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Volumn 30, Issue 5, 2012, Pages 355-375

The chicken or the egg: PHEX, FGF23 and SIBLINGs unscrambled

Author keywords

ASARM; DMP1; FGF23; KLOTHO; MEPE; PHEX

Indexed keywords

FIBROBLAST GROWTH FACTOR 23; MATRIX EXTRACELLULAR PHOSPHOGLYCOPROTEIN; METALLOPROTEINASE; OVOCLEIDIN 116; PHOSPHATE REGULATING GENE WITH HOMOLOGIES TO ENDOPEPTIDASES ON THE X CHROMOSOME PROTEIN; PHOSPHOPROTEIN; SMALL INTEGRIN BINDING LIGAND INTERACTING GLYCOPROTEIN; UNCLASSIFIED DRUG;

EID: 84863314939     PISSN: 02636484     EISSN: 10990844     Source Type: Journal    
DOI: 10.1002/cbf.2841     Document Type: Review
Times cited : (55)

References (219)
  • 1
    • 78649925696 scopus 로고    scopus 로고
    • What makes an egg unique? Clues from evolutionary scenarios of egg-specific genes
    • Tian X, Gautron J, Monget P, Pascal G. What makes an egg unique? Clues from evolutionary scenarios of egg-specific genes. Biol Reprod 2010; 83(6): 893-900.
    • (2010) Biol Reprod , vol.83 , Issue.6 , pp. 893-900
    • Tian, X.1    Gautron, J.2    Monget, P.3    Pascal, G.4
  • 2
    • 0032747266 scopus 로고    scopus 로고
    • Molecular cloning and ultrastructural localization of the core protein of an eggshell matrix proteoglycan, ovocleidin-116
    • Hincke MT, Gautron J, Tsang CP, McKee MD, Nys Y. Molecular cloning and ultrastructural localization of the core protein of an eggshell matrix proteoglycan, ovocleidin-116. J Biol Chem 1999; 274(46): 32915-32923.
    • (1999) J Biol Chem , vol.274 , Issue.46 , pp. 32915-32923
    • Hincke, M.T.1    Gautron, J.2    Tsang, C.P.3    McKee, M.D.4    Nys, Y.5
  • 3
    • 84858081678 scopus 로고    scopus 로고
    • Tooth dentin defects reflect genetic disorders affecting bone mineralization
    • Opsahl Vital S, Gaucher C, Bardet C, et al. Tooth dentin defects reflect genetic disorders affecting bone mineralization. Bone 2012; 50(4): 989-997.
    • (2012) Bone , vol.50 , Issue.4 , pp. 989-997
    • Opsahl Vital, S.1    Gaucher, C.2    Bardet, C.3
  • 4
    • 78649643608 scopus 로고    scopus 로고
    • OC-116, the chicken ortholog of mammalian MEPE found in eggshell, is also expressed in bone cells
    • Bardet C, Vincent C, Lajarille MC, Jaffredo T, Sire JY. OC-116, the chicken ortholog of mammalian MEPE found in eggshell, is also expressed in bone cells. J Exp Zool B Mol Dev Evol 2010; 314(8): 653-662.
    • (2010) J Exp Zool B Mol Dev Evol , vol.314 , Issue.8 , pp. 653-662
    • Bardet, C.1    Vincent, C.2    Lajarille, M.C.3    Jaffredo, T.4    Sire, J.Y.5
  • 5
    • 73849099954 scopus 로고    scopus 로고
    • MEPE evolution in mammals reveals regions and residues of prime functional importance
    • Bardet C, Delgado S, Sire JY. MEPE evolution in mammals reveals regions and residues of prime functional importance. Cell Mol Life Sci 2010; 67(2): 305-320.
    • (2010) Cell Mol Life Sci , vol.67 , Issue.2 , pp. 305-320
    • Bardet, C.1    Delgado, S.2    Sire, J.Y.3
  • 6
    • 49449103896 scopus 로고    scopus 로고
    • Ovocleidin (OC 116) is present in avian skeletal tissues
    • Horvat-Gordon M, Yu F, Burns D, Leach RM, Jr. Ovocleidin (OC 116) is present in avian skeletal tissues. Poult Sci 2008; 87(8): 1618-1623.
    • (2008) Poult Sci , vol.87 , Issue.8 , pp. 1618-1623
    • Horvat-Gordon, M.1    Yu, F.2    Burns, D.3    Leach Jr., R.M.4
  • 7
    • 10644283823 scopus 로고    scopus 로고
    • Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution
    • Consortium ICS
    • Consortium ICS. Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution. Nature 2004; 432(7018): 695-716.
    • (2004) Nature , vol.432 , Issue.7018 , pp. 695-716
  • 8
    • 0037237957 scopus 로고    scopus 로고
    • Six genes expressed in bones and teeth encode the current members of the SIBLING family of proteins
    • Fisher LW, Fedarko NS. Six genes expressed in bones and teeth encode the current members of the SIBLING family of proteins. Connect Tissue Res 2003; 44(Suppl 1): 33-40.
    • (2003) Connect Tissue Res , vol.44 , Issue.SUPPL. 1 , pp. 33-40
    • Fisher, L.W.1    Fedarko, N.S.2
  • 9
    • 0034235036 scopus 로고    scopus 로고
    • MEPE, a new gene expressed in bone marrow and tumors causing osteomalacia
    • Rowe PS, de Zoysa PA, Dong R, et al. MEPE, a new gene expressed in bone marrow and tumors causing osteomalacia. Genomics 2000; 67(1): 54-68.
    • (2000) Genomics , vol.67 , Issue.1 , pp. 54-68
    • Rowe, P.S.1    de Zoysa, P.A.2    Dong, R.3
  • 10
    • 11244352700 scopus 로고    scopus 로고
    • The wrickkened-pathways of FGF23, MEPE and PHEX
    • Rowe PSN. The wrickkened-pathways of FGF23, MEPE and PHEX. Crit Rev Oral Biol Med 2004; 15(5): 264-281.
    • (2004) Crit Rev Oral Biol Med , vol.15 , Issue.5 , pp. 264-281
    • Rowe, P.S.N.1
  • 11
    • 80051791241 scopus 로고    scopus 로고
    • The SCPP gene family and the complexity of hard tissues in vertebrates
    • Kawasaki K. The SCPP gene family and the complexity of hard tissues in vertebrates. Cells Tissues Organs 2011; 194(2-4): 108-112.
    • (2011) Cells Tissues Organs , vol.194 , Issue.2-4 , pp. 108-112
    • Kawasaki, K.1
  • 12
    • 33745617174 scopus 로고    scopus 로고
    • Evolutionary genetics of vertebrate tissue mineralization: the origin and evolution of the secretory calcium-binding phosphoprotein family
    • Kawasaki K, Weiss KM. Evolutionary genetics of vertebrate tissue mineralization: the origin and evolution of the secretory calcium-binding phosphoprotein family. J Exp Zoolog B Mol Dev Evol 2006; 306(3): 295-316.
    • (2006) J Exp Zoolog B Mol Dev Evol , vol.306 , Issue.3 , pp. 295-316
    • Kawasaki, K.1    Weiss, K.M.2
  • 13
    • 23444436222 scopus 로고
    • Dinucleotide repeat polymorphism at the DXS1683 locus
    • Econs MJ, Francis F, Rowe PSN, et al. Dinucleotide repeat polymorphism at the DXS1683 locus. Hum Mol Genet 1994; 3(4): 680.
    • (1994) Hum Mol Genet , vol.3 , Issue.4 , pp. 680
    • Econs, M.J.1    Francis, F.2    Rowe, P.S.N.3
  • 14
    • 14444280391 scopus 로고    scopus 로고
    • Genomic organisation of the human PEX gene mutated in X-linked dominant hypophosphataemic rickets
    • Francis F, Strom TM, Hennig S, et al. Genomic organisation of the human PEX gene mutated in X-linked dominant hypophosphataemic rickets. Gen Res 1997; 7(6): 573-585.
    • (1997) Gen Res , vol.7 , Issue.6 , pp. 573-585
    • Francis, F.1    Strom, T.M.2    Hennig, S.3
  • 15
    • 0028020989 scopus 로고
    • Molecular biology of hypophosphataemic rickets and oncogenic osteomalacia
    • Rowe PSN. Molecular biology of hypophosphataemic rickets and oncogenic osteomalacia. Hum Genet 1994; 94(5): 457-467.
    • (1994) Hum Genet , vol.94 , Issue.5 , pp. 457-467
    • Rowe, P.S.N.1
  • 16
    • 0031828575 scopus 로고    scopus 로고
    • The role of the PHEX gene (PEX), in families with X-linked hypophosphataemic rickets
    • Rowe PSN. The role of the PHEX gene (PEX), in families with X-linked hypophosphataemic rickets. Curr Opin Nephrol Hypertens 1998; 7(4): 367-376.
    • (1998) Curr Opin Nephrol Hypertens , vol.7 , Issue.4 , pp. 367-376
    • Rowe, P.S.N.1
  • 17
    • 4243403618 scopus 로고    scopus 로고
    • Finding mutations in disease genes
    • 1 ed. Econs MJ (ed.). Totowa New Jersey: Humana Press Inc
    • Rowe PSN. Finding mutations in disease genes. In Genetics of Osteoporosis and Metabolic Bone Disease. 1 ed. Econs MJ (ed.). Totowa New Jersey: Humana Press Inc; 2000; 431-446.
    • (2000) Genetics of Osteoporosis and Metabolic Bone Disease , pp. 431-446
    • Rowe, P.S.N.1
  • 18
    • 0028606975 scopus 로고
    • Rapid isolation of DNA sequences flanking microsatellite repeats
    • Rowe PSN, Francis F, Goulding J. Rapid isolation of DNA sequences flanking microsatellite repeats. Nucleic Acids Res 1994; 22(23): 5135-5136.
    • (1994) Nucleic Acids Res , vol.22 , Issue.23 , pp. 5135-5136
    • Rowe, P.S.N.1    Francis, F.2    Goulding, J.3
  • 19
    • 0028091087 scopus 로고
    • refining the genetic-map for the region flanking the x-linked hypophosphatemic rickets locus (xp22.1-22.2)
    • Rowe PSN, Goulding J, Read A, et al. refining the genetic-map for the region flanking the x-linked hypophosphatemic rickets locus (xp22.1-22.2). Hum Genet 1994; 93(3): 291-294.
    • (1994) Hum Genet , vol.93 , Issue.3 , pp. 291-294
    • Rowe, P.S.N.1    Goulding, J.2    Read, A.3
  • 20
    • 0027219492 scopus 로고
    • New markers for linkage analysis of hypophosphataemic rickets
    • Rowe PSN, Goulding J, Read AP, et al. New markers for linkage analysis of hypophosphataemic rickets. Hum Genet 1993; 91: 571-575.
    • (1993) Hum Genet , vol.91 , pp. 571-575
    • Rowe, P.S.N.1    Goulding, J.2    Read, A.P.3
  • 21
    • 0030022097 scopus 로고    scopus 로고
    • The gene for X-linked hypophosphataemic rickets maps to a 200-300kb region in Xp22.1, and is located on a single YAC containing a putative vitamin D response element (VDRE)
    • Rowe PSN, Goulding JN, Francis F, et al. The gene for X-linked hypophosphataemic rickets maps to a 200-300kb region in Xp22.1, and is located on a single YAC containing a putative vitamin D response element (VDRE). Hum Genet 1996; 97(3): 345-352.
    • (1996) Hum Genet , vol.97 , Issue.3 , pp. 345-352
    • Rowe, P.S.N.1    Goulding, J.N.2    Francis, F.3
  • 22
    • 8244251430 scopus 로고    scopus 로고
    • Distribution of mutations in the PEX gene in families with X-linked hypophosphataemic rickets (HYP)
    • Rowe PSN, Oudet C, Francis F, et al. Distribution of mutations in the PEX gene in families with X-linked hypophosphataemic rickets (HYP). Hum Mol Genet 1997; 6: 539-549.
    • (1997) Hum Mol Genet , vol.6 , pp. 539-549
    • Rowe, P.S.N.1    Oudet, C.2    Francis, F.3
  • 23
    • 0026760085 scopus 로고
    • Three DNA markers for hypophosphataemic rickets
    • Rowe PSN, Read AP, Mountford RC, et al. Three DNA markers for hypophosphataemic rickets. Hum Genet 1992; 89: 539-542.
    • (1992) Hum Genet , vol.89 , pp. 539-542
    • Rowe, P.S.N.1    Read, A.P.2    Mountford, R.C.3
  • 24
    • 0029160578 scopus 로고
    • A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphatemic rickets. The HYP Consortium
    • HYP-consortium
    • HYP-consortium, Francis F, Hennig S, et al. A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphatemic rickets. The HYP Consortium. Nat Genet 1995; 11(2): 130-136.
    • (1995) Nat Genet , vol.11 , Issue.2 , pp. 130-136
    • Francis, F.1    Hennig, S.2
  • 25
    • 0029878274 scopus 로고    scopus 로고
    • Candidate 56 and 58 kDa protein(s) responsible for mediating the renal defects in oncogenic hypophosphataemic osteomalacia
    • Rowe PSN, Ong A, Cockerill F, Goulding J, Hewison M. Candidate 56 and 58 kDa protein(s) responsible for mediating the renal defects in oncogenic hypophosphataemic osteomalacia. Bone 1996; 18(2): 159-169.
    • (1996) Bone , vol.18 , Issue.2 , pp. 159-169
    • Rowe, P.S.N.1    Ong, A.2    Cockerill, F.3    Goulding, J.4    Hewison, M.5
  • 26
    • 0036606203 scopus 로고    scopus 로고
    • M13 endopeptidases: new conserved motifs correlated with structure, and simultaneous phylogenetic occurrence of PHEX and the bony fish
    • Bianchetti L, Oudet C, Poch O. M13 endopeptidases: new conserved motifs correlated with structure, and simultaneous phylogenetic occurrence of PHEX and the bony fish. Proteins 2002; 47(4): 481-188.
    • (2002) Proteins , vol.47 , Issue.4 , pp. 481-188
    • Bianchetti, L.1    Oudet, C.2    Poch, O.3
  • 28
    • 0038201945 scopus 로고    scopus 로고
    • Exploring the structure and function of zinc metallopeptidases: old enzymes and new discoveries
    • Turner AJ. Exploring the structure and function of zinc metallopeptidases: old enzymes and new discoveries. Biochem Soc Trans 2003; 31(Pt 3): 723-727.
    • (2003) Biochem Soc Trans , vol.31 , Issue.PART 3 , pp. 723-727
    • Turner, A.J.1
  • 29
    • 0035112440 scopus 로고    scopus 로고
    • The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function
    • Turner AJ, Isaac RE, Coates D. The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function. Bioessays 2001; 23(3): 261-269.
    • (2001) Bioessays , vol.23 , Issue.3 , pp. 261-269
    • Turner, A.J.1    Isaac, R.E.2    Coates, D.3
  • 30
    • 33947385485 scopus 로고    scopus 로고
    • Phosphorylated acidic serine-aspartate-rich MEPE-associated motif peptide from matrix extracellular phosphoglycoprotein inhibits phosphate regulating gene with homologies to endopeptidases on the X-chromosome enzyme activity
    • Liu S, Rowe PS, Vierthaler L, Zhou J, Quarles LD. Phosphorylated acidic serine-aspartate-rich MEPE-associated motif peptide from matrix extracellular phosphoglycoprotein inhibits phosphate regulating gene with homologies to endopeptidases on the X-chromosome enzyme activity. J Endocrinol 2007; 192(1): 261-267.
    • (2007) J Endocrinol , vol.192 , Issue.1 , pp. 261-267
    • Liu, S.1    Rowe, P.S.2    Vierthaler, L.3    Zhou, J.4    Quarles, L.D.5
  • 31
    • 41549134046 scopus 로고    scopus 로고
    • Degradation of MEPE, DMP1, and release of SIBLING ASARM-peptides (minhibins): ASARM-peptide(s) are directly responsible for defective mineralization in HYP
    • Martin A, David V, Laurence JS, et al. Degradation of MEPE, DMP1, and release of SIBLING ASARM-peptides (minhibins): ASARM-peptide(s) are directly responsible for defective mineralization in HYP. Endocrinology 2008; 149(4): 1757-1772.
    • (2008) Endocrinology , vol.149 , Issue.4 , pp. 1757-1772
    • Martin, A.1    David, V.2    Laurence, J.S.3
  • 32
    • 12344250943 scopus 로고    scopus 로고
    • Surface Plasmon Resonance (SPR) confirms MEPE binds to PHEX via the MEPE-ASARM-motif: a model for impaired mineralization in X-linked rickets (HYP)
    • Rowe PSN, Garrett IR, Schwarz PM, et al. Surface Plasmon Resonance (SPR) confirms MEPE binds to PHEX via the MEPE-ASARM-motif: a model for impaired mineralization in X-linked rickets (HYP). Bone 2005; 36(1): 33-46.
    • (2005) Bone , vol.36 , Issue.1 , pp. 33-46
    • Rowe, P.S.N.1    Garrett, I.R.2    Schwarz, P.M.3
  • 33
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley LA, Sternberg MJ. Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 2009; 4(3): 363-371.
    • (2009) Nat Protoc , vol.4 , Issue.3 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 34
    • 77953229051 scopus 로고    scopus 로고
    • Phosphorylation-dependent inhibition of mineralization by osteopontin ASARM peptides is regulated by PHEX cleavage
    • Addison W, Masica D, Gray J, McKee MD. Phosphorylation-dependent inhibition of mineralization by osteopontin ASARM peptides is regulated by PHEX cleavage. J Bone Miner Res 2009; 25(4): 695-705.
    • (2009) J Bone Miner Res , vol.25 , Issue.4 , pp. 695-705
    • Addison, W.1    Masica, D.2    Gray, J.3    McKee, M.D.4
  • 35
    • 69249117464 scopus 로고    scopus 로고
    • Matrix extracellular phosphoglycoprotein (MEPE) is a new bone renal hormone and vascularization modulator
    • David V, Martin A, Hedge AM, Rowe PS. Matrix extracellular phosphoglycoprotein (MEPE) is a new bone renal hormone and vascularization modulator. Endocrinology 2009; 150(9): 4012-4023.
    • (2009) Endocrinology , vol.150 , Issue.9 , pp. 4012-4023
    • David, V.1    Martin, A.2    Hedge, A.M.3    Rowe, P.S.4
  • 36
    • 0038343128 scopus 로고    scopus 로고
    • Human recombinant endopeptidase PHEX has a strict S1' specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein
    • Campos M, Couture C, Hirata IY, et al. Human recombinant endopeptidase PHEX has a strict S1' specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein. Biochem J 2003; 373(1): 271-279.
    • (2003) Biochem J , vol.373 , Issue.1 , pp. 271-279
    • Campos, M.1    Couture, C.2    Hirata, I.Y.3
  • 37
    • 52949134423 scopus 로고    scopus 로고
    • MEPE-ASARM peptides control extracellular matrix mineralization by binding to hydroxyapatite - an inhibition regulated by PHEX cleavage of ASARM
    • Addison W, Nakano Y, Loisel T, Crine P, McKee M. MEPE-ASARM peptides control extracellular matrix mineralization by binding to hydroxyapatite - an inhibition regulated by PHEX cleavage of ASARM. J Bone Miner Res 2008; 23(10): 1638-1649.
    • (2008) J Bone Miner Res , vol.23 , Issue.10 , pp. 1638-1649
    • Addison, W.1    Nakano, Y.2    Loisel, T.3    Crine, P.4    McKee, M.5
  • 38
    • 33748376254 scopus 로고    scopus 로고
    • Correction of the mineralization defect in hyp mice treated with protease inhibitors CA074 and pepstatin
    • Rowe PS, Matsumoto N, Jo OD, et al. Correction of the mineralization defect in hyp mice treated with protease inhibitors CA074 and pepstatin. Bone 2006; 39(4): 773-786.
    • (2006) Bone , vol.39 , Issue.4 , pp. 773-786
    • Rowe, P.S.1    Matsumoto, N.2    Jo, O.D.3
  • 39
    • 79954637641 scopus 로고    scopus 로고
    • Sclerostin is a locally acting regulator of late-osteoblast/pre-osteocyte differentiation and regulates mineralization through a MEPE-ASARM dependent mechanism
    • Atkins GJ, Rowe PS, Lim HP, et al. Sclerostin is a locally acting regulator of late-osteoblast/pre-osteocyte differentiation and regulates mineralization through a MEPE-ASARM dependent mechanism. J Bone Miner Res 2011; 27(7): 1425-1436.
    • (2011) J Bone Miner Res , vol.27 , Issue.7 , pp. 1425-1436
    • Atkins, G.J.1    Rowe, P.S.2    Lim, H.P.3
  • 41
    • 10744226781 scopus 로고    scopus 로고
    • MEPE has the properties of an osteoblastic phosphatonin and minhibin
    • Rowe PSN, Kumagai Y, Gutierrez G, et al. MEPE has the properties of an osteoblastic phosphatonin and minhibin. Bone 2004; 34(2): 303-319.
    • (2004) Bone , vol.34 , Issue.2 , pp. 303-319
    • Rowe, P.S.N.1    Kumagai, Y.2    Gutierrez, G.3
  • 43
    • 44449138422 scopus 로고    scopus 로고
    • Matrix extracellular phosphoglycoprotein causes phosphaturia in rats by inhibiting tubular phosphate reabsorption
    • Dobbie H, Unwin RJ, Faria NJ, Shirley DG. Matrix extracellular phosphoglycoprotein causes phosphaturia in rats by inhibiting tubular phosphate reabsorption. Nephrol Dial Transplant 2008; 23(2): 730-733.
    • (2008) Nephrol Dial Transplant , vol.23 , Issue.2 , pp. 730-733
    • Dobbie, H.1    Unwin, R.J.2    Faria, N.J.3    Shirley, D.G.4
  • 44
    • 57149108326 scopus 로고    scopus 로고
    • The phosphatonin matrix extracellular phosphoglycoprotein (MEPE) inhibits renal intestinal phosphate transport in vivo
    • Marks J, Churchill LJ, Edward SD, Unwin R. The phosphatonin matrix extracellular phosphoglycoprotein (MEPE) inhibits renal intestinal phosphate transport in vivo. J Am Soc Nephrol 2008; 19(12): 2313-2320.
    • (2008) J Am Soc Nephrol , vol.19 , Issue.12 , pp. 2313-2320
    • Marks, J.1    Churchill, L.J.2    Edward, S.D.3    Unwin, R.4
  • 45
    • 77957228924 scopus 로고    scopus 로고
    • Direct micropuncture evidence that matrix extracellular phosphoglycoprotein inhibits proximal tubular phosphate reabsorption
    • Shirley DG, Faria NJ, Unwin RJ, Dobbie H. Direct micropuncture evidence that matrix extracellular phosphoglycoprotein inhibits proximal tubular phosphate reabsorption. Nephrol Dial Transplant 2010; 25(10): 3191-315.
    • (2010) Nephrol Dial Transplant , vol.25 , Issue.10 , pp. 3191-3315
    • Shirley, D.G.1    Faria, N.J.2    Unwin, R.J.3    Dobbie, H.4
  • 46
    • 77957226068 scopus 로고    scopus 로고
    • Welcome to MEPE in the renal proximal tubule
    • Friedlander G. Welcome to MEPE in the renal proximal tubule. Nephrol Dial Transplant 2010; 25(10): 3135-3136.
    • (2010) Nephrol Dial Transplant , vol.25 , Issue.10 , pp. 3135-3136
    • Friedlander, G.1
  • 47
    • 0034963551 scopus 로고    scopus 로고
    • Phosphorylated osteopontin peptides suppress crystallization by inhibiting the growth of calcium oxalate crystals
    • Hoyer JR, Asplin JR, Otvos L. Phosphorylated osteopontin peptides suppress crystallization by inhibiting the growth of calcium oxalate crystals. Kidney Int 2001; 60(1): 77-82.
    • (2001) Kidney Int , vol.60 , Issue.1 , pp. 77-82
    • Hoyer, J.R.1    Asplin, J.R.2    Otvos, L.3
  • 48
    • 0014684364 scopus 로고
    • Diphosphonates inhibit formation of calcium phosphate crystals in vitro and pathological calcification in vivo
    • Francis MD, Russell RG, Fleisch H. Diphosphonates inhibit formation of calcium phosphate crystals in vitro and pathological calcification in vivo. Science 1969; 165(899): 1264-1266.
    • (1969) Science , vol.165 , Issue.899 , pp. 1264-1266
    • Francis, M.D.1    Russell, R.G.2    Fleisch, H.3
  • 49
    • 34247527341 scopus 로고    scopus 로고
    • Thermodynamic roles of basic amino acids in statherin recognition of hydroxyapatite
    • Epub 2007 Mar 29.
    • Goobes R, Goobes G, Shaw WJ, Drobny GP, Campbell CT, Stayton PS. Thermodynamic roles of basic amino acids in statherin recognition of hydroxyapatite. Biochemistry 2007; 46(16):4725-4733 Epub 2007 Mar 29.
    • (2007) Biochemistry , vol.46 , Issue.16 , pp. 4725-4733
    • Goobes, R.1    Goobes, G.2    Shaw, W.J.3    Drobny, G.P.4    Campbell, C.T.5    Stayton, P.S.6
  • 50
    • 0017348985 scopus 로고
    • Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva
    • Schlesinger DH, Hay DI. Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva. J Biol Chem 1977; 252(5): 1689-1695.
    • (1977) J Biol Chem , vol.252 , Issue.5 , pp. 1689-1695
    • Schlesinger, D.H.1    Hay, D.I.2
  • 51
    • 33750454816 scopus 로고    scopus 로고
    • Loss of DMP1 causes rickets and osteomalacia and identifies a role for osteocytes in mineral metabolism
    • Feng JQ, Ward LM, Liu S, et al. Loss of DMP1 causes rickets and osteomalacia and identifies a role for osteocytes in mineral metabolism. Nat Genet 2006; 38(11): 1310-1315.
    • (2006) Nat Genet , vol.38 , Issue.11 , pp. 1310-1315
    • Feng, J.Q.1    Ward, L.M.2    Liu, S.3
  • 52
    • 33750427897 scopus 로고    scopus 로고
    • DMP1 mutations in autosomal recessive hypophosphatemia implicate a bone matrix protein in the regulation of phosphate homeostasis
    • Lorenz-Depiereux B, Bastepe M, Benet-Pages A, et al. DMP1 mutations in autosomal recessive hypophosphatemia implicate a bone matrix protein in the regulation of phosphate homeostasis. Nat Genet 2006; 38(11): 1248-1250.
    • (2006) Nat Genet , vol.38 , Issue.11 , pp. 1248-1250
    • Lorenz-Depiereux, B.1    Bastepe, M.2    Benet-Pages, A.3
  • 53
    • 0037449817 scopus 로고    scopus 로고
    • Targeted disruption of the osteoblast/osteocyte factor 45 gene (OF45) results in increased bone formation and bone mass
    • Gowen LC, Petersen DN, Mansolf AL, et al. Targeted disruption of the osteoblast/osteocyte factor 45 gene (OF45) results in increased bone formation and bone mass. J Biol Chem 2003; 278(3): 1998-2007.
    • (2003) J Biol Chem , vol.278 , Issue.3 , pp. 1998-2007
    • Gowen, L.C.1    Petersen, D.N.2    Mansolf, A.L.3
  • 54
    • 79953297925 scopus 로고    scopus 로고
    • Genetic analysis of vertebral trabecular bone density and cross-sectional area in older men
    • Zmuda JM, Yerges-Armstrong LM, Moffett SP, et al. Genetic analysis of vertebral trabecular bone density and cross-sectional area in older men. Osteoporos Int 2011; 22(4): 1079-1090.
    • (2011) Osteoporos Int , vol.22 , Issue.4 , pp. 1079-1090
    • Zmuda, J.M.1    Yerges-Armstrong, L.M.2    Moffett, S.P.3
  • 55
    • 79960653147 scopus 로고    scopus 로고
    • Molecular disease map of bone characterizing the postmenopausal osteoporosis phenotype
    • Jemtland R, Holden M, Reppe S, et al. Molecular disease map of bone characterizing the postmenopausal osteoporosis phenotype. J Bone Miner Res 2011; 26(8): 1793-1801.
    • (2011) J Bone Miner Res , vol.26 , Issue.8 , pp. 1793-1801
    • Jemtland, R.1    Holden, M.2    Reppe, S.3
  • 56
    • 78049233765 scopus 로고    scopus 로고
    • European bone mineral density loci are also associated with BMD in East-Asian populations
    • PMCID: 2951352.
    • Styrkarsdottir U, Halldorsson BV, Gudbjartsson DF, et al. European bone mineral density loci are also associated with BMD in East-Asian populations. PLoS One 2010; 5(10):e13217. PMCID: 2951352.
    • (2010) PLoS One , vol.5 , Issue.10
    • Styrkarsdottir, U.1    Halldorsson, B.V.2    Gudbjartsson, D.F.3
  • 57
    • 70350646912 scopus 로고    scopus 로고
    • Twenty bone-mineral-density loci identified by large-scale meta-analysis of genome-wide association studies
    • Rivadeneira F, Styrkarsdottir U, Estrada K, et al. Twenty bone-mineral-density loci identified by large-scale meta-analysis of genome-wide association studies. Nat Genet 2009; 41(11): 1199-1206.
    • (2009) Nat Genet , vol.41 , Issue.11 , pp. 1199-1206
    • Rivadeneira, F.1    Styrkarsdottir, U.2    Estrada, K.3
  • 58
    • 78650180083 scopus 로고    scopus 로고
    • Inhibition of osteoclastogenesis by mechanically loaded osteocytes: involvement of MEPE
    • PMCID: 2964475.
    • Kulkarni RN, Bakker AD, Everts V, Klein-Nulend J. Inhibition of osteoclastogenesis by mechanically loaded osteocytes: involvement of MEPE. Calcif Tissue Int 2010; 87(5):461-468. PMCID: 2964475.
    • (2010) Calcif Tissue Int , vol.87 , Issue.5 , pp. 461-468
    • Kulkarni, R.N.1    Bakker, A.D.2    Everts, V.3    Klein-Nulend, J.4
  • 59
    • 34247571847 scopus 로고    scopus 로고
    • MEPE expression in osteocytes during orthodontic tooth movement
    • PMCID: 1868431.
    • Gluhak-Heinrich J, Pavlin D, Yang W, MacDougall M, Harris SE. MEPE expression in osteocytes during orthodontic tooth movement. Arch Oral Biol 2007; 52(7):684-690. PMCID: 1868431.
    • (2007) Arch Oral Biol , vol.52 , Issue.7 , pp. 684-690
    • Gluhak-Heinrich, J.1    Pavlin, D.2    Yang, W.3    MacDougall, M.4    Harris, S.E.5
  • 60
    • 38449108005 scopus 로고    scopus 로고
    • Regulation of osteoclast differentiation and function by phosphate: potential role of osteoclasts in the skeletal abnormalities in hypophosphatemic conditions
    • Hayashibara T, Hiraga T, Sugita A, et al. Regulation of osteoclast differentiation and function by phosphate: potential role of osteoclasts in the skeletal abnormalities in hypophosphatemic conditions. J Bone Miner Res 2007; 22(11): 1743-1751.
    • (2007) J Bone Miner Res , vol.22 , Issue.11 , pp. 1743-1751
    • Hayashibara, T.1    Hiraga, T.2    Sugita, A.3
  • 61
    • 43749122869 scopus 로고    scopus 로고
    • DMP1 and MEPE expression are elevated in osteocytes after mechanical loading in vivo: theoretical role in controlling mineral quality in the perilacunar matrix
    • Harris SE, Gluhak-Heinrich J, Harris MA, et al. DMP1 and MEPE expression are elevated in osteocytes after mechanical loading in vivo: theoretical role in controlling mineral quality in the perilacunar matrix. J Musculoskelet Neuronal Interact 2007; 7(4): 313-315.
    • (2007) J Musculoskelet Neuronal Interact , vol.7 , Issue.4 , pp. 313-315
    • Harris, S.E.1    Gluhak-Heinrich, J.2    Harris, M.A.3
  • 62
    • 2442675051 scopus 로고    scopus 로고
    • Matrix extracellular phosphoglycoprotein (MEPE) is highly expressed in osteocytes in human bone
    • Nampei A, Hashimoto J, Hayashida K, et al. Matrix extracellular phosphoglycoprotein (MEPE) is highly expressed in osteocytes in human bone. J Bone Miner Metab 2004; 22(3): 176-184.
    • (2004) J Bone Miner Metab , vol.22 , Issue.3 , pp. 176-184
    • Nampei, A.1    Hashimoto, J.2    Hayashida, K.3
  • 63
    • 35548953505 scopus 로고    scopus 로고
    • Immunolocalization of SIBLING and RUNX2 proteins during vertical distraction osteogenesis in the human mandible
    • Amir LR, Jovanovic A, Perdijk FB, Toyosawa S, Everts V, Bronckers AL. Immunolocalization of SIBLING and RUNX2 proteins during vertical distraction osteogenesis in the human mandible. J Histochem Cytochem 2007; 55(11): 1095-1104.
    • (2007) J Histochem Cytochem , vol.55 , Issue.11 , pp. 1095-1104
    • Amir, L.R.1    Jovanovic, A.2    Perdijk, F.B.3    Toyosawa, S.4    Everts, V.5    Bronckers, A.L.6
  • 65
    • 58149109303 scopus 로고    scopus 로고
    • Recent advances in the renal-skeletal-gut axis that controls phosphate homeostasis
    • Kiela PR, Ghishan FK. Recent advances in the renal-skeletal-gut axis that controls phosphate homeostasis. Lab Invest 2009; 89(1): 7-14.
    • (2009) Lab Invest , vol.89 , Issue.1 , pp. 7-14
    • Kiela, P.R.1    Ghishan, F.K.2
  • 66
    • 69249205598 scopus 로고    scopus 로고
    • A paradigm of integrative physiology, the crosstalk between bone and energy metabolisms
    • Confavreux CB, Levine RL, Karsenty G. A paradigm of integrative physiology, the crosstalk between bone and energy metabolisms. Mol Cell Endocrinol 2009; 310(1-2): 21-9.
    • (2009) Mol Cell Endocrinol , vol.310 , Issue.1-2 , pp. 21-29
    • Confavreux, C.B.1    Levine, R.L.2    Karsenty, G.3
  • 67
    • 84860337972 scopus 로고    scopus 로고
    • PHEX & MEPE ASARM-motif regulate a novel bone-renal and fat-mass pathway (abstract)
    • Abstract:
    • David V, Martin A, Hedge AM, Rowe PS. PHEX & MEPE ASARM-motif regulate a novel bone-renal and fat-mass pathway (abstract). J Bone Miner Res 2009; 24(Suppl 1): Abstract:.
    • (2009) J Bone Miner Res , vol.24 , Issue.SUPPL. 1
    • David, V.1    Martin, A.2    Hedge, A.M.3    Rowe, P.S.4
  • 68
    • 0034680755 scopus 로고    scopus 로고
    • Identification of osteoblast/osteocyte factor 45 (OF45), a bone-specific cDNA encoding an RGD-containing protein that is highly expressed in osteoblasts and osteocytes
    • Petersen DN, Tkalcevic GT, Mansolf AL, Rivera-Gonzalez R, Brown TA. Identification of osteoblast/osteocyte factor 45 (OF45), a bone-specific cDNA encoding an RGD-containing protein that is highly expressed in osteoblasts and osteocytes. J Biol Chem 2000; 275(46): 36172-36180.
    • (2000) J Biol Chem , vol.275 , Issue.46 , pp. 36172-36180
    • Petersen, D.N.1    Tkalcevic, G.T.2    Mansolf, A.L.3    Rivera-Gonzalez, R.4    Brown, T.A.5
  • 69
    • 0035874943 scopus 로고    scopus 로고
    • Mepe, the gene encoding a tumor-secreted protein in oncogenic hypophosphatemic osteomalacia, is expressed in bone
    • Argiro L, Desbarats M, Glorieux FH, Ecarot B. Mepe, the gene encoding a tumor-secreted protein in oncogenic hypophosphatemic osteomalacia, is expressed in bone. Genomics 2001; 74(3): 342-351.
    • (2001) Genomics , vol.74 , Issue.3 , pp. 342-351
    • Argiro, L.1    Desbarats, M.2    Glorieux, F.H.3    Ecarot, B.4
  • 70
    • 0026621517 scopus 로고
    • Isolation, characterization and immunolocalization of a 53-kDal dentin sialoprotein (DSP)
    • Butler WT, Bhown M, Brunn JC, et al. Isolation, characterization and immunolocalization of a 53-kDal dentin sialoprotein (DSP). Matrix 1992; 12(5): 343-351.
    • (1992) Matrix , vol.12 , Issue.5 , pp. 343-351
    • Butler, W.T.1    Bhown, M.2    Brunn, J.C.3
  • 71
    • 0028031161 scopus 로고
    • Cloning and sequence determination of rat dentin sialoprotein, a novel dentin protein
    • Ritchie HH, Hou H, Veis A, Butler WT. Cloning and sequence determination of rat dentin sialoprotein, a novel dentin protein. J Biol Chem 1994; 269(5): 3698-3702.
    • (1994) J Biol Chem , vol.269 , Issue.5 , pp. 3698-3702
    • Ritchie, H.H.1    Hou, H.2    Veis, A.3    Butler, W.T.4
  • 72
    • 0019332638 scopus 로고
    • Noncollagenous proteins of dentin. A re-examination of proteins from rat incisor dentin utilizing techniques to avoid artifacts
    • Linde A, Bhown M, Butler WT. Noncollagenous proteins of dentin. A re-examination of proteins from rat incisor dentin utilizing techniques to avoid artifacts. J Biol Chem 1980; 255(12): 5931-5942.
    • (1980) J Biol Chem , vol.255 , Issue.12 , pp. 5931-5942
    • Linde, A.1    Bhown, M.2    Butler, W.T.3
  • 73
    • 0031021422 scopus 로고    scopus 로고
    • Dentin phosphoprotein and dentin sialoprotein are cleavage products expressed from a single transcript coded by a gene on human chromosome 4. Dentin phosphoprotein DNA sequence determination
    • MacDougall M, Simmons D, Luan X, Nydegger J, Feng J, Gu TT. Dentin phosphoprotein and dentin sialoprotein are cleavage products expressed from a single transcript coded by a gene on human chromosome 4. Dentin phosphoprotein DNA sequence determination. J Biol Chem 1997; 272: 835-842.
    • (1997) J Biol Chem , vol.272 , pp. 835-842
    • MacDougall, M.1    Simmons, D.2    Luan, X.3    Nydegger, J.4    Feng, J.5    Gu, T.T.6
  • 74
    • 0029810860 scopus 로고    scopus 로고
    • Sequence determination of an extremely acidic rat dentin phosphoprotein
    • Ritchie HH, Wang LH. Sequence determination of an extremely acidic rat dentin phosphoprotein. J Biol Chem 1996; 271(36): 21695-21698.
    • (1996) J Biol Chem , vol.271 , Issue.36 , pp. 21695-21698
    • Ritchie, H.H.1    Wang, L.H.2
  • 75
    • 20444432696 scopus 로고    scopus 로고
    • Dentin glycoprotein: the protein in the middle of the dentin sialophosphoprotein chimera
    • Yamakoshi Y, Hu JC, Fukae M, Zhang H, Simmer JP. Dentin glycoprotein: the protein in the middle of the dentin sialophosphoprotein chimera. J Biol Chem 2005; 280(17): 17472-17479.
    • (2005) J Biol Chem , vol.280 , Issue.17 , pp. 17472-17479
    • Yamakoshi, Y.1    Hu, J.C.2    Fukae, M.3    Zhang, H.4    Simmer, J.P.5
  • 76
    • 78650935427 scopus 로고    scopus 로고
    • Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp)
    • Tsuchiya S, Simmer JP, Hu JC, Richardson AS, Yamakoshi F, Yamakoshi Y. Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp). J Bone Miner Res 2011; 26(1): 220-228.
    • (2011) J Bone Miner Res , vol.26 , Issue.1 , pp. 220-228
    • Tsuchiya, S.1    Simmer, J.P.2    Hu, J.C.3    Richardson, A.S.4    Yamakoshi, F.5    Yamakoshi, Y.6
  • 77
    • 11244270453 scopus 로고    scopus 로고
    • Serum MEPE-ASARM-peptides are elevated in X-linked rickets (HYP): implications for phosphaturia and rickets
    • Bresler D, Bruder J, Mohnike KL, Fraser D, Rowe PSN. Serum MEPE-ASARM-peptides are elevated in X-linked rickets (HYP): implications for phosphaturia and rickets. J Endocrinol 2004; 183: R1-9.
    • (2004) J Endocrinol , vol.183
    • Bresler, D.1    Bruder, J.2    Mohnike, K.L.3    Fraser, D.4    Rowe, P.S.N.5
  • 80
    • 79954617739 scopus 로고    scopus 로고
    • MEPE activated by furin promotes pulpal cell adhesion
    • Wang HG, Kawashima N, Iwata T, et al. MEPE activated by furin promotes pulpal cell adhesion. J Dent Res 2011; 90(4): 529-534.
    • (2011) J Dent Res , vol.90 , Issue.4 , pp. 529-534
    • Wang, H.G.1    Kawashima, N.2    Iwata, T.3
  • 81
    • 49149124472 scopus 로고    scopus 로고
    • ASARM-truncated MEPE and AC-100 enhance osteogenesis by promoting osteoprogenitor adhesion
    • Sprowson AP, McCaskie AW, Birch MA. ASARM-truncated MEPE and AC-100 enhance osteogenesis by promoting osteoprogenitor adhesion. J Orthop Res 2008; 26(9): 1256-1262.
    • (2008) J Orthop Res , vol.26 , Issue.9 , pp. 1256-1262
    • Sprowson, A.P.1    McCaskie, A.W.2    Birch, M.A.3
  • 82
    • 57449114377 scopus 로고    scopus 로고
    • Dentin noncollagenous matrix proteins in familial hypophosphatemic rickets
    • Gaucher C, Boukpessi T, Septier D, et al. Dentin noncollagenous matrix proteins in familial hypophosphatemic rickets. Cells Tissues Organs 2009; 189(1-4): 219-223.
    • (2009) Cells Tissues Organs , vol.189 , Issue.1-4 , pp. 219-223
    • Gaucher, C.1    Boukpessi, T.2    Septier, D.3
  • 83
    • 21644453949 scopus 로고    scopus 로고
    • A fragment of the hypophosphatemic factor, MEPE, requires inducible cyclooxygenase-2 to exert potent anabolic effects on normal human marrow osteoblast precursors
    • Nagel DE, Khosla S, Sanyal A, Rosen DM, Kumagai Y, Riggs BL. A fragment of the hypophosphatemic factor, MEPE, requires inducible cyclooxygenase-2 to exert potent anabolic effects on normal human marrow osteoblast precursors. J Cell Biochem 2004; 93(6): 1107-1114.
    • (2004) J Cell Biochem , vol.93 , Issue.6 , pp. 1107-1114
    • Nagel, D.E.1    Khosla, S.2    Sanyal, A.3    Rosen, D.M.4    Kumagai, Y.5    Riggs, B.L.6
  • 84
    • 33644831899 scopus 로고    scopus 로고
    • The impact of bioactive molecules to stimulate tooth repair and regeneration as part of restorative dentistry
    • Goldberg M, Lacerda-Pinheiro S, Jegat N, et al. The impact of bioactive molecules to stimulate tooth repair and regeneration as part of restorative dentistry. Dent Clin North Am 2006; 50(2): 277-298.
    • (2006) Dent Clin North Am , vol.50 , Issue.2 , pp. 277-298
    • Goldberg, M.1    Lacerda-Pinheiro, S.2    Jegat, N.3
  • 85
    • 3042778752 scopus 로고    scopus 로고
    • Dentonin, a fragment of MEPE, enhanced dental pulp stem cell proliferation
    • Liu H, Li W, Gao C, Kumagai Y, Blacher RW, DenBesten PK. Dentonin, a fragment of MEPE, enhanced dental pulp stem cell proliferation. J Dent Res 2004; 83(6): 496-499.
    • (2004) J Dent Res , vol.83 , Issue.6 , pp. 496-499
    • Liu, H.1    Li, W.2    Gao, C.3    Kumagai, Y.4    Blacher, R.W.5    DenBesten, P.K.6
  • 87
    • 47249127594 scopus 로고    scopus 로고
    • Expression and processing of small integrin-binding ligand N-linked glycoproteins in mouse odontoblastic cells
    • Chen S, Chen L, Jahangiri A, et al. Expression and processing of small integrin-binding ligand N-linked glycoproteins in mouse odontoblastic cells. Arch Oral Biol 2008; 53(9):879-889.
    • (2008) Arch Oral Biol , vol.53 , Issue.9 , pp. 879-889
    • Chen, S.1    Chen, L.2    Jahangiri, A.3
  • 88
    • 0029146115 scopus 로고
    • Osteopontin and related phosphorylated sialoproteins: effects on mineralization
    • Boskey AL. Osteopontin and related phosphorylated sialoproteins: effects on mineralization. Ann N Y Acad Sci 1995; 760: 249-256.
    • (1995) Ann N Y Acad Sci , vol.760 , pp. 249-256
    • Boskey, A.L.1
  • 89
    • 73649134967 scopus 로고    scopus 로고
    • MEPE's diverse effects on mineralization
    • Boskey AL, Chiang P, Fermanis A, et al. MEPE's diverse effects on mineralization. Calcif Tissue Int 2010; 86(1): 42-46.
    • (2010) Calcif Tissue Int , vol.86 , Issue.1 , pp. 42-46
    • Boskey, A.L.1    Chiang, P.2    Fermanis, A.3
  • 90
    • 80051514375 scopus 로고    scopus 로고
    • Primary structure and phosphorylation of dentin matrix protein 1 (DMP1) and dentin phosphophoryn (DPP) uniquely determine their role in biomineralization
    • PMCID: 3171794.
    • Deshpande AS, Fang PA, Zhang X, Jayaraman T, Sfeir C, Beniash E. Primary structure and phosphorylation of dentin matrix protein 1 (DMP1) and dentin phosphophoryn (DPP) uniquely determine their role in biomineralization. Biomacromolecules 2011; 12(8):2933-2945. PMCID: 3171794.
    • (2011) Biomacromolecules , vol.12 , Issue.8 , pp. 2933-2945
    • Deshpande, A.S.1    Fang, P.A.2    Zhang, X.3    Jayaraman, T.4    Sfeir, C.5    Beniash, E.6
  • 91
    • 77957288774 scopus 로고    scopus 로고
    • Abnormal presence of the matrix extracellular phosphoglycoprotein-derived acidic serine- and aspartate-rich motif peptide in human hypophosphatemic dentin
    • PMCID: 2913338.
    • Boukpessi T, Gaucher C, Leger T, et al. Abnormal presence of the matrix extracellular phosphoglycoprotein-derived acidic serine- and aspartate-rich motif peptide in human hypophosphatemic dentin. Am J Pathol 2010; 177(2):803-12. PMCID: 2913338.
    • (2010) Am J Pathol , vol.177 , Issue.2 , pp. 803-812
    • Boukpessi, T.1    Gaucher, C.2    Leger, T.3
  • 93
    • 77957675490 scopus 로고    scopus 로고
    • DMP1 C-terminal mutant mice recapture the human ARHR tooth phenotype
    • Jiang B, Cao Z, Lu Y, et al. DMP1 C-terminal mutant mice recapture the human ARHR tooth phenotype. J Bone Miner Res 2010; 25(10): 2155-2164.
    • (2010) J Bone Miner Res , vol.25 , Issue.10 , pp. 2155-2164
    • Jiang, B.1    Cao, Z.2    Lu, Y.3
  • 94
    • 24944550165 scopus 로고    scopus 로고
    • Renal expression of SIBLING proteins and their partner matrix metalloproteinases (MMPs)
    • Ogbureke KU, Fisher LW. Renal expression of SIBLING proteins and their partner matrix metalloproteinases (MMPs). Kidney Int 2005; 68(1): 155-166.
    • (2005) Kidney Int , vol.68 , Issue.1 , pp. 155-166
    • Ogbureke, K.U.1    Fisher, L.W.2
  • 95
    • 0032574725 scopus 로고    scopus 로고
    • Targeted inactivation of Npt2 in mice leads to severe renal phosphate wasting, hypercalciuria, and skeletal abnormalities
    • Beck L, Karaplis AC, Amizuka N, Hewson AS, Ozawa H, Tenenhouse HS. Targeted inactivation of Npt2 in mice leads to severe renal phosphate wasting, hypercalciuria, and skeletal abnormalities. Proc Natl Acad Sci USA 1998; 95: 5372-5377.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5372-5377
    • Beck, L.1    Karaplis, A.C.2    Amizuka, N.3    Hewson, A.S.4    Ozawa, H.5    Tenenhouse, H.S.6
  • 96
    • 0012311140 scopus 로고    scopus 로고
    • Renal calcification in mice homozygous for the disrupted type IIa Na/Pi cotransporter gene Npt2
    • Chau H, El-Maadawy S, McKee MD, Tenenhouse HS. Renal calcification in mice homozygous for the disrupted type IIa Na/Pi cotransporter gene Npt2. J Bone Miner Res 2003; 18(4): 644-657.
    • (2003) J Bone Miner Res , vol.18 , Issue.4 , pp. 644-657
    • Chau, H.1    El-Maadawy, S.2    McKee, M.D.3    Tenenhouse, H.S.4
  • 97
    • 0034748185 scopus 로고    scopus 로고
    • Identification of the type II Na(+)-Pi cotransporter (Npt2) in the osteoclast and the skeletal phenotype of Npt2-/- mice
    • Gupta A, Tenenhouse HS, Hoag HM, et al. Identification of the type II Na(+)-Pi cotransporter (Npt2) in the osteoclast and the skeletal phenotype of Npt2-/- mice. Bone 2001; 29(5): 467-476.
    • (2001) Bone , vol.29 , Issue.5 , pp. 467-476
    • Gupta, A.1    Tenenhouse, H.S.2    Hoag, H.M.3
  • 98
    • 2142652987 scopus 로고    scopus 로고
    • 1{alpha}-Hydroxylase gene ablation and Pi supplementation inhibit renal calcification in mice homozygous for the disrupted Na/Pi cotransporter gene Npt2a
    • Tenenhouse HS, Gauthier C, Chau H, St-Arnaud R. 1{alpha}-Hydroxylase gene ablation and Pi supplementation inhibit renal calcification in mice homozygous for the disrupted Na/Pi cotransporter gene Npt2a. Am J Physiol Renal Physiol 2003; 286(4): F675-681.
    • (2003) Am J Physiol Renal Physiol , vol.286 , Issue.4
    • Tenenhouse, H.S.1    Gauthier, C.2    Chau, H.3    St-Arnaud, R.4
  • 99
    • 33644987045 scopus 로고    scopus 로고
    • Effects of aldosterone on the vasculature
    • Schiffrin EL. Effects of aldosterone on the vasculature. Hypertension 2006; 47(3): 312-318.
    • (2006) Hypertension , vol.47 , Issue.3 , pp. 312-318
    • Schiffrin, E.L.1
  • 100
    • 2142694344 scopus 로고    scopus 로고
    • Aldosterone enhances ischemia-induced neovascularization through angiotensin II-dependent pathway
    • Michel F, Ambroisine ML, Duriez M, Delcayre C, Levy BI, Silvestre JS. Aldosterone enhances ischemia-induced neovascularization through angiotensin II-dependent pathway. Circulation 2004; 109(16): 1933-1927.
    • (2004) Circulation , vol.109 , Issue.16 , pp. 1933-1927
    • Michel, F.1    Ambroisine, M.L.2    Duriez, M.3    Delcayre, C.4    Levy, B.I.5    Silvestre, J.S.6
  • 101
    • 33846963787 scopus 로고    scopus 로고
    • Aldosterone impairs vascular reactivity by decreasing glucose-6-phosphate dehydrogenase activity
    • Leopold JA, Dam A, Maron BA, et al. Aldosterone impairs vascular reactivity by decreasing glucose-6-phosphate dehydrogenase activity. Nat Med 2007; 13(2): 189-197.
    • (2007) Nat Med , vol.13 , Issue.2 , pp. 189-197
    • Leopold, J.A.1    Dam, A.2    Maron, B.A.3
  • 102
    • 58649096984 scopus 로고    scopus 로고
    • Activation of renin-angiotensin system induces osteoporosis independently of hypertension
    • Asaba Y, Ito M, Fumoto T, et al. Activation of renin-angiotensin system induces osteoporosis independently of hypertension. J Bone Miner Res 2008; 24(3): 241-250.
    • (2008) J Bone Miner Res , vol.24 , Issue.3 , pp. 241-250
    • Asaba, Y.1    Ito, M.2    Fumoto, T.3
  • 103
    • 46749101660 scopus 로고    scopus 로고
    • Angiotensin II accelerates osteoporosis by activating osteoclasts
    • Epub 008 Feb 6.
    • Shimizu H, Nakagami H, Osako MK, et al. Angiotensin II accelerates osteoporosis by activating osteoclasts. FASEB J 2008; 22(7):2465-2475. Epub 008 Feb 6.
    • (2008) FASEB J , vol.22 , Issue.7 , pp. 2465-2475
    • Shimizu, H.1    Nakagami, H.2    Osako, M.K.3
  • 104
    • 80052318645 scopus 로고    scopus 로고
    • Cross talk between the renin-angiotensin-aldosterone system and vitamin D-FGF-23-klotho in chronic kidney disease
    • PMCID: 3171931.
    • de Borst MH, Vervloet MG, ter Wee PM, Navis G. Cross talk between the renin-angiotensin-aldosterone system and vitamin D-FGF-23-klotho in chronic kidney disease. J Am Soc Nephrol 2011; 22(9):1603-1609. PMCID: 3171931.
    • (2011) J Am Soc Nephrol , vol.22 , Issue.9 , pp. 1603-1609
    • de Borst, M.H.1    Vervloet, M.G.2    ter Wee, P.M.3    Navis, G.4
  • 105
    • 38849170631 scopus 로고    scopus 로고
    • Aberrant Phex function in osteoblasts and osteocytes alone underlies murine X-linked hypophosphatemia
    • Yuan B, Takaiwa M, Clemens TL, et al. Aberrant Phex function in osteoblasts and osteocytes alone underlies murine X-linked hypophosphatemia. J Clin Invest 2008; 118(2): 722-734.
    • (2008) J Clin Invest , vol.118 , Issue.2 , pp. 722-734
    • Yuan, B.1    Takaiwa, M.2    Clemens, T.L.3
  • 106
    • 80051687775 scopus 로고    scopus 로고
    • Bone proteins PHEX and DMP1 regulate fibroblastic growth factor Fgf23 expression in osteocytes through a common pathway involving FGF receptor (FGFR) signaling
    • Martin A, Liu S, David V, et al. Bone proteins PHEX and DMP1 regulate fibroblastic growth factor Fgf23 expression in osteocytes through a common pathway involving FGF receptor (FGFR) signaling. FASEB J 2011; 25(8): 2551-2562.
    • (2011) FASEB J , vol.25 , Issue.8 , pp. 2551-2562
    • Martin, A.1    Liu, S.2    David, V.3
  • 107
    • 80051940630 scopus 로고    scopus 로고
    • Dentin matrix protein 1 (DMP1) signals via cell surface integrin
    • PMCID: 3190986.
    • Wu H, Teng PN, Jayaraman T, et al. Dentin matrix protein 1 (DMP1) signals via cell surface integrin. J Biol Chem 2011; 286(34):29462-29469. PMCID: 3190986.
    • (2011) J Biol Chem , vol.286 , Issue.34 , pp. 29462-29469
    • Wu, H.1    Teng, P.N.2    Jayaraman, T.3
  • 108
    • 80051795991 scopus 로고    scopus 로고
    • Activation of the ERK1/2 mitogen-activated protein kinase cascade by dentin matrix protein 1 promotes osteoblast differentiation
    • PMCID: 3178087.
    • Eapen A, Ramachandran A, Pratap J, George A. Activation of the ERK1/2 mitogen-activated protein kinase cascade by dentin matrix protein 1 promotes osteoblast differentiation. Cells Tissues Organs. 2011; 194(2-4):255-260. PMCID: 3178087.
    • (2011) Cells Tissues Organs , vol.194 , Issue.2-4 , pp. 255-260
    • Eapen, A.1    Ramachandran, A.2    Pratap, J.3    George, A.4
  • 109
    • 84860333695 scopus 로고    scopus 로고
    • Mechanism of hexa-D-arginine curative effects on the HYP phenotype (abstract)
    • Yuan B, Bowman S, Blank R, Lindberg I, Drezner MK. Mechanism of hexa-D-arginine curative effects on the HYP phenotype (abstract). J Bone Miner Res 2011; 26(Suppl 1):SA0032:.
    • (2011) J Bone Miner Res , vol.26 , Issue.SUPPL. 1
    • Yuan, B.1    Bowman, S.2    Blank, R.3    Lindberg, I.4    Drezner, M.K.5
  • 110
    • 84860336825 scopus 로고    scopus 로고
    • Hexa-D-arginine reversal of osteoblast 7B2 dysregulation in HYP-mice normalizes the HYP biochemical phenotype (abstract)
    • Presentation No: #1015)
    • Yuan B, Meudt J, Blank R, Feng J, Drezner MK. Hexa-D-arginine reversal of osteoblast 7B2 dysregulation in HYP-mice normalizes the HYP biochemical phenotype (abstract). J Bone Miner Res 2010; 25(Suppl 1):(Presentation No: #1015).
    • (2010) J Bone Miner Res , vol.25 , Issue.SUPPL. 1
    • Yuan, B.1    Meudt, J.2    Blank, R.3    Feng, J.4    Drezner, M.K.5
  • 111
    • 44449098317 scopus 로고    scopus 로고
    • Bone sialoprotein binding to matrix metalloproteinase-2 alters enzyme inhibition kinetics
    • PMCID: 2484124.
    • Jain A, Fisher LW, Fedarko NS. Bone sialoprotein binding to matrix metalloproteinase-2 alters enzyme inhibition kinetics. Biochemistry 2008; 47(22):5986-5995. PMCID: 2484124.
    • (2008) Biochemistry , vol.47 , Issue.22 , pp. 5986-5995
    • Jain, A.1    Fisher, L.W.2    Fedarko, N.S.3
  • 112
    • 3042703295 scopus 로고    scopus 로고
    • Three small integrin-binding ligand N-linked glycoproteins (SIBLINGs) bind and activate specific matrix metalloproteinases
    • Fedarko NS, Jain A, Karadag A, Fisher LW. Three small integrin-binding ligand N-linked glycoproteins (SIBLINGs) bind and activate specific matrix metalloproteinases. FASEB J 2004; 18(6): 734-736.
    • (2004) FASEB J , vol.18 , Issue.6 , pp. 734-736
    • Fedarko, N.S.1    Jain, A.2    Karadag, A.3    Fisher, L.W.4
  • 114
    • 29244468885 scopus 로고    scopus 로고
    • Dentin matrix protein 1 enhances invasion potential of colon cancer cells by bridging matrix metalloproteinase-9 to integrins and CD44
    • PMCID: 1350722.
    • Karadag A, Fedarko NS, Fisher LW. Dentin matrix protein 1 enhances invasion potential of colon cancer cells by bridging matrix metalloproteinase-9 to integrins and CD44. Cancer Res 2005; 65(24):11545-11552. PMCID: 1350722.
    • (2005) Cancer Res , vol.65 , Issue.24 , pp. 11545-11552
    • Karadag, A.1    Fedarko, N.S.2    Fisher, L.W.3
  • 115
    • 2942679170 scopus 로고    scopus 로고
    • Bone sialoprotein, matrix metalloproteinase 2, and alpha(v)beta3 integrin in osteotropic cancer cell invasion
    • Karadag A, Ogbureke KU, Fedarko NS, Fisher LW. Bone sialoprotein, matrix metalloproteinase 2, and alpha(v)beta3 integrin in osteotropic cancer cell invasion. J Natl Cancer Inst 2004; 96(12): 956-965.
    • (2004) J Natl Cancer Inst , vol.96 , Issue.12 , pp. 956-965
    • Karadag, A.1    Ogbureke, K.U.2    Fedarko, N.S.3    Fisher, L.W.4
  • 116
    • 84857322517 scopus 로고    scopus 로고
    • DPP activates integrin-mediated anchorage-dependent signals in undifferentiated mesenchymal cells
    • Eapen AS, Ramachandran A, George A. DPP activates integrin-mediated anchorage-dependent signals in undifferentiated mesenchymal cells. J Biol Chem 2011; 287(8): 5211-5224.
    • (2011) J Biol Chem , vol.287 , Issue.8 , pp. 5211-5224
    • Eapen, A.S.1    Ramachandran, A.2    George, A.3
  • 118
    • 9244256793 scopus 로고    scopus 로고
    • Stimulation of reparative dentin formation by ex vivo gene therapy using dental pulp stem cells electrotransfected with growth/differentiation factor 11 (GDF11)
    • Nakashima M, Iohara K, Ishikawa M, et al. Stimulation of reparative dentin formation by ex vivo gene therapy using dental pulp stem cells electrotransfected with growth/differentiation factor 11 (GDF11). Hum Gene Ther 2004; 15(11): 1045-1053.
    • (2004) Hum Gene Ther , vol.15 , Issue.11 , pp. 1045-1053
    • Nakashima, M.1    Iohara, K.2    Ishikawa, M.3
  • 119
    • 24944550068 scopus 로고    scopus 로고
    • Downregulation of osteoblast PHEX expression by PTH
    • Alos N, Ecarot B. Downregulation of osteoblast PHEX expression by PTH. Bone 2005; 37(4): 589-598.
    • (2005) Bone , vol.37 , Issue.4 , pp. 589-598
    • Alos, N.1    Ecarot, B.2
  • 120
    • 70350330869 scopus 로고    scopus 로고
    • Bone formation regulates circulating concentrations of fibroblast growth factor 23
    • Samadfam R, Richard C, Nguyen-Yamamoto L, Bolivar I, Goltzman D. Bone formation regulates circulating concentrations of fibroblast growth factor 23. Endocrinology 2009; 150(11): 4835-4845.
    • (2009) Endocrinology , vol.150 , Issue.11 , pp. 4835-4845
    • Samadfam, R.1    Richard, C.2    Nguyen-Yamamoto, L.3    Bolivar, I.4    Goltzman, D.5
  • 121
    • 0037931728 scopus 로고    scopus 로고
    • Dual functional roles of dentin matrix protein 1. Implications in biomineralization and gene transcription by activation of intracellular Ca2+ store
    • Narayanan K, Ramachandran A, Hao J, He G, Park KW, Cho M, George A. Dual functional roles of dentin matrix protein 1. Implications in biomineralization and gene transcription by activation of intracellular Ca2+ store. J Biol Chem 2003; 278(19): 17500-17508.
    • (2003) J Biol Chem , vol.278 , Issue.19 , pp. 17500-17508
    • Narayanan, K.1    Ramachandran, A.2    Hao, J.3    He, G.4    Park, K.W.5    Cho, M.6    George, A.7
  • 122
    • 84860336834 scopus 로고    scopus 로고
    • DMP1 does not function as a co-transcriptional factor (abstract)
    • Yuan B, Lin S, Cao Z, et al. DMP1 does not function as a co-transcriptional factor (abstract). J Bone Miner Res 2011; 26(Suppl 1): MO0112.
    • (2011) J Bone Miner Res , vol.26 , Issue.SUPPL. 1
    • Yuan, B.1    Lin, S.2    Cao, Z.3
  • 123
    • 21044437394 scopus 로고    scopus 로고
    • Increased cathepsin D release by HYP mouse osteoblast cells
    • Matsumoto N, Jo OD, Shih RN, et al. Increased cathepsin D release by HYP mouse osteoblast cells. Am J Physiol Endocrinol Metab 2005; 289(1): E123-132.
    • (2005) Am J Physiol Endocrinol Metab , vol.289 , Issue.1
    • Matsumoto, N.1    Jo, O.D.2    Shih, R.N.3
  • 124
    • 19344367077 scopus 로고    scopus 로고
    • Altered cathepsin D metabolism in PHEX antisense human osteoblast cells
    • Matsumoto N, Jo OD, Shih RN, Yanagawa N. Altered cathepsin D metabolism in PHEX antisense human osteoblast cells. Biochem Biophys Res Commun 2005; 332(1): 248-253.
    • (2005) Biochem Biophys Res Commun , vol.332 , Issue.1 , pp. 248-253
    • Matsumoto, N.1    Jo, O.D.2    Shih, R.N.3    Yanagawa, N.4
  • 125
    • 0036156762 scopus 로고    scopus 로고
    • Effects of PHEX antisense in human osteoblast cells
    • Shih NR, Jo OD, Yanagawa N. Effects of PHEX antisense in human osteoblast cells. J Am Soc Nephrol 2002; 13(2): 394-399.
    • (2002) J Am Soc Nephrol , vol.13 , Issue.2 , pp. 394-399
    • Shih, N.R.1    Jo, O.D.2    Yanagawa, N.3
  • 126
    • 69949159609 scopus 로고    scopus 로고
    • Molecular regulation of matrix extracellular phosphoglycoprotein expression by bone morphogenetic protein-2
    • Cho YD, Yoon WJ, Woo KM, et al. Molecular regulation of matrix extracellular phosphoglycoprotein expression by bone morphogenetic protein-2. J Biol Chem 2009; 284(37): 25230.
    • (2009) J Biol Chem , vol.284 , Issue.37 , pp. 25230
    • Cho, Y.D.1    Yoon, W.J.2    Woo, K.M.3
  • 127
    • 43549106530 scopus 로고    scopus 로고
    • MEPE over-expression in osteocytes of DMP1 null mice by activation of the PKA/CREB pathway
    • Yang W, Harris SE, Raw P, Feng J, Gluhak-Heinrich J. MEPE over-expression in osteocytes of DMP1 null mice by activation of the PKA/CREB pathway. J Bone Miner Res 2006; 21: S136-S.
    • (2006) J Bone Miner Res , vol.21
    • Yang, W.1    Harris, S.E.2    Raw, P.3    Feng, J.4    Gluhak-Heinrich, J.5
  • 128
    • 33846223018 scopus 로고    scopus 로고
    • Mechanically induced DMP1 and MEPE expression in osteocytes: correlation to mechanical strain, osteogenic response and gene expression threshold
    • Gluhak-Heinrich J, Yang W, Bonewald LF, Robling AG, Turner CH, Harris SE. Mechanically induced DMP1 and MEPE expression in osteocytes: correlation to mechanical strain, osteogenic response and gene expression threshold. J Bone Miner Res 2005; 20(9): S73-S.
    • (2005) J Bone Miner Res , vol.20 , Issue.9
    • Gluhak-Heinrich, J.1    Yang, W.2    Bonewald, L.F.3    Robling, A.G.4    Turner, C.H.5    Harris, S.E.6
  • 129
    • 0142059612 scopus 로고    scopus 로고
    • Mechanical loading stimulates dentin matrix protein 1 (DMP1) expression in osteocytes in vivo
    • Gluhak-Heinrich J, Ye L, Bonewald LF, et al. Mechanical loading stimulates dentin matrix protein 1 (DMP1) expression in osteocytes in vivo. J Bone Miner Res 2003; 18(5): 807-817.
    • (2003) J Bone Miner Res , vol.18 , Issue.5 , pp. 807-817
    • Gluhak-Heinrich, J.1    Ye, L.2    Bonewald, L.F.3
  • 130
    • 0030029816 scopus 로고    scopus 로고
    • Secretion of osteopontin by macrophages and its accumulation at tissue surfaces during wound healing in mineralized tissues: a potential requirement for macrophage adhesion and phagocytosis
    • McKee MD, Nanci A. Secretion of osteopontin by macrophages and its accumulation at tissue surfaces during wound healing in mineralized tissues: a potential requirement for macrophage adhesion and phagocytosis. Anat Rec 1996; 245(2): 394-409.
    • (1996) Anat Rec , vol.245 , Issue.2 , pp. 394-409
    • McKee, M.D.1    Nanci, A.2
  • 131
    • 80054979878 scopus 로고    scopus 로고
    • Cell line IDG-SW3 replicates osteoblast-to-late-osteocyte differentiation in vitro and accelerates bone formation in vivo
    • Woo SM, Rosser J, Dusevich V, Kalajzic I, Bonewald LF. Cell line IDG-SW3 replicates osteoblast-to-late-osteocyte differentiation in vitro and accelerates bone formation in vivo. J Bone Miner Res 2011; 26(11): 2634-2646.
    • (2011) J Bone Miner Res , vol.26 , Issue.11 , pp. 2634-2646
    • Woo, S.M.1    Rosser, J.2    Dusevich, V.3    Kalajzic, I.4    Bonewald, L.F.5
  • 132
    • 81155148568 scopus 로고    scopus 로고
    • Sost downregulation and local WNT signaling are required for the osteogenic response to mechanical loading
    • Tu X, Rhee Y, Condon K, et al. Sost downregulation and local WNT signaling are required for the osteogenic response to mechanical loading. Bone 2011; 50(11): 209-217.
    • (2011) Bone , vol.50 , Issue.11 , pp. 209-217
    • Tu, X.1    Rhee, Y.2    Condon, K.3
  • 133
    • 79251530211 scopus 로고    scopus 로고
    • The biological function of DMP-1 in osteocyte maturation is mediated by its 57-kDa c-terminal fragment
    • Lu Y, Yuan B, Qin C, et al. The biological function of DMP-1 in osteocyte maturation is mediated by its 57-kDa c-terminal fragment. J Bone Miner Res 2011; 26(2): 331-340.
    • (2011) J Bone Miner Res , vol.26 , Issue.2 , pp. 331-340
    • Lu, Y.1    Yuan, B.2    Qin, C.3
  • 134
  • 136
    • 29744463149 scopus 로고    scopus 로고
    • 1alpha,25-dihydroxyvitamin D3 inhibits prostate cancer cell invasion via modulation of selective proteases
    • Bao BY, Yeh SD, Lee YF. 1alpha, 25-dihydroxyvitamin D3 inhibits prostate cancer cell invasion via modulation of selective proteases. Carcinogenesis 2006; 27(1): 32-42.
    • (2006) Carcinogenesis , vol.27 , Issue.1 , pp. 32-42
    • Bao, B.Y.1    Yeh, S.D.2    Lee, Y.F.3
  • 137
    • 23944524055 scopus 로고    scopus 로고
    • Different cysteine proteinases involved in bone resorption and osteoclast formation
    • Brage M, Abrahamson M, Lindstrom V, Grubb A, Lerner UH. Different cysteine proteinases involved in bone resorption and osteoclast formation. Calcif Tissue Int 2005; 76(6): 439-447.
    • (2005) Calcif Tissue Int , vol.76 , Issue.6 , pp. 439-447
    • Brage, M.1    Abrahamson, M.2    Lindstrom, V.3    Grubb, A.4    Lerner, U.H.5
  • 138
    • 34250818686 scopus 로고    scopus 로고
    • Cystatin C stimulates the differentiation of mouse osteoblastic cells and bone formation
    • Danjo A, Yamaza T, Kido MA, et al. Cystatin C stimulates the differentiation of mouse osteoblastic cells and bone formation. Biochem Biophys Res Commun 2007; 360(1): 199-204.
    • (2007) Biochem Biophys Res Commun , vol.360 , Issue.1 , pp. 199-204
    • Danjo, A.1    Yamaza, T.2    Kido, M.A.3
  • 140
    • 0023905240 scopus 로고
    • Identification of latent procathepsins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro
    • Nishimura Y, Kawabata T, Kato K. Identification of latent procathepsins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro. Arch Biochem Biophys 1988; 261(1): 64-71.
    • (1988) Arch Biochem Biophys , vol.261 , Issue.1 , pp. 64-71
    • Nishimura, Y.1    Kawabata, T.2    Kato, K.3
  • 141
    • 0036838193 scopus 로고    scopus 로고
    • Role of abnormal neutral endopeptidase-like activities in HYP mouse bone cells in renal phosphate transport
    • Dubois SG, Ruchon AF, Delalandre A, Boileau G, Lajeunesse D. Role of abnormal neutral endopeptidase-like activities in HYP mouse bone cells in renal phosphate transport. Am J Physiol Cell Physiol 2002; 283(5): C1414-1421.
    • (2002) Am J Physiol Cell Physiol , vol.283 , Issue.5
    • Dubois, S.G.1    Ruchon, A.F.2    Delalandre, A.3    Boileau, G.4    Lajeunesse, D.5
  • 142
    • 0021995698 scopus 로고
    • Healing of bone disease in X-linked hypophosphatemic rickets/osteomalacia. Induction and maintenance with phosphorus and calcitriol
    • Harrell RM, Lyles KW, Harrelson JM, Friedman NE, Drezner MK. Healing of bone disease in X-linked hypophosphatemic rickets/osteomalacia. Induction and maintenance with phosphorus and calcitriol. J Clin Invest 1985; 75: 1858-1868.
    • (1985) J Clin Invest , vol.75 , pp. 1858-1868
    • Harrell, R.M.1    Lyles, K.W.2    Harrelson, J.M.3    Friedman, N.E.4    Drezner, M.K.5
  • 143
    • 0020187970 scopus 로고
    • Healing of bone lesions with 1,25-dihydroxyvitamin D3 in the young X-linked hypophosphataemic male mouse
    • Marie PJ, Travers R, Glorieux FH. Healing of bone lesions with 1, 25-dihydroxyvitamin D3 in the young X-linked hypophosphataemic male mouse. Endocrinology 1982; 111: 904-911.
    • (1982) Endocrinology , vol.111 , pp. 904-911
    • Marie, P.J.1    Travers, R.2    Glorieux, F.H.3
  • 144
    • 77951626687 scopus 로고    scopus 로고
    • Treatment of X-linked hypophosphatemia with calcitriol and phosphate increases circulating fibroblast growth factor 23 concentrations
    • PMCID: 2853995.
    • Imel EA, DiMeglio LA, Hui SL, Carpenter TO, Econs MJ. Treatment of X-linked hypophosphatemia with calcitriol and phosphate increases circulating fibroblast growth factor 23 concentrations. J Clin Endocrinol Metab 2010;95(4):1846-1850. PMCID: 2853995.
    • (2010) J Clin Endocrinol Metab , vol.95 , Issue.4 , pp. 1846-1850
    • Imel, E.A.1    DiMeglio, L.A.2    Hui, S.L.3    Carpenter, T.O.4    Econs, M.J.5
  • 145
    • 49449085022 scopus 로고    scopus 로고
    • Matrix extracellular phosphoglycoprotein (MEPE) correlates with serum phosphorus prior to and during octreotide treatment and following excisional surgery in hypophosphatemic linear sebaceous nevus syndrome
    • Hoffman WH, Jain A, Chen H, Fedarko NS. Matrix extracellular phosphoglycoprotein (MEPE) correlates with serum phosphorus prior to and during octreotide treatment and following excisional surgery in hypophosphatemic linear sebaceous nevus syndrome. Am J Med Genet A 2008; 146A(16): 2164-2168.
    • (2008) Am J Med Genet A , vol.146 A , Issue.16 , pp. 2164-2168
    • Hoffman, W.H.1    Jain, A.2    Chen, H.3    Fedarko, N.S.4
  • 146
    • 0016758368 scopus 로고
    • Action of 1,25-dihydroxyvitamin D3 and a diphosphonate on calcium metabolism in rats
    • Bonjour JP, Trechsel U, Fleisch H, Schenk R, DeLuca HF, Baxter LA. Action of 1, 25-dihydroxyvitamin D3 and a diphosphonate on calcium metabolism in rats. Am J Physiol 1975; 229(2): 402-408.
    • (1975) Am J Physiol , vol.229 , Issue.2 , pp. 402-408
    • Bonjour, J.P.1    Trechsel, U.2    Fleisch, H.3    Schenk, R.4    DeLuca, H.F.5    Baxter, L.A.6
  • 148
    • 0026658426 scopus 로고
    • Dual action of phosphonoformic acid on Na(+)-phosphate cotransport in opossum kidney cells
    • Loghman-Adham M, Dousa TP. Dual action of phosphonoformic acid on Na(+)-phosphate cotransport in opossum kidney cells. Am J Physiol 1992; 263(2 Pt 2): F301-10.
    • (1992) Am J Physiol , vol.263 , Issue.2 PART 2
    • Loghman-Adham, M.1    Dousa, T.P.2
  • 149
    • 0027025335 scopus 로고
    • Phosphate transport in brush border membranes from uremic rats. Response to phosphonoformic acid
    • Loghman-Adham M, Szczepanska-Konkel M, Dousa TP. Phosphate transport in brush border membranes from uremic rats. Response to phosphonoformic acid. J Am Soc Nephrol 1992; 3(6): 1253-1259.
    • (1992) J Am Soc Nephrol , vol.3 , Issue.6 , pp. 1253-1259
    • Loghman-Adham, M.1    Szczepanska-Konkel, M.2    Dousa, T.P.3
  • 150
    • 0023285487 scopus 로고
    • Inhibition of Na + -Pi cotransporter in small gut brush border by phosphonocarboxylic acids
    • Loghman-Adham M, Szczepanska-Konkel M, Yusufi AN, Van Scoy M, Dousa TP. Inhibition of Na + -Pi cotransporter in small gut brush border by phosphonocarboxylic acids. Am J Physiol 1987; 252(2 Pt 1): G244-9.
    • (1987) Am J Physiol , vol.252 , Issue.2 PART 1
    • Loghman-Adham, M.1    Szczepanska-Konkel, M.2    Yusufi, A.N.3    Van Scoy, M.4    Dousa, T.P.5
  • 151
    • 0023552808 scopus 로고
    • Comparative effects of intravenous diphosphonates on calcium and skeletal metabolism in man
    • McCloskey EV, Yates AJ, Beneton MN, Galloway J, Harris S, Kanis JA. Comparative effects of intravenous diphosphonates on calcium and skeletal metabolism in man. Bone 1987; 8(Suppl 1): S35-41.
    • (1987) Bone , vol.8 , Issue.SUPPL. 1
    • McCloskey, E.V.1    Yates, A.J.2    Beneton, M.N.3    Galloway, J.4    Harris, S.5    Kanis, J.A.6
  • 153
    • 0019798269 scopus 로고
    • Tubular handling of phosphate along the nephron of thyroparathyroidectomized rats injected with ethane-1-hydroxy-1,1-diphosphonate
    • Muhlbauer RC, Bonjour JP, Fleisch H. Tubular handling of phosphate along the nephron of thyroparathyroidectomized rats injected with ethane-1-hydroxy-1, 1-diphosphonate. Clin Sci (Lond) 1981; 60(2): 171-177.
    • (1981) Clin Sci (Lond) , vol.60 , Issue.2 , pp. 171-177
    • Muhlbauer, R.C.1    Bonjour, J.P.2    Fleisch, H.3
  • 154
    • 0016582540 scopus 로고
    • Changes in the renal and extrarenal handling of phosphate induced by disodium etidronate (EHDP) in man
    • Walton RJ, Russell RG, Smith R. Changes in the renal and extrarenal handling of phosphate induced by disodium etidronate (EHDP) in man. Clin Sci Mol Med 1975; 49(1): 45-56.
    • (1975) Clin Sci Mol Med , vol.49 , Issue.1 , pp. 45-56
    • Walton, R.J.1    Russell, R.G.2    Smith, R.3
  • 155
    • 0019036223 scopus 로고
    • Effect of diphosphonate treatment on phosphate transport by renal brush border vesicles
    • Stoll R, Fleisch H, Bonjour JP. Effect of diphosphonate treatment on phosphate transport by renal brush border vesicles. Am J Physiol 1980; 239(1): F13-16.
    • (1980) Am J Physiol , vol.239 , Issue.1
    • Stoll, R.1    Fleisch, H.2    Bonjour, J.P.3
  • 156
    • 0023024866 scopus 로고
    • Phosphonocarboxylic acids as specific inhibitors of Na+- dependent transport of phosphate across renal brush border membrane
    • Szczepanska-Konkel M, Yusufi ANK, VanScoy M, Webster SK, Dousa TP. Phosphonocarboxylic acids as specific inhibitors of Na+- dependent transport of phosphate across renal brush border membrane. J Biol Chem 1986; 261: 6375-6383.
    • (1986) J Biol Chem , vol.261 , pp. 6375-6383
    • Szczepanska-Konkel, M.1    Yusufi, A.N.K.2    VanScoy, M.3    Webster, S.K.4    Dousa, T.P.5
  • 157
    • 0017390312 scopus 로고
    • Relation between bone mineralization, Ca absorption, and plasma Ca in phosphonate-treated rats
    • Trechsel U, Schenk R, Bonjour JP, Russell RG, Fleisch H. Relation between bone mineralization, Ca absorption, and plasma Ca in phosphonate-treated rats. Am J Physiol 1977; 232(3): E298-305.
    • (1977) Am J Physiol , vol.232 , Issue.3
    • Trechsel, U.1    Schenk, R.2    Bonjour, J.P.3    Russell, R.G.4    Fleisch, H.5
  • 158
    • 0024243973 scopus 로고
    • Mechanism of phosphaturia elicited by administration of phosphonoformate in vivo
    • VanScoy M, Loghman-Adham M, Onsgard M, et al. Mechanism of phosphaturia elicited by administration of phosphonoformate in vivo. Am J Physiol 1988; 255(5 Pt 2): F984-994.
    • (1988) Am J Physiol , vol.255 , Issue.5 PART 2
    • VanScoy, M.1    Loghman-Adham, M.2    Onsgard, M.3
  • 159
    • 12144268396 scopus 로고    scopus 로고
    • Phosphatonin washout in HYP mice proximal tubules: evidence for posttranscriptional regulation
    • Epub 2004 Sep 28.
    • Baum M, Moe OW, Zhang J, Dwarakanath V, Quigley R. Phosphatonin washout in HYP mice proximal tubules: evidence for posttranscriptional regulation. Am J Physiol Renal Physiol 2005; 288(2):F363-370 Epub 2004 Sep 28.
    • (2005) Am J Physiol Renal Physiol , vol.288 , Issue.2
    • Baum, M.1    Moe, O.W.2    Zhang, J.3    Dwarakanath, V.4    Quigley, R.5
  • 160
    • 0030051013 scopus 로고    scopus 로고
    • Normal phosphate transport in cells from the S2 and S3 segments of HYP-mouse proximal renal tubules
    • Nesbitt T, Byun JK, Drezner MK. Normal phosphate transport in cells from the S2 and S3 segments of HYP-mouse proximal renal tubules. Endocrinology 1996; 137: 943-948.
    • (1996) Endocrinology , vol.137 , pp. 943-948
    • Nesbitt, T.1    Byun, J.K.2    Drezner, M.K.3
  • 161
    • 0029114670 scopus 로고
    • Phosphate transport in immortalized cell cultures from the renal proximal tubule of normal and HYP mice: evidence that the HYP gene locus product is an extrarenal factor
    • Nesbitt T, Econs MJ, Byun JK, Martel J, Tenenhouse HS, Drezner MK. Phosphate transport in immortalized cell cultures from the renal proximal tubule of normal and HYP mice: evidence that the HYP gene locus product is an extrarenal factor. J Bone Miner Res 1995; 10: 1327-1333.
    • (1995) J Bone Miner Res , vol.10 , pp. 1327-1333
    • Nesbitt, T.1    Econs, M.J.2    Byun, J.K.3    Martel, J.4    Tenenhouse, H.S.5    Drezner, M.K.6
  • 162
    • 0023655107 scopus 로고
    • Interactions of [14C]phosphonoformic acid with renal cortical brush-border membranes. Relationship to the Na+-phosphate co-transporter
    • Szczepanska-Konkel M, Yusufi AN, Dousa TP. Interactions of [14C]phosphonoformic acid with renal cortical brush-border membranes. Relationship to the Na+-phosphate co-transporter. J Biol Chem 1987; 262(17): 8000-8010.
    • (1987) J Biol Chem , vol.262 , Issue.17 , pp. 8000-8010
    • Szczepanska-Konkel, M.1    Yusufi, A.N.2    Dousa, T.P.3
  • 163
    • 0031443905 scopus 로고    scopus 로고
    • Interaction of alkyl/arylphosphonates, phosphonocarboxylates and diphosphonates with different anion transport systems in the proximal renal tubule
    • Ullrich KJ, Rumrich G, Burke TR, Shirazi-Beechey SP, Lang H. Interaction of alkyl/arylphosphonates, phosphonocarboxylates and diphosphonates with different anion transport systems in the proximal renal tubule. J Pharmacol Exp Ther 1997; 283(3): 1223-1229.
    • (1997) J Pharmacol Exp Ther , vol.283 , Issue.3 , pp. 1223-1229
    • Ullrich, K.J.1    Rumrich, G.2    Burke, T.R.3    Shirazi-Beechey, S.P.4    Lang, H.5
  • 164
    • 77950665927 scopus 로고    scopus 로고
    • Physiological role of alkaline phosphatase explored in hypophosphatasia
    • Whyte MP. Physiological role of alkaline phosphatase explored in hypophosphatasia. Ann N Y Acad Sci 2010; 1192: 190-200.
    • (2010) Ann N Y Acad Sci , vol.1192 , pp. 190-200
    • Whyte, M.P.1
  • 165
    • 0032963140 scopus 로고    scopus 로고
    • 1,25-(OH)(2)D-3 down-regulates expression of PHEX, a marker of the mature osteoblast
    • Ecarot B, Desbarats M. 1, 25-(OH)(2)D-3 down-regulates expression of PHEX, a marker of the mature osteoblast. Endocrinology 1999; 140(3): 1192-1199.
    • (1999) Endocrinology , vol.140 , Issue.3 , pp. 1192-1199
    • Ecarot, B.1    Desbarats, M.2
  • 166
    • 8744315936 scopus 로고    scopus 로고
    • 1,25-dihydroxyvitamin D3 down-regulation of PHEX gene expression is mediated by apparent repression of a 110 kDa transfactor that binds to a polyadenine element in the promoter
    • Hines ER, Kolek OI, Jones MD, et al. 1, 25-dihydroxyvitamin D3 down-regulation of PHEX gene expression is mediated by apparent repression of a 110 kDa transfactor that binds to a polyadenine element in the promoter. J Biol Chem 2004; 279(45): 46406-46414.
    • (2004) J Biol Chem , vol.279 , Issue.45 , pp. 46406-46414
    • Hines, E.R.1    Kolek, O.I.2    Jones, M.D.3
  • 167
    • 0347723963 scopus 로고    scopus 로고
    • Bone morphogenetic protein-1/tolloid-like proteinases process dentin matrix protein-1
    • Steiglitz BM, Ayala M, Narayanan K, George A, Greenspan DS. Bone morphogenetic protein-1/tolloid-like proteinases process dentin matrix protein-1. J Biol Chem 2004; 279(2): 980-986.
    • (2004) J Biol Chem , vol.279 , Issue.2 , pp. 980-986
    • Steiglitz, B.M.1    Ayala, M.2    Narayanan, K.3    George, A.4    Greenspan, D.S.5
  • 168
    • 57749105419 scopus 로고    scopus 로고
    • Dentin matrix protein-1 isoforms promote differential cell attachment and migration
    • PMCID: 2583300.
    • von Marschall Z, Fisher LW. Dentin matrix protein-1 isoforms promote differential cell attachment and migration. J Biol Chem. 2008; 283(47):32730-40. PMCID: 2583300.
    • (2008) J Biol Chem , vol.283 , Issue.47 , pp. 32730-32740
    • von Marschall, Z.1    Fisher, L.W.2
  • 169
    • 56349162283 scopus 로고    scopus 로고
    • Lrp5 controls bone formation by inhibiting serotonin synthesis in the duodenum
    • PMCID: 2614332.
    • Yadav VK, Ryu JH, Suda N, et al. Lrp5 controls bone formation by inhibiting serotonin synthesis in the duodenum. Cell. 2008; 135(5):825-37. PMCID: 2614332.
    • (2008) Cell , vol.135 , Issue.5 , pp. 825-837
    • Yadav, V.K.1    Ryu, J.H.2    Suda, N.3
  • 170
    • 78651495664 scopus 로고    scopus 로고
    • Leptin-dependent serotonin control of appetite: temporal specificity, transcriptional regulation, and therapeutic implications
    • Yadav VK, Oury F, Tanaka K, et al. Leptin-dependent serotonin control of appetite: temporal specificity, transcriptional regulation, and therapeutic implications. J Exp Med 2011; 208(1): 41-52.
    • (2011) J Exp Med , vol.208 , Issue.1 , pp. 41-52
    • Yadav, V.K.1    Oury, F.2    Tanaka, K.3
  • 171
    • 45349084061 scopus 로고    scopus 로고
    • Reciprocal regulation of bone and energy metabolism
    • Lee NK, Karsenty G. Reciprocal regulation of bone and energy metabolism. Trends Endocrinol Metab 2008; 19(5): 161-166.
    • (2008) Trends Endocrinol Metab , vol.19 , Issue.5 , pp. 161-166
    • Lee, N.K.1    Karsenty, G.2
  • 172
    • 80051960097 scopus 로고    scopus 로고
    • LRP5, serotonin and bone: complexity, contradictions and conundrums
    • Goltzman D. LRP5, serotonin and bone: complexity, contradictions and conundrums. J Bone Miner Res 2011; 26(9): 2002-2011.
    • (2011) J Bone Miner Res , vol.26 , Issue.9 , pp. 2002-2011
    • Goltzman, D.1
  • 173
    • 79958171733 scopus 로고    scopus 로고
    • Lrp5 functions in bone to regulate bone mass
    • PMCID: 3113461.
    • Cui Y, Niziolek PJ, Macdonald BT, et al. Lrp5 functions in bone to regulate bone mass. Nat Med 2011; 17(6):684-691. PMCID: 3113461.
    • (2011) Nat Med , vol.17 , Issue.6 , pp. 684-691
    • Cui, Y.1    Niziolek, P.J.2    Macdonald, B.T.3
  • 174
    • 79960008594 scopus 로고    scopus 로고
    • Bone: evidence for local effects of LRP5 on bone mass
    • Price S. Bone: evidence for local effects of LRP5 on bone mass. Nat Rev Rheumatol 2011; 7(7): 373.
    • (2011) Nat Rev Rheumatol , vol.7 , Issue.7 , pp. 373
    • Price, S.1
  • 175
    • 77957747818 scopus 로고    scopus 로고
    • The two faces of serotonin in bone biology
    • PMCID: 2953449.
    • Ducy P, Karsenty G. The two faces of serotonin in bone biology. J Cell Biol 2010; 191(1):7-13. PMCID: 2953449.
    • (2010) J Cell Biol , vol.191 , Issue.1 , pp. 7-13
    • Ducy, P.1    Karsenty, G.2
  • 176
    • 79953694768 scopus 로고    scopus 로고
    • 5-HT and bone biology
    • Ducy P. 5-HT and bone biology. Curr Opin Pharmacol 2011; 11(1): 34-38.
    • (2011) Curr Opin Pharmacol , vol.11 , Issue.1 , pp. 34-38
    • Ducy, P.1
  • 177
    • 79953038259 scopus 로고    scopus 로고
    • The osteoblast: an insulin target cell controlling glucose homeostasis
    • Clemens TL, Karsenty G. The osteoblast: an insulin target cell controlling glucose homeostasis. J Bone Miner Res 2011; 26(4): 677-680.
    • (2011) J Bone Miner Res , vol.26 , Issue.4 , pp. 677-680
    • Clemens, T.L.1    Karsenty, G.2
  • 178
    • 59149093623 scopus 로고    scopus 로고
    • Adipocyte differentiation of bone marrow-derived mesenchymal stem cells: cross talk with the osteoblastogenic program
    • Muruganandan S, Roman AA, Sinal CJ. Adipocyte differentiation of bone marrow-derived mesenchymal stem cells: cross talk with the osteoblastogenic program. Cell Mol Life Sci 2009; 66(2): 236-253.
    • (2009) Cell Mol Life Sci , vol.66 , Issue.2 , pp. 236-253
    • Muruganandan, S.1    Roman, A.A.2    Sinal, C.J.3
  • 179
    • 73449145111 scopus 로고    scopus 로고
    • FGF23 is mainly synthesized by osteocytes in the regularly distributed osteocytic lacunar canalicular system established after physiological bone remodeling
    • Ubaidus S, Li M, Sultana S, et al. FGF23 is mainly synthesized by osteocytes in the regularly distributed osteocytic lacunar canalicular system established after physiological bone remodeling. J Electron Microsc (Tokyo) 2009; 58(6): 381-392.
    • (2009) J Electron Microsc (Tokyo) , vol.58 , Issue.6 , pp. 381-392
    • Ubaidus, S.1    Li, M.2    Sultana, S.3
  • 180
    • 84860336832 scopus 로고    scopus 로고
    • PHEX and fat energy metabolism across a bone-renal axis (abstract)
    • Abstract:
    • Rowe PS, Hedge AM, David V, Zelenchuk L. PHEX and fat energy metabolism across a bone-renal axis (abstract). J Bone Miner Res 2011; 26(Suppl 1): Abstract:.
    • (2011) J Bone Miner Res , vol.26 , Issue.SUPPL. 1
    • Rowe, P.S.1    Hedge, A.M.2    David, V.3    Zelenchuk, L.4
  • 181
    • 0022560637 scopus 로고
    • Vitamin D3 improves impaired glucose tolerance and insulin secretion in the vitamin D-deficient rat in vivo
    • Cade C, Norman AW. Vitamin D3 improves impaired glucose tolerance and insulin secretion in the vitamin D-deficient rat in vivo. Endocrinology 1986; 119(1): 84-90.
    • (1986) Endocrinology , vol.119 , Issue.1 , pp. 84-90
    • Cade, C.1    Norman, A.W.2
  • 182
    • 0023113882 scopus 로고
    • Rapid normalization/stimulation by 1,25-dihydroxyvitamin D3 of insulin secretion and glucose tolerance in the vitamin D-deficient rat
    • Cade C, Norman AW. Rapid normalization/stimulation by 1, 25-dihydroxyvitamin D3 of insulin secretion and glucose tolerance in the vitamin D-deficient rat. Endocrinology 1987; 120(4): 1490-1497.
    • (1987) Endocrinology , vol.120 , Issue.4 , pp. 1490-1497
    • Cade, C.1    Norman, A.W.2
  • 183
    • 0026577755 scopus 로고
    • Altered proximal tubule glucose metabolism in X-linked hypophosphatemic mice
    • Capparelli AW, Roh D, Dhiman JK, Jo OD, Yanagawa N. Altered proximal tubule glucose metabolism in X-linked hypophosphatemic mice. Endocrinology 1992; 130(1): 328-334.
    • (1992) Endocrinology , vol.130 , Issue.1 , pp. 328-334
    • Capparelli, A.W.1    Roh, D.2    Dhiman, J.K.3    Jo, O.D.4    Yanagawa, N.5
  • 186
    • 0029035481 scopus 로고
    • Altered osteoblast gluconeogenesis in X-linked hypophosphatemic mice is associated with a depressed intracellular pH
    • Rifas L, Gupta A, Hruska KA, Avioli LV. Altered osteoblast gluconeogenesis in X-linked hypophosphatemic mice is associated with a depressed intracellular pH. Calcif Tissue Int 1995; 57(1): 60-63.
    • (1995) Calcif Tissue Int , vol.57 , Issue.1 , pp. 60-63
    • Rifas, L.1    Gupta, A.2    Hruska, K.A.3    Avioli, L.V.4
  • 187
    • 0035988632 scopus 로고    scopus 로고
    • Up-regulation of liver glucose-6-phosphatase in X-linked hypophosphatemic mice
    • Xie W, Mechin MC, Dubois SG, Lajeunesse D, van de Werve G. Up-regulation of liver glucose-6-phosphatase in X-linked hypophosphatemic mice. Horm Metab Res 2002; 34(6): 288-292.
    • (2002) Horm Metab Res , vol.34 , Issue.6 , pp. 288-292
    • Xie, W.1    Mechin, M.C.2    Dubois, S.G.3    Lajeunesse, D.4    van de Werve, G.5
  • 188
    • 0037364216 scopus 로고    scopus 로고
    • Impaired insulin secretory capacity in mice lacking a functional vitamin D receptor
    • Zeitz U, Weber K, Soegiarto DW, Wolf E, Balling R, Erben RG. Impaired insulin secretory capacity in mice lacking a functional vitamin D receptor. FASEB J 2003; 17(3): 509-511.
    • (2003) FASEB J , vol.17 , Issue.3 , pp. 509-511
    • Zeitz, U.1    Weber, K.2    Soegiarto, D.W.3    Wolf, E.4    Balling, R.5    Erben, R.G.6
  • 189
    • 33846566785 scopus 로고    scopus 로고
    • Ablation of vitamin D signaling rescues bone, mineral, and glucose homeostasis in Fgf-23 deficient mice
    • Hesse M, Frohlich LF, Zeitz U, Lanske B, Erben RG. Ablation of vitamin D signaling rescues bone, mineral, and glucose homeostasis in Fgf-23 deficient mice. Matrix Biol 2007; 26(2): 20.
    • (2007) Matrix Biol , vol.26 , Issue.2 , pp. 20
    • Hesse, M.1    Frohlich, L.F.2    Zeitz, U.3    Lanske, B.4    Erben, R.G.5
  • 190
    • 0033812019 scopus 로고    scopus 로고
    • Decreased insulin production and increased insulin sensitivity in the KLOTHO mutant mouse, a novel animal model for human aging
    • Utsugi T, Ohno T, Ohyama Y, et al. Decreased insulin production and increased insulin sensitivity in the KLOTHO mutant mouse, a novel animal model for human aging. Metabolism 2000; 49(9): 1118-1123.
    • (2000) Metabolism , vol.49 , Issue.9 , pp. 1118-1123
    • Utsugi, T.1    Ohno, T.2    Ohyama, Y.3
  • 191
    • 0030724491 scopus 로고    scopus 로고
    • Mutation of the mouse klotho gene leads to a syndrome resembling ageing
    • Kuro-o M, Matsumura Y, Aizawa H, et al. Mutation of the mouse klotho gene leads to a syndrome resembling ageing. Nature 1997; 390(6655): 45-51.
    • (1997) Nature , vol.390 , Issue.6655 , pp. 45-51
    • Kuro-o, M.1    Matsumura, Y.2    Aizawa, H.3
  • 192
    • 77949891834 scopus 로고    scopus 로고
    • Evidence against a direct role of KLOTHO in insulin resistance
    • Lorenzi O, Veyrat-Durebex C, Wollheim CB, et al. Evidence against a direct role of KLOTHO in insulin resistance. Pflugers Arch 2009; 459(3): 465-473.
    • (2009) Pflugers Arch , vol.459 , Issue.3 , pp. 465-473
    • Lorenzi, O.1    Veyrat-Durebex, C.2    Wollheim, C.B.3
  • 193
    • 78349252613 scopus 로고    scopus 로고
    • KLOTHO, FGF23, and FGF receptors in chronic kidney disease: a yin-yang situation?
    • Drueke TB. KLOTHO, FGF23, and FGF receptors in chronic kidney disease: a yin-yang situation? Kidney Int 2010; 78(11): 1057-60.
    • (2010) Kidney Int , vol.78 , Issue.11 , pp. 1057-1060
    • Drueke, T.B.1
  • 194
    • 64749099761 scopus 로고    scopus 로고
    • Glucose control by the kidney: an emerging target in diabetes
    • Marsenic O. Glucose control by the kidney: an emerging target in diabetes. Am J Kidney Dis 2009; 53(5): 875-883.
    • (2009) Am J Kidney Dis , vol.53 , Issue.5 , pp. 875-883
    • Marsenic, O.1
  • 195
    • 0035146344 scopus 로고    scopus 로고
    • Renal gluconeogenesis: its importance in human glucose homeostasis
    • Gerich JE, Meyer C, Woerle HJ, Stumvoll M. Renal gluconeogenesis: its importance in human glucose homeostasis. Diabetes Care 2001; 24(2): 382-391.
    • (2001) Diabetes Care , vol.24 , Issue.2 , pp. 382-391
    • Gerich, J.E.1    Meyer, C.2    Woerle, H.J.3    Stumvoll, M.4
  • 196
    • 0015903863 scopus 로고
    • Ionic control of renal gluconeogenesis. IV. Effect of extracellular phosphate concentration
    • Kurokawa K, Rasmussen H. Ionic control of renal gluconeogenesis. IV. Effect of extracellular phosphate concentration. Biochim Biophys Acta 1973; 313(1): 59-71.
    • (1973) Biochim Biophys Acta , vol.313 , Issue.1 , pp. 59-71
    • Kurokawa, K.1    Rasmussen, H.2
  • 197
    • 0031834073 scopus 로고    scopus 로고
    • Effects of hypophosphatemia on glucose tolerance and insulin secretion
    • Paula FJ, Plens AE, Foss MC. Effects of hypophosphatemia on glucose tolerance and insulin secretion. Horm Metab Res 1998; 30(5): 281-4.
    • (1998) Horm Metab Res , vol.30 , Issue.5 , pp. 281-284
    • Paula, F.J.1    Plens, A.E.2    Foss, M.C.3
  • 198
    • 0019134702 scopus 로고
    • Hypophosphatemia and glucose intolerance: evidence for tissue insensitivity to insulin
    • DeFronzo RA, Lang R. Hypophosphatemia and glucose intolerance: evidence for tissue insensitivity to insulin. N Engl J Med 1980; 303(22): 1259-1263.
    • (1980) N Engl J Med , vol.303 , Issue.22 , pp. 1259-1263
    • DeFronzo, R.A.1    Lang, R.2
  • 199
    • 0033569577 scopus 로고    scopus 로고
    • Up-regulation of liver glucose-6-phosphatase in rats fed with a P(i)-deficient diet
    • PMCID: 1220566.
    • Xie W, Li Y, Mechin MC, Van De Werve G. Up-regulation of liver glucose-6-phosphatase in rats fed with a P(i)-deficient diet. Biochem J 1999;343(Pt 2):393-6. PMCID: 1220566.
    • (1999) Biochem J , vol.343 , Issue.PART 2 , pp. 393-396
    • Xie, W.1    Li, Y.2    Mechin, M.C.3    Van De Werve, G.4
  • 200
    • 0034669008 scopus 로고    scopus 로고
    • Dietary P(i) deprivation in rats affects liver cAMP, glycogen, key steps of gluconeogenesis and glucose production
    • PMCID: 1221451.
    • Xie W, Tran TL, Finegood DT, van de Werve G. Dietary P(i) deprivation in rats affects liver cAMP, glycogen, key steps of gluconeogenesis and glucose production. Biochem J 2000; 352(Pt 1):227-32. PMCID: 1221451.
    • (2000) Biochem J , vol.352 , Issue.PART 1 , pp. 227-232
    • Xie, W.1    Tran, T.L.2    Finegood, D.T.3    van de Werve, G.4
  • 201
    • 84858403830 scopus 로고    scopus 로고
    • Acute hyperinsulinemia is followed by increased serum concentrations of fibroblast growth factor 23 in type 2 diabetes patients
    • Winther K, Nybo M, Vind B, Pedersen SM, Hojlund K, Rasmussen LM. Acute hyperinsulinemia is followed by increased serum concentrations of fibroblast growth factor 23 in type 2 diabetes patients. Scand J Clin Lab Invest 2012; 72: 108-113.
    • (2012) Scand J Clin Lab Invest , vol.72 , pp. 108-113
    • Winther, K.1    Nybo, M.2    Vind, B.3    Pedersen, S.M.4    Hojlund, K.5    Rasmussen, L.M.6
  • 202
    • 0023653165 scopus 로고
    • Evidence for an essential histidine in neutral endopeptidase 24.11
    • Bateman RCJ, Hersh LB. Evidence for an essential histidine in neutral endopeptidase 24.11. Biochemistry 1987; 26: 4237-4242.
    • (1987) Biochemistry , vol.26 , pp. 4237-4242
    • Bateman, R.C.J.1    Hersh, L.B.2
  • 203
    • 0026808805 scopus 로고
    • Charge polarity reversal inverses the specificity of neutral endopeptidase-24.11
    • Beaumont A, Barbe B, Le Moual H, et al. Charge polarity reversal inverses the specificity of neutral endopeptidase-24.11. J Biol Chem 1992; 267(4): 2138-2141.
    • (1992) J Biol Chem , vol.267 , Issue.4 , pp. 2138-2141
    • Beaumont, A.1    Barbe, B.2    Le Moual, H.3
  • 204
    • 0026650421 scopus 로고
    • Analysis of the importance of arginine 102 in neutral endopeptidase (enkephalinase) catalysis
    • Kim YA, Shriver B, Quay T, Hersh LB. Analysis of the importance of arginine 102 in neutral endopeptidase (enkephalinase) catalysis. J Biol Chem 1992; 267(17): 12330-12335.
    • (1992) J Biol Chem , vol.267 , Issue.17 , pp. 12330-12335
    • Kim, Y.A.1    Shriver, B.2    Quay, T.3    Hersh, L.B.4
  • 206
    • 0035878581 scopus 로고    scopus 로고
    • Disease-causingmissense mutations in the PHEX gene interfere with membrane targeting of the recombinant protein
    • Sabbagh Y, Boileau G, DesGroseillers L, Tenenhouse HS. Disease-causingmissense mutations in the PHEX gene interfere with membrane targeting of the recombinant protein. Hum Mol Genet 2001; 10(15): 1539-1546.
    • (2001) Hum Mol Genet , vol.10 , Issue.15 , pp. 1539-1546
    • Sabbagh, Y.1    Boileau, G.2    DesGroseillers, L.3    Tenenhouse, H.S.4
  • 207
    • 0033939658 scopus 로고    scopus 로고
    • PHEXdb, a locus-specific database for mutations causing X-linked hypophosphatemia
    • Sabbagh Y, Jones AO, Tenenhouse HS. PHEXdb, a locus-specific database for mutations causing X-linked hypophosphatemia. Hum Mutat 2000; 16(1): 1-6.
    • (2000) Hum Mutat , vol.16 , Issue.1 , pp. 1-6
    • Sabbagh, Y.1    Jones, A.O.2    Tenenhouse, H.S.3
  • 208
    • 0030478481 scopus 로고    scopus 로고
    • LALNVIEW: a graphical viewer for pairwise sequence alignments
    • Duret L, Gasteiger E, Perriere G. LALNVIEW: a graphical viewer for pairwise sequence alignments. Comput Appl Biosci 1996; 12: 507-510.
    • (1996) Comput Appl Biosci , vol.12 , pp. 507-510
    • Duret, L.1    Gasteiger, E.2    Perriere, G.3
  • 210
  • 211
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen TN, Brunak S, von Heijne G, Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 2011; 8(10): 785-786.
    • (2011) Nat Methods , vol.8 , Issue.10 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 213
    • 67649184798 scopus 로고    scopus 로고
    • Dentin extracellular matrix molecules implanted into exposed pulps generate reparative dentin: a novel strategy in regenerative dentistry
    • Goldberg M, Six N, Chaussain C, DenBesten P, Veis A, Poliard A. Dentin extracellular matrix molecules implanted into exposed pulps generate reparative dentin: a novel strategy in regenerative dentistry. J Dent Res 2009; 88(5): 396-399.
    • (2009) J Dent Res , vol.88 , Issue.5 , pp. 396-399
    • Goldberg, M.1    Six, N.2    Chaussain, C.3    DenBesten, P.4    Veis, A.5    Poliard, A.6
  • 214
    • 2942748650 scopus 로고    scopus 로고
    • A synthetic peptide fragment of human MEPE stimulates new bone formation in vitro and in vivo
    • Hayashibara T, Hiraga T, Yi B, et al. A synthetic peptide fragment of human MEPE stimulates new bone formation in vitro and in vivo. J Bone Miner Res 2004; 19(3): 455-462.
    • (2004) J Bone Miner Res , vol.19 , Issue.3 , pp. 455-462
    • Hayashibara, T.1    Hiraga, T.2    Yi, B.3
  • 215
    • 81355138197 scopus 로고    scopus 로고
    • Cooperative effects in differentiation and proliferation between PDGF-BB and matrix derived synthetic peptides in human osteoblasts
    • Vordemvenne T, Paletta JR, Hartensuer R, Pap T, Raschke MJ, Ochman S. Cooperative effects in differentiation and proliferation between PDGF-BB and matrix derived synthetic peptides in human osteoblasts. BMC Musculoskelet Disord 2011; 12(1): 263.
    • (2011) BMC Musculoskelet Disord , vol.12 , Issue.1 , pp. 263
    • Vordemvenne, T.1    Paletta, J.R.2    Hartensuer, R.3    Pap, T.4    Raschke, M.J.5    Ochman, S.6
  • 216
    • 42449096306 scopus 로고    scopus 로고
    • Osteocalcin differentially regulates beta cell and adipocyte gene expression and affects the development of metabolic diseases in wild-type mice
    • PMCID: 2278202.
    • Ferron M, Hinoi E, Karsenty G, Ducy P. Osteocalcin differentially regulates beta cell and adipocyte gene expression and affects the development of metabolic diseases in wild-type mice. Proc Natl Acad Sci USA. 2008; 105(13):5266-70. PMCID: 2278202.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.13 , pp. 5266-5270
    • Ferron, M.1    Hinoi, E.2    Karsenty, G.3    Ducy, P.4
  • 217
    • 77955035304 scopus 로고    scopus 로고
    • Insulin signaling in osteoblasts integrates bone remodeling and energy metabolism
    • PMCID: 2910411.
    • Ferron M, Wei J, Yoshizawa T, et al. Insulin signaling in osteoblasts integrates bone remodeling and energy metabolism. Cell 2010; 142(2):296-308. PMCID: 2910411.
    • (2010) Cell , vol.142 , Issue.2 , pp. 296-308
    • Ferron, M.1    Wei, J.2    Yoshizawa, T.3
  • 218
    • 78049518505 scopus 로고    scopus 로고
    • The central regulation of bone mass, the first link between bone remodeling and energy metabolism
    • Karsenty G, Oury F. The central regulation of bone mass, the first link between bone remodeling and energy metabolism. J Clin Endocrinol Metab 2010; 95(11): 4795-4801.
    • (2010) J Clin Endocrinol Metab , vol.95 , Issue.11 , pp. 4795-4801
    • Karsenty, G.1    Oury, F.2
  • 219
    • 0026088974 scopus 로고
    • Phosphate depletion impairs insulin secretion by pancreatic islets
    • Zhou XJ, Fadda GZ, Perna AF, Massry SG. Phosphate depletion impairs insulin secretion by pancreatic islets. Kidney Int 1991; 39(1): 120-128.
    • (1991) Kidney Int , vol.39 , Issue.1 , pp. 120-128
    • Zhou, X.J.1    Fadda, G.Z.2    Perna, A.F.3    Massry, S.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.