Mineralisation of soft and hard tissues and the stability of biofluids

Journal of Structural Biology

Volumn 185, Issue 3, 2014, Pages 383-396

  Holt, Carl ^a   Lenton, Samuel ^b,c   Nylander, Tommy ^d   Sørensen, Esben S ^e   Teixeira, Susana C M ^b,c  

^a UNIVERSITY OF GLASGOW   (United Kingdom)

^b KEELE UNIVERSITY   (United Kingdom)

^c INSTITUT LAUE LANGEVIN   (France)

^d LUND UNIVERSITY   (Sweden)

^e AARHUS UNIVERSITY   (Denmark)

Author keywords

Biocalcification; Blood serum; Milk; Osteopontin; Saliva; Urine

Indexed keywords

ARTIFICIAL BLOOD; CALCIUM; CALCIUM PHOSPHATE; CASEIN; CASEIN PHOSPHOPEPTIDE; CHLORIDE; CITRIC ACID; MAGNESIUM; OSTEOPONTIN; PHOSPHOPEPTIDE; POTASSIUM; SODIUM; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ARTICLE; BIOMINERALIZATION; BODY FLUID; BREAST MILK; CHEMICAL COMPOSITION; CHEMICAL STRUCTURE; IONIC STRENGTH; LIGHT SCATTERING; NEUTRON SCATTERING; OSMOLALITY; PH; PRECIPITATION; PRIORITY JOURNAL; SALIVA; SERUM; SOLUBILITY; THERMODYNAMICS; URINE;

BIOCALCIFICATION; BLOOD SERUM; MILK; OSTEOPONTIN; SALIVA; URINE;

BODY FLUIDS; CALCIUM PHOSPHATES; HUMANS; OSTEOPONTIN; PEPTIDES;

EID: 84894504806     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2013.11.009     Document Type: Article

References (135)

1. Addadi L., Vidavsky N., Weiner S. Transient precursor amorphous phases in biomineralization. In the footsteps of Heinz A. Lowenstam. Z. Kristallogr. 2012, 227:711-717.
2. Aoki T., Umeda T., Kako Y. The least number of phosphate groups for cross-linking of casein by colloidal calcium phosphate. J. Dairy Sci. 1992, 75:971-975.
3. Ashby R., Györy A.Z. A thermodynamic equilibrium model for calcium salt urolithiasis: clinical application. Exp. Nephrol. 1997, 5:246-252.
4. Ashby R.A., Byrne J.P., Györy A.Z. Urine is a saturated equilibrium and not a metastable supersaturated solution: evidence from crystalluria and the general composition of calcium salt and uric acid calculi. Urol. Res. 1999, 27:297-305.
5. Asplin J.R., Arsenault D., Parks J.H., Coe F.L., Hoyer J.R. Contribution of human uropontin to inhibition of calcium oxalate crystallization. Kidney Int. 1998, 53:194-199.
6. Baht G.S., Hunter G.K., Goldberg H.A. Bone sialoprotein-collagen interaction promotes hydroxyapatite nucleation. Matrix Biol. 2008, 27:600-608.
7. Barros N.M.T., Hoac B., Neves R.L., Addison W.N., Assis D.M., Murshed M., Carmona A.K., McKee M.D. Proteolytic processing of osteopontin by PHEX and accumulation of osteopontin fragments in Hyp mouse bone, the murine model of X-linked hypophosphatemia. J. Bone Miner. Res. 2013, 28:688-699.
8. Bautista D.S., Denstedt J., Chambers A.F., Harris J.F. Low-molecular-weight variants of osteopontin generated by serine proteinases in urine of patients with kidney stones. J. Cell. Biochem. 1996, 61:402-409.
9. Beniash E., Metzler R.A., Lam R.S.K., Gilbert P.U.P.A. Transient amorphous calcium phosphate in forming enamel. J. Struct. Biol. 2009, 166:133-143.
10. Berthon G. Critical evalution of the stability-constants of metal-complexes of amino-acids with polar side-chains. Pure Appl. Chem. 1995, 67:1117-1240.
11. Bisaz S., Felix R., Neuman W.F., Fleisch H. Quantitative-determination of inhibitors of calcium-phosphate precipitation in whole urine. Miner. Electrolyte Metab. 1978, 1:74-83.
12. Boskey A.L., Christensen B., Taleb H., Sørensen E.S. Post-translational modification of osteopontin: effects on in vitro hydroxyapatite formation and growth. Biochem. Biophys. Res. Commun. 2012, 419:333-338.
13. Boskey A.L., Chiang P., Fermanis A., Brown J., Taleb H., David V., Rowe P.S.N. MEPE's diverse effects on mineralization. Calcif. Tissue Int. 2010, 86:42-46.
14. Brown C.M., Ackermann D.K., Purich D.L. EQUIL93 - A tool for experimental and clinical urolithiasis. Urol. Res. 1994, 22:119-126.
15. Christensen B., Schack L., Klaning E., Sørensen E.S. Osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a novel substrate for plasmin and cathepsin D. J. Biol. Chem. 2010, 285:7929-7937.
16. Christoffersen M.R., Christoffersen J., Kibalczyc W. Apparent solubilities of 2 amorphous calcium phosphates and of octacalcium phosphate in the temperature-range 30-42-degrees-C. J. Cryst. Growth 1990, 106:349-354.
17. Clegg R.A., Holt C. An E. coli over-expression system for multiply-phosphorylated proteins and its use in a study of calcium phosphate sequestration by novel recombinant phosphopeptides. Protein Expr. Purif. 2009, 67:23-34.
18. Cross K.J., Huq N.L., Palamara J.E., Perich J.W., Reynolds E.C. Physicochemical characterization of casein phosphopeptide-amorphous calcium phosphate nanocomplexes. J. Biol. Chem. 2005, 280:15362-15369.
19. Dewhurst, C.D., 2008. D33 - a third small-angle neutron scattering instrument at the Institut Laue Langevin. Meas. Sci. Technol. 19: Article Number: 034007.
20. Dewhurst C.D. Modelling of wavelength cut-off filters and polarising mirrors in a neutron guide. Nucl. Instrum. Meth. Phys. Res. Sect. A 2012, 683:16-23.
21. Ellegård K.H., Gammelgård-Larsen C., Sørensen E.S., Fedosov S. Process scale chromatographic isolation, characterization and identification of tryptic bioactive casein phosphopeptides. Int. Dairy J. 1999, 9:639-652.
22. Fedarko, N.S., Jain, A., Karadag, A., Fisher, L.W., 2004. Three small integrin-binding ligand N-linked glycoproteins (SIBLINGs) bind and activate specific matrix metalloproteinases. Faseb J. 18, 734.
23. Fiore C.E., Celotta G., Politi G.G., Di Pino L., Castelli Z., Mangiafico R.A., Signorelli S.S., Pennisi P. Association of high alpha(2)-Heremans-Schmid glycoprotein/fetuin concentration in serum and intima-media thickness in patients with atherosclerotic vascular disease and low bone mass. Atherosclerosis 2007, 195:110-115.
24. Fleisch H. Inhibitors of calcium-phosphate precipitation and their role in biological mineralization. J. Cryst. Growth 1981, 53:120-134.
25. Gal J.Y., Fovet Y., Adib-Yadzi M. About a synthetic saliva for in vitro studies. Talanta 2001, 53:1103-1115.
26. George A., Veis A. Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition. Chem. Rev. 2008, 108:4670-4693.
27. Gericke A., Qin C., Spevak L., Fujimoto Y., Butler W.T., Sørensen E.S., Boskey A.L. Importance of phosphorylation for osteopontin regulation of biomineralization. Calcif. Tissue Int. 2005, 77:45-54.
28. Gericke A., Qin C., Spevak L., Fujimoto Y., Butler W.T., Sorensen E.S., Boskey A.L. Importance of phosphorylation for osteopontin regulation of biomineralization. Calcif. Tissue Int. 2005, 77:45-54.
29. Gericke A., Qin C., Sun Y., Redfern R., Redfern D., Fujimoto Y., Taleb H., Butler W.T., Boskey A.L. Different forms of DMP1 play distinct roles in mineralization. J. Dent. Res. 2010, 89:355-359.
30. Giachelli C.M., Schwartz S.M., Liaw L. Molecular and cellular biology of osteopontin - potential role in cardiovascular-disease. Trends Cardiovasc. Med. 1995, 5:88-95.
31. Glinkina I.V., Durov V.A., Mel'nitchenko G.A. Modelling of electrolyte mixtures with application to chemical equilibria in mixtures - prototypes of blood's plasma and calcification of soft tissues. J. Mol. Liq. 2004, 110:63-67.
32. Gower L.B. Biomimetic model systems for investigating the amorphous precursor pathway and its role in biomineralization. Chem. Rev. 2008, 108:4551-4627.
33. Grassinger J., Haylock D.N., Storan M.J., Haines G.O., Williams B., Whitty G.A., Vinson A.R., Be C.L., Li S., Sørensen E.S., Tam P.P.L., Denhardt D.T., Sheppard D., Choong P.F., Nilsson S.K. Thrombin-cleaved osteopontin regulates hemopoietic stem and progenitor cell functions through interactions with alpha(9)beta(1) and alpha(4)beta(1) integrins. Blood 2009, 114:49-59.
34. Grøn P. Saturation of human saliva with calcium phosphates. Arch. Oral Biol. 1973, 18:1385-1392.
35. Grøn P. State of calcium and inorganic orthophosphate in human saliva. Arch. Oral Biol. 1973, 18:1365-1378.
36. Györy A.Z., Ashby R. Equilibrium versus supersaturated urine hypothesis in calcium salt urolithiasis: a new theoretical and practical approach to a clinical problem. Scanning Microsc. 1999, 13:261-265.
37. Hay D.I. Salivary factors in caries models. Adv. Dent. Res. 1995, 9:239-243.
38. Hay D.I., Moreno E.C., Schlesinger D.H. Phosphoprotein-inhibitors of calcium-phosphate precipitation from salivary secretions. Inorg. Perspect. Biol. Med. 1979, 2:271-285.
39. Hay D.I., Schluckebier S.K., Moreno E.C. Equilibrium dialysis and ultrafiltration studies of calcium and phosphate binding by human salivary proteins - implications for salivary supersaturation with respect to calcium-phosphate salts. Calcif. Tissue Int. 1982, 34:531-538.
40. Hecker A., Quennedey B., Testeniere O., Quennedey A., Graf F., Luquet G. Orchestin, a calcium-binding phosphoprotein, is a matrix component of two successive transitory calcified biomineralizations cyclically elaborated by a terrestrial crustacean. J. Struct. Biol. 2004, 146:310-324.
41. Holt C. Inorganic conctituents of milk 3. The colloidal calcium phosphate of cows' milk. J. Dairy Res. 1982, 49:29-38.
42. Holt C. Swelling of golgi vesicles in mammary secretory-cells and its relation to the yield and quantitative composition of milk. J. Theor. Biol. 1983, 101:247-261.
43. Holt C. Interrelationships of the concentrations of some ionic constituents of human-milk and comparison with cow and goat milk. Comp. Biochem. Physiol. a-Physiol. 1993, 104:35-41.
44. Holt C. The milk salts and their interaction with casein. Advanced Dairy Chemistry 1997, 233-254. Chapman and Hall, London. P.F. Fox (Ed.).
45. Holt C. An equilibrium thermodynamic model of the sequestration of calcium phosphate by casein micelles and its application to the calculation of the partition of salts in milk. Eur. Biophys. J. Biophys. Lett. 2004, 33:421-434.
46. Holt C. Unfolded phosphoproteins enable soft and hard tissues to coexist in the same organism with relative ease. Curr. Opin. Struct. Biol. 2013, 23:420-425.
47. Holt C., Jenness R. Interrelationships of constituents and partition of salts in milk samples from 8 species. Comp. Biochem. Physiol. A-Physiol. 1984, 77:275-282.
48. Holt C., Carver J.A. Darwinian transformation of a scarcely nutritious fluid into milk. J. Evol. Biol. 2012, 25:1253-1263.
49. Holt C., Dalgleish D.G., Jenness R. Inorganic constituents of milk. 2. Calculation of the ion equilibria in milk diffusate and comparison with experiment. Anal. Biochem. 1981, 113:154-163.
50. Holt C., Ormrod I.H.L., Thomas P.C. Inorganic constituents of milk. 5. Ion activity product for calcium-phosphate in diffusates prepared from goats milk. J. Dairy Res. 1994, 61:423-426.
51. Holt C., Wahlgren N.M., Drakenberg T. Ability of a beta-casein phosphopeptide to modulate the precipitation of calcium phosphate by forming amorphous dicalcium phosphate nanoclusters. Biochem. J. 1996, 314:1035-1039.
52. Holt C., Sorensen E.S., Clegg R.A. Role of calcium phosphate nanoclusters in the control of calcification. FEBS J. 2009, 276:2308-2323.
53. Holt C., Timmins P.A., Errington N., Leaver J. A core-shell model of calcium phosphate nanoclusters stabilized by beta-casein phosphopeptides, derived from sedimentation equilibrium and small-angle X-ray and neutron-scattering measurements. Eur. J. Biochem. 1998, 252:73-78.
54. Hunter G.K., Goldberg H.A. Nucleation of hydroxyapatite by bone sialoprotein. Proc Natl Acad Sci USA 1993, 90:8562-8565.
55. Hunter G.K., O'Young J., Grohe B., Karttunen M., Goldberg H.A. The flexible polyelectrolyte hypothesis of protein-biomineral interaction. Langmuir 2010, 26:18639-18646.
56. Ito S., Saito T., Amano K. In vitro apatite induction by osteopontin: interfacial energy for hydroxyapatite nucleation on osteopontin. J Biomed Mater Res A 2004, 69:11-16.
57. Jahnen-Dechent W., Heiss A., Schaefer C., Ketteler M. Fetuin-a regulation of calcified matrix metabolism. Circ. Res. 2011, 108:1494-1509.
58. Jenness R., Holt C. Casein and lactose concentrations in milk of 31 species are negatively correlated. Experientia 1987, 43:1015-1018.
59. Johnsson M.S.A., Nancollas G.H. The role of brushite and octacalcium phosphate in apatite formation. Crit. Rev. Oral Biol. Med. 1992, 3:61-82.
60. Jono S., McKee M.D., Murry C.E., Shioi A., Nishizawa Y., Mori K., Morii H., Giachelli C.M. Phosphate regulation of vascular smooth muscle cell calcification. Circ. Res. 2000, 87:E10-E17.
61. Kavanagh J.P. A critical appraisal of the hypothesis that urine is a saturated equilibrium with respect to stone-forming calcium salts. BJU Int. 2001, 87:589-598.
62. Kawasaki K., Lafont A.-G., Sire J.-Y. The evolution of casein genes from tooth genes before the origin of mammals. Mol. Biol. Evol. 2011, 28:2053-2061.
63. Kokubo T., Kushitani H., Sakka S., Kitsugi T., Yamamuro T. Solutions able to reproduce in vivo surface-structure changes in bioactive glass-ceramic A-W3. J. Biomed. Mater. Res. 1990, 24:721-734.
64. Kroening T.A., Mukerji P., Hards R.G. Analysis of beta-casein and its phosphoforms in human milk. Nutr. Res. 1998, 18:1175-1186.
65. Lange C., Li C., Manjubala I., Wagermaier W., Kuehnisch J., Kolanczyk M., Mundlos S., Knaus P., Fratzl P. Fetal and postnatal mouse bone tissue contains more calcium than is present in hydroxyapatite. J. Struct. Biol. 2011, 176:159-167.
66. Lanteri P., Lombardi G., Colombini A., Grasso D., Banfi G. Stability of osteopontin in plasma and serum. Clin. Chem. Lab. Med. 2012, 50:1979-1984.
67. Larsen M.J., Pearce E.I.F. Saturation of human saliva with respect to calcium salts. Arch. Oral Biol. 2003, 48:317-322.
68. Lau W.L., Festing M.H., Giachelli C.M. Phosphate and vascular calcification: emerging role of the sodium-dependent phosphate co-transporter PiT-1. Thromb. Haemost. 2010, 104:464-470.
69. Lefèvre C.M., Sharp J.A., Nicholas K.R. Evolution of lactation: ancient origin and extreme adaptations of the lactation system. Annu. Rev. Genomics Hum. Genet. 2010, 11:219-238.
70. Linder P.W., Little J.C. Prediction by computer modeling of the precipitation of stone-forming solids from urine. Inorg. Chim. Acta-Bioinorg. Chem. 1986, 123:137-145.
71. Little E.M., Holt C. An equilibrium thermodynamic model of the sequestration of calcium phosphate by casein phosphopeptides. Eur. Biophys. J. Biophys. Lett. 2004, 33:435-447.
72. Lyster R.L.J. Calculation by computer of individual concentrations in a simulated milk salt solution. 2. An extension to the previous model. J. Dairy Res. 1981, 48:85-89.
73. Madapallimattam G., Bennick A. Phosphopeptides derived from human salivary acidic proline-rich proteins- biological activities and concentration in saliva. Biochem. J. 1990, 270:297-304.
74. Mahamid J., Aichmayer B., Shimoni E., Ziblat R., Li C., Siegel S., Paris O., Fratzl P., Weiner S., Addadi L. Mapping amorphous calcium phosphate transformation into crystalline mineral from the cell to the bone in zebrafish fin rays. Proc. Nat. Acad. Sci. USA 2010, 107:6316-6321.
75. Marangella M., Daniele P.G., Ronzani M., Sonego S., Linari F. Urine saturation with calcium salts in normal subjects and idiopathic calcium stone-formers estimated by an improved computer-model system. Urol. Res. 1985, 13:189-193.
76. May P.M., Murray K. JESS, A Joint Expert Speciation System. 2. The thermodynamic database. Talanta 1991, 38:1419-1426.
77. May P.M., Murray K. JESS, A Joint Expert Speciation System. 1. Raison d'etre. Talanta 1991, 38:1409-1417.
78. May P.M., Linder P.W., Williams D.R. Computer simulation of metal-ion equilibria in biofluids-models for low-molecular-weight complex distribution of calcium (II), magnesium (II), manganese (II), iron (III), copper (II), zinc (II) and lead (II) ions in human blood plasma. J. Chem. Soc.-Dalton Trans. 1977, 588-595.
79. Mazzali M., Kipari T., Ophascharoensuk V., Wesson J.A., Johnson R., Hughes J. Osteopontin - a molecule for all seasons. QJM Int. J. Med. 2002, 95:3-13.
80. 2O at 5, 15, 25 and 37°C. J. R. Natl. Bureau Stand. Sect. a-Phys. Chem. 1977, 81:273-281.
81. Mekmene O., Le Graet Y., Gaucheron F. A model for predicting salt equilibria in milk and mineral-enriched milks. Food Chem. 2009, 116:233-239.
82. Mekmene O., Le Graet Y., Gaucheron F. Theoretical model for calculating ionic equilibria in milk as a function of pH: comparison to experiment. J. Agric. Food Chem. 2010, 58:4440-4447.
83. Messana I., Cabras T., Pisano E., Sanna M.T., Olianas A., Manconi B., Pellegrini M., Paludetti G., Scarano E., Fiorita A., Agostino S., Contucci A.M., Calo L., Picciotti P.M., Manni A., Bennick A., Vitali A., Fanali C., Inzitari R., Castagnola M. Trafficking and postsecretory events responsible for the formation of secreted human salivary peptides: a proteomics approach. Mol. Cell. Proteomics 2008, 7:911-926.
84. Meyer J.L., Eanes E.D. Thermodynamic analysis of secondary transition in spontaneous precipitation of calcium-phosphate. Calcif. Tissue Res. 1978, 25:209-216.
85. Min W., Shiraga H., Chalko C., Goldfarb S., Krishna G.G., Hoyer J.R. Quantitative studies of human urinary excretion of uropontin. Kidney Int. 1998, 53:189-193.
86. Nelson L.S., Holt C., Hukins D.W.L. The EXAFSspectra of poorly crystalline calcium phosphate preparations from heated milk. Physica B 1989, 158:103-104.
87. Nishio S., Iseda T., Takeda H., Iwata H., Yokoyama M. Inhibitory effect of calcium phosphate-associated proteins on calcium oxalate crystallization: alpha2-HS-glycoprotein, prothrombin-F1 and osteopontin. BJU Int. 2000, 86:543-548.
88. Nudelman F., Bomans P.H.H., George A., de With G., Sommerdijk N.A.J.M. The role of the amorphous phase on the biomimetic mineralization of collagen. Faraday Discuss. 2012, 159:357-370.
89. Nudelman F., Pieterse K., George A., Bomans P.H.H., Friedrich H., Brylka L.J., Hilbers P.A.J., de With G., Sommerdijk N.A.J.M. The role of collagen in bone apatite formation in the presence of hydroxyapatite nucleation inhibitors. Nat. Mater. 2010, 9:1004-1009.
90. Oftedal O.T. The evolution of milk secretion and its ancient origins. Animal 2012, 6:355-368.
91. Olszta M.J., Cheng X., Jee S.S., Kumar R., Kim Y.-Y., Kaufman M.J., Douglas E.P., Gower L.B. Bone structure and formation: a new perspective. Mater. Sci. Eng. R-Rep. 2007, 58:77-116.
92. Ormrod I.H.L., Holt C., Thomas P.C. The inorganic constituents of milk. 4. Diffusible calcium and magnesium concentrations in goats milk and the effect of starvation. J. Dairy Res. 1982, 49:179-186.
93. Pak C.Y.C., Maalouf N.M., Rodgers K., Poindexter J.R. Comparison of semi-empirical and computer derived methods for estimating urinary saturation of calcium oxalate. J. Urol. 2009, 182:2951-2956.
94. Pak C.Y.C., Adams-Huet B., Poindexter J.R., Pearle M.S., Peterson R.D., Moe O.W. Relative effect of urinary calcium and oxalate on saturation of calcium oxalate. Kidney Int. 2004, 66:2032-2037.
95. Politi L., Chiaraluce R., Consalvi V., Cerulli N., Scandurra R. Oxalate, phosphate and sulfate determination in serum and urine by ion chromatography. Clin. Chim. Acta 1989, 184:155-165.
96. Posner A.S., Betts F. Synthetic amorphous calcium-phosphate and its relation to bone-mineral structure. Acc. Chem. Res. 1975, 8:273-281.
97. Poth A.G., Deeth H.C., Alewood P.F., Holland J.W. Analysis of the human casein phosphoproteome by 2-D electrophoresis and MALDI-TOF/TOF MS reveals new phosphoforms. J. Proteome Res. 2008, 7:5017-5027.
98. Prasad M., Butler W.T., Qin C. Dentin sialophosphoprotein in biomineralization. Connect. Tissue Res. 2010, 51:404-417.
99. Price P.A., Nguyen T.M.T., Williamson M.K. Biochemical characterization of the serum fetuin-mineral complex. J. Biol. Chem. 2003, 278:22153-22160.
100. Ramamoorthy S., Manning P.G. Equilibrium studies of solutions containing A13+, Ca2+ or Cd2+ and cysteine, orthophosphate and a carboxylic-acid. J. Inorg. Nucl. Chem. 1975, 37:363-367.
101. Rice G., Barber A., O'Connor A., Stevens G., Kentish S. A theoretical and experimental analysis of calcium speciation and precipitation in dairy ultrafiltration permeate. Int. Dairy J. 2010, 20:694-706.
102. Robertson W.G., Peacock M., Nordin B.E.C. Activity products in stone-forming and non-stone-forming urine. Clin. Sci. 1968, 34:579-594.
103. Rodgers A., Allie-Hamdulay S., Jackson G. Therapeutic action of citrate in urolithiasis explained by chemical speciation: increase in pH is the determinant factor. Nephrol. Dial. Transplant. 2006, 21:361-369.
104. Rodriguez D.E., Thula T., Toro E.J., Yeh Y.-W., Holt C., Holliday L.S., Gower L.B. Multifunctional role of osteopontin in directing intrafibrillar mineralization of collagen and activation of osteoclasts. Acta Biomaterialia 2013, 10:494-507.
105. Rufenacht H.S., Fleisch H. Measurement of inhibitors of calcium-phosphate precipitation in plasma ultrafiltrate. Am. J. Physiol. 1984, 246:F648-F655.
106. Rykke M., Young A., Rolla G., Devold T., Smistad G. Transmission electron microscopy of human saliva. Colloids Surf., B 1997, 9:257-267.
107. Rykke M., Young A., Devold T., Smistad G., Rolla G. Fractionation of salivary micelle-like structures by gel chromatography. Eur. J. Oral Sci. 1997, 105:495-501.
108. Schipper R.G., Silletti E., Vinyerhoeds M.H. Saliva as research material: biochemical, physicochemlical and practical aspects. Arch. Oral Biol. 2007, 52:1114-1135.
109. Shanahan C.M., Crouthamel M.H., Kapustin A., Giachelli C.M. Arterial calcification in chronic kidney disease: key roles for calcium and phosphate. Circ. Res. 2011, 109:697-711.
110. Sheinfeld J., Finlayson B., Reid F. Ultrafiltration evidence of ion binding by macromolecules in urine. Invest. Urol. 1978, 15:462-464.
111. Silwood C.J.L., Grootveld M., Lynch E. H-1 NMR investigations of the molecular nature of low-molecular-mass calcium ions in biofluids. J. Biol. Inorg. Chem. 2002, 7:46-57.
112. Sørensen E.S., Hojrup P., Petersen T.E. Posttranslational modifications of bovine osteopontin - identification of 28 phosphorylation and 3 O-glycosylation sites. Protein Sci. 1995, 4:2040-2049.
113. Spielman A.I., Bernstein A., Hay D.I., Blum M., Bennick A. Purification and characterization of a rabbit salivary protein, a potent inhibitor of crystal-growth of calcium-phosphate salts. Arch. Oral Biol. 1991, 36:55-63.
114. Taylor E.N., Curhan G.C. Differences in 24-hour urine composition between black and white women. J. Am. Soc. Nephrol. 2007, 18:654-659.
115. Teti A., Farina A.R., Villanova I., Tiberio A., Tacconelli A., Sciortino G., Chambers A.F., Gulino A., Mackay A.R. Activation of MMP-2 by human GCT23 giant cell tumour cells induced by osteopontin, bone sialoprotein and GRGDSP peptides is RGD and cell shape change dependent. Int. J. Cancer 1998, 77:82-93.
116. Thachepan S., Li M., Mann S. Mesoscale crystallization of calcium phosphate nanostructures in protein (casein) micelles. Nanoscale 2010, 2:2400-2405.
117. Thurgood L.A., Grover P.K., Ryall R.L. High calcium concentration and calcium oxalate crystals cause significant inaccuracies in the measurement of urinary osteopontin by enzyme linked immunosorbent assay. Urol. Res. 2008, 36:103-110.
118. Tiselius H.-G., Lindback B., Fornander A.-M., Nilsson M.-A. Studies on the role of calcium phosphate in the process of calcium oxalate crystal formation. Urol. Res. 2009, 37:181-192.
119. Toribara T.Y., Terepka A.R., Dewey P.A. The ultrafiltrable calcium of human serum. 1. Ultrafiltration methods and normal values. J. Clin. Invest. 1957, 36:738-748.
120. Trechsel U., Aeby O., Fleisch H. New device for ultrafiltration - ultrafiltrability of calcium and inorganic-phosphate in human-serum. Clin. Chim. Acta 1976, 69:367-373.
121. van Kemenade M.J.J.M., de Bruyn P.L. A kinetic study of precipitation from supersaturated calcium phosphate solutions. J. Colloid Interface Sci. 1987, 118:564-585.
122. Vitorino R., Alves R., Barros A., Caseiro A., Ferreira R., Lobo M.C., Bastos A., Duarte J., Carvalho D., Santos L.L., Amado F.L. Finding new posttranslational modifications in salivary proline-rich proteins. Proteomics 2010, 10:3732-3742.
123. Volmer, M., Weber, A., 1926. Germ-formation in oversaturated figures. Z. Phys. Chem. Stochiometrie Verwandtschaftslehre 119, 277-301.
124. Wald J., Wiese S., Eckert T., Jahnen-Dechent W., Richtering W., Heiss A. Formation and stability kinetics of calcium phosphate-fetuin-A colloidal particles probed by time-resolved dynamic light scattering. Soft Matter 2011, 7:2869-2874.
125. Wald J., Wiese S., Eckert T., Jahnen-Dechent W., Heiss A., Richtering W. Fetuin-A mediated formation and ripening of colloidal calciprotein particles. Eur. Biophys. J. Biophys. Lett. 2011, 40:64-65.
126. Walser M. Ion association 6. Interactions between calcium, magnesium, inorganic phosphate, citrate and protein in normal human plasma. J. Clin. Invest. 1961, 40:723.
127. Walser M. Separate effects of hyperparathyroidism, hypercalcaemia of malignancy, renal failure, and acidosis on state of calcium, phosphate and other ions in plasma. J. Clin. Invest. 1962, 41:1454.
128. Wang L., Nancollas G.H. Pathways to biomineralization and biodemineralization of calcium phosphates: the thermodynamic and kinetic controls. Dalton Trans. 2009, 2665-2672.
129. Weiner, S., Addadi, L., 2011. Crystallization Pathways in Biomineralization. In: Clarke, D.R.F.P. (Ed.), Annu. Rev. Mater. Res., vol. 41, pp. 21-40.
130. Wendelin-Saarenhovi M., Oikonen M., Loo B.-M., Juonala M., Kahonen M., Viikari J.S.A., Raitakari O.T. Plasma osteopontin is not associated with vascular markers of subclinical atherosclerosis in a population of young adults without symptoms of cardiovascular disease. the cardiovascular risk in young finns study. Scand. J. Clin. Lab. Invest. 2011, 71:683-689.
131. White J.C.D., Davies D.T. The relation between the chemical composition of milk and the stability of the caseinate complex. 1. General introduction, description of samples, methods and chemical composition of samples. J. Dairy Res. 1958, 25:236-255.
132. Xie B., Nancollas G.H. How to control the size and morphology of apatite nanocrystals in bone. Proc. Nat. Acad. Sci. USA 2010, 107:22369-22370.
133. Yang X., Wang L., Qin Y., Sun Z., Henneman Z.J., Moradian-Oldak J., Nancollas G.H. How amelogenin orchestrates the organization of hierarchical elongated microstructures of apatite. J. Phys. Chem. B 2010, 114:2293-2300.
134. Young A. Co-aggregation of micelle-like globules from human submandibular/sublingual and parotid saliva. Collid. Surf. B-Bioint. 1999, 13:241-249.
135. Young A., Rykke M., Rolla G. Quantitative and qualitative analyses of human salivary micelle-like globules. Acta Odontol. Scand. 1999, 57:105-110.