminal deletion mutants (deletion of C-terminal 45, 50, or 62 amino acids) did not have correct apical expression. A more detailed mutational analysis indicated that a domain (amino acids WLHSL) in the cytoplasmic C terminus is required for apical expression of NaPi-IIc in renal epithelial cells. We conclude that targeting of NaPi-IIc to the apical cell surface is regulated by a unique amino acid motif in the cytoplasmic C-terminal domain.

scholarly journals Urinary macromolecular inhibition of crystal adhesion to renal epithelial cells is impaired in male stone formers

2005 ◽  
Vol 68 (4) ◽  
pp. 1784-1792 ◽  
Author(s):  
Vivek Kumar ◽  
Lourdes Peña de la Vega ◽  
Gerard Farell ◽  
John C. Lieske
Keyword(s):  
Epithelial Cells ◽  
Renal Epithelial Cells ◽  
Stone Formers ◽  
Crystal Adhesion

Adhesion of calcium oxalate monohydrate crystals to anionic sites on the surface of renal epithelial cells

1996 ◽  
Vol 270 (1) ◽  
pp. F192-F199 ◽  
Author(s):  
J. C. Lieske ◽  
R. Leonard ◽  
H. Swift ◽  
F. G. Toback
Keyword(s):  
Epithelial Cells ◽  
Cell Surface ◽  
Calcium Oxalate ◽  
Kidney Stones ◽  
Membrane Surface ◽  
Calcium Oxalate Monohydrate ◽  
Apical Surface ◽  
Renal Epithelial Cells ◽  
Renal Tubular Cells

Adhesion of microcrystals to the apical surface of renal tubular cells could be a critical step in the formation of kidney stones. The role of membrane surface charge as a determinant of the interaction between renal epithelial cells (BSC-1 line) and the most common crystal in kidney stones, calcium oxalate monohydrate (COM), was studied in a tissue culture model system. Adhesion of COM crystals to cells was blocked by cationized ferritin. Other cations that bind to cells including cetylpyridinium chloride and polylysine, as well as cationic dyes such as Alcian blue, also inhibited adhesion of COM crystals, but not all polycations shared this effect. Specific lectins including Triticum vulgaris (wheat germ agglutinin) blocked crystal binding to the cells. Furthermore, treatment of cells with neuraminidase inhibited binding of crystals. Therefore, anionic cell surface sialic acid residues appear to function as COM crystal receptors that can be blocked by specific cations or lectins. In vivo, alterations in the structure, function, quantity, or availability of these anionic cell surface molecules could lead to crystal retention and formation of renal calculi.

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