TY - JOUR
T1 - Adhesion of calcium oxalate monohydrate crystals to anionic sites on the surface of renal epithelial cells
AU - Lieske, John C.
AU - Leonard, Rebbecca
AU - Swift, Hewson
AU - Gary Toback, F.
PY - 1996
Y1 - 1996
N2 - 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.
AB - 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.
KW - Alcian blue
KW - Ferritin
KW - Lectin
KW - Nephrolithiasis
KW - Neuraminidase
KW - Triticum vulgaris lectin
KW - Wheat germ agglutinin
UR - http://www.scopus.com/inward/record.url?scp=0030047621&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030047621&partnerID=8YFLogxK
U2 - 10.1152/ajprenal.1996.270.1.f192
DO - 10.1152/ajprenal.1996.270.1.f192
M3 - Article
C2 - 8769839
AN - SCOPUS:0030047621
SN - 0002-9513
VL - 270
SP - F192-F199
JO - American Journal of Physiology
JF - American Journal of Physiology
IS - 1 PART 2
ER -