Epitaxial Relationships in Urolithiasis: The Brushite—Whewellite System

1977 ◽  
Vol 52 (2) ◽  
pp. 143-148 ◽  
Author(s):  
J. L. Meyer ◽  
J. H. Bergert ◽  
L. H. Smith

1. Whewellite (calcium oxalate monohydrate) crystals were found to induce epitaxially the heterogeneous nucleation of brushite (calcium monohydrogen phosphate dihydrate) from its metastable supersaturated solution in approximately one-quarter of the time required for spontaneous precipitation in the absence of added nucleating agents. Scanning electron-microscope observation of the crystalline phase showed brushite crystals originating from the whewellite seed crystals. 2. Crystal growth, upon nucleation, proceeded rapidly, and the metastable solutions quickly approached saturation. 3. Brushite crystals also induced the precipitation of calcium oxalate crystals in about one-quarter of the time required for spontaneous precipitation; however, the rate of crystal growth was considerably slower. In support of the chemical data, scanning electron micrographs showed few crystals of calcium oxalate nucleated on the surface of the brushite seed. 4. The results provide some insight into the cause of stones containing calcium oxalate or calcium phosphate (or both), which form in the normally acid environment of human urine.

1987 ◽  
Vol 118 (2) ◽  
pp. 379-386 ◽  
Author(s):  
R.P. Singh ◽  
S.S. Gaur ◽  
D.J. White ◽  
G.H. Nancollas

2021 ◽  
Vol 28 ◽  
Author(s):  
Priyadarshini ◽  
Abhishek Negi ◽  
Chetna Faujdar ◽  
Lokesh Nigam ◽  
Naidu Subbarao

Background: Human serum albumin (HSA) is one of the most abundant proteins in the blood plasma, urine as well as in the organic matrix of renal calculi. Macromolecules present in the urine modulate kidney stone formation either by stimulating or inhibiting crystallization process. Objective: In the present study, effect of HSA protein on the growth of calcium oxalate monohydrate crystal (COM) was investigated. Methods: Crystal growth assay was used to measure oxalate depletion in the crystal seeded solution in the presence of HSA. HSA concentrations exhibiting effect on crystal growth were selected for FTIR and XRD analysis. In silico docking was performed on seven different binding sites of HSA. Results: Albumin is playing dual role in growth of calcium oxalate crystallization. FTIR and XRD studies further revealed HSA exerted strain over crystal thus affecting its structure by interacting with amino acids of its pocket 1. Docking results indicate that out of 7 binding pocket in protein, calcium oxalate interacts with Arg-186 and Lys-190 amino acids of pocket 1. Conclusion: Our study confirms the role of HSA in calcium oxalate crystallization where acidic amino acids arginine and lysine are binding with COM crystals, revealing molecular interaction of macromolecule and crystal in urolithiasis.


1975 ◽  
Vol 49 (5) ◽  
pp. 369-374 ◽  
Author(s):  
J. L. Meyer ◽  
J. H. Bergert ◽  
L. H. Smith

Chemical kinetic data, complemented with scanning electron-microscope observations of the crystalline phase, show that seed crystals of hydroxyapatite have the ability to induce the growth of calcium oxalate monohydrate crystals epitaxially from a metastable supersaturated solution of calcium oxalate. The rate of growth of calcium oxalate crystals is dependent on the surface area of the seed material and follows a second-order rate law. It is suggested that there may be a causal relationship between the occurrence of apatite crystals in the urinary tract and the formation of both ‘pure’ and mixed urinary stones containing calcium oxalate. Under similar experimental conditions, however, seed crystals of calcium oxalate monohydrate appeared unable to induce epitaxially the growth of calcium phosphate crystals from a supersaturated calcium phosphate solution, indicating the absence of an epitaxial relationship between calcium oxalate monohydrate and the initially precipitating calcium phosphate phase(s).


1981 ◽  
Vol 61 (4) ◽  
pp. 487-491 ◽  
Author(s):  
P. G. Werness ◽  
Jan H. Bergert ◽  
Karen E. Lee

1. The crystal growth inhibitory activity of mixtures of known inhibitors and of mixtures of known inhibitors with normal urine was determined in calcium oxalate monohydrate and hydroxyapatite seeded crystal growth systems. 2. The inhibitory activity of the mixtures was compared with the measured activity of the individual components of the mixtures. All mixtures had inhibitory activity equal to the sum of the activities of their components, with the exception of RNA/urine mixtures in the calcium oxalate monohydrate system. 3. RNA/urine mixtures had inhibitory activity toward calcium oxalate monohydrate crystal growth which was less than would be predicted from the activity of the RNA and of the urine which were added. This reduced inhibitory activity was shown to be due probably to hydrolysis of RNA by the ribonuclease activity normally present in urine. 4. The results of these experiments make it possible to determine quantitatively the contribution of various naturally occurring urinary crystal growth inhibitors to the total measured inhibition observed in urine.


2008 ◽  
Vol 294 (2) ◽  
pp. F355-F361 ◽  
Author(s):  
Phulwinder K. Grover ◽  
Lauren A. Thurgood ◽  
David E. Fleming ◽  
Wilhelm van Bronswijk ◽  
Tingting Wang ◽  
...  

We have previously proposed that intracrystalline proteins would increase intracellular proteolytic disruption and dissolution of calcium oxalate (CaOx) crystals. Chauvet MC, Ryall RL. J Struct Biol 151: 12–17, 2005; Fleming DE, van Riessen A, Chauvet MC, Grover PK, Hunter B, van Bronswijk W, Ryall RL. J Bone Miner Res 18: 1282–1291, 2003; Ryall RL, Fleming DE, Doyle IR, Evans NA, Dean CJ, Marshall VR. J Struct Biol 134: 5–14, 2001. The aim of this investigation was to determine the effect of increasing concentrations of intracrystalline protein on the rate of CaOx crystal dissolution in Madin-Darby canine kidney (MDCKII) cells. Crystal matrix extract (CME) was isolated from urinary CaOx monohydrate (COM) crystals. Cold and [14C]oxalate-labeled COM crystals were precipitated from ultrafiltered urine containing 0–5 mg/l CME. Crystal surface area was estimated from scanning electron micrographs, and synchrotron X-ray diffraction was used to determine nonuniform strain and crystallite size. Radiolabeled crystals were added to MDCKII cells and crystal dissolution, expressed as radioactive label released into the medium, was measured. Increasing CME content did not significantly alter crystal surface area. However, nonuniform strain increased and crystallite size decreased in a dose-response manner, both reaching saturation at a CME concentration of 3 mg/ and demonstrating unequivocally the inclusion of increasing quantities of proteins in the crystals. This was confirmed by Western blotting. Crystal dissolution also followed saturation kinetics, increasing proportionally with final CME concentration and reaching a plateau at a concentration of ∼2 mg/l. These findings were complemented by field emission scanning electron microscopy, which showed that crystal degradation also increased relative to CME concentration. Intracrystalline proteins enhance degradation and dissolution of CaOx crystals and thus may constitute a natural defense against urolithiasis. The findings have significant ramifications in biomineral metabolism and pathogenesis of renal stones.


1984 ◽  
Vol 247 (5) ◽  
pp. F765-F772 ◽  
Author(s):  
Y. Nakagawa ◽  
V. Abram ◽  
F. L. Coe

Glycoproteins that slow the growth rate of calcium oxalate monohydrate crystals were purified from rat kidney homogenate and urine by selective heat denaturation (for rat kidney homogenate), DEAE-cellulose column chromatography, and gel permeation column chromatography. Both kidney and urine inhibitors were glycoproteins with an apparent mol wt of 1.4 X 10(4), as determined by high-performance liquid chromatography. They contained gamma-carboxyglutamic acid and a high percentage of aspartic acid and glutamic acid but had few aromatic amino acid residues. Both inhibitors contained fucose, mannose, glucose, galactose, glucosamine, galactosamine, and N-acetylneuraminic acid but no glucuronic acid. Kinetic studies suggest that purified inhibitors bind to calcium oxalate monohydrate seed crystals according to a Langmuir adsorption isotherm with similar dissociation constants of 14 X 10(-8)M for rat urine inhibitor and 8.7 X 10(-8) M for rat kidney inhibitor. The isolation of similar glycoproteins from kidney and urine suggests that urinary crystal growth inhibitor may be produced in the kidneys.


2003 ◽  
Vol 774 ◽  
Author(s):  
Isa O. Benítez ◽  
Rénal Backov ◽  
Saeed R. Khan ◽  
Daniel R. Talham

AbstractThe precipitation of calcium oxalate monohydrate (COM) at phospholipid monolayers has been observed in-situ by Brewster angle microscopy (BAM). A monolayer of 1,2-dipalmitoylsn-glycero-3-phosphocholine (DPPC) compressed to a LC state over a calcium oxalate subphase shows the growth of COM as very bright spots. The identity of COM was confirmed in a transferred film by scanning electron microscopy. BAM can also be used to determine where COM precipitates when the monolayer has two phases at equilibrium. Monolayers of DPPC and 1,2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (DPPG) crystallize COM at phase boundaries. In addition, phase separated binary phospholipid mixtures of DPPC and 1,2-dimiristoyl-sn-glycero-3-phosphocholine (DMPC) have been prepared and monitored by BAM. The crystal growth in this case is confined to domains of DPPC due to its ability to form a liquid condensed phase.


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