메뉴 건너뛰기




Volumn 22, Issue 1, 2012, Pages 61-86

Regulation of bone-renal mineral and energy metabolism: The PHEX, FGF23, DMP1, MEPE ASARM pathway

Author keywords

DMP1; FGF23; Kidney disease; KLOTHO; MEPE; Osteomalacia; PHEX; Rickets

Indexed keywords

DENTIN MATRIX PROTEIN 1; FIBROBLAST GROWTH FACTOR 23; GLYCOPROTEIN; INSULIN; LEPTIN; MATRIX EXTRACELLULAR PHOSPHOGLYCOPROTEIN; PHOSPHATE; PHOSPHATE REGULATING GENE WITH HOMOLOGIES TO ENDOPEPTIDASES ON THE X CHROMOSOME PROTEIN; SEROTONIN; SHORT INTEGRIN BINDING LIGAND INTERACTING GLYCOPROTEIN; UNCLASSIFIED DRUG;

EID: 84860321172     PISSN: 10454403     EISSN: None     Source Type: Journal    
DOI: 10.1615/CritRevEukarGeneExpr.v22.i1.50     Document Type: Review
Times cited : (127)

References (201)
  • 1
    • 0009342231 scopus 로고
    • An historic case of rickets: Being an account of the medical examination of the remains of Princess Elizabeth
    • daughter of King Charles I., who died at Carrisbrooke Castle, September 8, 1650
    • Burland C. An historic case of rickets: being an account of the medical examination of the remains of Princess Elizabeth, daughter of King Charles I., who died at Carrisbrooke Castle, September 8, 1650. Practitioner. 1918;100:391-5.
    • (1918) Practitioner , vol.100 , pp. 391-395
    • Burland, C.1
  • 2
    • 85038456047 scopus 로고
    • Rickets
    • second daughter of King Charles 1
    • T.E.C. J. Princess Elizabeth, second daughter of King Charles 1, and rickets. Pediatrics. 1979;64(2):241.
    • (1979) Pediatrics , vol.64 , Issue.2 , pp. 241
    • Elizabeth, T.E.C.J.P.1
  • 3
    • 33749252378 scopus 로고    scopus 로고
    • Rickets in the 17th century
    • O'Riordan JL. Rickets in the 17th century. J Bone Miner Res. 2006;21(10):1506-10.
    • (2006) J Bone Miner Res , vol.21 , Issue.10 , pp. 1506-1510
    • O'Riordan, J.L.1
  • 5
    • 0023352778 scopus 로고
    • Elmer McCollum and the disappearance of rickets
    • Rafter GW. Elmer McCollum and the disappearance of rickets. Perspect Biol Med. 1987;30(4):527-34.
    • (1987) Perspect Biol Med , vol.30 , Issue.4 , pp. 527-534
    • Rafter, G.W.1
  • 6
    • 0001343748 scopus 로고
    • The geographical distribution and aetiology of rickets
    • Palm T. The geographical distribution and aetiology of rickets. Practitioner. 1890;45(270-279):321-42.
    • (1890) Practitioner , vol.45 , Issue.270-279 , pp. 321-342
    • Palm, T.1
  • 10
    • 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):457-67.
    • (1994) Hum Genet , vol.94 , Issue.5 , pp. 457-467
    • Rowe, P.S.N.1
  • 11
    • 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 Hyperten. 1998;7(4):367-76.
    • (1998) Curr Opin Nephrol Hyperten , vol.7 , Issue.4 , pp. 367-376
    • Rowe, P.S.N.1
  • 12
    • 4243403618 scopus 로고    scopus 로고
    • Finding mutations in disease genes
    • In: Econs MJ, editor, 1 ed. Totowa, NJ: Humana Press
    • Rowe PSN. Finding mutations in disease genes. In: Econs MJ, editor. Genetics of osteoporosis and metabolic bone disease. 1 ed. Totowa, NJ: Humana Press; 2000. p. 431-46.
    • (2000) Genetics of Osteoporosis and Metabolic Bone Disease , pp. 431-446
    • Rowe, P.S.N.1
  • 13
    • 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):5135-36.
    • (1994) Nucleic Acids Res , vol.22 , Issue.23 , pp. 5135-5136
    • Rowe, P.S.N.1    Francis, F.2    Goulding, J.3
  • 20
    • 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):159-69.
    • (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
  • 21
    • 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):264-81.
    • (2004) Crit Rev Oral Biol Med , vol.15 , Issue.5 , pp. 264-281
    • Rowe, P.S.N.1
  • 22
    • 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):261-7.
    • (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
  • 23
    • 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, Schwarz PM, Lafer EM, Hedge AM, Rowe PS. 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):1757-72.
    • (2008) Endocrinology , vol.149 , Issue.4 , pp. 1757-1772
    • Martin, A.1    David, V.2    Laurence, J.S.3    Schwarz, P.M.4    Lafer, E.M.5    Hedge, A.M.6    Rowe, P.S.7
  • 24
    • 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, Carnes DL, Lafer EM, Mundy GR, Gutierrez GE. 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    Carnes, D.L.4    Lafer, E.M.5    Mundy, G.R.6    Gutierrez, G.E.7
  • 25
    • 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
  • 26
    • 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):4012-23.
    • (2009) EndocriNology , vol.150 , Issue.9 , pp. 4012-4023
    • David, V.1    Martin, A.2    Hedge, A.M.3    Rowe, P.S.4
  • 27
    • 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, Juliano MA, Loisel TP, Crine P, Juliano L, Boileau G, Carmona AK. 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):271-9.
    • (2003) Biochem J , vol.373 , Issue.1 , pp. 271-279
    • Campos, M.1    Couture, C.2    Hirata, I.Y.3    Juliano, M.A.4    Loisel, T.P.5    Crine, P.6    Juliano, L.7    Boileau, G.8    Carmona, A.K.9
  • 28
    • 11244270453 scopus 로고    scopus 로고
    • Serum MEPE-ASARM-peptides are elevated in Xlinked rickets (HYP): Implications for phosphaturia and rickets
    • Bresler D, Bruder J, Mohnike KL, Fraser D, Rowe PSN. Serum MEPE-ASARM-peptides are elevated in Xlinked 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
  • 32
    • 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):1638-49.
    • (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
  • 33
    • 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, Welldon KJ, Ormsby R, Wijenayaka AR, Zelenchuk L, Evdokiou A, Findlay DM. 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):1425-36
    • (2011) J Bone Miner Res , vol.27 , Issue.7 , pp. 1425-1436
    • Atkins, G.J.1    Rowe, P.S.2    Lim, H.P.3    Welldon, K.J.4    Ormsby, R.5    Wijenayaka, A.R.6    Zelenchuk, L.7    Evdokiou, A.8    Findlay, D.M.9
  • 35
    • 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):730-3.
    • (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
  • 36
    • 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):2313-20.
    • (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
  • 37
    • 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):3191-5.
    • (2010) Nephrol Dial Transplant , vol.25 , Issue.10 , pp. 3191-3195
    • Shirley, D.G.1    Faria, N.J.2    Unwin, R.J.3    Dobbie, H.4
  • 38
    • 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):3135-6.
    • (2010) Nephrol Dial Transplant , vol.25 , Issue.10 , pp. 3135-3136
    • Friedlander, G.1
  • 39
    • 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
  • 40
    • 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):1264-6.
    • (1969) Science , vol.165 , Issue.899 , pp. 1264-1266
    • Francis, M.D.1    Russell, R.G.2    Fleisch, H.3
  • 41
    • 34247527341 scopus 로고    scopus 로고
    • Thermodynamic roles of basic amino acids in statherin recognition of hydroxyapatite
    • 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):4725-33.
    • (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
  • 42
    • 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):1689-95.
    • (1977) J Biol Chem , vol.252 , Issue.5 , pp. 1689-1695
    • Schlesinger, D.H.1    Hay, D.I.2
  • 50
    • 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. Calcified Tissue Int. 2010;87(5):461-8. PMCID: 2964475.
    • (2010) Calcified Tissue Int , vol.87 , Issue.5 , pp. 461-468
    • Kulkarni, R.N.1    Bakker, A.D.2    Everts, V.3    Klein-Nulend, J.4
  • 51
  • 52
    • 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, Wang L, Hata K, Ooshima T, Yoneda T. 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):1743-51.
    • (2007) J Bone Miner Res , vol.22 , Issue.11 , pp. 1743-1751
    • Hayashibara, T.1    Hiraga, T.2    Sugita, A.3    Wang, L.4    Hata, K.5    Ooshima, T.6    Yoneda, T.7
  • 55
  • 57
    • 58149109303 scopus 로고    scopus 로고
    • Recent advances in the renalskeletal-gut axis that controls phosphate homeostasis
    • Kiela PR, Ghishan FK. Recent advances in the renalskeletal-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
  • 58
    • 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
  • 59
    • 84860337972 scopus 로고    scopus 로고
    • PHEX & MEPE ASARM-motif regulate a novel bone-renal and fat-mass pathway (Abstract)
    • Abstract available from
    • 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 available from: http://www.asbmr.org/Meetings/AnnualMeeting/AbstractDetail.aspx?aid=d79d078c-e7b7-48de-ab35-83b08139efdd.
    • (2009) J Bone Miner Res , vol.24 , Issue.1 SUPPL.
    • David, V.1    Martin, A.2    Hedge, A.M.3    Rowe, P.S.4
  • 60
    • 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, RiveraGonzalez 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):36172-80.
    • (2000) J Biol Chem , vol.275 , Issue.46 , pp. 36172-36180
    • Petersen, D.N.1    Tkalcevic, G.T.2    Mansolf, A.L.3    Riveragonzalez, R.4    Brown, T.A.5
  • 61
    • 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):342-51.
    • (2001) Genomics , vol.74 , Issue.3 , pp. 342-351
    • Argiro, L.1    Desbarats, M.2    Glorieux, F.H.3    Ecarot, B.4
  • 63
    • 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):3698-702.
    • (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
  • 64
    • 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):5931-42.
    • (1980) J Biol Chem , vol.255 , Issue.12 , pp. 5931-5942
    • Linde, A.1    Bhown, M.2    Butler, W.T.3
  • 65
    • 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;272:835-42.
    • (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
  • 66
    • 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):21695-8.
    • (1996) J Biol Chem , vol.271 , Issue.36 , pp. 21695-21698
    • Ritchie, H.H.1    Wang, L.H.2
  • 67
    • 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):17472-9.
    • (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
  • 68
    • 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 Min Res. 2011;26(1):220-8.
    • (2011) J Bone Min 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
  • 69
    • 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):481-8.
    • (2002) Proteins , vol.47 , Issue.4 , pp. 481-488
    • Bianchetti, L.1    Oudet, C.2    Poch, O.3
  • 71
    • 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):723-7.
    • (2003) Biochem Soc Trans , vol.31 , Issue.3 Pt , pp. 723-727
    • Turner, A.J.1
  • 72
    • 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):261-9.
    • (2001) Bioessays , vol.23 , Issue.3 , pp. 261-269
    • Turner, A.J.1    Isaac, R.E.2    Coates, D.3
  • 73
    • 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.1 SUPPL. , pp. 33-40
    • Fisher, L.W.1    Fedarko, N.S.2
  • 76
    • 73849099954 scopus 로고    scopus 로고
    • MEPE evolution in mammals reveals regions and residues of prime functional importance
    • 305-302
    • 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):305-2.
    • (2010) Cell Mol Life Sci , vol.67 , Issue.2
    • Bardet, C.1    Delgado, S.2    Sire, J.Y.3
  • 78
    • 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):1256-62.
    • (2008) J Orthop Res , vol.26 , Issue.9 , pp. 1256-1262
    • Sprowson, A.P.1    McCaskie, A.W.2    Birch, M.A.3
  • 80
    • 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):1107-14.
    • (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
  • 82
    • 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):496-9.
    • (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
  • 84
    • 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, Chen B, Wu Y, Chuang HH, Qin C, MacDougall M. Expression and processing of small integrin-binding ligand N-linked glycoproteins in mouse odontoblastic cells. Arch Oral Biol. 2008;53(9):879-89.
    • (2008) Arch Oral Biol , vol.53 , Issue.9 , pp. 879-889
    • Chen, S.1    Chen, L.2    Jahangiri, A.3    Chen, B.4    Wu, Y.5    Chuang, H.H.6    Qin, C.7    Macdougall, M.8
  • 85
    • 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;760:249-56.
    • (1995) Ann N Y Acad Sci , vol.760 , pp. 249-256
    • Boskey, A.L.1
  • 87
    • 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):2933-45. 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
  • 88
    • 77957288774 scopus 로고    scopus 로고
    • Abnormal presence of the matrix extracellular phosphoglycoprotein-derived acidic serineand aspartate-rich motif peptide in human hypophosphatemic dentin
    • PMCID: 2913338
    • Boukpessi T, Gaucher C, Leger T, Salmon B, Le Faouder J, Willig C, Rowe PS, Garabedian M, Meilhac O, Chaussain C. Abnormal presence of the matrix extracellular phosphoglycoprotein-derived acidic serineand 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    Salmon, B.4    le Faouder, J.5    Willig, C.6    Rowe, P.S.7    Garabedian, M.8    Meilhac, O.9    Chaussain, C.10
  • 91
    • 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):155-66.
    • (2005) Kidney Int , vol.68 , Issue.1 , pp. 155-166
    • Ogbureke, K.U.1    Fisher, L.W.2
  • 92
    • 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 U S A. 1998;95:5372-7.
    • (1998) Proc Natl Acad Sci U S A , 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
  • 93
    • 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):644-57.
    • (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
  • 94
    • 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, Wang D, Khadeer MA, Namba N, Feng X, Hruska KA. Identification of the type II Na(+)-Pi cotransporter (Npt2) in the osteoclast and the skeletal phenotype of Npt2-/mice. Bone. 2001;29(5):467-76.
    • (2001) Bone , vol.29 , Issue.5 , pp. 467-476
    • Gupta, A.1    Tenenhouse, H.S.2    Hoag, H.M.3    Wang, D.4    Khadeer, M.A.5    Namba, N.6    Feng, X.7    Hruska, K.A.8
  • 95
    • 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):F675-81.
    • (2003) Am J Physiol Renal Physiol , vol.286 , Issue.4
    • Tenenhouse, H.S.1    Gauthier, C.2    Chau, H.3    St-Arnaud, R.4
  • 96
    • 33644987045 scopus 로고    scopus 로고
    • Effects of aldosterone on the vasculature
    • Schiffrin EL. Effects of aldosterone on the vasculature. Hypertension. 2006;47(3):312-8.
    • (2006) Hypertension , vol.47 , Issue.3 , pp. 312-318
    • Schiffrin, E.L.1
  • 97
    • 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):1933-7.
    • (2004) Circulation , vol.109 , Issue.16 , pp. 1933-1937
    • Michel, F.1    Ambroisine, M.L.2    Duriez, M.3    Delcayre, C.4    Levy, B.I.5    Silvestre, J.S.6
  • 101
    • 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):1603-9. PMCID: 3171931.
    • (2011) J Am Soc Nephrol , vol.22 , Issue.9 , pp. 1603-1609
    • de Borst, M.H.1    Vervloet, M.G.2    Ter, W.P.M.3    Navis, G.4
  • 102
    • 38849170631 scopus 로고    scopus 로고
    • Aberrant Phex function in osteoblasts and osteocytes alone underlies murine X-linked hypophosphatemia
    • Yuan B, Takaiwa M, Clemens TL, Feng JQ, Kumar R, Rowe PS, Xie Y, Drezner MK. Aberrant Phex function in osteoblasts and osteocytes alone underlies murine X-linked hypophosphatemia. J Clin Invest. 2008;118(2):722-34.
    • (2008) J Clin Invest , vol.118 , Issue.2 , pp. 722-734
    • Yuan, B.1    Takaiwa, M.2    Clemens, T.L.3    Feng, J.Q.4    Kumar, R.5    Rowe, P.S.6    Xie, Y.7    Drezner, M.K.8
  • 103
    • 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, Li H, Karydis A, Feng JQ, Quarles LD. 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):2551-62.
    • (2011) Faseb J , vol.25 , Issue.8 , pp. 2551-2562
    • Martin, A.1    Liu, S.2    David, V.3    Li, H.4    Karydis, A.5    Feng, J.Q.6    Quarles, L.D.7
  • 105
    • 84860333695 scopus 로고    scopus 로고
    • Mechanism of hexa-D-arginine curative effects on the HYP phenotype (abstract)
    • (Suppl 1), SA0032, Abstract available from
    • 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. Abstract available from: http://www.abstracts2view.com/asbmr/view.php?nu=ASBMR11L_A11007509-52&terms=.
    • (2011) J Bone Miner Res , vol.26
    • Yuan, B.1    Bowman, S.2    Blank, R.3    Lindberg, I.4    Drezner, M.K.5
  • 106
    • 84860336825 scopus 로고    scopus 로고
    • HexaD-arginine reversal of osteoblast 7B2 dysregulation in Hyp-mice normalizes the HYP biochemical phenotype (abstract)
    • (Presentation No: #1015). Abstract available from
    • Yuan B, Meudt J, Blank R, Feng J, Drezner MK. HexaD-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). Abstract available from: http://www.asbmr.org/Meetings/AnnualMeeting/AbstractDetail.aspx?aid=c5c1b1c6-9d98-4ec8-bafa-833ec5088097.
    • (2010) J Bone Miner Res , vol.25 , Issue.1 SUPPL.
    • Yuan, B.1    Meudt, J.2    Blank, R.3    Feng, J.4    Drezner, M.K.5
  • 107
    • 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):5986-95. PMCID: 2484124.
    • (2008) Biochemistry , vol.47 , Issue.22 , pp. 5986-5995
    • Jain, A.1    Fisher, L.W.2    Fedarko, N.S.3
  • 108
    • 3042703295 scopus 로고    scopus 로고
    • Three small integrin-binding ligand N-linked glycoproteins (SIB-LINGs) bind and activate specific matrix metalloproteinases
    • Fedarko NS, Jain A, Karadag A, Fisher LW. Three small integrin-binding ligand N-linked glycoproteins (SIB-LINGs) bind and activate specific matrix metalloproteinases. FASEB J. 2004;18.(6):734-6.
    • (2004) FASEB J , vol.18 , Issue.6 , pp. 734-736
    • Fedarko, N.S.1    Jain, A.2    Karadag, A.3    Fisher, L.W.4
  • 109
    • 0035671826 scopus 로고    scopus 로고
    • Elevated serum bone sialoprotein and osteopontin in colon, breast, prostate, and lung cancer
    • Fedarko NS, Jain A, Karadag A, Van Eman MR, Fisher LW. Elevated serum bone sialoprotein and osteopontin in colon, breast, prostate, and lung cancer. Clin Cancer Res. 2001;7(12):4060-6.
    • (2001) Clin Cancer Res , vol.7 , Issue.12 , pp. 4060-4066
    • Fedarko, N.S.1    Jain, A.2    Karadag, A.3    van Eman, M.R.4    Fisher, L.W.5
  • 110
    • 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):11545-52. PMCID: 1350722.
    • (2005) Cancer Res , vol.65 , Issue.24 , pp. 11545-11552
    • Karadag, A.1    Fedarko, N.S.2    Fisher, L.W.3
  • 111
    • 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):956-65.
    • (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
  • 112
    • 84860337992 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.
    • (2011) J Biol Chem
    • Eapen, A.S.1    Ramachandran, A.2    George, A.3
  • 114
    • 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, Ito M, Tomokiyo A, Tanaka T, Akamine A. 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):1045-53.
    • (2004) Hum Gene Ther , vol.15 , Issue.11 , pp. 1045-1053
    • Nakashima, M.1    Iohara, K.2    Ishikawa, M.3    Ito, M.4    Tomokiyo, A.5    Tanaka, T.6    Akamine, A.7
  • 115
    • 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):589-98.
    • (2005) Bone , vol.37 , Issue.4 , pp. 589-598
    • Alos, N.1    Ecarot, B.2
  • 116
    • 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):4835-45.
    • (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
  • 117
    • 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):17500-8.
    • (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
  • 118
    • 84860336834 scopus 로고    scopus 로고
    • DMP1 does not function as a co-transcriptional factor (abstract)
    • MO0112. Abstract available from
    • Yuan B, Lin S, Cao Z, Liu Y, Lu Y, Drezner MK, Feng J. DMP1 does not function as a co-transcriptional factor (abstract). J Bone Miner Res 2011;26(Suppl 1):MO0112. Abstract available from: (http://www.abstracts2view.com/asbmr/view.php?nu=ASBMR11L_A1100701-127&terms=).
    • (2011) J Bone Miner Res , vol.26 , Issue.1 SUPPL.
    • Yuan, B.1    Lin, S.2    Cao, Z.3    Liu, Y.4    Lu, Y.5    Drezner, M.K.6    Feng, J.7
  • 120
    • 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):248-53.
    • (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
  • 121
    • 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):394-9.
    • (2002) J Am Soc Nephrol , vol.13 , Issue.2 , pp. 394-399
    • Shih, N.R.1    Jo, O.D.2    Yanagawa, N.3
  • 122
    • 69949159609 scopus 로고    scopus 로고
    • Molecular regulation of matrix extracellular phosphoglycoprotein expression by bone morphogenetic protein-2
    • Cho YD, Yoon WJ, Woo KM, Baek JH, Lee G, Cho JY, Ryoo HM. 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    Baek, J.H.4    Lee, G.5    Cho, J.Y.6    Ryoo, H.M.7
  • 123
    • 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):2634-46
    • (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
  • 127
  • 129
    • 29744463149 scopus 로고    scopus 로고
    • 1α,25-dihydroxyvitamin D3 inhibits prostate cancer cell invasion via modulation of selective proteases
    • Bao BY, Yeh SD, Lee YF. 1α,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
  • 130
    • 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. Calcified Tissue Int. 2005;76(6):439-47.
    • (2005) Calcified 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
  • 132
    • 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):C1414-21.
    • (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
  • 133
    • 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;75:1858-68.
    • (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
  • 134
    • 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;111:904-11.
    • (1982) Endocrinology , vol.111 , pp. 904-911
    • Marie, P.J.1    Travers, R.2    Glorieux, F.H.3
  • 135
    • 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):1846-50. 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
  • 136
    • 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):2164-8.
    • (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
  • 137
  • 139
    • 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
  • 140
    • 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):1253-9.
    • (1992) J Am Soc Nephrol , vol.3 , Issue.6 , pp. 1253-1259
    • Loghman-Adham, M.1    Szczepanska-Konkel, M.2    Dousa, T.P.3
  • 142
    • 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.1 SUPPL.
    • McCloskey, E.V.1    Yates, A.J.2    Beneton, M.N.3    Galloway, J.4    Harris, S.5    Kanis, J.A.6
  • 144
    • 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):171-7.
    • (1981) Clin Sci (Lond) , vol.60 , Issue.2 , pp. 171-177
    • Muhlbauer, R.C.1    Bonjour, J.P.2    Fleisch, H.3
  • 145
    • 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
  • 146
    • 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):F13-6.
    • (1980) Am J Physiol , vol.239 , Issue.1
    • Stoll, R.1    Fleisch, H.2    Bonjour, J.P.3
  • 147
    • 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;261:6375-83.
    • (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
  • 148
    • 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
  • 150
    • 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):F363-70 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
  • 151
    • 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;137:943-8.
    • (1996) Endocrinology , vol.137 , pp. 943-948
    • Nesbitt, T.1    Byun, J.K.2    Drezner, M.K.3
  • 152
    • 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;10:1327-33.
    • (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
  • 153
    • 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):8000-10.
    • (1987) J Biol Chem , vol.262 , Issue.17 , pp. 8000-8010
    • Szczepanska-Konkel, M.1    Yusufi, A.N.2    Dousa, T.P.3
  • 154
    • 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):1223-9.
    • (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
  • 155
    • 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):1192-9.
    • (1999) Endocrinology , vol.140 , Issue.3 , pp. 1192-1199
    • Ecarot, B.1    Desbarats, M.2
  • 156
    • 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, Serey SH, Sirjani NB, Kiela PR, Jurutka PW, Haussler MR, Collins JF, Ghishan FK. 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):46406-14
    • (2004) J Biol Chem , vol.279 , Issue.45 , pp. 46406-46414
    • Hines, E.R.1    Kolek, O.I.2    Jones, M.D.3    Serey, S.H.4    Sirjani, N.B.5    Kiela, P.R.6    Jurutka, P.W.7    Haussler, M.R.8    Collins, J.F.9    Ghishan, F.K.10
  • 157
    • 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):980-6.
    • (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
  • 158
    • 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
  • 160
    • 78651495664 scopus 로고    scopus 로고
    • Leptin-dependent serotonin control of appetite: Temporal specificity, transcriptional regulation, and therapeutic implications
    • Yadav VK, Oury F, Tanaka K, Thomas T, Wang Y, Cremers S, Hen R, Krust A, Chambon P, Karsenty G. 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    Thomas, T.4    Wang, Y.5    Cremers, S.6    Hen, R.7    Krust, A.8    Chambon, P.9    Karsenty, G.10
  • 161
    • 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):161-6.
    • (2008) Trends Endocrinol Metab , vol.19 , Issue.5 , pp. 161-166
    • Lee, N.K.1    Karsenty, G.2
  • 162
    • 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):2002-11
    • (2011) J Bone Miner Res , vol.26 , Issue.9 , pp. 2002-2011
    • Goltzman, D.1
  • 164
    • 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
  • 165
    • 80055119531 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. 2010.
    • (2010) J Bone Miner Res
    • Clemens, T.L.1    Karsenty, G.2
  • 166
    • 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):236-53.
    • (2009) Cell Mol Life Sci , vol.66 , Issue.2 , pp. 236-253
    • Muruganandan, S.1    Roman, A.A.2    Sinal, C.J.3
  • 167
    • 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, de Freitas PH, Oda K, Maeda T, Takagi R, Amizuka N. 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):381-92.
    • (2009) J Electron Microsc (Tokyo) , vol.58 , Issue.6 , pp. 381-392
    • Ubaidus, S.1    Li, M.2    Sultana, S.3    de Freitas, P.H.4    Oda, K.5    Maeda, T.6    Takagi, R.7    Amizuka, N.8
  • 168
    • 84860336832 scopus 로고    scopus 로고
    • PHEX and Fat Energy Metabolism across a Bone-Renal Axis (Abstract)
    • Abstract available from
    • 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 available from: http://www.abstracts2view.com/asbmr/view.php?nu=ASBMR11L_A11007466-89&terms=.
    • (2011) J Bone Miner Res , vol.26 , Issue.1 SUPPL.
    • Rowe, P.S.1    Hedge, A.M.2    David, V.3    Zelenchuk, L.4
  • 169
    • 0022560637 scopus 로고
    • Vitamin D3 improves impaired glucose tolerance and insulin secretion in the vitamin Ddeficient rat in vivo
    • Cade C, Norman AW. Vitamin D3 improves impaired glucose tolerance and insulin secretion in the vitamin Ddeficient 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
  • 170
    • 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):1490-7.
    • (1987) EndocriNology , vol.120 , Issue.4 , pp. 1490-1497
    • Cade, C.1    Norman, A.W.2
  • 171
    • 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):328-34.
    • (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
  • 174
    • 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):60-3.
    • (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
  • 175
    • 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):288-92.
    • (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
  • 176
    • 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):509-11.
    • (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
  • 177
    • 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):75-84.
    • (2007) Matrix Biol , vol.26 , Issue.2 , pp. 75-84
    • Hesse, M.1    Frohlich, L.F.2    Zeitz, U.3    Lanske, B.4    Erben, R.G.5
  • 181
    • 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
  • 182
    • 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):875-83.
    • (2009) Am J Kidney Dis , vol.53 , Issue.5 , pp. 875-883
    • Marsenic, O.1
  • 183
    • 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):382-91.
    • (2001) Diabetes Care , vol.24 , Issue.2 , pp. 382-391
    • Gerich, J.E.1    Meyer, C.2    Woerle, H.J.3    Stumvoll, M.4
  • 184
    • 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
  • 185
    • 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
  • 186
    • 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):1259-63.
    • (1980) N Engl J Med , vol.303 , Issue.22 , pp. 1259-1263
    • Defronzo, R.A.1    Lang, R.2
  • 187
    • 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.2 PART , pp. 393-396
    • Xie, W.1    Li, Y.2    Mechin, M.C.3    van de Werve, G.4
  • 188
    • 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.1 PART , pp. 227-232
    • Xie, W.1    Tran, T.L.2    Finegood, D.T.3    van de Werve, G.4
  • 189
    • 84860333243 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. 2011.
    • (2011) Scand J Clin Lab InVest
    • Winther, K.1    Nybo, M.2    Vind, B.3    Pedersen, S.M.4    Hojlund, K.5    Rasmussen, L.M.6
  • 190
    • 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;12:507-10.
    • (1996) Comput Appl Biosci , vol.12 , pp. 507-510
    • Duret, L.1    Gasteiger, E.2    Perriere, G.3
  • 192
  • 193
    • 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):785-6.
    • (2011) Nat Methods , vol.8 , Issue.10 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 195
    • 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):396-9.
    • (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
  • 197
    • 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
  • 198
    • 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 U S A. 2008;105(13):5266-70. PMCID: 2278202.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.13 , pp. 5266-5270
    • Ferron, M.1    Hinoi, E.2    Karsenty, G.3    Ducy, P.4
  • 199
    • 77955035304 scopus 로고    scopus 로고
    • Insulin signaling in osteoblasts integrates bone remodeling and energy metabolism
    • PMCID: 2910411
    • Ferron M, Wei J, Yoshizawa T, Del Fattore A, DePinho RA, Teti A, Ducy P, Karsenty G. 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    del Fattore, A.4    Depinho, R.A.5    Teti, A.6    Ducy, P.7    Karsenty, G.8
  • 200
    • 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):4795-801.
    • (2010) J Clin Endocrinol Metab , vol.95 , Issue.11 , pp. 4795-4801
    • Karsenty, G.1    Oury, F.2
  • 201
    • 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):120-8.
    • (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.