메뉴 건너뛰기




Volumn 93, Issue 12, 2014, Pages 3065-3072

Phosvitin phosphorus is involved in chicken embryo bone formation through dephosphorylation

Author keywords

Bone formation; Chicken embryo development; Dephosphorylation; Phosvitin

Indexed keywords

NITROGEN; PHOSPHORUS; PHOSVITIN;

EID: 84929032620     PISSN: 00325791     EISSN: 15253171     Source Type: Journal    
DOI: 10.3382/ps.2014-04098     Document Type: Article
Times cited : (37)

References (30)
  • 1
    • 0029997944 scopus 로고    scopus 로고
    • Endochondral and intramembranous fetal bone development: Osteoblastic cell proliferation, and expression of alkaline phosphatase, m-twist, and histone H4
    • Alborzi, A., K. Mac, C. A. Glackin, and S. S. Murray. 1996. Endochondral and intramembranous fetal bone development: Osteoblastic cell proliferation, and expression of alkaline phosphatase, m-twist, and histone H4. J. Craniofac. Genet. Dev. Biol. 16:94-106.
    • (1996) J. Craniofac. Genet. Dev. Biol , vol.16 , pp. 94-106
    • Alborzi, A.1    Mac, K.2    Glackin, C.A.3    Murray, S.S.4
  • 2
    • 33644818657 scopus 로고    scopus 로고
    • Hypophosphatemia: An evidence-based approach to its clinical consequences and management
    • Amanzadeh, J., and R. F. Reilly. 2006. Hypophosphatemia: An evidence-based approach to its clinical consequences and management. Nat. Clin. Pract. Nephrol. 2:136-148.
    • (2006) Nat. Clin. Pract. Nephrol , vol.2 , pp. 136-148
    • Amanzadeh, J.1    Reilly, R.F.2
  • 3
    • 0021760617 scopus 로고
    • Amino acid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene
    • Byrne, B. M., A. D. van het Schip, J. A. van de Klundert, A. C. Arnberg, M. Gruber, and G. Ab. 1984. Amino acid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene. Biochemistry 23:4275-4279.
    • (1984) Biochemistry , vol.23 , pp. 4275-4279
    • Byrne, B.M.1    Van Het Schip, A.D.2    Van De Klundert, J.A.3    Arnberg, A.C.4    Gruber, M.5    Ab, G.6
  • 4
    • 0025357111 scopus 로고
    • Protein secondary structure in water from second-derivative amide I infrared spectra
    • Dong, A., P. Huang, and W. S. Caughey. 1990. Protein secondary structure in water from second-derivative amide I infrared spectra. Biochemistry 29:3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 6
    • 0024307419 scopus 로고
    • Mechanism of calcification: Role of collagen fibrils and collagen-phosphoprotein complexes in vitro and in vivo
    • Glimcher, M. J. 1989. Mechanism of calcification: Role of collagen fibrils and collagen-phosphoprotein complexes in vitro and in vivo. Anat. Rec. 224:139-153.
    • (1989) Anat. Rec , vol.224 , pp. 139-153
    • Glimcher, M.J.1
  • 7
    • 34547594593 scopus 로고    scopus 로고
    • Bone sialoprotein expression enhances osteoblast differentiation and matrix mineralization in vitro
    • Gordon, J. A. R., C. E. Tye, A. V. Sampaio, T. M. Underhill, G. K. Hunter, and H. A. Goldberg. 2007. Bone sialoprotein expression enhances osteoblast differentiation and matrix mineralization in vitro. Bone 41:462-473.
    • (2007) Bone , vol.41 , pp. 462-473
    • Gordon, J.A.R.1    Tye, C.E.2    Sampaio, A.V.3    Underhill, T.M.4    Hunter, G.K.5    Goldberg, H.A.6
  • 8
    • 45949127671 scopus 로고
    • Iron binding by phosvitin: Variation of rate of iron release as a function of the degree of saturation of iron binding sites
    • Grogan, J., and G. Taborsky. 1986. Iron binding by phosvitin: Variation of rate of iron release as a function of the degree of saturation of iron binding sites. J. Inorg. Biochem. 26:237-246.
    • (1986) J. Inorg. Biochem , vol.26 , pp. 237-246
    • Grogan, J.1    Taborsky, G.2
  • 9
    • 62649101871 scopus 로고    scopus 로고
    • Temporal and spatial localization of the dentin matrix proteins during dentin biomineralization
    • Hao, J., R. Amsaveni, and G. Anne. 2009. Temporal and spatial localization of the dentin matrix proteins during dentin biomineralization. J. Histochem. Cytochem. 57:227-237.
    • (2009) J. Histochem. Cytochem , vol.57 , pp. 227-237
    • Hao, J.1    Amsaveni, R.2    Anne, G.3
  • 10
    • 12244287601 scopus 로고    scopus 로고
    • Dentin matrix protein 1 initiates hydroxyapatite formation in vitro
    • He, G., T. Dahl, A. Veis, and A. George. 2003. Dentin matrix protein 1 initiates hydroxyapatite formation in vitro. Connect. Tissue Res. 44:240-245.
    • (2003) Connect. Tissue Res , vol.44 , pp. 240-245
    • He, G.1    Dahl, T.2    Veis, A.3    George, A.4
  • 11
    • 1642441997 scopus 로고    scopus 로고
    • Dentin matrix protein 1 immobilized on type I collagen fibrils facilitates apatite deposition in vitro
    • He, G., and A. George. 2004. Dentin matrix protein 1 immobilized on type I collagen fibrils facilitates apatite deposition in vitro. J. Biol. Chem. 279:11649-11656.
    • (2004) J. Biol. Chem , vol.279 , pp. 11649-11656
    • He, G.1    George, A.2
  • 12
    • 0018781475 scopus 로고
    • Iron (III)-phosphoprotein chelates: Stoichiometric equilibrium constant for interaction of iron (III) and phosphorylserine residues of phosvitin and casein
    • Hegenauer, J., P. Saltman, and G. Nace. 1979. Iron (III)-phosphoprotein chelates: Stoichiometric equilibrium constant for interaction of iron (III) and phosphorylserine residues of phosvitin and casein. Biochemistry 18:3865-3879.
    • (1979) Biochemistry , vol.18 , pp. 3865-3879
    • Hegenauer, J.1    Saltman, P.2    Nace, G.3
  • 13
    • 84985986055 scopus 로고    scopus 로고
    • The effect of culturing chicken embryos in recipient egg shells on activity of bone ALP
    • Li, z. D., F. Sakurai, and H. C. Li. 1997. The effect of culturing chicken embryos in recipient egg shells on activity of bone ALP. Chinese Journal of Animal and Veterinary Sciences 28:44-48.
    • (1997) Chinese Journal of Animal and Veterinary Sciences , vol.28 , pp. 44-48
    • Li, Z.D.1    Sakurai, F.2    Li, H.C.3
  • 14
    • 0026784911 scopus 로고
    • Characteristics of phosphorylated and nonphosphorylated dentine phosphoprotein
    • MacDougall, M., C. S. Harold, and M. David. 1992. Characteristics of phosphorylated and nonphosphorylated dentine phosphoprotein. Biochem. J. 287:651-655.
    • (1992) Biochem. J. , vol.287 , pp. 651-655
    • MacDougall, M.1    Harold, C.S.2    David, M.3
  • 16
    • 84867769941 scopus 로고    scopus 로고
    • Influence of 63Ser phosphorylation and dephosphorylation on the structure of the stathmin helical nucleation sequence: A molecular dynamics study
    • Missimer, J. H., M. O. Steinmetz, W. F. van Gunsteren, and J. Dolenc. 2012. Influence of 63Ser phosphorylation and dephosphorylation on the structure of the stathmin helical nucleation sequence: A molecular dynamics study. Biochemistry 51:8455-8463.
    • (2012) Biochemistry , vol.51 , pp. 8455-8463
    • Missimer, J.H.1    Steinmetz, M.O.2    Van Gunsteren, W.F.3    Dolenc, J.4
  • 17
    • 34250192949 scopus 로고    scopus 로고
    • Nutrition of the developing embryo and hatchling
    • Moran, E. T. 2007. Nutrition of the developing embryo and hatchling. Poult. Sci. 86:1043-1049.
    • (2007) Poult. Sci. , vol.86 , pp. 1043-1049
    • Moran, E.T.1
  • 18
    • 34247898040 scopus 로고
    • A modified single solution method for the determination of phosphate in natural waters
    • Murphy, J., and J. P. Riley. 1962. A modified single solution method for the determination of phosphate in natural waters. Anal. Chim. Acta 27:31-36.
    • (1962) Anal. Chim. Acta , vol.27 , pp. 31-36
    • Murphy, J.1    Riley, J.P.2
  • 19
    • 18444369001 scopus 로고    scopus 로고
    • Effect of phosvitin on the nucleation and growth of calcium phosphates in physiological solutions
    • Onuma, K. 2005. Effect of phosvitin on the nucleation and growth of calcium phosphates in physiological solutions. J. Phys. Chem. B 109:8257-8262.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 8257-8262
    • Onuma, K.1
  • 20
    • 44449094581 scopus 로고    scopus 로고
    • The role of metal ions in emulsion characteristics and flocculation behaviour of phosvitin-stabilised emulsions
    • Oscar, C., B. Corinne, D. B. Elisabeth, G. D. Catherine, and A. Marc. 2008. The role of metal ions in emulsion characteristics and flocculation behaviour of phosvitin-stabilised emulsions. Food Hydrocoll. 22:1243-1253.
    • (2008) Food Hydrocoll , vol.22 , pp. 1243-1253
    • Oscar, C.1    Corinne, B.2    Elisabeth, D.B.3    Catherine, G.D.4    Marc, A.5
  • 21
    • 0030636280 scopus 로고    scopus 로고
    • Trace mineral metabolism in the avian embryo
    • Richards, M. P. 1997. Trace mineral metabolism in the avian embryo. Poult. Sci. 76:152-164.
    • (1997) Poult. Sci. , vol.76 , pp. 152-164
    • Richards, M.P.1
  • 22
    • 0036606717 scopus 로고    scopus 로고
    • Natural variation in the extent of phosphorylation of bone phosphoproteins as a function of in vivo new bone formation induced by demineralized bone matrix in soft tissue and bony environments
    • Salih, E., J. Wang, J. Mah, and R. Fluckiger. 2002. Natural variation in the extent of phosphorylation of bone phosphoproteins as a function of in vivo new bone formation induced by demineralized bone matrix in soft tissue and bony environments. Biochem. J. 364:465-474.
    • (2002) Biochem. J. , vol.364 , pp. 465-474
    • Salih, E.1    Wang, J.2    Mah, J.3    Fluckiger, R.4
  • 23
    • 67749113165 scopus 로고    scopus 로고
    • Hypophosphatemia: The common denominator of all rickets
    • Tiosano, D., and z. Hochberg. 2009. Hypophosphatemia: The common denominator of all rickets. J. Bone Miner. Metab. 27:392-401.
    • (2009) J. Bone Miner. Metab , vol.27 , pp. 392-401
    • Tiosano, D.1    Hochberg, Z.2
  • 24
    • 56349134816 scopus 로고    scopus 로고
    • Biocompatibility and bone mineralization potential of 45S5 bioglass-derived glass-ceramic scaffolds in chick embryos
    • Vargas, G. E., R. V. Mesones, O. Bretcanu, J. M. P. López, A. R. Boccaccini, and A. Gorustovich. 2009. Biocompatibility and bone mineralization potential of 45S5 Bioglass-derived glass-ceramic scaffolds in chick embryos. Acta Biomater. 5:374-380.
    • (2009) Acta Biomater , vol.5 , pp. 374-380
    • Vargas, G.E.1    Mesones, R.V.2    Bretcanu, O.3    López, J.M.P.4    Boccaccini, A.R.5    Gorustovich, A.6
  • 25
    • 84879836180 scopus 로고    scopus 로고
    • The effects of threonine phosphorylation on the stability and dynamics of the central molecular switch region of 18.5-kDa myelin basic protein
    • Vassall, K. A., K. Bessonov, M. De Avila, E. Polverini, and G. Harauz. 2013. The effects of threonine phosphorylation on the stability and dynamics of the central molecular switch region of 18.5-kDa myelin basic protein. PLoS oNE 8:e68175.
    • (2013) PLoS ONE , vol.8
    • Vassall, K.A.1    Bessonov, K.2    De Avila, M.3    Polverini, E.4    Harauz, G.5
  • 26
    • 34548786649 scopus 로고    scopus 로고
    • Chicken embryo utilization of egg micronutrient
    • Vieira, S. L. 2007. Chicken embryo utilization of egg micronutrient. Braz. J. Poult. Sci. 9:1-8.
    • (2007) Braz. J. Poult. Sci. , vol.9 , pp. 1-8
    • Vieira, S.L.1
  • 28
    • 84863262534 scopus 로고    scopus 로고
    • Gene expression analyses of subchondral bone in early experimental osteoarthritis by microarray
    • Zhang, R., H. Fang, Y. Chen, J. Shen, H. Lu, C. zeng, and J. Ren. 2012. Gene expression analyses of subchondral bone in early experimental osteoarthritis by microarray. PLoS oNE 7:e32356.
    • (2012) PLoS ONE , vol.7
    • Zhang, R.1    Fang, H.2    Chen, Y.3    Shen, J.4    Lu, H.5    Zeng, C.6    Ren, J.7
  • 29
    • 81755187207 scopus 로고    scopus 로고
    • Simply and effectively preparing high-purity phosvitin using polyethylene glycol and anion-exchange chromatography
    • Zhang, X., N. Qiu, F. Geng, and M. Ma. 2011. Simply and effectively preparing high-purity phosvitin using polyethylene glycol and anion-exchange chromatography. J. Sep. Sci. 34:3295-3301.
    • (2011) J. Sep. Sci. , vol.34 , pp. 3295-3301
    • Zhang, X.1    Qiu, N.2    Geng, F.3    Ma, M.4
  • 30
    • 84875595401 scopus 로고    scopus 로고
    • Determination study of total nitrogen in soil and plant by continuous flow analytical system
    • Zhang, Y., A. Xu, H. Shang, and A. Ma. 2006. Determination study of total nitrogen in soil and plant by continuous flow analytical system. Nat. Sci. Ed. 34:128-131.
    • (2006) Nat. Sci. Ed. , vol.34 , pp. 128-131
    • Zhang, Y.1    Xu, A.2    Shang, H.3    Ma, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.