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Volumn 380, Issue 1-2, 2007, Pages 13-23

Hepatic surgery-related hypophosphatemia

Author keywords

Hypophosphatemia; Liver; Metabolic stress; Nucleotide metabolism; Phosphatonins

Indexed keywords

FIBROBLAST GROWTH FACTOR 23; FRIZZLED PROTEIN; GLYCOPROTEIN; NUCLEOTIDE; PARATHYROID HORMONE; PHOSPHATE; PHOSPHATONIN DERIVATIVE; UNCLASSIFIED DRUG; VITAMIN D;

EID: 33947713045     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cca.2007.01.027     Document Type: Review
Times cited : (30)

References (123)
  • 2
    • 0026554110 scopus 로고
    • Hypophosphataemia after major hepatic resection
    • George R., and Shiu M.H. Hypophosphataemia after major hepatic resection. Surgery 111 (1992) 281-286
    • (1992) Surgery , vol.111 , pp. 281-286
    • George, R.1    Shiu, M.H.2
  • 4
    • 12144282408 scopus 로고    scopus 로고
    • Hypophosphataemia after right hepatectomy for living donor liver transplantation
    • Burak K.W., Rosen C.B., Fidler J.L., et al. Hypophosphataemia after right hepatectomy for living donor liver transplantation. Can J Gastroenterol 18 (2004) 729-733
    • (2004) Can J Gastroenterol , vol.18 , pp. 729-733
    • Burak, K.W.1    Rosen, C.B.2    Fidler, J.L.3
  • 5
    • 0031926966 scopus 로고    scopus 로고
    • The clinical implications of hypophosphatemia following major hepatic resection or cryosurgery
    • Buell S.E., Berger A.C., Polkin J.S., Kuo P.S., and Johnson L.B. The clinical implications of hypophosphatemia following major hepatic resection or cryosurgery. Arch Surg 133 (1998) 757-761
    • (1998) Arch Surg , vol.133 , pp. 757-761
    • Buell, S.E.1    Berger, A.C.2    Polkin, J.S.3    Kuo, P.S.4    Johnson, L.B.5
  • 6
    • 25444528711 scopus 로고    scopus 로고
    • Hypophosphataemia: an update on its aetiology and treatment
    • Gaasbeek A., and Meinders A.E. Hypophosphataemia: an update on its aetiology and treatment. Am J Med 10 (2005) 1094-1101
    • (2005) Am J Med , vol.10 , pp. 1094-1101
    • Gaasbeek, A.1    Meinders, A.E.2
  • 7
    • 0041377996 scopus 로고    scopus 로고
    • Intravenous phosphate in the intensive care unit: More aggressive treatment for moderate hypophosphataemia
    • Charron T., Bernard F., Skrobik Y., Simoneau N., Gagnon N., and Leblank M. Intravenous phosphate in the intensive care unit: More aggressive treatment for moderate hypophosphataemia. Intensive Care Med 8 (2003) 1273-1278
    • (2003) Intensive Care Med , vol.8 , pp. 1273-1278
    • Charron, T.1    Bernard, F.2    Skrobik, Y.3    Simoneau, N.4    Gagnon, N.5    Leblank, M.6
  • 8
    • 0021068428 scopus 로고
    • High dose intravenous phosphorus therapy for severe, complicated hypophosphatemia
    • Vannatta J.B., Andress D.L., Wang R., and Papper S. High dose intravenous phosphorus therapy for severe, complicated hypophosphatemia. South Med J 76 (1983) 1424-1426
    • (1983) South Med J , vol.76 , pp. 1424-1426
    • Vannatta, J.B.1    Andress, D.L.2    Wang, R.3    Papper, S.4
  • 9
    • 0024651580 scopus 로고
    • Postoperative hypophosphatemia: a multifactorial problem
    • Tucker S.B., and Schimmel E.M. Postoperative hypophosphatemia: a multifactorial problem. Nutr Rev 47 (1989) 111-116
    • (1989) Nutr Rev , vol.47 , pp. 111-116
    • Tucker, S.B.1    Schimmel, E.M.2
  • 10
    • 0024598467 scopus 로고
    • Physiologic regulation of the serum concentration of 1,25-dihydroxyvitamin D by phosphorus in normal men
    • Portale A.A., Halloran B.P., and Morris Jr. R.C. Physiologic regulation of the serum concentration of 1,25-dihydroxyvitamin D by phosphorus in normal men. J Clin Invest 83 (1989) 1494-1499
    • (1989) J Clin Invest , vol.83 , pp. 1494-1499
    • Portale, A.A.1    Halloran, B.P.2    Morris Jr., R.C.3
  • 11
    • 0031695635 scopus 로고    scopus 로고
    • The influence of hyperinsulinaemia on calcium-phosphate metabolism in renal
    • Nowicki M., Kokot F., and Surdacki A. The influence of hyperinsulinaemia on calcium-phosphate metabolism in renal. Nephrol Dial Transplant 13 (1998) 2566-2571
    • (1998) Nephrol Dial Transplant , vol.13 , pp. 2566-2571
    • Nowicki, M.1    Kokot, F.2    Surdacki, A.3
  • 13
    • 0036203628 scopus 로고    scopus 로고
    • Postdialytic rebound of serum phosphorus: pathogenetic and clinical insights
    • Minutolo R., Bellizzi V., Cioffi M., et al. Postdialytic rebound of serum phosphorus: pathogenetic and clinical insights. J Am Soc Nephrol 13 (2002) 1046-1054
    • (2002) J Am Soc Nephrol , vol.13 , pp. 1046-1054
    • Minutolo, R.1    Bellizzi, V.2    Cioffi, M.3
  • 14
    • 0032754618 scopus 로고    scopus 로고
    • Metabolic aspects of phosphate replacement therapy for hypophosphatemia after renal transplantation: impact on muscular phosphate content, mineral metabolism, and acid/base homeostasis
    • Ambuhl P.M., Meier D., Wolf B., Dydak U., Boesiger P., and Binswanger U. Metabolic aspects of phosphate replacement therapy for hypophosphatemia after renal transplantation: impact on muscular phosphate content, mineral metabolism, and acid/base homeostasis. Am J Kidney Dis 34 (1999) 875-883
    • (1999) Am J Kidney Dis , vol.34 , pp. 875-883
    • Ambuhl, P.M.1    Meier, D.2    Wolf, B.3    Dydak, U.4    Boesiger, P.5    Binswanger, U.6
  • 15
    • 0017032590 scopus 로고
    • Hypophosphatemia: mouse model for human familial hypophosphatemic (vitamin D-resistant) rickets
    • Eicher E.M., Southard J.L., Scriver C.R., and Glorieux F.H. Hypophosphatemia: mouse model for human familial hypophosphatemic (vitamin D-resistant) rickets. Proc Natl Acad Sci U S A 73 (1976) 4667-4671
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 4667-4671
    • Eicher, E.M.1    Southard, J.L.2    Scriver, C.R.3    Glorieux, F.H.4
  • 16
    • 0024330123 scopus 로고
    • Parabiosis suggests a humoral factor is involved in X-linked hypophosphatemia in mice
    • Meyer Jr. R.A., Meyer M.H., and Gray R.W. Parabiosis suggests a humoral factor is involved in X-linked hypophosphatemia in mice. J Bone Miner Res 4 (1989) 493-500
    • (1989) J Bone Miner Res , vol.4 , pp. 493-500
    • Meyer Jr., R.A.1    Meyer, M.H.2    Gray, R.W.3
  • 17
    • 23444447617 scopus 로고
    • Brief report: inhibition of renal phosphate transport by a tumor product in a patient with oncogenic osteomalacia
    • Cai Q., Hodgson S.F., Kao P.C., et al. Brief report: inhibition of renal phosphate transport by a tumor product in a patient with oncogenic osteomalacia. N Engl J Med 330 (1994) 1645-1649
    • (1994) N Engl J Med , vol.330 , pp. 1645-1649
    • Cai, Q.1    Hodgson, S.F.2    Kao, P.C.3
  • 18
    • 0028363099 scopus 로고
    • Tumor-induced osteomalacia-unveiling a new hormone
    • Econs M.J., and Drezner M.K. Tumor-induced osteomalacia-unveiling a new hormone. N Engl J Med 330 (1994) 1679-1681
    • (1994) N Engl J Med , vol.330 , pp. 1679-1681
    • Econs, M.J.1    Drezner, M.K.2
  • 19
    • 0030469460 scopus 로고    scopus 로고
    • Hypophosphatemia induced in mice by transplantation of a tumor-derived cell line from a patient with oncogenic rickets
    • Chalew S.A., Lovechild J.C., Brown C.M., and Sun C.-C.J. Hypophosphatemia induced in mice by transplantation of a tumor-derived cell line from a patient with oncogenic rickets. J Pediatr Endocrinol Metab 9 (1996) 593-597
    • (1996) J Pediatr Endocrinol Metab , vol.9 , pp. 593-597
    • Chalew, S.A.1    Lovechild, J.C.2    Brown, C.M.3    Sun, C.-C.J.4
  • 20
    • 33646529865 scopus 로고    scopus 로고
    • The roles of specific genes implicated as circulating factors involved in normal and disordered phosphate homeostasis: frizzled related protein-4, matrix extracellular phosphoglycoprotein, and fibroblast growth factor 23
    • White K.E., Larsson T.E., and Econs M.J. The roles of specific genes implicated as circulating factors involved in normal and disordered phosphate homeostasis: frizzled related protein-4, matrix extracellular phosphoglycoprotein, and fibroblast growth factor 23. Endocr Rev 27 (2006) 221-241
    • (2006) Endocr Rev , vol.27 , pp. 221-241
    • White, K.E.1    Larsson, T.E.2    Econs, M.J.3
  • 21
    • 0141500265 scopus 로고    scopus 로고
    • Evidence for a bone-kidney axis regulating phosphate homeostasis
    • Qurales L.D. Evidence for a bone-kidney axis regulating phosphate homeostasis. J Clin Invest 112 (2003) 642-646
    • (2003) J Clin Invest , vol.112 , pp. 642-646
    • Qurales, L.D.1
  • 22
    • 0347362503 scopus 로고    scopus 로고
    • The phosphatonin pathway: new insights in phosphate homeostasis
    • Schiavi S.C., and Kumar R. The phosphatonin pathway: new insights in phosphate homeostasis. Kidney Int 65 (2004) 1-14
    • (2004) Kidney Int , vol.65 , pp. 1-14
    • Schiavi, S.C.1    Kumar, R.2
  • 23
    • 11244352700 scopus 로고    scopus 로고
    • The wrickkened pathways of FGF23, MEPE and PHEX
    • Rowe P.S. The wrickkened pathways of FGF23, MEPE and PHEX. Crit Rev Oral Biol Med 15 (2004) 264-281
    • (2004) Crit Rev Oral Biol Med , vol.15 , pp. 264-281
    • Rowe, P.S.1
  • 24
    • 0031452349 scopus 로고    scopus 로고
    • Autosomaldominant hypophosphatemic rickets is linked to chromosome 12p13
    • Econs M.J., McEnery P.T., Lennon F., and Speer M.C. Autosomaldominant hypophosphatemic rickets is linked to chromosome 12p13. J Clin Invest 100 (1997) 2653-2657
    • (1997) J Clin Invest , vol.100 , pp. 2653-2657
    • Econs, M.J.1    McEnery, P.T.2    Lennon, F.3    Speer, M.C.4
  • 25
    • 0033763097 scopus 로고    scopus 로고
    • Autosomal dominant hypophosphatemicrickets is associated with mutations in FGF23
    • The ADHR Consortium. Autosomal dominant hypophosphatemicrickets is associated with mutations in FGF23. Nat Genet 26 (2000) 345-348
    • (2000) Nat Genet , vol.26 , pp. 345-348
    • The ADHR Consortium1
  • 26
    • 14344279878 scopus 로고    scopus 로고
    • Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia
    • Shimada T., Mizutani S., Muto T., et al. Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia. Proc Natl Acad Sci U S A 98 (2001) 6500-6505
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6500-6505
    • Shimada, T.1    Mizutani, S.2    Muto, T.3
  • 27
    • 9144231813 scopus 로고    scopus 로고
    • Most osteomalacia-associated mesenchymal tumors are a single histopathologic entity: an analysis of 32 cases and a comprehensive review of the literature
    • Folpe A.L., Fanburg-Smith J.C., Billings S.D., et al. Most osteomalacia-associated mesenchymal tumors are a single histopathologic entity: an analysis of 32 cases and a comprehensive review of the literature. Am J Surg Pathol 28 (2004) 1-30
    • (2004) Am J Surg Pathol , vol.28 , pp. 1-30
    • Folpe, A.L.1    Fanburg-Smith, J.C.2    Billings, S.D.3
  • 28
  • 29
    • 85047691059 scopus 로고    scopus 로고
    • FGF-23 in fibrous dysplasia of bone and its relationship to renal phosphate wasting
    • Riminucci M., Collins M.T., Fedarko N.S., et al. FGF-23 in fibrous dysplasia of bone and its relationship to renal phosphate wasting. J Clin Invest 112 (2003) 83-92
    • (2003) J Clin Invest , vol.112 , pp. 83-92
    • Riminucci, M.1    Collins, M.T.2    Fedarko, N.S.3
  • 30
    • 17844392596 scopus 로고    scopus 로고
    • Fibroblast growth factor 23 reduces expression of type IIa Na+/Pi co-transporter by signaling through a receptor functionally distinct from the known FGFRs in opossum kidney cells
    • Yan X., Yokote H., Jing X., et al. Fibroblast growth factor 23 reduces expression of type IIa Na+/Pi co-transporter by signaling through a receptor functionally distinct from the known FGFRs in opossum kidney cells. Genes Cells 10 (2005) 489-502
    • (2005) Genes Cells , vol.10 , pp. 489-502
    • Yan, X.1    Yokote, H.2    Jing, X.3
  • 31
    • 2342648890 scopus 로고    scopus 로고
    • Resolution of severe, adolescent-onset hypophosphatemic rickets following resection of an FGF-23-producing tumour of the distal ulna
    • Ward L.M., Rauch F., White K.E., et al. Resolution of severe, adolescent-onset hypophosphatemic rickets following resection of an FGF-23-producing tumour of the distal ulna. Bone 34 (2004) 905-911
    • (2004) Bone , vol.34 , pp. 905-911
    • Ward, L.M.1    Rauch, F.2    White, K.E.3
  • 32
    • 0033775213 scopus 로고    scopus 로고
    • Proximal tubular phosphate reabsorption: molecular mechanisms
    • Murer H., Hernando N., Forster I., and Biber J. Proximal tubular phosphate reabsorption: molecular mechanisms. Physiol Rev 80 (2000) 1373-1409
    • (2000) Physiol Rev , vol.80 , pp. 1373-1409
    • Murer, H.1    Hernando, N.2    Forster, I.3    Biber, J.4
  • 33
    • 0035259577 scopus 로고    scopus 로고
    • Cytochrome P450 enzymes in the bioactivation of vitamin D to its hormonal form
    • Wikvall K. Cytochrome P450 enzymes in the bioactivation of vitamin D to its hormonal form. Int J Mol Med 7 (2001) 201-209
    • (2001) Int J Mol Med , vol.7 , pp. 201-209
    • Wikvall, K.1
  • 34
    • 2142746439 scopus 로고    scopus 로고
    • FGF-23 is a potent regulator of vitamin D metabolism and phosphate homeostasis
    • Shimada T., Hasegawa H., Yamazaki Y., et al. FGF-23 is a potent regulator of vitamin D metabolism and phosphate homeostasis. J Bone Miner Res 19 (2004) 429-435
    • (2004) J Bone Miner Res , vol.19 , pp. 429-435
    • Shimada, T.1    Hasegawa, H.2    Yamazaki, Y.3
  • 35
    • 20444404265 scopus 로고    scopus 로고
    • Genetic dissection of phosphate- and vitamin D-mediated regulation of circulating Fgf23 concentrations
    • Yu X., Sabbagh Y., Davis S.I., Demay M.B., and White K.E. Genetic dissection of phosphate- and vitamin D-mediated regulation of circulating Fgf23 concentrations. Bone 36 (2005) 971-977
    • (2005) Bone , vol.36 , pp. 971-977
    • Yu, X.1    Sabbagh, Y.2    Davis, S.I.3    Demay, M.B.4    White, K.E.5
  • 36
    • 15944376583 scopus 로고    scopus 로고
    • Fibroblast growth factor-23 relationship to dietary phosphate and renal phosphate handling in healthy young men
    • Ferrari S.L., Bonjour J.P., and Rizzoli R. Fibroblast growth factor-23 relationship to dietary phosphate and renal phosphate handling in healthy young men. J Clin Endocrinol Metab 90 (2005) 1519-1524
    • (2005) J Clin Endocrinol Metab , vol.90 , pp. 1519-1524
    • Ferrari, S.L.1    Bonjour, J.P.2    Rizzoli, R.3
  • 37
    • 26844568409 scopus 로고    scopus 로고
    • Vitamin D receptor-independent FGF23 actions in regulating phosphate and vitamin D metabolism
    • Shimada T., Yamazaki Y., Takahashi M., et al. Vitamin D receptor-independent FGF23 actions in regulating phosphate and vitamin D metabolism. Am J Physiol Renal Physiol 289 (2005) F1088-F1095
    • (2005) Am J Physiol Renal Physiol , vol.289
    • Shimada, T.1    Yamazaki, Y.2    Takahashi, M.3
  • 39
    • 20444404265 scopus 로고    scopus 로고
    • Genetic dissection of phosphate- and vitamin D-mediated regulation of circulating Fgf23 concentrations
    • Yu X., Sabbagh Y., Davis S.I., Demay M.B., and White K.E. Genetic dissection of phosphate- and vitamin D-mediated regulation of circulating Fgf23 concentrations. Bone 36 (2005) 971-977
    • (2005) Bone , vol.36 , pp. 971-977
    • Yu, X.1    Sabbagh, Y.2    Davis, S.I.3    Demay, M.B.4    White, K.E.5
  • 40
    • 27844501565 scopus 로고    scopus 로고
    • Dietary and serum phosphorus regulate fibroblast growth factor 23 expression and 1,25-dihydroxyvitamin D metabolism in mice
    • Perwad F., Azam N., Zhang M.Y., Yamashita T., Tenenhouse H.S., and Portale A.A. Dietary and serum phosphorus regulate fibroblast growth factor 23 expression and 1,25-dihydroxyvitamin D metabolism in mice. Endocrinology 146 (2005) 5358-5364
    • (2005) Endocrinology , vol.146 , pp. 5358-5364
    • Perwad, F.1    Azam, N.2    Zhang, M.Y.3    Yamashita, T.4    Tenenhouse, H.S.5    Portale, A.A.6
  • 41
    • 8444223088 scopus 로고    scopus 로고
    • Bone as a source of FGF23: regulation by phosphate?
    • Mirams M., Robinson B.G., Mason R.S., and Nelson A.E. Bone as a source of FGF23: regulation by phosphate?. Bone 35 (2004) 1192-1199
    • (2004) Bone , vol.35 , pp. 1192-1199
    • Mirams, M.1    Robinson, B.G.2    Mason, R.S.3    Nelson, A.E.4
  • 42
    • 1642416884 scopus 로고    scopus 로고
    • Targeted ablation of Fgf23 demonstrates an essential physiological role of FGF23 in phosphate and vitamin D metabolism
    • Shimada T., Kakitani M., Yamazaki Y., et al. Targeted ablation of Fgf23 demonstrates an essential physiological role of FGF23 in phosphate and vitamin D metabolism. J Clin Invest 113 (2004) 561-568
    • (2004) J Clin Invest , vol.113 , pp. 561-568
    • Shimada, T.1    Kakitani, M.2    Yamazaki, Y.3
  • 43
    • 23044460989 scopus 로고    scopus 로고
    • Fibroblast growth factor-23 in patients with Graves' disease before and after antithyroid therapy: its important role in serum phosphate regulation
    • Yamashita H., Yamazaki Y., Hasegawa H., et al. Fibroblast growth factor-23 in patients with Graves' disease before and after antithyroid therapy: its important role in serum phosphate regulation. J Clin Endocrinol Metab 90 (2005) 4211-4215
    • (2005) J Clin Endocrinol Metab , vol.90 , pp. 4211-4215
    • Yamashita, H.1    Yamazaki, Y.2    Hasegawa, H.3
  • 44
    • 19444372426 scopus 로고    scopus 로고
    • Vitamin D and phosphate regulate fibroblast growth factor-23 in K-562 cells
    • Ito M., Sakai Y., Furumoto M., et al. Vitamin D and phosphate regulate fibroblast growth factor-23 in K-562 cells. Am J Physiol Endocrinol Metab 288 (2005) E1101-E1109
    • (2005) Am J Physiol Endocrinol Metab , vol.288
    • Ito, M.1    Sakai, Y.2    Furumoto, M.3
  • 45
    • 23944501314 scopus 로고    scopus 로고
    • Role of the vitamin D receptor in FGF23 action on phosphate metabolism
    • Inoue Y., Segawa H., Kaneko I., et al. Role of the vitamin D receptor in FGF23 action on phosphate metabolism. Biochem J 390 (2005) 325-331
    • (2005) Biochem J , vol.390 , pp. 325-331
    • Inoue, Y.1    Segawa, H.2    Kaneko, I.3
  • 46
    • 27444437568 scopus 로고    scopus 로고
    • Fibroblast growth factor-23 is regulated by 1alpha,25-dihydroxyvitamin D
    • Collins M.T., Lindsay J.R., Jain A., et al. Fibroblast growth factor-23 is regulated by 1alpha,25-dihydroxyvitamin D. J Bone Miner Res 20 (2005) 1944-1950
    • (2005) J Bone Miner Res , vol.20 , pp. 1944-1950
    • Collins, M.T.1    Lindsay, J.R.2    Jain, A.3
  • 47
    • 33646367420 scopus 로고    scopus 로고
    • Fibroblast growth factor 23 is a counter-regulatory phosphaturic hormone for vitamin D
    • Liu S., Tang W., Zhou J., et al. Fibroblast growth factor 23 is a counter-regulatory phosphaturic hormone for vitamin D. J Am Soc Nephrol 17 (2006) 1305-1315
    • (2006) J Am Soc Nephrol , vol.17 , pp. 1305-1315
    • Liu, S.1    Tang, W.2    Zhou, J.3
  • 48
    • 28444486604 scopus 로고    scopus 로고
    • 1alpha,25-Dihydroxyvitamin D3 upregulates FGF23 gene expression in bone: the final link in a renal-gastrointestinal-skeletal axis that controls phosphate transport
    • Kolek O.I., Hines E.R., Jones M.D., et al. 1alpha,25-Dihydroxyvitamin D3 upregulates FGF23 gene expression in bone: the final link in a renal-gastrointestinal-skeletal axis that controls phosphate transport. Am J Physiol Gastrointest Liver Physiol 289 (2005) G1036-G1042
    • (2005) Am J Physiol Gastrointest Liver Physiol , vol.289
    • Kolek, O.I.1    Hines, E.R.2    Jones, M.D.3
  • 49
    • 19944433609 scopus 로고    scopus 로고
    • Circulating FGF-23 is regulated by 1alpha,25-dihydroxyvitamin D3 and phosphorus in vivo
    • Saito H., Maeda A., Ohtomo S., et al. Circulating FGF-23 is regulated by 1alpha,25-dihydroxyvitamin D3 and phosphorus in vivo. J Biol Chem 280 (2005) 2543-2549
    • (2005) J Biol Chem , vol.280 , pp. 2543-2549
    • Saito, H.1    Maeda, A.2    Ohtomo, S.3
  • 50
    • 26844564690 scopus 로고    scopus 로고
    • Analysis of the biochemical mechanisms for the endocrine actions of fibroblast growth factor-23
    • Yu X., Ibrahimi O.A., Goetz R., et al. Analysis of the biochemical mechanisms for the endocrine actions of fibroblast growth factor-23. Endocrinology 146 (2005) 4647-4656
    • (2005) Endocrinology , vol.146 , pp. 4647-4656
    • Yu, X.1    Ibrahimi, O.A.2    Goetz, R.3
  • 51
    • 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 390 (1997) 745-751
    • (1997) Nature , vol.390 , pp. 745-751
    • Kuro-o, M.1    Matsumura, Y.2    Aizawa, H.3
  • 52
    • 33845631059 scopus 로고    scopus 로고
    • Klotho converts canonical FGF receptor into a specific receptor for FGF23
    • Urakawa I., Yamazaki Y., Shimada T., et al. Klotho converts canonical FGF receptor into a specific receptor for FGF23. Nature 444 (2006) 770-774
    • (2006) Nature , vol.444 , pp. 770-774
    • Urakawa, I.1    Yamazaki, Y.2    Shimada, T.3
  • 53
    • 33749576547 scopus 로고    scopus 로고
    • The role of mutant UDP-N-acetyl-alpha-d-galactosamine-polypeptide N-acetylgalactosaminyltransferase 3 in regulating serum intact fibroblast growth factor 23 and matrix extracellular phosphoglycoprotein in heritable tumoral calcinosis
    • Garringer H.J., Fisher C., Larsson T.E., et al. The role of mutant UDP-N-acetyl-alpha-d-galactosamine-polypeptide N-acetylgalactosaminyltransferase 3 in regulating serum intact fibroblast growth factor 23 and matrix extracellular phosphoglycoprotein in heritable tumoral calcinosis. J Clin Endocrinol Metab 91 (2006) 4037-4042
    • (2006) J Clin Endocrinol Metab , vol.91 , pp. 4037-4042
    • Garringer, H.J.1    Fisher, C.2    Larsson, T.E.3
  • 54
    • 13544270218 scopus 로고    scopus 로고
    • An FGF23 missense mutation causes familial tumoral calcinosis with hyperphosphatemia
    • Benet-Pages A., Orlik P., Strom T.M., and Lorenz-Depiereux B. An FGF23 missense mutation causes familial tumoral calcinosis with hyperphosphatemia. Hum Mol Genet 14 (2005) 385-390
    • (2005) Hum Mol Genet , vol.14 , pp. 385-390
    • Benet-Pages, A.1    Orlik, P.2    Strom, T.M.3    Lorenz-Depiereux, B.4
  • 55
    • 23844457598 scopus 로고    scopus 로고
    • Fibroblast growth factor-23 mutants causing familial tumoral calcinosis are differentially processed
    • Larsson T., Davis S.I., Garringer H.J., et al. Fibroblast growth factor-23 mutants causing familial tumoral calcinosis are differentially processed. Endocrinology 146 (2005) 3883-3891
    • (2005) Endocrinology , vol.146 , pp. 3883-3891
    • Larsson, T.1    Davis, S.I.2    Garringer, H.J.3
  • 56
    • 26244454531 scopus 로고    scopus 로고
    • A novel mutation in fibroblast growth factor 23 gene as a cause of tumoral calcinosis
    • Araya K., Fukumoto S., Backenroth R., et al. A novel mutation in fibroblast growth factor 23 gene as a cause of tumoral calcinosis. J Clin Endocrinol Metab 90 (2005) 5523-5527
    • (2005) J Clin Endocrinol Metab , vol.90 , pp. 5523-5527
    • Araya, K.1    Fukumoto, S.2    Backenroth, R.3
  • 57
    • 29144527562 scopus 로고    scopus 로고
    • Inhibition of intestinal sodium-dependent inorganic phosphate transport by fibroblast growth factor 23
    • Miyamoto K., Ito M., Kuwahata M., Kato S., and Segawa H. Inhibition of intestinal sodium-dependent inorganic phosphate transport by fibroblast growth factor 23. Ther Apher Dial 9 (2005) 331-335
    • (2005) Ther Apher Dial , vol.9 , pp. 331-335
    • Miyamoto, K.1    Ito, M.2    Kuwahata, M.3    Kato, S.4    Segawa, H.5
  • 58
    • 0029160578 scopus 로고
    • A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphatemic rickets
    • The PEX Consortium. A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphatemic rickets. Nat Genet 11 (1995) 130-136
    • (1995) Nat Genet , vol.11 , pp. 130-136
    • The PEX Consortium1
  • 59
    • 14444280391 scopus 로고    scopus 로고
    • Genomic organization of the human PEX gene mutated in X-linked dominant hypophosphatemic rickets
    • Francis F., Strom T.M., Hennig S., et al. Genomic organization of the human PEX gene mutated in X-linked dominant hypophosphatemic rickets. Genome Res 7 (1997) 573-585
    • (1997) Genome Res , vol.7 , pp. 573-585
    • Francis, F.1    Strom, T.M.2    Hennig, S.3
  • 60
    • 0030938927 scopus 로고    scopus 로고
    • Pex/PEX tissue distribution and evidence for a deletion in the 3_region of the Pex gene in X-linked hypophosphatemic mice
    • Beck L., Soumounou Y., Martel J., et al. Pex/PEX tissue distribution and evidence for a deletion in the 3_region of the Pex gene in X-linked hypophosphatemic mice. J Clin Invest 99 (1997) 1200-1209
    • (1997) J Clin Invest , vol.99 , pp. 1200-1209
    • Beck, L.1    Soumounou, Y.2    Martel, J.3
  • 61
    • 0031896742 scopus 로고    scopus 로고
    • Pex mRNA is localized in developing mouse osteoblasts and odontoblasts
    • Ruchon A.F., Marcinkiewicz M., Siegfried G., et al. Pex mRNA is localized in developing mouse osteoblasts and odontoblasts. J Histochem Cytochem 46 (1998) 459-468
    • (1998) J Histochem Cytochem , vol.46 , pp. 459-468
    • Ruchon, A.F.1    Marcinkiewicz, M.2    Siegfried, G.3
  • 62
    • 9644303231 scopus 로고    scopus 로고
    • Homozygous ablation of fibroblast growth factor-23 results in hyperphosphatemia and impaired skeletogenesis, and reverses hypophosphatemia in Phex-deficient mice
    • Sitara D., Razzaque M.S., Hesse M., et al. Homozygous ablation of fibroblast growth factor-23 results in hyperphosphatemia and impaired skeletogenesis, and reverses hypophosphatemia in Phex-deficient mice. Matrix Biol 23 (2004) 421-432
    • (2004) Matrix Biol , vol.23 , pp. 421-432
    • Sitara, D.1    Razzaque, M.S.2    Hesse, M.3
  • 64
    • 0141844575 scopus 로고    scopus 로고
    • Regulation of fibroblastic growth factor 23 expression but not degradation by PHEX
    • Liu S., Guo R., Simpson L.G., Xiao Z.S., Burnham C.E., and Quarles L.D. Regulation of fibroblastic growth factor 23 expression but not degradation by PHEX. J Biol Chem 278 (2003) 37419-37426
    • (2003) J Biol Chem , vol.278 , pp. 37419-37426
    • Liu, S.1    Guo, R.2    Simpson, L.G.3    Xiao, Z.S.4    Burnham, C.E.5    Quarles, L.D.6
  • 65
    • 0034805353 scopus 로고    scopus 로고
    • FGF-23 inhibits renal tubular phosphate transport and is a PHEX substrate
    • Bowe A.E., Finnegan R., Jan de Beur S.M., et al. FGF-23 inhibits renal tubular phosphate transport and is a PHEX substrate. Biochem Biophys Res Commun 284 (2001) 977-981
    • (2001) Biochem Biophys Res Commun , vol.284 , pp. 977-981
    • Bowe, A.E.1    Finnegan, R.2    Jan de Beur, S.M.3
  • 68
    • 2342481131 scopus 로고    scopus 로고
    • FGF-23 in patients with end-stage renal disease on hemodialysis
    • Imanishi Y., Inaba M., Nakatsuka K., et al. FGF-23 in patients with end-stage renal disease on hemodialysis. Kidney Int 65 (2004) 1943-1946
    • (2004) Kidney Int , vol.65 , pp. 1943-1946
    • Imanishi, Y.1    Inaba, M.2    Nakatsuka, K.3
  • 69
    • 20844461345 scopus 로고    scopus 로고
    • Pretreatment serum FGF-23 levels predict the efficacy of calcitriol therapy in dialysis patients
    • Kazama J.J., Sato F., Omori K., et al. Pretreatment serum FGF-23 levels predict the efficacy of calcitriol therapy in dialysis patients. Kidney Int 67 (2005) 1120-1125
    • (2005) Kidney Int , vol.67 , pp. 1120-1125
    • Kazama, J.J.1    Sato, F.2    Omori, K.3
  • 70
    • 33747231852 scopus 로고    scopus 로고
    • FGF-23 and sFRP-4 in chronic kidney disease and post-renal transplantation
    • Pande S., Ritter C.S., Rothstein M., et al. FGF-23 and sFRP-4 in chronic kidney disease and post-renal transplantation. Nephron Physiol 104 (2006) 23-32
    • (2006) Nephron Physiol , vol.104 , pp. 23-32
    • Pande, S.1    Ritter, C.S.2    Rothstein, M.3
  • 71
    • 33749508711 scopus 로고    scopus 로고
    • Post-transplant hypophosphatemia: tertiary 'hyper-phosphatoninism'?
    • Bhan I., Shah A., Holmes J., et al. Post-transplant hypophosphatemia: tertiary 'hyper-phosphatoninism'?. Kidney Int 70 (2006) 1486-1494
    • (2006) Kidney Int , vol.70 , pp. 1486-1494
    • Bhan, I.1    Shah, A.2    Holmes, J.3
  • 72
    • 0030905162 scopus 로고    scopus 로고
    • A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors
    • Rattner A., Hsieh J.C., Smallwood P.M., et al. A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors. Proc Natl Acad Sci U S A 94 (1997) 2859-2863
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2859-2863
    • Rattner, A.1    Hsieh, J.C.2    Smallwood, P.M.3
  • 73
    • 0036714307 scopus 로고    scopus 로고
    • Secreted frizzled-related proteins: searching for relationships and patterns
    • Jones S.E., and Jomary C. Secreted frizzled-related proteins: searching for relationships and patterns. Bioessays 24 (2002) 811-820
    • (2002) Bioessays , vol.24 , pp. 811-820
    • Jones, S.E.1    Jomary, C.2
  • 74
    • 0033118492 scopus 로고    scopus 로고
    • A new secreted protein that binds to Wnt proteins and inhibits their activities
    • Hsieh J.C., Kodjabachian L., Rebbert M.L., et al. A new secreted protein that binds to Wnt proteins and inhibits their activities. Nature 398 (1999) 431-436
    • (1999) Nature , vol.398 , pp. 431-436
    • Hsieh, J.C.1    Kodjabachian, L.2    Rebbert, M.L.3
  • 75
    • 1642499389 scopus 로고    scopus 로고
    • Wnt-frizzled signaling to G-proteincoupled effectors
    • Wang H.Y., and Malbon C.C. Wnt-frizzled signaling to G-proteincoupled effectors. Cell Mol Life Sci 61 (2004) 69-75
    • (2004) Cell Mol Life Sci , vol.61 , pp. 69-75
    • Wang, H.Y.1    Malbon, C.C.2
  • 76
    • 85047693146 scopus 로고    scopus 로고
    • Secreted frizzled related protein 4 is a potent tumor-derived phosphaturic agent
    • Berndt T., Craig T.A., Bowe A.E., et al. Secreted frizzled related protein 4 is a potent tumor-derived phosphaturic agent. J Clin Invest 112 (2003) 785-794
    • (2003) J Clin Invest , vol.112 , pp. 785-794
    • Berndt, T.1    Craig, T.A.2    Bowe, A.E.3
  • 77
    • 0036095905 scopus 로고    scopus 로고
    • Tumors associated with oncogenic osteomalacia express genes important in bone and mineral metabolism
    • De Beur S.M., Finnegan R.B., Vassiliadis J., et al. Tumors associated with oncogenic osteomalacia express genes important in bone and mineral metabolism. J Bone Miner Res 17 (2002) 1102-1110
    • (2002) J Bone Miner Res , vol.17 , pp. 1102-1110
    • De Beur, S.M.1    Finnegan, R.B.2    Vassiliadis, J.3
  • 78
    • 0032574725 scopus 로고    scopus 로고
    • Targeted inactivation of Npt2 in mice leads to severe renal phosphate wasting, hypercalciuria, and skeletal abnormalities
    • Beck L., Karaplis A.C., Amizuka N., Hewson A.S., Ozawa H., and Tenenhouse H.S. Targeted inactivation of Npt2 in mice leads to severe renal phosphate wasting, hypercalciuria, and skeletal abnormalities. Proc Natl Acad Sci U S A 95 (1998) 5372-5377
    • (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
  • 79
    • 0031755898 scopus 로고    scopus 로고
    • Differential expression, abundance, and regulation of Na_-phosphate cotransporter genes in murine kidney
    • Tenenhouse H.S., Roy S., Martel J., and Gauthier C. Differential expression, abundance, and regulation of Na_-phosphate cotransporter genes in murine kidney. Am J Physiol 275 (1998) F527-F553
    • (1998) Am J Physiol , vol.275
    • Tenenhouse, H.S.1    Roy, S.2    Martel, J.3    Gauthier, C.4
  • 80
    • 29144490730 scopus 로고    scopus 로고
    • Secreted frizzled-related protein-4 reduces sodium-phosphate co-transporter abundance and activity in proximal tubule cells
    • Berndt T.J., Bielesz B., Craig T.A., et al. Secreted frizzled-related protein-4 reduces sodium-phosphate co-transporter abundance and activity in proximal tubule cells. Pflugers Arch 451 (2006) 579-587
    • (2006) Pflugers Arch , vol.451 , pp. 579-587
    • Berndt, T.J.1    Bielesz, B.2    Craig, T.A.3
  • 81
    • 0034235036 scopus 로고    scopus 로고
    • MEPE, a new gene expressed in bone marrow and tumors causing osteomalacia
    • Rowe P.S., de Zoysa P.A., Dong R., et al. MEPE, a new gene expressed in bone marrow and tumors causing osteomalacia. Genomics 67 (2000) 54-68
    • (2000) Genomics , vol.67 , pp. 54-68
    • Rowe, P.S.1    de Zoysa, P.A.2    Dong, R.3
  • 82
    • 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 D.N., Tkalcevic G.T., Mansolf A.L., Rivera-Gonzalez R., and Brown T.A. 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 275 (2000) 36172-36180
    • (2000) J Biol Chem , vol.275 , pp. 36172-36180
    • Petersen, D.N.1    Tkalcevic, G.T.2    Mansolf, A.L.3    Rivera-Gonzalez, R.4    Brown, T.A.5
  • 83
    • 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 F.H., and Ecarot B. Mepe, the gene encoding a tumor-secreted protein in oncogenic hypophosphatemic osteomalacia, is expressed in bone. Genomics 74 (2001) 342-351
    • (2001) Genomics , vol.74 , pp. 342-351
    • Argiro, L.1    Desbarats, M.2    Glorieux, F.H.3    Ecarot, B.4
  • 84
    • 3242729536 scopus 로고    scopus 로고
    • Evidence of downregulation of matrix extracellular phosphoglycoprotein during terminal differentiation in human osteoblasts
    • Siggelkow H., Schmidt E., Hennies B., and Hufner M. Evidence of downregulation of matrix extracellular phosphoglycoprotein during terminal differentiation in human osteoblasts. Bone 35 (2004) 570-576
    • (2004) Bone , vol.35 , pp. 570-576
    • Siggelkow, H.1    Schmidt, E.2    Hennies, B.3    Hufner, M.4
  • 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 R.W., and DenBesten P.K. Dentonin, a fragment of MEPE, enhanced dental pulp stem cell proliferation. J Dent Res 83 (2004) 496-499
    • (2004) J Dent Res , vol.83 , pp. 496-499
    • Liu, H.1    Li, W.2    Gao, C.3    Kumagai, Y.4    Blacher, R.W.5    DenBesten, P.K.6
  • 86
    • 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 22 (2004) 176-184
    • (2004) J Bone Miner Metab , vol.22 , pp. 176-184
    • Nampei, A.1    Hashimoto, J.2    Hayashida, K.3
  • 87
    • 3142782934 scopus 로고    scopus 로고
    • Mepe is expressed during skeletal development and regeneration
    • Lu C., Huang S., Miclau T., Helms J.A., and Colnot C. Mepe is expressed during skeletal development and regeneration. Histochem Cell Biol 121 (2004) 493-499
    • (2004) Histochem Cell Biol , vol.121 , pp. 493-499
    • Lu, C.1    Huang, S.2    Miclau, T.3    Helms, J.A.4    Colnot, C.5
  • 88
    • 0035996513 scopus 로고    scopus 로고
    • MEPE/OF45, a new dentin/bone matrix protein and candidate gene for dentin diseases mapping to chromosome 4q21
    • MacDougall M., Simmons D., Gu T.T., and Dong J. MEPE/OF45, a new dentin/bone matrix protein and candidate gene for dentin diseases mapping to chromosome 4q21. Connect Tissue Res 43 (2002) 320-330
    • (2002) Connect Tissue Res , vol.43 , pp. 320-330
    • MacDougall, M.1    Simmons, D.2    Gu, T.T.3    Dong, J.4
  • 89
    • 0017348985 scopus 로고
    • Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva
    • Schlesinger D.H., and Hay D.I. Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva. J Biol Chem 252 (1977) 1689-1695
    • (1977) J Biol Chem , vol.252 , pp. 1689-1695
    • Schlesinger, D.H.1    Hay, D.I.2
  • 90
    • 0032514626 scopus 로고    scopus 로고
    • A peptide that inhibits hydroxyapatite growth is in an extended conformation on the crystal surface
    • Long J.R., Dindot J.L., Zebroski H., et al. A peptide that inhibits hydroxyapatite growth is in an extended conformation on the crystal surface. Proc Natl Acad Sci U S A 95 (1998) 12083-12087
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12083-12087
    • Long, J.R.1    Dindot, J.L.2    Zebroski, H.3
  • 91
    • 12244271018 scopus 로고    scopus 로고
    • Osteopontin is a critical inhibitor of calcium oxalate crystal formation and retention in renal tubules
    • Wesson J.A., Johnson R.J., Mazzali M., et al. Osteopontin is a critical inhibitor of calcium oxalate crystal formation and retention in renal tubules. J Am Soc Nephrol 14 (2003) 139-147
    • (2003) J Am Soc Nephrol , vol.14 , pp. 139-147
    • Wesson, J.A.1    Johnson, R.J.2    Mazzali, M.3
  • 92
    • 4644312298 scopus 로고    scopus 로고
    • Expression of SIBLINGs and their partner MMPs in salivary glands
    • Ogbureke K.U.E., and Fisher L.W. Expression of SIBLINGs and their partner MMPs in salivary glands. J Dent Res 83 (2004) 664-670
    • (2004) J Dent Res , vol.83 , pp. 664-670
    • Ogbureke, K.U.E.1    Fisher, L.W.2
  • 93
    • 24944550165 scopus 로고    scopus 로고
    • Renal expression of SIBLING proteins and their partner matrix metalloproteinases (MMPs)
    • Ogbureke K.U., and Fisher L.W. Renal expression of SIBLING proteins and their partner matrix metalloproteinases (MMPs). Kidney Int 68 (2005) 155-166
    • (2005) Kidney Int , vol.68 , pp. 155-166
    • Ogbureke, K.U.1    Fisher, L.W.2
  • 94
    • 26944499850 scopus 로고    scopus 로고
    • Role of matrix extracellular phosphoglycoprotein in the pathogenesis of X-linked hypophosphatemia
    • Liu S., Brown T.A., Zhou J., et al. Role of matrix extracellular phosphoglycoprotein in the pathogenesis of X-linked hypophosphatemia. J Am Soc Nephrol 16 (2005) 1645-1653
    • (2005) J Am Soc Nephrol , vol.16 , pp. 1645-1653
    • Liu, S.1    Brown, T.A.2    Zhou, J.3
  • 95
    • 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 K., Fraser W.D., and Rowe P.S. Serum MEPE-ASARM-peptides are elevated in X-linked rickets (HYP): implications for phosphaturia and rickets. J Endocrinol 183 (2004) R1-R9
    • (2004) J Endocrinol , vol.183
    • Bresler, D.1    Bruder, J.2    Mohnike, K.3    Fraser, W.D.4    Rowe, P.S.5
  • 97
    • 10744226781 scopus 로고    scopus 로고
    • MEPE has the properties of an osteoblastic phosphatonin and minhibin
    • Rowe P.S., Kumagai Y., Gutierrez G., et al. MEPE has the properties of an osteoblastic phosphatonin and minhibin. Bone 34 (2004) 303-319
    • (2004) Bone , vol.34 , pp. 303-319
    • Rowe, P.S.1    Kumagai, Y.2    Gutierrez, G.3
  • 98
    • 0032709548 scopus 로고    scopus 로고
    • Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis
    • Toomes C., James J., Wood A.J., et al. Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis. Nat Genet 23 (1999) 421-424
    • (1999) Nat Genet , vol.23 , pp. 421-424
    • Toomes, C.1    James, J.2    Wood, A.J.3
  • 99
    • 12344250943 scopus 로고    scopus 로고
    • Surface plasmon resonance (SPR) confirms that MEPE binds to PHEX via the MEPE-ASARM motif: a model for impaired mineralization in X-linked rickets (HYP)
    • Rowe P.S., Garrett I.R., Schwarz P.M., et al. Surface plasmon resonance (SPR) confirms that MEPE binds to PHEX via the MEPE-ASARM motif: a model for impaired mineralization in X-linked rickets (HYP). Bone 36 (2005) 33-46
    • (2005) Bone , vol.36 , pp. 33-46
    • Rowe, P.S.1    Garrett, I.R.2    Schwarz, P.M.3
  • 100
    • 4043120646 scopus 로고    scopus 로고
    • Serum levels of matrix extracellular phosphoglycoprotein (MEPE) in normal humans correlate with serum phosphorus, parathyroid hormone and bone mineral density
    • Jain A., Fedarko N.S., Collins M.T., et al. Serum levels of matrix extracellular phosphoglycoprotein (MEPE) in normal humans correlate with serum phosphorus, parathyroid hormone and bone mineral density. J Clin Endocrinol Metab 89 (2004) 4158-4161
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 4158-4161
    • Jain, A.1    Fedarko, N.S.2    Collins, M.T.3
  • 101
    • 0037449817 scopus 로고    scopus 로고
    • Targeted disruption of the osteoblast/osteocyte factor 45 gene (OF45) results in increased bone formation and bone mass
    • Gowen L.C., Petersen D.N., Mansolf A.L., et al. Targeted disruption of the osteoblast/osteocyte factor 45 gene (OF45) results in increased bone formation and bone mass. J Biol Chem 278 (2003) 1998-2007
    • (2003) J Biol Chem , vol.278 , pp. 1998-2007
    • Gowen, L.C.1    Petersen, D.N.2    Mansolf, A.L.3
  • 102
    • 33645484538 scopus 로고    scopus 로고
    • Matrix extracellular phosphoglycoprotein (MEPE) fragments circulate in excess in patients with tumor-induced osteomalacia (TIO) and X linked hypophosphatemic rickets
    • Jan de Beur S.M., Jain A., Khan M., and Fedarko N.S. Matrix extracellular phosphoglycoprotein (MEPE) fragments circulate in excess in patients with tumor-induced osteomalacia (TIO) and X linked hypophosphatemic rickets. J Bone Miner Res 19 (2004) S101
    • (2004) J Bone Miner Res , vol.19
    • Jan de Beur, S.M.1    Jain, A.2    Khan, M.3    Fedarko, N.S.4
  • 103
    • 26244435308 scopus 로고    scopus 로고
    • Phosphate diabetes, tubular phosphate reabsorption and phosphatonins
    • Laroche M., and Boyer J.F. Phosphate diabetes, tubular phosphate reabsorption and phosphatonins. Joint Bone Spine 72 (2005) 376-381
    • (2005) Joint Bone Spine , vol.72 , pp. 376-381
    • Laroche, M.1    Boyer, J.F.2
  • 104
    • 12744277958 scopus 로고    scopus 로고
    • Hepatic resection-related hypophosphatemia is of renal origin as manifested by isolated hyperphosphaturia
    • Salem R.R., and Tray K. Hepatic resection-related hypophosphatemia is of renal origin as manifested by isolated hyperphosphaturia. Ann Surg 241 (2005) 343-348
    • (2005) Ann Surg , vol.241 , pp. 343-348
    • Salem, R.R.1    Tray, K.2
  • 105
    • 0033756474 scopus 로고    scopus 로고
    • Cathepsin B contributes to TNF-alpha-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c
    • Guicciardi M.E., Deussing J., Miyoshi H., et al. Cathepsin B contributes to TNF-alpha-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c. J Clin Invest 106 (2000) 1127-1137
    • (2000) J Clin Invest , vol.106 , pp. 1127-1137
    • Guicciardi, M.E.1    Deussing, J.2    Miyoshi, H.3
  • 106
    • 0020618620 scopus 로고
    • Defective adenosine triphosphate synthesis. An explanation for skeletal muscle dysfunction in phosphate-deficient mice
    • Hettleman B.D., Sabina R.L., Drezner M.K., Holmes E.W., and Swain J.L. Defective adenosine triphosphate synthesis. An explanation for skeletal muscle dysfunction in phosphate-deficient mice. J Clin Invest 72 (1983) 582-589
    • (1983) J Clin Invest , vol.72 , pp. 582-589
    • Hettleman, B.D.1    Sabina, R.L.2    Drezner, M.K.3    Holmes, E.W.4    Swain, J.L.5
  • 107
    • 0022498525 scopus 로고
    • Studies on the specific activity of [gamma-32P]ATP in adipose and other tissue preparations incubated with medium containing [32P]phosphate
    • Hopkirk T.J., and Denton R.M. Studies on the specific activity of [gamma-32P]ATP in adipose and other tissue preparations incubated with medium containing [32P]phosphate. Biochim Biophys Acta 885 (1986) 195-205
    • (1986) Biochim Biophys Acta , vol.885 , pp. 195-205
    • Hopkirk, T.J.1    Denton, R.M.2
  • 108
    • 0018746169 scopus 로고
    • Factors affecting the rate of purine ribonucleotide dephosphorylation in human erythrocytes
    • Whelan J.M., and Bagnara A.S. Factors affecting the rate of purine ribonucleotide dephosphorylation in human erythrocytes. Biochim Biophys Acta 563 (1979) 466-478
    • (1979) Biochim Biophys Acta , vol.563 , pp. 466-478
    • Whelan, J.M.1    Bagnara, A.S.2
  • 109
    • 0024603280 scopus 로고
    • Postoperative and glucose-induced hypophosphatemia in relation to adenosine triphosphate and 2,3-diphosphoglycerate in erythrocytes
    • Rasmussen A., Kimose H.H., Segel E., and Hessoy I. Postoperative and glucose-induced hypophosphatemia in relation to adenosine triphosphate and 2,3-diphosphoglycerate in erythrocytes. Acta Chir Scand 155 (1989) 81-87
    • (1989) Acta Chir Scand , vol.155 , pp. 81-87
    • Rasmussen, A.1    Kimose, H.H.2    Segel, E.3    Hessoy, I.4
  • 111
    • 0015879019 scopus 로고
    • Reduced red cell 2,3-diphosphoglycerate and adenosine triphosphate, hypophosphatemia, and increased hemoglobin-oxygen affinity after cardiac surgery
    • Young J.A., Lichtman M.A., and Cohen J. Reduced red cell 2,3-diphosphoglycerate and adenosine triphosphate, hypophosphatemia, and increased hemoglobin-oxygen affinity after cardiac surgery. Circulation 47 (1973) 1313-1318
    • (1973) Circulation , vol.47 , pp. 1313-1318
    • Young, J.A.1    Lichtman, M.A.2    Cohen, J.3
  • 112
    • 0032754618 scopus 로고    scopus 로고
    • Metabolic aspects of phosphate replacement therapy for hypophosphatemia after renal transplantation: impact on muscular phosphate content, mineral metabolism, and acid/base homeostasis
    • Ambuhl P.M., Meier D., Wolf B., Dydak U., Boesiger P., and Binswanger U. Metabolic aspects of phosphate replacement therapy for hypophosphatemia after renal transplantation: impact on muscular phosphate content, mineral metabolism, and acid/base homeostasis. Am J Kidney Dis 34 (1999) 875-883
    • (1999) Am J Kidney Dis , vol.34 , pp. 875-883
    • Ambuhl, P.M.1    Meier, D.2    Wolf, B.3    Dydak, U.4    Boesiger, P.5    Binswanger, U.6
  • 113
    • 0033857091 scopus 로고    scopus 로고
    • Chronic metabolic acidosis in azotemic rats on a high-phosphate diet halts the progression of renal disease
    • Jara A., Felsenfeld A.J., Bover J., and Kleeman C.R. Chronic metabolic acidosis in azotemic rats on a high-phosphate diet halts the progression of renal disease. Kidney Int 58 (2000) 1023-1032
    • (2000) Kidney Int , vol.58 , pp. 1023-1032
    • Jara, A.1    Felsenfeld, A.J.2    Bover, J.3    Kleeman, C.R.4
  • 114
    • 0020430434 scopus 로고
    • Intracellular inorganic phosphate and ATP levels in human blood erythrocytes, leucocytes and platelets in normal subjects and in diseases associated with altered phosphate metabolism
    • Preston C.J., Noorwali A., Chaalla A., et al. Intracellular inorganic phosphate and ATP levels in human blood erythrocytes, leucocytes and platelets in normal subjects and in diseases associated with altered phosphate metabolism. Adv Exp Med Biol 151 (1982) 147-155
    • (1982) Adv Exp Med Biol , vol.151 , pp. 147-155
    • Preston, C.J.1    Noorwali, A.2    Chaalla, A.3
  • 115
    • 0025091916 scopus 로고
    • Regulation of platelet AMP deaminase activity in situ
    • Verhoeven A.J., Marszalek J., and Holmsen H. Regulation of platelet AMP deaminase activity in situ. Biochem J 265 (1990) 267-275
    • (1990) Biochem J , vol.265 , pp. 267-275
    • Verhoeven, A.J.1    Marszalek, J.2    Holmsen, H.3
  • 116
    • 0023902429 scopus 로고
    • Nucleotides, nucleosides, and oxypurines in human kidney measured by use of reversed-phase HPLC
    • Massen J.G., van der Vusse G.J., Work M., and Kootstra G. Nucleotides, nucleosides, and oxypurines in human kidney measured by use of reversed-phase HPLC. Clin Chem 34 (1988) 1087-1090
    • (1988) Clin Chem , vol.34 , pp. 1087-1090
    • Massen, J.G.1    van der Vusse, G.J.2    Work, M.3    Kootstra, G.4
  • 117
    • 0030330838 scopus 로고    scopus 로고
    • Erythrocyte 2,3-diphosphoglycerate depletion associated with hypophosphatemia detected by routine arterial blood gas analysis
    • Larsen V.H., Waldau T., Gravesen H., and Siggaard-Andersen O. Erythrocyte 2,3-diphosphoglycerate depletion associated with hypophosphatemia detected by routine arterial blood gas analysis. Scand J Clin Lab Invest Suppl 224 (1996) 83-87
    • (1996) Scand J Clin Lab Invest Suppl , vol.224 , pp. 83-87
    • Larsen, V.H.1    Waldau, T.2    Gravesen, H.3    Siggaard-Andersen, O.4
  • 118
    • 0842329606 scopus 로고    scopus 로고
    • Treatment of hypophosphatemia using a protocol based on patient weight and serum phosphorus level in a surgical intensive care unit
    • Taylor B.E., Huey W.Y., Buchman T.G., Boyle W.A., and Coopersmith C.M. Treatment of hypophosphatemia using a protocol based on patient weight and serum phosphorus level in a surgical intensive care unit. J Am Coll Surg 198 (2004) 198-204
    • (2004) J Am Coll Surg , vol.198 , pp. 198-204
    • Taylor, B.E.1    Huey, W.Y.2    Buchman, T.G.3    Boyle, W.A.4    Coopersmith, C.M.5
  • 119
    • 0029157325 scopus 로고
    • Treatment of hypophosphatemia in patients receiving specialized nutrition support using a graduated dosing scheme: results from a prospective clinical trial
    • Clark S., Sacks G., Dickerson R., Kudsk K., and Brown R. Treatment of hypophosphatemia in patients receiving specialized nutrition support using a graduated dosing scheme: results from a prospective clinical trial. Crit Care Med 23 (1995) 1504-1511
    • (1995) Crit Care Med , vol.23 , pp. 1504-1511
    • Clark, S.1    Sacks, G.2    Dickerson, R.3    Kudsk, K.4    Brown, R.5
  • 120
    • 0021068428 scopus 로고
    • High dose intravenous phosphorus therapy for severe, complicated hypophosphatemia
    • Vannatta J.B., Andress D.L., Whang R., et al. High dose intravenous phosphorus therapy for severe, complicated hypophosphatemia. South Med J 76 (1983) 1424-1426
    • (1983) South Med J , vol.76 , pp. 1424-1426
    • Vannatta, J.B.1    Andress, D.L.2    Whang, R.3
  • 121
    • 85047691476 scopus 로고    scopus 로고
    • Science in medicine: how does blood glucose control with insulin save lives in intensive care?
    • Van den Berghe G. Science in medicine: how does blood glucose control with insulin save lives in intensive care?. J Clin Invest 114 (2004) 1187-1195
    • (2004) J Clin Invest , vol.114 , pp. 1187-1195
    • Van den Berghe, G.1
  • 122
    • 0035700770 scopus 로고    scopus 로고
    • Insulin (GIK) improves central mixed and hepatic venous oxygenation in clinical cardiac surgery
    • Lindholm L., Bengtsson A., Hansdottir V., Westerlind A., and Jeppsson A. Insulin (GIK) improves central mixed and hepatic venous oxygenation in clinical cardiac surgery. Scand Cardiovasc J 35 (2001) 347-352
    • (2001) Scand Cardiovasc J , vol.35 , pp. 347-352
    • Lindholm, L.1    Bengtsson, A.2    Hansdottir, V.3    Westerlind, A.4    Jeppsson, A.5
  • 123
    • 17744379615 scopus 로고    scopus 로고
    • Randomized, double-blind comparison of lactated Ringer's solution and 0.9% NaCl during renal transplantation
    • Catherine C.M.N., Frumento R.J., Hardy M.A., et al. Randomized, double-blind comparison of lactated Ringer's solution and 0.9% NaCl during renal transplantation. Anesth Analg 100 (2005) 1518-1524
    • (2005) Anesth Analg , vol.100 , pp. 1518-1524
    • Catherine, C.M.N.1    Frumento, R.J.2    Hardy, M.A.3


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