Raising Urinary Citrate Lowers Calcium Oxalate and Calcium Phosphate Crystal Formation in Whole Urine

1983 ◽  
Vol 38 (3) ◽  
pp. 179-181 ◽  
Author(s):  
P.C. Hallson ◽  
G.A. Rose ◽  
S. Sulaiman
Keyword(s):  
Calcium Phosphate ◽  
Calcium Oxalate ◽  
Crystal Formation ◽  
Calcium Phosphate Crystal ◽  
Whole Urine ◽  
Urinary Citrate

XRD study of calcium-phosphate crystal formation on dentine surface

2013 ◽  
Author(s):  
Nadezda O. Bessudnova ◽  
Alexandr Skaptsov ◽  
Sergey B. Venig ◽  
Andrey N. Gribov ◽  
Vsevolod S. Atkin
Keyword(s):  
Calcium Phosphate ◽  
Crystal Formation ◽  
Xrd Study ◽  
Calcium Phosphate Crystal ◽  
Dentine Surface

Studies on the role of calcium phosphate in the process of calcium oxalate crystal formation

2009 ◽  
Vol 37 (4) ◽  
pp. 181-192 ◽  
Author(s):  
Hans-Göran Tiselius ◽  
Bengt Lindbäck ◽  
Anne-Marie Fornander ◽  
Mari-Anne Nilsson
Keyword(s):  
Calcium Phosphate ◽  
Calcium Oxalate ◽  
Crystal Formation ◽  
Calcium Oxalate Crystal

Magnesium Reduces Calcium Oxalate Crystal Formation in Human Whole Urine

1982 ◽  
Vol 62 (1) ◽  
pp. 17-19 ◽  
Author(s):  
P. C. Hallson ◽  
G. A. Rose ◽  
S. Sulaiman
Keyword(s):  
Calcium Oxalate ◽  
Inverse Correlation ◽  
Normal Volunteer ◽  
Urine Samples ◽  
Magnesium Concentration ◽  
Crystal Formation ◽  
Calcium Oxalate Crystal ◽  
Isotopic Methods ◽  
Whole Urine

1. A low urinary magnesium was induced in normal volunteer subjects by giving cellulose phosphate; magnesium was added in vitro to yield urine samples of normal and high magnesium concentrations 2. After rapid evaporation of these urine samples at pH 5.3 to standard osmolality the calcium oxalate crystals were measured by microscopy and isotopic methods 3. There was a clear inverse correlation between magnesium concentration and calcium oxalate crystal formation 4. The case for treating calcium oxalate urolithiasis with magnesium is strengthened.

Renal calcinosis and stone formation in mice lacking osteopontin, Tamm-Horsfall protein, or both

2007 ◽  
Vol 293 (6) ◽  
pp. F1935-F1943 ◽  
Author(s):  
Lan Mo ◽  
Lucy Liaw ◽  
Andrew P. Evan ◽  
Andre J. Sommer ◽  
John C. Lieske ◽  
...  
Keyword(s):  
Calcium Phosphate ◽  
Calcium Oxalate ◽  
Stone Formation ◽  
Calcium Oxalate Monohydrate ◽  
Wild Type ◽  
Mineral Salts ◽  
Calcium Oxalate Crystallization ◽  
Whole Urine ◽  
Normal Urine

Although often supersaturated with mineral salts such as calcium phosphate and calcium oxalate, normal urine possesses an innate ability to keep them from forming harmful crystals. This inhibitory activity has been attributed to the presence of urinary macromolecules, although controversies abound regarding their role, or lack thereof, in preventing renal mineralization. Here, we show that 10% of the mice lacking osteopontin (OPN) and 14.3% of the mice lacking Tamm-Horsfall protein (THP) spontaneously form interstitial deposits of calcium phosphate within the renal papillae, events never seen in wild-type mice. Lack of both proteins causes renal crystallization in 39.3% of the double-null mice. Urinalysis revealed elevated concentrations of urine phosphorus and brushite (calcium phosphate) supersaturation in THP-null and OPN/THP-double null mice, suggesting that impaired phosphorus handling may be linked to interstitial papillary calcinosis in THP- but not in OPN-null mice. In contrast, experimentally induced hyperoxaluria provokes widespread intratubular calcium oxalate crystallization and stone formation in OPN/THP-double null mice, while completely sparing the wild-type controls. Whole urine from OPN-, THP-, or double-null mice all possessed a dramatically reduced ability to inhibit the adhesion of calcium oxalate monohydrate crystals to renal epithelial cells. These data establish OPN and THP as powerful and functionally synergistic inhibitors of calcium phosphate and calcium oxalate crystallization in vivo and suggest that defects in either molecule may contribute to renal calcinosis and stone formation, an exceedingly common condition that afflicts up to 12% males and 5% females.

Stimulation of calcium phosphate crystal formation by implant surfaces with electret properties

2015 ◽  
Vol 15 (4) ◽  
pp. 200-203
Author(s):  
V.V. Starikov ◽  
S.L. Starikova ◽  
A.G. Mamalis ◽  
S.N. Lavrynenko
Keyword(s):  
Calcium Phosphate ◽  
Crystal Formation ◽  
Calcium Phosphate Crystal ◽  
Stimulation Of

In Vitro Effects of Cementum Protein 1 (CEMP1) on Calcium Phosphate Crystal Formation and its Role During the Mineralization Process

2009 ◽  
Vol 1244 ◽  
Author(s):  
Enrique Romo-Arévalo ◽  
Eduardo Villarreal-Ramírez ◽  
Juan L. Chávez-Pacheco ◽  
Cristina Piña-Barba ◽  
M. Aguilar-Franco ◽  
...  
Keyword(s):  
Calcium Phosphate ◽  
Molecular Mechanisms ◽  
Periodontal Regeneration ◽  
Octacalcium Phosphate ◽  
Cellular Adhesion ◽  
Crystal Nucleation ◽  
Crystal Formation ◽  
Calcium Phosphate Crystal ◽  
Hydroxyapatite Crystals

ABSTRACTCementum contains specific molecules that could serve to identify, isolate and characterize the cementoblast lineage and to determine the cellular and molecular mechanisms that regulate the cementogenesis process, since it plays a key role during the periodontal regeneration process. One of these molecules is the human cementum protein 1 (CEMP1); which has a molecular weight of 25,9 kDa. In vitro experiments have shown that CEMP1 promotes cellular adhesion and differentiation. In addition, this protein has been implied in regulating the degree of deposition, composition and morphology of hydroxyapatite crystals formed by putative cementoblast in vitro. Therefore, it is possible that CEMP1 promotes the formation, growth and regulates the morphology of hydroxyapatite crystals in vitro. We have produced a human recombinant CEMP1 (hrCEMP1) in a prokaryotic system. The hrCEMP1 purification was realized using the column NiTA HisPrep FF/16. Assays of calcium phosphate crystal growth were realized by means of capillary counterdiffusion system. Our results demonstrated that hrCEMP1 promotes octacalcium phosphate crystal nucleation and possesses high affinity for hydroxyapatite. We infer that hrCEMP1 plays a key role during the regeneration of mineralized tissues.

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