Identification of osteopontin in human dental calculus matrix

Kido, Jun‐ichi; Kasahara, Chika; Ohishi, Keiji; Nishikawa, Shingo; Ishida, Hiroshi; Yamashita, Kikuji; Kitamura, Seiichiro; Kohri, Kenjiro; Nagata, Toshihiko

doi:10.1016/0003-9969(95)00056-u

Cited by 20 publications

(9 citation statements)

References 22 publications

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“…4) (35)(36)(37)(38)(39)(40)(41)(42). In vitro, osteopontin is a potent inhibitor of hydroxyapatite crystal growth (43), and we recently confirmed that addition of osteopontin also inhibits smooth muscle cell culture calcification.…”

Section: Osteopontin Is a Potent Inhibitor Of Vascular Cell Calcificamentioning

confidence: 75%

Ectopic calcification: new concepts in cellular regulation

Giachelli¹

2001

Zeitschrift f�r Kardiologie

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Section: Osteopontin Is a Potent Inhibitor Of Vascular Cell Calcificamentioning

confidence: 75%

Ectopic calcification: new concepts in cellular regulation

Giachelli¹

2001

Zeitschrift f�r Kardiologie

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“…S was detected also in brain calcinosis along with Na, Mg and K [48]. Osteopontin, which has previously been detected in JDM deposits [8], was found in several other forms of pathological calcification: human pulp stones [49], urinary stones [50], human atherosclerotic lesions [51], and dental calculus [52]. Note that although dental calculus, pulp stones and urinary stones contain osteopontin (a known bone formation protein), they are very different from bone as well.…”

Section: Discussionmentioning

confidence: 99%

Microstructure and mineral composition of dystrophic calcification associated with the idiopathic inflammatory myopathies

et al. 2009

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IntroductionCalcified deposits (CDs) in skin and muscles are common in juvenile dermatomyositis (DM), and less frequent in adult DM. Limited information exists about the microstructure and composition of these deposits, and no information is available on their elemental composition and contents, mineral density (MD) and stiffness. We determined the microstructure, chemical composition, MD and stiffness of CDs obtained from DM patients.MethodsSurgically-removed calcinosis specimens were analyzed with fourier transform infrared microspectroscopy in reflectance mode (FTIR-RM) to map their spatial distribution and composition, and with scanning electron microscopy/silicon drift detector energy dispersive X-ray spectrometry (SEM/SDD-EDS) to obtain elemental maps. X-ray diffraction (XRD) identified their mineral structure, X-ray micro-computed tomography (μCT) mapped their internal structure and 3D distribution, quantitative backscattered electron (qBSE) imaging assessed their morphology and MD, nanoindentation measured their stiffness, and polarized light microscopy (PLM) evaluated the organic matrix composition.ResultsSome specimens were composed of continuous carbonate apatite containing small amounts of proteins with a mineral to protein ratio much higher than in bone, and other specimens contained scattered agglomerates of various sizes with similar composition (FTIR-RM). Continuous or fragmented mineralization was present across the entire specimens (μCT). The apatite was much more crystallized than bone and dentin, and closer to enamel (XRD) and its calcium/phophorous ratios were close to stoichiometric hydroxyapatite (SEM/SDD-EDS). The deposits also contained magnesium and sodium (SEM/SDD-EDS). The MD (qBSE) was closer to enamel than bone and dentin, as was the stiffness (nanoindentation) in the larger dense patches. Large mineralized areas were typically devoid of collagen; however, collagen was noted in some regions within the mineral or margins (PLM). qBSE, FTIR-RM and SEM/SDD-EDS maps suggest that the mineral is deposited first in a fragmented pattern followed by a wave of mineralization that incorporates these particles. Calcinosis masses with shorter duration appeared to have islands of mineralization, whereas longstanding deposits were solidly mineralized.ConclusionsThe properties of the mineral present in the calcinosis masses are closest to that of enamel, while clearly differing from bone. Calcium and phosphate, normally present in affected tissues, may have precipitated as carbonate apatite due to local loss of mineralization inhibitors.

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“…Kohri et al

^{(^{(1)})}

identified OPN as one of the major organic components of kidney stones by cloning and sequencing cDNA encoding urinary stone protein. OPN is a 44‐kDa phosphorylated glycoprotein originally identified in bone

^{(^{(4,5)})}

and has an RGD (arginine‐glycine‐aspartate) amino acid sequence functioning as an adhesion motif of the protein to integrins and CD44.

^{(^{(6,7)})}

OPN contains a series of aspartic acid domain(s) with high affinity to hydroxyapatite.

^{(^{(8)})}

The expression of OPN has been shown not only in physiological but also in pathological calcification, including atherosclerosis, breast cancer, dental calculus, pilomatricomas, and kidney stones.

^{(^{(9–12)})}

Changes in the expression level of OPN during experimental kidney stone formation have been extensively studied in rat models. After 4 wk of ethylene glycol, a precursor of oxalate, administration to rats, a dramatic increase in the expression of OPN protein and mRNA was found in renal epithelial cells, and the resulting kidney crystals also contained OPN.

^{(^{(1,3,13)})}

The results of hyperoxaluric rat models indicated that direct or indirect oxalate stimulus activates OPN expression in the epithelial cells of distal tubules.…”

Section: Introductionmentioning

confidence: 99%

Morphological Conversion of Calcium Oxalate Crystals Into Stones Is Regulated by Osteopontin in Mouse Kidney

Okada

Nomura

Saeki

et al. 2008

Journal of Bone and Mineral Research

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An important process in kidney stone formation is the conversion of retentive crystals in renal tubules to concrete stones. Osteopontin (OPN) is the major component of the kidney calcium-containing stone matrix. In this study, we estimated OPN function in early morphological changes of calcium oxalate crystals using OPN knockout mice: 100 mg/kg glyoxylate was intra-abdominally injected into wildtype mice (WT) and OPN knockout mice (KO) for a week, and 24-h urine oxalate excretion showed no significant difference between WT and KO. Kidney crystal depositions were clearly detected by Pizzolato staining but not by von Kossa staining in both genotypes, and the number of crystals in KO was significantly fewer than in WT. Morphological observation by polarized light optical microphotography and scanning electron microphotography (SEM) showed large flower-shaped crystals growing in renal tubules in WT and small and uniform crystals in KO. X-ray diffraction detected the crystal components as calcium oxalate monohydrate in both genotypes. Immunohistochemical staining of OPN showed that the WT crystals contained OPN protein but not KO crystals. We concluded that OPN plays a crucial role in the morphological conversion of calcium oxalate crystals to stones in mouse kidneys.

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Identification of osteopontin in human dental calculus matrix

Cited by 20 publications

References 22 publications

Ectopic calcification: new concepts in cellular regulation

Ectopic calcification: new concepts in cellular regulation

Microstructure and mineral composition of dystrophic calcification associated with the idiopathic inflammatory myopathies

Morphological Conversion of Calcium Oxalate Crystals Into Stones Is Regulated by Osteopontin in Mouse Kidney

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