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Volumn 276, Issue 8, 2009, Pages 2308-2323

Role of calcium phosphate nanoclusters in the control of calcification

Author keywords

Casein; Dentin matrix acidic phosphoprotein 1; Fetuin; Natively unfolded protein; Osteopontin

Indexed keywords

CALCIUM PHOSPHATE; CASEIN; OSTEOPONTIN; PHOSPHOPEPTIDE; PHOSPHOPROTEIN; PLASMIN; PROTEIN;

EID: 63049110383     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.06958.x     Document Type: Article
Times cited : (76)

References (50)
  • 1
    • 0018622059 scopus 로고
    • Calcium measurements in serum and plasma - Total and ionized
    • Robertson WG Marshall RW (1979) Calcium measurements in serum and plasma - total and ionized. CRC Crit Rev Clin Lab Sci 11, 271 304.
    • (1979) CRC Crit Rev Clin Lab Sci , vol.11 , pp. 271-304
    • Robertson, W.G.1    Marshall, R.W.2
  • 2
    • 1042292794 scopus 로고    scopus 로고
    • Modelling of electrolyte mixtures with application to chemical equilibria in mixtures - Prototypes of blood's plasma and calcification of soft tissues
    • Glinkina IV, Durov VA Mel'nitchenko GA (2004) Modelling of electrolyte mixtures with application to chemical equilibria in mixtures - prototypes of blood's plasma and calcification of soft tissues. J Mol Liquids 110, 63 67.
    • (2004) J Mol Liquids , vol.110 , pp. 63-67
    • Glinkina, I.V.1    Durov, V.A.2    Mel'Nitchenko, G.A.3
  • 3
    • 0036363729 scopus 로고    scopus 로고
    • H-1 NMR investigations of the molecular nature of low-molecular-mass calcium ions in biofluids
    • Silwood CJL, Grootveld M Lynch E (2002) H-1 NMR investigations of the molecular nature of low-molecular-mass calcium ions in biofluids. J Biol Inorg Chem 7, 46 57.
    • (2002) J Biol Inorg Chem , vol.7 , pp. 46-57
    • Silwood, C.J.L.1    Grootveld, M.2    Lynch, E.3
  • 4
    • 17444435173 scopus 로고    scopus 로고
    • Calcium salt urolithiasis - Review of theory for diagnosis and management
    • Gyory AZ Ashby R (1999) Calcium salt urolithiasis - review of theory for diagnosis and management. Clin Nephrol 51, 197 208.
    • (1999) Clin Nephrol , vol.51 , pp. 197-208
    • Gyory, A.Z.1    Ashby, R.2
  • 5
    • 0019564975 scopus 로고
    • Inorganic constituents of milk. 2. Calculation of the ion equilibria in milk diffusate and comparison with experiment
    • Holt C, Dalgleish DG Jenness R (1981) Inorganic constituents of milk. 2. Calculation of the ion equilibria in milk diffusate and comparison with experiment. Anal Biochem 113, 154 163.
    • (1981) Anal Biochem , vol.113 , pp. 154-163
    • Holt, C.1    Dalgleish, D.G.2    Jenness, R.3
  • 6
    • 0038422941 scopus 로고    scopus 로고
    • The inhibition of calcium phosphate precipitation by fetuin is accompanied by the formation of a fetuin-mineral complex
    • Price PA Lim JE (2003) The inhibition of calcium phosphate precipitation by fetuin is accompanied by the formation of a fetuin-mineral complex. J Biol Chem 278, 22144 22152.
    • (2003) J Biol Chem , vol.278 , pp. 22144-22152
    • Price, P.A.1    Lim, J.E.2
  • 8
    • 11444251527 scopus 로고    scopus 로고
    • Inflammation and vascular calcification
    • Moe SM Chen NX (2005) Inflammation and vascular calcification. Blood Purif 23, 64 71.
    • (2005) Blood Purif , vol.23 , pp. 64-71
    • Moe, S.M.1    Chen, N.X.2
  • 9
    • 0037040254 scopus 로고    scopus 로고
    • Discovery of a high molecular weight complex of calcium, phosphate, fetuin, and matrix gamma-carboxyglutamic acid protein in the serum of etidronate-treated rats
    • Price PA, Thomas GR, Pardini AW, Figueira WF, Caputo JM Williamson MK (2002) Discovery of a high molecular weight complex of calcium, phosphate, fetuin, and matrix gamma-carboxyglutamic acid protein in the serum of etidronate-treated rats. J Biol Chem 277, 3926 3934.
    • (2002) J Biol Chem , vol.277 , pp. 3926-3934
    • Price, P.A.1    Thomas, G.R.2    Pardini, A.W.3    Figueira, W.F.4    Caputo, J.M.5    Williamson, M.K.6
  • 10
    • 0038645812 scopus 로고    scopus 로고
    • Structural basis of calcification inhibition by alpha(2)-HS glycoprotein/fetuin-A - Formation of colloidal calciprotein particles
    • Heiss A, DuChesne A, Denecke B, Grotzinger J, Yamamoto K, Renne T Jahnen-Dechent W (2003) Structural basis of calcification inhibition by alpha(2)-HS glycoprotein/fetuin-A - formation of colloidal calciprotein particles. J Biol Chem 278, 13333 13341.
    • (2003) J Biol Chem , vol.278 , pp. 13333-13341
    • Heiss, A.1    Duchesne, A.2    Denecke, B.3    Grotzinger, J.4    Yamamoto, K.5    Renne, T.6    Jahnen-Dechent, W.7
  • 11
    • 0020519414 scopus 로고
    • Swelling of Golgi vesicles in mammary secretory-cells and its relation to the yield and quantitative composition of milk
    • Holt C (1983) Swelling of Golgi vesicles in mammary secretory-cells and its relation to the yield and quantitative composition of milk. J Theor Biol 101, 247 261.
    • (1983) J Theor Biol , vol.101 , pp. 247-261
    • Holt, C.1
  • 12
    • 0029670230 scopus 로고    scopus 로고
    • Ability of a beta-casein phosphopeptide to modulate the precipitation of calcium phosphate by forming amorphous dicalcium phosphate nanoclusters
    • Holt C, Wahlgren NM Drakenberg T (1996) Ability of a beta-casein phosphopeptide to modulate the precipitation of calcium phosphate by forming amorphous dicalcium phosphate nanoclusters. Biochem J 314, 1035 1039.
    • (1996) Biochem J , vol.314 , pp. 1035-1039
    • Holt, C.1    Wahlgren, N.M.2    Drakenberg, T.3
  • 13
    • 2442702509 scopus 로고    scopus 로고
    • An equilibrium thermodynamic model of the sequestration of calcium phosphate by casein phosphopeptides
    • Little EM Holt C (2004) An equilibrium thermodynamic model of the sequestration of calcium phosphate by casein phosphopeptides. Eur Biophys J Biophys Lett 33, 435 447.
    • (2004) Eur Biophys J Biophys Lett , vol.33 , pp. 435-447
    • Little, E.M.1    Holt, C.2
  • 14
    • 0032520111 scopus 로고    scopus 로고
    • 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
    • Holt C, Timmins PA, Errington N Leaver J (1998) 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 252, 73 78.
    • (1998) Eur J Biochem , vol.252 , pp. 73-78
    • Holt, C.1    Timmins, P.A.2    Errington, N.3    Leaver, J.4
  • 16
    • 2442701167 scopus 로고    scopus 로고
    • 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
    • Holt C (2004) 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 33, 421 434.
    • (2004) Eur Biophys J Biophys Lett , vol.33 , pp. 421-434
    • Holt, C.1
  • 18
    • 0020461049 scopus 로고
    • Structure of bovine-milk calcium-phosphate determined by x-ray absorption-spectroscopy
    • Holt C, Hasnain SS Hukins DWL (1982) Structure of bovine-milk calcium-phosphate determined by x-ray absorption-spectroscopy. Biochim Biophys Acta 719, 299 303.
    • (1982) Biochim Biophys Acta , vol.719 , pp. 299-303
    • Holt, C.1    Hasnain, S.S.2    Hukins, D.W.L.3
  • 19
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure, functions and interactions
    • In. (. Fox, P.F. McSweeney, P.L.H., eds), pp. Kluwer Academic/Plenum, New York, NY.
    • Kruif CGd Holt C (2003) Casein micelle structure, functions and interactions. In Advanced Dairy Chemistry (Fox PF McSweeney PLH, eds), pp. 675 698. Kluwer Academic/Plenum, New York, NY.
    • (2003) Advanced Dairy Chemistry , pp. 675-698
    • Cgd, K.1    Holt, C.2
  • 20
    • 0021772513 scopus 로고
    • Nature of micellar calcium-phosphate in cows milk as studied by high-resolution electron-microscopy
    • Lyster RLJ, Mann S, Parker SB Williams RJP (1984) Nature of micellar calcium-phosphate in cows milk as studied by high-resolution electron-microscopy. Biochim Biophys Acta 801, 315 317.
    • (1984) Biochim Biophys Acta , vol.801 , pp. 315-317
    • Lyster, R.L.J.1    Mann, S.2    Parker, S.B.3    Williams, R.J.P.4
  • 22
    • 0033731371 scopus 로고    scopus 로고
    • Osteopontin: A versatile regulator of inflammation and biomineralization
    • Giachelli CM Steitz S (2000) Osteopontin: a versatile regulator of inflammation and biomineralization. Matrix Biol 19, 615 622.
    • (2000) Matrix Biol , vol.19 , pp. 615-622
    • Giachelli, C.M.1    Steitz, S.2
  • 23
    • 0037388133 scopus 로고    scopus 로고
    • Mineralized tissue and vertebrate evolution: The secretory calcium-binding phosphoprotein gene cluster
    • Kawasaki K Weiss KM (2003) Mineralized tissue and vertebrate evolution: the secretory calcium-binding phosphoprotein gene cluster. Proc Natl Acad Sci USA 100, 4060 4065.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4060-4065
    • Kawasaki, K.1    Weiss, K.M.2
  • 24
    • 34347406726 scopus 로고    scopus 로고
    • Gene duplication and the evolution of vertebrate skeletal mineralization
    • Kawasaki K, Buchanan AV Weiss KM (2007) Gene duplication and the evolution of vertebrate skeletal mineralization. Cells Tissues Organs 186, 7 24.
    • (2007) Cells Tissues Organs , vol.186 , pp. 7-24
    • Kawasaki, K.1    Buchanan, A.V.2    Weiss, K.M.3
  • 26
    • 0028875692 scopus 로고
    • Posttranslational modifications of bovine osteopontin - Identification of 28 phosphorylation and 3 O-glycosylation sites
    • Sorensen ES, Hojrup P Petersen TE (1995) Posttranslational modifications of bovine osteopontin - identification of 28 phosphorylation and 3 O-glycosylation sites. Protein Sci 4, 2040 2049.
    • (1995) Protein Sci , vol.4 , pp. 2040-2049
    • Sorensen, E.S.1    Hojrup, P.2    Petersen, T.E.3
  • 27
    • 0029977717 scopus 로고    scopus 로고
    • Nucleation and inhibition of hydroxyapatite formation by mineralized tissue proteins
    • Hunter GK, Hauschka PV, Poole AR, Rosenberg LC Goldberg HA (1996) Nucleation and inhibition of hydroxyapatite formation by mineralized tissue proteins. Biochem J 317, 59 64.
    • (1996) Biochem J , vol.317 , pp. 59-64
    • Hunter, G.K.1    Hauschka, P.V.2    Poole, A.R.3    Rosenberg, L.C.4    Goldberg, H.A.5
  • 28
    • 25844489058 scopus 로고    scopus 로고
    • Phosphorylation of phosphophoryn is crucial for its function as a mediator of biomineralization
    • He G, Ramachandran A, Dahl T, George S, Schultz D, Cookson D, Veis A George A (2005) Phosphorylation of phosphophoryn is crucial for its function as a mediator of biomineralization. J Biol Chem 280, 33109 33114.
    • (2005) J Biol Chem , vol.280 , pp. 33109-33114
    • He, G.1    Ramachandran, A.2    Dahl, T.3    George, S.4    Schultz, D.5    Cookson, D.6    Veis, A.7    George, A.8
  • 29
    • 0028129454 scopus 로고
    • Modulation of crystal-formation by bone phosphoproteins - Role of glutamic acid-rich sequences in the nucleation of hydroxyapatite by bone sialoprotein
    • Hunter GK Goldberg HA (1994) Modulation of crystal-formation by bone phosphoproteins - role of glutamic acid-rich sequences in the nucleation of hydroxyapatite by bone sialoprotein. Biochem J 302, 175 179.
    • (1994) Biochem J , vol.302 , pp. 175-179
    • Hunter, G.K.1    Goldberg, H.A.2
  • 30
    • 0019928245 scopus 로고
    • Phase transformation during precipitation of calcium salts
    • In. (. Nancollas, G.H., ed.), pp. Springer-Verlag, Berlin.
    • Nancollas GH (1982) Phase transformation during precipitation of calcium salts. In Biological Mineralization and Demineralization (Nancollas GH, ed.), pp. 79 99. Springer-Verlag, Berlin.
    • (1982) Biological Mineralization and Demineralization , pp. 79-99
    • Nancollas, G.H.1
  • 32
    • 44349192171 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins based on the meta approach
    • Ishida T Kinoshita K (2008) Prediction of disordered regions in proteins based on the meta approach. Bioinformatics 24, 1344 1348.
    • (2008) Bioinformatics , vol.24 , pp. 1344-1348
    • Ishida, T.1    Kinoshita, K.2
  • 33
    • 0030952249 scopus 로고    scopus 로고
    • Crystal structure of chicken riboflavin-binding protein
    • Monaco HL (1997) Crystal structure of chicken riboflavin-binding protein. EMBO J 16, 1475 1483.
    • (1997) EMBO J , vol.16 , pp. 1475-1483
    • Monaco, H.L.1
  • 35
    • 0001517504 scopus 로고
    • Caseins as rheomorphic proteins - Interpretation of primary and secondary structures of the alpha-S1-caseins, beta-caseins and kappa-caseins
    • Holt C Sawyer L (1993) Caseins as rheomorphic proteins - interpretation of primary and secondary structures of the alpha-S1-caseins, beta-caseins and kappa-caseins. J Chem Soc Faraday Trans 89, 2683 2692.
    • (1993) J Chem Soc Faraday Trans , vol.89 , pp. 2683-2692
    • Holt, C.1    Sawyer, L.2
  • 36
    • 33745617174 scopus 로고    scopus 로고
    • Evolutionary genetics of vertebrate tissue mineralization: The origin of secretory calcium-binding and evolution of the phosphoprotein family
    • Kawasaki K Weiss KM (2006) Evolutionary genetics of vertebrate tissue mineralization: the origin of secretory calcium-binding and evolution of the phosphoprotein family. J Exp Zool B Mol Dev Evol 306B, 295 316.
    • (2006) J Exp Zool B Mol Dev Evol , vol.306 , pp. 295-316
    • Kawasaki, K.1    Weiss, K.M.2
  • 37
    • 0001035402 scopus 로고    scopus 로고
    • Scattering form factor of block copolymer micelles
    • Pedersen JS Gerstenberg MC (1996) Scattering form factor of block copolymer micelles. Macromolecules 29, 1363 1365.
    • (1996) Macromolecules , vol.29 , pp. 1363-1365
    • Pedersen, J.S.1    Gerstenberg, M.C.2
  • 38
    • 0038402091 scopus 로고    scopus 로고
    • Process scale chromatographic isolation, characterization and identification of tryptic bioactive casein phosphopeptides
    • Ellegard KH, Gammelgard-Larsen C, Sorensen ES Fedosov S (1999) Process scale chromatographic isolation, characterization and identification of tryptic bioactive casein phosphopeptides. Int Dairy J 9, 639 652.
    • (1999) Int Dairy J , vol.9 , pp. 639-652
    • Ellegard, K.H.1    Gammelgard-Larsen, C.2    Sorensen, E.S.3    Fedosov, S.4
  • 39
    • 0001575623 scopus 로고
    • The cataphoresis of suspended particles. Part 1. - The equation of cataphoresis
    • Henry DC (1931) The cataphoresis of suspended particles. Part 1. - The equation of cataphoresis. Proc R Soc Lond A 133, 106 129.
    • (1931) Proc R Soc Lond A , vol.133 , pp. 106-129
    • Henry, D.C.1
  • 41
    • 57349158632 scopus 로고    scopus 로고
    • Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition
    • George A Veis A (2008) Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition. Chem Rev 108, 4670 4693.
    • (2008) Chem Rev , vol.108 , pp. 4670-4693
    • George, A.1    Veis, A.2
  • 42
    • 0035991230 scopus 로고    scopus 로고
    • Bone origin of the serum complex of calcium, phosphate, fetuin, and matrix Gla protein: Biochemical evidence for the cancellous bone-remodeling compartment
    • Price PA, Caputo JM Williamson MK (2002) Bone origin of the serum complex of calcium, phosphate, fetuin, and matrix Gla protein: biochemical evidence for the cancellous bone-remodeling compartment. J Bone Miner Res 17, 1171 1179.
    • (2002) J Bone Miner Res , vol.17 , pp. 1171-1179
    • Price, P.A.1    Caputo, J.M.2    Williamson, M.K.3
  • 43
    • 0037483052 scopus 로고    scopus 로고
    • Biochemical characterization of the serum fetuin-mineral complex
    • Price PA, Nguyen TMT Williamson MK (2003) Biochemical characterization of the serum fetuin-mineral complex. J Biol Chem 278, 22153 22160.
    • (2003) J Biol Chem , vol.278 , pp. 22153-22160
    • Price, P.A.1    Nguyen, T.M.T.2    Williamson, M.K.3
  • 45
    • 0030670589 scopus 로고    scopus 로고
    • Efficient discovery of conserved patterns using a pattern graph
    • Jonassen I (1997) Efficient discovery of conserved patterns using a pattern graph. Comput Appl Biosci 13, 509 522.
    • (1997) Comput Appl Biosci , vol.13 , pp. 509-522
    • Jonassen, I.1
  • 46
    • 0000009417 scopus 로고    scopus 로고
    • The milk salts and their interaction with casein
    • In. (. Fox, P.F., ed.), pp. Chapman & Hall, London.
    • Holt C (1997) The milk salts and their interaction with casein. In Advanced Dairy Chemistry (Fox PF, ed.), pp. 233 256. Chapman & Hall, London.
    • (1997) Advanced Dairy Chemistry , pp. 233-256
    • Holt, C.1
  • 47
    • 5444272701 scopus 로고
    • Scattering function for semiflexible polymers - Dirac versus Kratky-Porod
    • Kholodenko AL (1993) Scattering function for semiflexible polymers - Dirac versus Kratky-Porod. Phys Lett A 178, 180 185.
    • (1993) Phys Lett A , vol.178 , pp. 180-185
    • Kholodenko, A.L.1
  • 48
    • 0033646742 scopus 로고    scopus 로고
    • Analysis of the conformation of worm-like chains by small-angle scattering: Monte-Carlo simulations in comparison to analytical theory
    • Potschke D, Hickl P, Ballauff M, Astrand PO Pedersen JS (2000) Analysis of the conformation of worm-like chains by small-angle scattering: Monte-Carlo simulations in comparison to analytical theory. Macromol Theory Simul 9, 345 353.
    • (2000) Macromol Theory Simul , vol.9 , pp. 345-353
    • Potschke, D.1    Hickl, P.2    Ballauff, M.3    Astrand, P.O.4    Pedersen, J.S.5
  • 49
    • 0037192212 scopus 로고    scopus 로고
    • Form factors of block copolymer micelles with excluded-volume interactions of the corona chains determined by Monte Carlo simulations
    • Svaneborg C Pedersen JS (2002) Form factors of block copolymer micelles with excluded-volume interactions of the corona chains determined by Monte Carlo simulations. Macromolecules 35, 1028 1037.
    • (2002) Macromolecules , vol.35 , pp. 1028-1037
    • Svaneborg, C.1    Pedersen, J.S.2
  • 50
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • Qi XL, Holt C, McNulty D, Clarke DT, Brownlow S Jones GR (1997) Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochem J 324, 341 346.
    • (1997) Biochem J , vol.324 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    McNulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6


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