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Volumn 98, Issue 4, 2016, Pages 398-416

Alkaline Phosphatase and Hypophosphatasia

Author keywords

Calcification; Enzyme replacement; Osteomalacia; Rickets; Seizures

Indexed keywords

ALKALINE PHOSPHATASE; ASFOTASE ALFA; PYROPHOSPHATE; ALPL PROTEIN, HUMAN;

EID: 84947750321     PISSN: 0171967X     EISSN: 14320827     Source Type: Journal    
DOI: 10.1007/s00223-015-0079-1     Document Type: Review
Times cited : (293)

References (137)
  • 1
    • 0000985304 scopus 로고
    • The possible significance of hexosephosphoric esters in ossification
    • Robison R (1923) The possible significance of hexosephosphoric esters in ossification. Biochem J 17:286
    • (1923) Biochem J , vol.17 , pp. 286
    • Robison, R.1
  • 2
    • 0039249476 scopus 로고
    • The significance of phosphoric esters in metabolism
    • New York University Press, New York
    • Robison R (1932) The significance of phosphoric esters in metabolism. New York University Press, New York
    • (1932)
    • Robison, R.1
  • 3
    • 0021339769 scopus 로고
    • Can biological calcification occur in the presence of pyrophosphate?
    • COI: 1:CAS:528:DyaL2cXhvVOluro%3D, PID: 6326671
    • Meyer JL (1984) Can biological calcification occur in the presence of pyrophosphate? Arch Biochem Biophys 231:1–8
    • (1984) Arch Biochem Biophys , vol.231 , pp. 1-8
    • Meyer, J.L.1
  • 4
    • 0011322884 scopus 로고
    • A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia
    • COI: 1:CAS:528:DyaL1cXmt1eku74%3D, PID: 3174660
    • Weiss MJ, Cole DE, Ray K, Whyte MP, Lafferty MA, Mulivor RA, Harris H (1988) A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. Proc Natl Acad Sci USA 85:7666–7669
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7666-76669
    • Weiss, M.J.1    Cole, D.E.2    Ray, K.3    Whyte, M.P.4    Lafferty, M.A.5    Mulivor, R.A.6    Harris, H.7
  • 5
    • 0000034593 scopus 로고
    • Hypophosphatasia; a new developmental anomaly
    • COI: 1:CAS:528:DyaH1MXjt1Wmuw%3D%3D, PID: 18110134
    • Rathbun JC (1948) Hypophosphatasia; a new developmental anomaly. Am J Dis Child 75:822–831
    • (1948) Am J Dis Child , vol.75 , pp. 822-831
    • Rathbun, J.C.1
  • 7
    • 79954584814 scopus 로고    scopus 로고
    • A molecular-based estimation of the prevalence of hypophosphatasia in the European population
    • PID: 21488855
    • Mornet E, Yvard A, Taillandier A, Fauvert D, Simon-Bouy B (2011) A molecular-based estimation of the prevalence of hypophosphatasia in the European population. Ann Hum Genet 75:439–445
    • (2011) Ann Hum Genet , vol.75 , pp. 439-445
    • Mornet, E.1    Yvard, A.2    Taillandier, A.3    Fauvert, D.4    Simon-Bouy, B.5
  • 8
    • 0027337157 scopus 로고
    • A homoallelic Gly317→Asp mutation in ALPL causes the perinatal (lethal) form of hypophosphatasia in Canadian mennonites
    • COI: 1:CAS:528:DyaK3sXmt1entro%3D, PID: 8406453
    • Greenberg CR, Taylor CL, Haworth JC, Seargeant LE, Philipps S, Triggs-Raine B, Chodirker BN (1993) A homoallelic Gly317→Asp mutation in ALPL causes the perinatal (lethal) form of hypophosphatasia in Canadian mennonites. Genomics 17:215–217
    • (1993) Genomics , vol.17 , pp. 215-217
    • Greenberg, C.R.1    Taylor, C.L.2    Haworth, J.C.3    Seargeant, L.E.4    Philipps, S.5    Triggs-Raine, B.6    Chodirker, B.N.7
  • 11
    • 0035937857 scopus 로고    scopus 로고
    • Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity
    • PID: 11124260
    • Le Du MH, Stigbrand T, Taussig MJ, Menez A, Stura EA (2001) Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity. J Biol Chem 276:9158–9165
    • (2001) J Biol Chem , vol.276 , pp. 9158-9165
    • Le Du, M.H.1    Stigbrand, T.2    Taussig, M.J.3    Menez, A.4    Stura, E.A.5
  • 12
    • 0037147253 scopus 로고    scopus 로고
    • Structural evidence of functional divergence in human alkaline phosphatases
    • PID: 12372831
    • Le Du M-H, Millán JL (2002) Structural evidence of functional divergence in human alkaline phosphatases. J Biol Chem 277:49808–49814
    • (2002) J Biol Chem , vol.277 , pp. 49808-49814
    • Le Du, M.-H.1    Millán, J.L.2
  • 13
    • 0026101190 scopus 로고
    • Gly429 is the major determinant of uncompetitive inhibition of human germ cell alkaline phosphatase by L-leucine
    • COI: 1:CAS:528:DyaK3MXhsF2lt78%3D, PID: 2001256
    • Hummer C, Millán JL (1991) Gly429 is the major determinant of uncompetitive inhibition of human germ cell alkaline phosphatase by L-leucine. Biochem J 274(Pt 1):91–95
    • (1991) Biochem J , vol.274 , pp. 91-95
    • Hummer, C.1    Millán, J.L.2
  • 14
    • 0026660288 scopus 로고
    • Molecular mechanism of uncompetitive inhibition of human placental and germ-cell alkaline phosphatase
    • COI: 1:CAS:528:DyaK38Xlt1Oitbk%3D, PID: 1520273
    • Hoylaerts MF, Manes T, Millán JL (1992) Molecular mechanism of uncompetitive inhibition of human placental and germ-cell alkaline phosphatase. Biochem J 286(Pt 1):23–30
    • (1992) Biochem J , vol.286 , pp. 23-30
    • Hoylaerts, M.F.1    Manes, T.2    Millán, J.L.3
  • 15
    • 0037151014 scopus 로고    scopus 로고
    • Function assignment to conserved residues in mammalian alkaline phosphatases
    • COI: 1:CAS:528:DC%2BD38XltVGrs7g%3D, PID: 11937510
    • Kozlenkov A, Manes T, Hoylaerts MF, Millan JL (2002) Function assignment to conserved residues in mammalian alkaline phosphatases. J Biol Chem 277:22992–22999
    • (2002) J Biol Chem , vol.277 , pp. 22992-22999
    • Kozlenkov, A.1    Manes, T.2    Hoylaerts, M.F.3    Millan, J.L.4
  • 16
    • 0024076973 scopus 로고
    • A putative functional domain of human placental alkaline phosphatase predicted from sequence comparisons
    • COI: 1:CAS:528:DyaL1cXlsVGhsbc%3D, PID: 3178778
    • Tsonis PA, Argraves WS, Millán JL (1988) A putative functional domain of human placental alkaline phosphatase predicted from sequence comparisons. Biochem J 254:623–624
    • (1988) Biochem J , vol.254 , pp. 623-624
    • Tsonis, P.A.1    Argraves, W.S.2    Millán, J.L.3
  • 17
    • 33747475602 scopus 로고    scopus 로고
    • Mammalian alkaline phosphatase catalysis requires active site structure stabilization via the N-terminal amino acid microenvironment
    • COI: 1:CAS:528:DC%2BD28XntFKltb4%3D, PID: 16893177
    • Hoylaerts MF, Ding L, Narisawa S, Van Kerckhoven S, Millán JL (2006) Mammalian alkaline phosphatase catalysis requires active site structure stabilization via the N-terminal amino acid microenvironment. Biochemistry 45:9756–9766
    • (2006) Biochemistry , vol.45 , pp. 9756-9766
    • Hoylaerts, M.F.1    Ding, L.2    Narisawa, S.3    Van Kerckhoven, S.4    Millán, J.L.5
  • 18
    • 0030928122 scopus 로고    scopus 로고
    • Mammalian alkaline phosphatases are allosteric enzymes
    • COI: 1:CAS:528:DyaK2sXlvFGiurg%3D, PID: 9278439
    • Hoylaerts MF, Manes T, Millán JL (1997) Mammalian alkaline phosphatases are allosteric enzymes. J Biol Chem 272:22781–22787
    • (1997) J Biol Chem , vol.272 , pp. 22781-22787
    • Hoylaerts, M.F.1    Manes, T.2    Millán, J.L.3
  • 19
    • 67649868096 scopus 로고    scopus 로고
    • Mild forms of hypophosphatasia mostly result from dominant negative effect of severe alleles or from compound heterozygosity for severe and moderate alleles
    • PID: 19500388
    • Fauvert D, Brun-Heath I, Lia-Baldini AS, Bellazi L, Taillandier A, Serre JL, de Mazancourt P, Mornet E (2009) Mild forms of hypophosphatasia mostly result from dominant negative effect of severe alleles or from compound heterozygosity for severe and moderate alleles. BMC Med Genet 10:51
    • (2009) BMC Med Genet , vol.10 , pp. 51
    • Fauvert, D.1    Brun-Heath, I.2    Lia-Baldini, A.S.3    Bellazi, L.4    Taillandier, A.5    Serre, J.L.6    de Mazancourt, P.7    Mornet, E.8
  • 20
    • 0035903096 scopus 로고    scopus 로고
    • Structural evidence for a functional role of human tissue nonspecific alkaline phosphatase in bone mineralization
    • COI: 1:CAS:528:DC%2BD3MXmsVejs74%3D, PID: 11395499
    • Mornet E, Stura E, Lia-Baldini AS, Stigbrand T, Menez A, Le Du MH (2001) Structural evidence for a functional role of human tissue nonspecific alkaline phosphatase in bone mineralization. J Biol Chem 276:31171–31178
    • (2001) J Biol Chem , vol.276 , pp. 31171-31178
    • Mornet, E.1    Stura, E.2    Lia-Baldini, A.S.3    Stigbrand, T.4    Menez, A.5    Le Du, M.H.6
  • 22
    • 0024224566 scopus 로고
    • Correlation between loss of alkaline phosphatase activity and accumulation of calcium during matrix vesicle-mediated mineralization
    • COI: 1:CAS:528:DyaL1cXlvVOrs7g%3D, PID: 3192545
    • Genge BR, Sauer GR, Wu LN, McLean FM, Wuthier RE (1988) Correlation between loss of alkaline phosphatase activity and accumulation of calcium during matrix vesicle-mediated mineralization. J Biol Chem 263:18513–18519
    • (1988) J Biol Chem , vol.263 , pp. 18513-18519
    • Genge, B.R.1    Sauer, G.R.2    Wu, L.N.3    McLean, F.M.4    Wuthier, R.E.5
  • 23
    • 0036965928 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored proteins: structure, function, and cleavage by phosphatidylinositol-specific phospholipase C
    • COI: 1:CAS:528:DC%2BD38Xos1aisrY%3D, PID: 12440695
    • Sharom FJ, Lehto MT (2002) Glycosylphosphatidylinositol-anchored proteins: structure, function, and cleavage by phosphatidylinositol-specific phospholipase C. Biochem Cell Biol 80:535–549
    • (2002) Biochem Cell Biol , vol.80 , pp. 535-549
    • Sharom, F.J.1    Lehto, M.T.2
  • 24
    • 0028304074 scopus 로고
    • Biosynthesis of glycosylphosphatidylinositol-anchored human placental alkaline phosphatase: evidence for a phospholipase C-sensitive precursor and its post-attachment conversion into a phospholipase C-resistant form
    • COI: 1:CAS:528:DyaK2cXksl2nsLg%3D, PID: 8037672
    • Wong YW, Low MG (1994) Biosynthesis of glycosylphosphatidylinositol-anchored human placental alkaline phosphatase: evidence for a phospholipase C-sensitive precursor and its post-attachment conversion into a phospholipase C-resistant form. Biochem J 301(Pt 1):205–209
    • (1994) Biochem J , vol.301 , pp. 205-209
    • Wong, Y.W.1    Low, M.G.2
  • 25
    • 0000708773 scopus 로고
    • Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase
    • COI: 1:CAS:528:DyaL2sXht1Wg, PID: 3532105
    • Weiss MJ, Henthorn PS, Lafferty MA, Slaughter C, Raducha M, Harris H (1986) Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase. Proc Natl Acad Sci USA 83:7182–7186
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7182-7186
    • Weiss, M.J.1    Henthorn, P.S.2    Lafferty, M.A.3    Slaughter, C.4    Raducha, M.5    Harris, H.6
  • 26
    • 0031036060 scopus 로고    scopus 로고
    • Human tissue non-specific alkaline phosphatases: sugar-moiety-induced enzymic and antigenic modulations and genetic aspects
    • COI: 1:CAS:528:DyaK2sXotFKmtQ%3D%3D, PID: 9020858
    • Nosjean O, Koyama I, Goseki M, Roux B, Komoda T (1997) Human tissue non-specific alkaline phosphatases: sugar-moiety-induced enzymic and antigenic modulations and genetic aspects. Biochem J 321(Pt 2):297–303
    • (1997) Biochem J , vol.321 , pp. 297-303
    • Nosjean, O.1    Koyama, I.2    Goseki, M.3    Roux, B.4    Komoda, T.5
  • 27
    • 70349432183 scopus 로고    scopus 로고
    • Glycosylation differences contribute to distinct catalytic properties among bone alkaline phosphatase isoforms
    • COI: 1:CAS:528:DC%2BD1MXhtFyjsr3I, PID: 19631305
    • Halling Linder C, Narisawa S, Millán JL, Magnusson P (2009) Glycosylation differences contribute to distinct catalytic properties among bone alkaline phosphatase isoforms. Bone 45:987–993
    • (2009) Bone , vol.45 , pp. 987-993
    • Halling Linder, C.1    Narisawa, S.2    Millán, J.L.3    Magnusson, P.4
  • 29
    • 0025184825 scopus 로고
    • Alkaline phosphatase (tissue-nonspecific isoenzyme) is a phosphoethanolamine and pyridoxal-5′-phosphate ectophosphatase: normal and hypophosphatasia fibroblast study
    • COI: 1:CAS:528:DyaK3MXlvFCisw%3D%3D, PID: 2220817
    • Fedde KN, Whyte MP (1990) Alkaline phosphatase (tissue-nonspecific isoenzyme) is a phosphoethanolamine and pyridoxal-5′-phosphate ectophosphatase: normal and hypophosphatasia fibroblast study. Am J Hum Genet 47:767–775
    • (1990) Am J Hum Genet , vol.47 , pp. 767-775
    • Fedde, K.N.1    Whyte, M.P.2
  • 33
    • 84885578342 scopus 로고    scopus 로고
    • Alkaline phosphatases contribute to uterine receptivity, implantation, decidualization, and defense against bacterial endotoxin in hamsters
    • COI: 1:CAS:528:DC%2BC3sXhslGht7zO, PID: 23929901
    • Lei W, Nguyen H, Brown N, Ni H, Kiffer-Moreira T, Reese J, Millan JL, Paria BC (2013) Alkaline phosphatases contribute to uterine receptivity, implantation, decidualization, and defense against bacterial endotoxin in hamsters. Reproduction 146:419–432
    • (2013) Reproduction , vol.146 , pp. 419-432
    • Lei, W.1    Nguyen, H.2    Brown, N.3    Ni, H.4    Kiffer-Moreira, T.5    Reese, J.6    Millan, J.L.7    Paria, B.C.8
  • 34
    • 84879224607 scopus 로고    scopus 로고
    • In vivo overexpression of tissue-nonspecific alkaline phosphatase increases skeletal mineralization and affects the phosphorylation status of osteopontin
    • COI: 1:CAS:528:DC%2BC3sXpvVOmsrg%3D, PID: 23427088
    • Narisawa S, Yadav MC, Millan JL (2013) In vivo overexpression of tissue-nonspecific alkaline phosphatase increases skeletal mineralization and affects the phosphorylation status of osteopontin. J Bone Miner Res 28:1587–1598
    • (2013) J Bone Miner Res , vol.28 , pp. 1587-1598
    • Narisawa, S.1    Yadav, M.C.2    Millan, J.L.3
  • 35
    • 84962631446 scopus 로고    scopus 로고
    • Whyte MP (2015) Hypophosphatasia: etiology, nosology, pathogenesis, diagnosis, and treatment. Nat Rev Endocrinol (in press)
    • Whyte MP (2015) Hypophosphatasia: etiology, nosology, pathogenesis, diagnosis, and treatment. Nat Rev Endocrinol (in press)
  • 36
    • 84925378783 scopus 로고    scopus 로고
    • Hypophosphatasia: validation and expansion of the clinical nosology for children from 25 years experience with 173 pediatric patients
    • COI: 1:CAS:528:DC%2BC2MXlsV2gt7s%3D, PID: 25731960
    • Whyte MP, Zhang F, Wenkert D, McAlister WH, Mack KE, Benigno MC, Coburn SP, Wagy S, Griffin DM, Ericson KL, Mumm S (2015) Hypophosphatasia: validation and expansion of the clinical nosology for children from 25 years experience with 173 pediatric patients. Bone 75:229–239
    • (2015) Bone , vol.75 , pp. 229-239
    • Whyte, M.P.1    Zhang, F.2    Wenkert, D.3    McAlister, W.H.4    Mack, K.E.5    Benigno, M.C.6    Coburn, S.P.7    Wagy, S.8    Griffin, D.M.9    Ericson, K.L.10    Mumm, S.11
  • 38
    • 34248573295 scopus 로고    scopus 로고
    • Pyridoxine-responsive seizures as the first symptom of infantile hypophosphatasia caused by two novel missense mutations (c.677T>C, p. M226T; c.1112C>T, p.T371I) of the tissue-nonspecific alkaline phosphatase gene
    • COI: 1:CAS:528:DC%2BD2sXlsF2msrc%3D, PID: 17395561
    • Baumgartner-Sigl S, Haberlandt E, Mumm S, Scholl-Burgi S, Sergi C, Ryan L, Ericson KL, Whyte MP, Hogler W (2007) Pyridoxine-responsive seizures as the first symptom of infantile hypophosphatasia caused by two novel missense mutations (c.677T>C, p. M226T; c.1112C>T, p.T371I) of the tissue-nonspecific alkaline phosphatase gene. Bone 40:1655–1661
    • (2007) Bone , vol.40 , pp. 1655-1661
    • Baumgartner-Sigl, S.1    Haberlandt, E.2    Mumm, S.3    Scholl-Burgi, S.4    Sergi, C.5    Ryan, L.6    Ericson, K.L.7    Whyte, M.P.8    Hogler, W.9
  • 41
    • 0018718890 scopus 로고
    • Adult hypophosphatasia. Clinical, laboratory, and genetic investigation of a large kindred with review of the literature
    • COI: 1:STN:280:DyaL3c%2FhtVygtQ%3D%3D
    • Whyte MP, Teitelbaum SL, Murphy WA, Bergfeld MA, Avioli LV (1979) Adult hypophosphatasia. Clinical, laboratory, and genetic investigation of a large kindred with review of the literature. Medicine (Baltimore) 58:329–347
    • (1979) Medicine (Baltimore) , vol.58 , pp. 329-347
    • Whyte, M.P.1    Teitelbaum, S.L.2    Murphy, W.A.3    Bergfeld, M.A.4    Avioli, L.V.5
  • 42
    • 0019940289 scopus 로고
    • Adult hypophosphatasia with chondrocalcinosis and arthropathy. Variable penetrance of hypophosphatasemia in a large Oklahoma kindred
    • COI: 1:STN:280:DyaL387nvFKhsw%3D%3D, PID: 7072744
    • Whyte MP, Murphy WA, Fallon MD (1982) Adult hypophosphatasia with chondrocalcinosis and arthropathy. Variable penetrance of hypophosphatasemia in a large Oklahoma kindred. Am J Med 72:631–641
    • (1982) Am J Med , vol.72 , pp. 631-641
    • Whyte, M.P.1    Murphy, W.A.2    Fallon, M.D.3
  • 43
    • 0029115393 scopus 로고
    • Mice lacking tissue non-specific alkaline phosphatase die from seizures due to defective metabolism of vitamin B-6
    • COI: 1:CAS:528:DyaK2MXnvFelsL0%3D, PID: 7550313
    • Waymire KG, Mahuren JD, Jaje JM, Guilarte TR, Coburn SP, MacGregor GR (1995) Mice lacking tissue non-specific alkaline phosphatase die from seizures due to defective metabolism of vitamin B-6. Nat Genet 11:45–51
    • (1995) Nat Genet , vol.11 , pp. 45-51
    • Waymire, K.G.1    Mahuren, J.D.2    Jaje, J.M.3    Guilarte, T.R.4    Coburn, S.P.5    MacGregor, G.R.6
  • 44
    • 1842409589 scopus 로고    scopus 로고
    • Inactivation of two mouse alkaline phosphatase genes and establishment of a model of infantile hypophosphatasia
    • COI: 1:CAS:528:DyaK2sXit1GqtLs%3D, PID: 9056646
    • Narisawa S, Frohlander N, Millan JL (1997) Inactivation of two mouse alkaline phosphatase genes and establishment of a model of infantile hypophosphatasia. Dev Dyn 208:432–446
    • (1997) Dev Dyn , vol.208 , pp. 432-446
    • Narisawa, S.1    Frohlander, N.2    Millan, J.L.3
  • 45
    • 0021811803 scopus 로고
    • Markedly increased circulating pyridoxal-5′-phosphate levels in hypophosphatasia. Alkaline phosphatase acts in vitamin B6 metabolism
    • COI: 1:STN:280:DyaL2M3ovF2hsw%3D%3D, PID: 4031070
    • Whyte MP, Mahuren JD, Vrabel LA, Coburn SP (1985) Markedly increased circulating pyridoxal-5′-phosphate levels in hypophosphatasia. Alkaline phosphatase acts in vitamin B6 metabolism. J Clin Invest 76:752–756
    • (1985) J Clin Invest , vol.76 , pp. 752-756
    • Whyte, M.P.1    Mahuren, J.D.2    Vrabel, L.A.3    Coburn, S.P.4
  • 46
    • 84873245968 scopus 로고    scopus 로고
    • Isozyme profile and tissue-origin of alkaline phosphatases in mouse serum
    • COI: 1:CAS:528:DC%2BC3sXjtFGmu7c%3D, PID: 23313280
    • Halling Linder C, Englund UH, Narisawa S, Millan JL, Magnusson P (2013) Isozyme profile and tissue-origin of alkaline phosphatases in mouse serum. Bone 53:399–408
    • (2013) Bone , vol.53 , pp. 399-408
    • Halling Linder, C.1    Englund, U.H.2    Narisawa, S.3    Millan, J.L.4    Magnusson, P.5
  • 47
    • 0033278045 scopus 로고    scopus 로고
    • Root development in mice lacking functional tissue non-specific alkaline phosphatase gene: inhibition of acellular cementum formation
    • COI: 1:CAS:528:DyaK1MXjvFeksrw%3D, PID: 10371245
    • Beertsen W, VandenBos T, Everts V (1999) Root development in mice lacking functional tissue non-specific alkaline phosphatase gene: inhibition of acellular cementum formation. J Dent Res 78:1221–1229
    • (1999) J Dent Res , vol.78 , pp. 1221-1229
    • Beertsen, W.1    VandenBos, T.2    Everts, V.3
  • 51
    • 84904511967 scopus 로고    scopus 로고
    • Tissue-nonspecific alkaline phosphatase deficiency causes abnormal craniofacial bone development in the Alpl(−/−) mouse model of infantile hypophosphatasia
    • COI: 1:CAS:528:DC%2BC2cXhtlGgsbvN, PID: 25014884
    • Liu J, Nam HK, Campbell C, Gasque KC, Millan JL, Hatch NE (2014) Tissue-nonspecific alkaline phosphatase deficiency causes abnormal craniofacial bone development in the Alpl(−/−) mouse model of infantile hypophosphatasia. Bone 67:81–94
    • (2014) Bone , vol.67 , pp. 81-94
    • Liu, J.1    Nam, H.K.2    Campbell, C.3    Gasque, K.C.4    Millan, J.L.5    Hatch, N.E.6
  • 52
    • 0035160863 scopus 로고    scopus 로고
    • Abnormal vitamin B6 metabolism in alkaline phosphatase knock-out mice causes multiple abnormalities, but not the impaired bone mineralization
    • COI: 1:CAS:528:DC%2BD3MXntVemtA%3D%3D, PID: 11169525
    • Narisawa S, Wennberg C, Millán JL (2001) Abnormal vitamin B6 metabolism in alkaline phosphatase knock-out mice causes multiple abnormalities, but not the impaired bone mineralization. J. Pathol. 193:125–133
    • (2001) J. Pathol. , vol.193 , pp. 125-133
    • Narisawa, S.1    Wennberg, C.2    Millán, J.L.3
  • 53
    • 62449219309 scopus 로고    scopus 로고
    • Generation of N-ethyl-N-nitrosourea-induced mouse mutants with deviations in plasma enzyme activities as novel organ-specific disease models
    • COI: 1:CAS:528:DC%2BD1MXls1Cms7s%3D, PID: 19151073
    • Aigner B, Rathkolb B, Klaften M, Sedlmeier R, Klempt M, Wagner S, Michel D, Mayer U, Klopstock T, de Angelis MH, Wolf E (2009) Generation of N-ethyl-N-nitrosourea-induced mouse mutants with deviations in plasma enzyme activities as novel organ-specific disease models. Exp Physiol 94:412–421
    • (2009) Exp Physiol , vol.94 , pp. 412-421
    • Aigner, B.1    Rathkolb, B.2    Klaften, M.3    Sedlmeier, R.4    Klempt, M.5    Wagner, S.6    Michel, D.7    Mayer, U.8    Klopstock, T.9    de Angelis, M.H.10    Wolf, E.11
  • 57
    • 0014877378 scopus 로고
    • Isolation and characterization of calcifying matrix vesicles from epiphyseal cartilage
    • COI: 1:CAS:528:DyaE3MXivVWmug%3D%3D, PID: 5274475
    • Ali SY, Sajdera SW, Anderson HC (1970) Isolation and characterization of calcifying matrix vesicles from epiphyseal cartilage. Proc Natl Acad Sci USA 67:1513–1520
    • (1970) Proc Natl Acad Sci USA , vol.67 , pp. 1513-1520
    • Ali, S.Y.1    Sajdera, S.W.2    Anderson, H.C.3
  • 58
    • 0018069154 scopus 로고
    • Ultrastructural localization of alkaline phosphatase in initial intramembranous osteogenesis
    • PID: 709934
    • Bernard GW (1978) Ultrastructural localization of alkaline phosphatase in initial intramembranous osteogenesis. Clin Orthop Relat Res 135:218–225
    • (1978) Clin Orthop Relat Res , vol.135 , pp. 218-225
    • Bernard, G.W.1
  • 59
    • 0026457186 scopus 로고
    • Immunolocalization of alkaline phosphatase in osteoblasts and matrix vesicles of human fetal bone
    • COI: 1:CAS:528:DyaK3sXht1Wntrk%3D, PID: 1472898
    • Morris DC, Masuhara K, Takaoka K, Ono K, Anderson HC (1992) Immunolocalization of alkaline phosphatase in osteoblasts and matrix vesicles of human fetal bone. Bone Miner 19:287–298
    • (1992) Bone Miner , vol.19 , pp. 287-298
    • Morris, D.C.1    Masuhara, K.2    Takaoka, K.3    Ono, K.4    Anderson, H.C.5
  • 60
    • 21144434783 scopus 로고    scopus 로고
    • Sustained osteomalacia of long bones despite major improvement in other hypophosphatasia-related mineral deficits in tissue nonspecific alkaline phosphatase/nucleotide pyrophosphatase phosphodiesterase 1 double-deficient mice
    • COI: 1:CAS:528:DC%2BD2MXlsFynsro%3D, PID: 15920156
    • Anderson HC, Harmey D, Camacho NP, Garimella R, Sipe JB, Tague S, Bi X, Johnson K, Terkeltaub R, Millan JL (2005) Sustained osteomalacia of long bones despite major improvement in other hypophosphatasia-related mineral deficits in tissue nonspecific alkaline phosphatase/nucleotide pyrophosphatase phosphodiesterase 1 double-deficient mice. Am J Pathol 166:1711–1720
    • (2005) Am J Pathol , vol.166 , pp. 1711-1720
    • Anderson, H.C.1    Harmey, D.2    Camacho, N.P.3    Garimella, R.4    Sipe, J.B.5    Tague, S.6    Bi, X.7    Johnson, K.8    Terkeltaub, R.9    Millan, J.L.10
  • 61
    • 0030696783 scopus 로고    scopus 로고
    • Matrix vesicles in osteomalacic hypophosphatasia bone contain apatite-like mineral crystals
    • COI: 1:STN:280:DyaK1c%2FmsF2ltg%3D%3D, PID: 9403706
    • Anderson HC, Hsu HH, Morris DC, Fedde KN, Whyte MP (1997) Matrix vesicles in osteomalacic hypophosphatasia bone contain apatite-like mineral crystals. Am J Pathol 151:1555–1561
    • (1997) Am J Pathol , vol.151 , pp. 1555-1561
    • Anderson, H.C.1    Hsu, H.H.2    Morris, D.C.3    Fedde, K.N.4    Whyte, M.P.5
  • 62
    • 1242316272 scopus 로고    scopus 로고
    • Impaired calcification around matrix vesicles of growth plate and bone in alkaline phosphatase-deficient mice
    • COI: 1:CAS:528:DC%2BD2cXitl2jtr0%3D, PID: 14982838
    • Anderson HC, Sipe JB, Hessle L, Dhanyamraju R, Atti E, Camacho NP, Millan JL (2004) Impaired calcification around matrix vesicles of growth plate and bone in alkaline phosphatase-deficient mice. Am J Pathol 164:841–847
    • (2004) Am J Pathol , vol.164 , pp. 841-847
    • Anderson, H.C.1    Sipe, J.B.2    Hessle, L.3    Dhanyamraju, R.4    Atti, E.5    Camacho, N.P.6    Millan, J.L.7
  • 63
    • 49749205640 scopus 로고
    • Excretion of inorganic pyrophosphate in hypophosphatasia
    • COI: 1:STN:280:DyaF2M7kt1Ohtg%3D%3D, PID: 14337825
    • Russell RG (1965) Excretion of inorganic pyrophosphate in hypophosphatasia. Lancet 2:461–464
    • (1965) Lancet , vol.2 , pp. 461-464
    • Russell, R.G.1
  • 64
    • 0015057271 scopus 로고
    • Inorganic pyrophosphate in plasma in normal persons and in patients with hypophosphatasia, osteogenesis imperfecta, and other disorders of bone
    • COI: 1:CAS:528:DyaE3MXhtlyis7g%3D, PID: 4324072
    • Russell RG, Bisaz S, Donath A, Morgan DB, Fleisch H (1971) Inorganic pyrophosphate in plasma in normal persons and in patients with hypophosphatasia, osteogenesis imperfecta, and other disorders of bone. J Clin Invest 50:961–969
    • (1971) J Clin Invest , vol.50 , pp. 961-969
    • Russell, R.G.1    Bisaz, S.2    Donath, A.3    Morgan, D.B.4    Fleisch, H.5
  • 65
    • 0014029045 scopus 로고
    • Effect of pyrophosphate on hydroxyapatite and its implications in calcium homeostasis
    • COI: 1:CAS:528:DyaF2sXis1Sqtw%3D%3D, PID: 4306793
    • Fleisch H, Russell RG, Straumann F (1966) Effect of pyrophosphate on hydroxyapatite and its implications in calcium homeostasis. Nature 212:901–903
    • (1966) Nature , vol.212 , pp. 901-903
    • Fleisch, H.1    Russell, R.G.2    Straumann, F.3
  • 66
    • 1642313676 scopus 로고    scopus 로고
    • Concerted regulation of inorganic pyrophosphate and osteopontin by Akp2, Enpp1, and Ank: an integrated model of the pathogenesis of mineralization disorders
    • COI: 1:CAS:528:DC%2BD2cXjsFemur0%3D, PID: 15039209
    • Harmey D, Hessle L, Narisawa S, Johnson KA, Terkeltaub R, Millán JL (2004) Concerted regulation of inorganic pyrophosphate and osteopontin by Akp2, Enpp1, and Ank: an integrated model of the pathogenesis of mineralization disorders. Am J Pathol 164:1199–1209
    • (2004) Am J Pathol , vol.164 , pp. 1199-1209
    • Harmey, D.1    Hessle, L.2    Narisawa, S.3    Johnson, K.A.4    Terkeltaub, R.5    Millán, J.L.6
  • 67
    • 0037047051 scopus 로고    scopus 로고
    • Tissue-nonspecific alkaline phosphatase and plasma cell membrane glycoprotein-1 are central antagonistic regulators of bone mineralization
    • COI: 1:CAS:528:DC%2BD38XlsVGgt70%3D, PID: 12082181
    • Hessle L, Johnson KA, Anderson HC, Narisawa S, Sali A, Goding JW, Terkeltaub R, Millan JL (2002) Tissue-nonspecific alkaline phosphatase and plasma cell membrane glycoprotein-1 are central antagonistic regulators of bone mineralization. Proc Natl Acad Sci USA 99:9445–9449
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9445-9449
    • Hessle, L.1    Johnson, K.A.2    Anderson, H.C.3    Narisawa, S.4    Sali, A.5    Goding, J.W.6    Terkeltaub, R.7    Millan, J.L.8
  • 69
    • 77951223976 scopus 로고    scopus 로고
    • Proteoliposomes harboring alkaline phosphatase and nucleotide pyrophosphatase as matrix vesicle biomimetics
    • COI: 1:CAS:528:DC%2BC3cXisFaktr0%3D, PID: 20048161
    • Simao AM, Yadav MC, Narisawa S, Bolean M, Pizauro JM, Hoylaerts MF, Ciancaglini P, Millan JL (2010) Proteoliposomes harboring alkaline phosphatase and nucleotide pyrophosphatase as matrix vesicle biomimetics. J Biol Chem 285:7598–7609
    • (2010) J Biol Chem , vol.285 , pp. 7598-7609
    • Simao, A.M.1    Yadav, M.C.2    Narisawa, S.3    Bolean, M.4    Pizauro, J.M.5    Hoylaerts, M.F.6    Ciancaglini, P.7    Millan, J.L.8
  • 70
    • 79251482785 scopus 로고    scopus 로고
    • Loss of skeletal mineralization by the simultaneous ablation of PHOSPHO1 and alkaline phosphatase function: a unified model of the mechanisms of initiation of skeletal calcification
    • COI: 1:CAS:528:DC%2BC3MXjt1Wqsr4%3D, PID: 20684022
    • Yadav MC, Simão AM, Narisawa S, Huesa C, McKee MD, Farquharson C, Millán JL (2011) Loss of skeletal mineralization by the simultaneous ablation of PHOSPHO1 and alkaline phosphatase function: a unified model of the mechanisms of initiation of skeletal calcification. J Bone Miner Res 26:286–297
    • (2011) J Bone Miner Res , vol.26 , pp. 286-297
    • Yadav, M.C.1    Simão, A.M.2    Narisawa, S.3    Huesa, C.4    McKee, M.D.5    Farquharson, C.6    Millán, J.L.7
  • 71
    • 84880262364 scopus 로고    scopus 로고
    • The role of phosphatases in the initiation of skeletal mineralization
    • COI: 1:CAS:528:DC%2BC3sXhsFyms77I, PID: 23183786
    • Millan JL (2013) The role of phosphatases in the initiation of skeletal mineralization. Calcif Tissue Int 93:299–306
    • (2013) Calcif Tissue Int , vol.93 , pp. 299-306
    • Millan, J.L.1
  • 72
    • 0014045713 scopus 로고
    • Association of inorganic-pyrophosphatase activity with human alkaline-phosphatase preparations
    • COI: 1:CAS:528:DyaF2sXosVWh, PID: 6030299
    • Moss DW, Eaton RH, Smith JK, Whitby LG (1967) Association of inorganic-pyrophosphatase activity with human alkaline-phosphatase preparations. Biochem J 102:53–57
    • (1967) Biochem J , vol.102 , pp. 53-57
    • Moss, D.W.1    Eaton, R.H.2    Smith, J.K.3    Whitby, L.G.4
  • 73
    • 0016755849 scopus 로고
    • Studies on matrix vesicles isolated from chick epiphyseal cartilage. Association of pyrophosphatase and ATPase activities with alkaline phosphatase
    • COI: 1:CAS:528:DyaE2MXktl2gtLc%3D, PID: 237558
    • Majeska RJ, Wuthier RE (1975) Studies on matrix vesicles isolated from chick epiphyseal cartilage. Association of pyrophosphatase and ATPase activities with alkaline phosphatase. Biochim Biophys Acta 391:51–60
    • (1975) Biochim Biophys Acta , vol.391 , pp. 51-60
    • Majeska, R.J.1    Wuthier, R.E.2
  • 74
    • 0019161422 scopus 로고
    • Stereospecific inhibition of alkaline phosphatase by L-tetramisole prevents in vitro cartilage calcification
    • COI: 1:CAS:528:DyaL3MXksVKgug%3D%3D, PID: 6449630
    • Fallon MD, Whyte MP, Teitelbaum SL (1980) Stereospecific inhibition of alkaline phosphatase by L-tetramisole prevents in vitro cartilage calcification. Lab Invest 43:489–494
    • (1980) Lab Invest , vol.43 , pp. 489-494
    • Fallon, M.D.1    Whyte, M.P.2    Teitelbaum, S.L.3
  • 75
    • 0027991788 scopus 로고
    • Phosphodiesterase activity is a novel property of alkaline phosphatase from osseous plate
    • COI: 1:CAS:528:DyaK2cXkslKqs7o%3D, PID: 8042997
    • Rezende AA, Pizauro JM, Ciancaglini P, Leone FA (1994) Phosphodiesterase activity is a novel property of alkaline phosphatase from osseous plate. Biochem J 301(Pt 2):517–522
    • (1994) Biochem J , vol.301 , pp. 517-522
    • Rezende, A.A.1    Pizauro, J.M.2    Ciancaglini, P.3    Leone, F.A.4
  • 77
    • 0032444219 scopus 로고    scopus 로고
    • Structure, evolution and action of vitamin B6-dependent enzymes
    • COI: 1:CAS:528:DyaK1MXhs1OqsQ%3D%3D, PID: 9914259
    • Jansonius JN (1998) Structure, evolution and action of vitamin B6-dependent enzymes. Curr Opin Struct Biol 8:759–769
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 759-769
    • Jansonius, J.N.1
  • 78
    • 0028914274 scopus 로고
    • Alkaline phosphatase: placental and tissue-nonspecific isoenzymes hydrolyze phosphoethanolamine, inorganic pyrophosphate, and pyridoxal 5′-phosphate. Substrate accumulation in carriers of hypophosphatasia corrects during pregnancy
    • COI: 1:CAS:528:DyaK2MXkslyksLc%3D, PID: 7706447
    • Whyte MP, Landt M, Ryan LM, Mulivor RA, Henthorn PS, Fedde KN, Mahuren JD, Coburn SP (1995) Alkaline phosphatase: placental and tissue-nonspecific isoenzymes hydrolyze phosphoethanolamine, inorganic pyrophosphate, and pyridoxal 5′-phosphate. Substrate accumulation in carriers of hypophosphatasia corrects during pregnancy. J Clin Invest 95:1440–1445
    • (1995) J Clin Invest , vol.95 , pp. 1440-1445
    • Whyte, M.P.1    Landt, M.2    Ryan, L.M.3    Mulivor, R.A.4    Henthorn, P.S.5    Fedde, K.N.6    Mahuren, J.D.7    Coburn, S.P.8
  • 79
    • 0025641050 scopus 로고
    • Increased plasma pyridoxal-5′-phosphate levels before and after pyridoxine loading in carriers of perinatal/infantile hypophosphatasia
    • COI: 1:STN:280:DyaK3M7nvFSqug%3D%3D, PID: 2079838
    • Chodirker BN, Coburn SP, Seargeant LE, Whyte MP, Greenberg CR (1990) Increased plasma pyridoxal-5′-phosphate levels before and after pyridoxine loading in carriers of perinatal/infantile hypophosphatasia. J Inherit Metab Dis 13:891–896
    • (1990) J Inherit Metab Dis , vol.13 , pp. 891-896
    • Chodirker, B.N.1    Coburn, S.P.2    Seargeant, L.E.3    Whyte, M.P.4    Greenberg, C.R.5
  • 80
    • 0023897043 scopus 로고
    • Perinatal hypophosphatasia: tissue levels of vitamin B6 are unremarkable despite markedly increased circulating concentrations of pyridoxal-5′-phosphate. Evidence for an ectoenzyme role for tissue-nonspecific alkaline phosphatase
    • COI: 1:CAS:528:DyaL1cXitVaktrY%3D, PID: 3350970
    • Whyte MP, Mahuren JD, Fedde KN, Cole FS, McCabe ER, Coburn SP (1988) Perinatal hypophosphatasia: tissue levels of vitamin B6 are unremarkable despite markedly increased circulating concentrations of pyridoxal-5′-phosphate. Evidence for an ectoenzyme role for tissue-nonspecific alkaline phosphatase. J Clin Invest 81:1234–1239
    • (1988) J Clin Invest , vol.81 , pp. 1234-1239
    • Whyte, M.P.1    Mahuren, J.D.2    Fedde, K.N.3    Cole, F.S.4    McCabe, E.R.5    Coburn, S.P.6
  • 81
    • 0027944629 scopus 로고
    • Stage-specific expression of alkaline phosphatase during neural development in the mouse
    • COI: 1:CAS:528:DyaK2MXis1Crt7c%3D, PID: 7533563
    • Narisawa S, Hasegawa H, Watanabe K, Millán JL (1994) Stage-specific expression of alkaline phosphatase during neural development in the mouse. Dev Dyn 201:227–235
    • (1994) Dev Dyn , vol.201 , pp. 227-235
    • Narisawa, S.1    Hasegawa, H.2    Watanabe, K.3    Millán, J.L.4
  • 83
    • 84871880144 scopus 로고    scopus 로고
    • Ablation of TNAP function compromises myelination and synaptogenesis in the mouse brain
    • COI: 1:CAS:528:DC%2BC38XhtF2jtrnF, PID: 22696173
    • Hanics J, Barna J, Xiao J, Millan JL, Fonta C, Negyessy L (2012) Ablation of TNAP function compromises myelination and synaptogenesis in the mouse brain. Cell Tissue Res 349:459–471
    • (2012) Cell Tissue Res , vol.349 , pp. 459-471
    • Hanics, J.1    Barna, J.2    Xiao, J.3    Millan, J.L.4    Fonta, C.5    Negyessy, L.6
  • 84
    • 0014667092 scopus 로고
    • O-phosphorylethanolamine ammonia lyase, a new pyridoxal phosphate-dependent enzyme
    • COI: 1:CAS:528:DyaF1MXksVKisr8%3D, PID: 5796745
    • Fleshood HL, Pitot HC (1969) O-phosphorylethanolamine ammonia lyase, a new pyridoxal phosphate-dependent enzyme. Biochem Biophys Res Commun 36:110–118
    • (1969) Biochem Biophys Res Commun , vol.36 , pp. 110-118
    • Fleshood, H.L.1    Pitot, H.C.2
  • 85
    • 0014940107 scopus 로고
    • The metabolism of O-phosphorylethanolamine in animal tissues. I. O-phosphorylethanolamine phospho-lyase: partial purification and characterization
    • COI: 1:CAS:528:DyaE3cXkvFCrsrk%3D, PID: 5498429
    • Fleshood HL, Pitot HC (1970) The metabolism of O-phosphorylethanolamine in animal tissues. I. O-phosphorylethanolamine phospho-lyase: partial purification and characterization. J Biol Chem 245:4414–4420
    • (1970) J Biol Chem , vol.245 , pp. 4414-4420
    • Fleshood, H.L.1    Pitot, H.C.2
  • 86
    • 0014899897 scopus 로고
    • The metabolism of O-phosphorylethanolamine in animal tissues. II. Metabolic regulation of O-phosphorylethanolamine phospho-lyase in vivo
    • COI: 1:CAS:528:DyaE3MXksVKgurY%3D, PID: 4322284
    • Fleshood HL, Pitot HC (1970) The metabolism of O-phosphorylethanolamine in animal tissues. II. Metabolic regulation of O-phosphorylethanolamine phospho-lyase in vivo. Arch Biochem Biophys 141:423–429
    • (1970) Arch Biochem Biophys , vol.141 , pp. 423-429
    • Fleshood, H.L.1    Pitot, H.C.2
  • 87
    • 0019184883 scopus 로고
    • Hypophosphatasia (adult form): quantitation of serum alkaline phosphatase isoenzyme activity in a large kindred
    • PID: 7379306
    • Millán JL, Whyte MP, Avioli LV, Fishman WH (1980) Hypophosphatasia (adult form): quantitation of serum alkaline phosphatase isoenzyme activity in a large kindred. Clin Chem 26:840–845
    • (1980) Clin Chem , vol.26 , pp. 840-845
    • Millán, J.L.1    Whyte, M.P.2    Avioli, L.V.3    Fishman, W.H.4
  • 88
    • 0033815250 scopus 로고    scopus 로고
    • Functional characterization of osteoblasts and osteoclasts from alkaline phosphatase knockout mice
    • COI: 1:CAS:528:DC%2BD3cXnsVCltbs%3D, PID: 11028439
    • Wennberg C, Hessle L, Lundberg P, Mauro S, Narisawa S, Lerner UH, Millán JL (2000) Functional characterization of osteoblasts and osteoclasts from alkaline phosphatase knockout mice. J Bone Miner Res 15:1879–1888
    • (2000) J Bone Miner Res , vol.15 , pp. 1879-1888
    • Wennberg, C.1    Hessle, L.2    Lundberg, P.3    Mauro, S.4    Narisawa, S.5    Lerner, U.H.6    Millán, J.L.7
  • 89
    • 10744228509 scopus 로고    scopus 로고
    • Linked deficiencies in extracellular PP(i) and osteopontin mediate pathologic calcification associated with defective PC-1 and ANK expression
    • COI: 1:CAS:528:DC%2BD3sXkslOhsLY%3D, PID: 12817751
    • Johnson K, Goding J, Van Etten D, Sali A, Hu SI, Farley D, Krug H, Hessle L, Millán JL, Terkeltaub R (2003) Linked deficiencies in extracellular PP(i) and osteopontin mediate pathologic calcification associated with defective PC-1 and ANK expression. J Bone Miner Res 18:994–1004
    • (2003) J Bone Miner Res , vol.18 , pp. 994-1004
    • Johnson, K.1    Goding, J.2    Van Etten, D.3    Sali, A.4    Hu, S.I.5    Farley, D.6    Krug, H.7    Hessle, L.8    Millán, J.L.9    Terkeltaub, R.10
  • 91
    • 0034831322 scopus 로고    scopus 로고
    • Binding of bone sialoprotein, osteopontin and synthetic polypeptides to hydroxyapatite
    • COI: 1:CAS:528:DC%2BD38Xlt12hsbc%3D, PID: 11696986
    • Goldberg HA, Warner KJ, Li MC, Hunter GK (2001) Binding of bone sialoprotein, osteopontin and synthetic polypeptides to hydroxyapatite. Connect Tissue Res 42:25–37
    • (2001) Connect Tissue Res , vol.42 , pp. 25-37
    • Goldberg, H.A.1    Warner, K.J.2    Li, M.C.3    Hunter, G.K.4
  • 92
    • 23944440915 scopus 로고    scopus 로고
    • Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications
    • COI: 1:CAS:528:DC%2BD2MXntFGmsLw%3D, PID: 15869464
    • Christensen B, Nielsen MS, Haselmann KF, Petersen TE, Sorensen ES (2005) Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications. Biochem J 390:285–292
    • (2005) Biochem J , vol.390 , pp. 285-292
    • Christensen, B.1    Nielsen, M.S.2    Haselmann, K.F.3    Petersen, T.E.4    Sorensen, E.S.5
  • 93
    • 0028301910 scopus 로고
    • Modulation of crystal formation by bone phosphoproteins: structural specificity of the osteopontin-mediated inhibition of hydroxyapatite formation
    • COI: 1:CAS:528:DyaK2cXkt12mt78%3D, PID: 8010953
    • Hunter GK, Kyle CL, Goldberg HA (1994) Modulation of crystal formation by bone phosphoproteins: structural specificity of the osteopontin-mediated inhibition of hydroxyapatite formation. Biochem J 300(Pt 3):723–728
    • (1994) Biochem J , vol.300 , pp. 723-728
    • Hunter, G.K.1    Kyle, C.L.2    Goldberg, H.A.3
  • 94
    • 0034733562 scopus 로고    scopus 로고
    • Phosphorylation of osteopontin is required for inhibition of vascular smooth muscle cell calcification
    • COI: 1:CAS:528:DC%2BD3cXkslags70%3D, PID: 10766759
    • Jono S, Peinado C, Giachelli CM (2000) Phosphorylation of osteopontin is required for inhibition of vascular smooth muscle cell calcification. J Biol Chem 275:20197–20203
    • (2000) J Biol Chem , vol.275 , pp. 20197-20203
    • Jono, S.1    Peinado, C.2    Giachelli, C.M.3
  • 95
    • 1642422853 scopus 로고    scopus 로고
    • Inhibition of hydroxyapatite formation by osteopontin phosphopeptides
    • COI: 1:CAS:528:DC%2BD2cXisVyku7w%3D, PID: 14678013
    • Pampena DA, Robertson KA, Litvinova O, Lajoie G, Goldberg HA, Hunter GK (2004) Inhibition of hydroxyapatite formation by osteopontin phosphopeptides. Biochem J 378:1083–1087
    • (2004) Biochem J , vol.378 , pp. 1083-1087
    • Pampena, D.A.1    Robertson, K.A.2    Litvinova, O.3    Lajoie, G.4    Goldberg, H.A.5    Hunter, G.K.6
  • 96
    • 77953229051 scopus 로고    scopus 로고
    • Phosphorylation-dependent inhibition of mineralization by osteopontin ASARM peptides is regulated by PHEX cleavage
    • COI: 1:CAS:528:DC%2BC3cXnt1Kjurc%3D, PID: 19775205
    • Addison WN, Masica DL, Gray JJ, McKee MD (2010) Phosphorylation-dependent inhibition of mineralization by osteopontin ASARM peptides is regulated by PHEX cleavage. J Bone Miner Res 25:695–705
    • (2010) J Bone Miner Res , vol.25 , pp. 695-705
    • Addison, W.N.1    Masica, D.L.2    Gray, J.J.3    McKee, M.D.4
  • 101
    • 0242380382 scopus 로고    scopus 로고
    • Management of craniosynostosis
    • PID: 12711969, quiz 2049
    • Panchal J, Uttchin V (2003) Management of craniosynostosis. Plast Reconstr Surg 111:2032–2048 quiz 2049
    • (2003) Plast Reconstr Surg , vol.111 , pp. 2032-2048
    • Panchal, J.1    Uttchin, V.2
  • 102
    • 84930200099 scopus 로고    scopus 로고
    • Enzyme replacement for craniofacial skeletal defects and craniosynostosis in murine hypophosphatasia
    • COI: 1:CAS:528:DC%2BC2MXps1els78%3D, PID: 25959417
    • Liu J, Campbell C, Nam HK, Caron A, Yadav MC, Millan JL, Hatch NE (2015) Enzyme replacement for craniofacial skeletal defects and craniosynostosis in murine hypophosphatasia. Bone 78:203–211
    • (2015) Bone , vol.78 , pp. 203-211
    • Liu, J.1    Campbell, C.2    Nam, H.K.3    Caron, A.4    Yadav, M.C.5    Millan, J.L.6    Hatch, N.E.7
  • 103
    • 84919340669 scopus 로고    scopus 로고
    • Improvement of the skeletal and dental hypophosphatasia phenotype in Alpl(−/−) mice by administration of soluble (non-targeted) chimeric alkaline phosphatase
    • COI: 1:CAS:528:DC%2BC2MXosFWlsg%3D%3D, PID: 25433339
    • Gasque KC, Foster BL, Kuss P, Yadav MC, Liu J, Kiffer-Moreira T, van Elsas A, Hatch N, Somerman MJ, Millan JL (2015) Improvement of the skeletal and dental hypophosphatasia phenotype in Alpl(−/−) mice by administration of soluble (non-targeted) chimeric alkaline phosphatase. Bone 72:137–147
    • (2015) Bone , vol.72 , pp. 137-147
    • Gasque, K.C.1    Foster, B.L.2    Kuss, P.3    Yadav, M.C.4    Liu, J.5    Kiffer-Moreira, T.6    van Elsas, A.7    Hatch, N.8    Somerman, M.J.9    Millan, J.L.10
  • 104
    • 77952113129 scopus 로고    scopus 로고
    • Incidence of perinatal complications in children with premature craniosynostosis
    • PID: 20121492
    • Weber B, Schwabegger AH, Oberaigner W, Rumer-Moser A, Steiner H (2010) Incidence of perinatal complications in children with premature craniosynostosis. J Perinat Med 38:319–325
    • (2010) J Perinat Med , vol.38 , pp. 319-325
    • Weber, B.1    Schwabegger, A.H.2    Oberaigner, W.3    Rumer-Moser, A.4    Steiner, H.5
  • 105
    • 0017738368 scopus 로고
    • The role of inhibitors and other factors in the pathogenesis of recurrent calcium-containing renal stones
    • COI: 1:CAS:528:DyaE2sXlvVaju74%3D, PID: 196803
    • Baumann JM, Bisaz S, Felix R, Fleisch H, Ganz U, Russell RG (1977) The role of inhibitors and other factors in the pathogenesis of recurrent calcium-containing renal stones. Clin Sci Mol Med 53:141–148
    • (1977) Clin Sci Mol Med , vol.53 , pp. 141-148
    • Baumann, J.M.1    Bisaz, S.2    Felix, R.3    Fleisch, H.4    Ganz, U.5    Russell, R.G.6
  • 106
    • 0025036910 scopus 로고
    • Prevalence of hypocitraturia and hypopyrophosphaturia in recurrent calcium stone formers: as isolated defects or associated with other metabolic abnormalities
    • COI: 1:STN:280:DyaK3M7nvFGmuw%3D%3D, PID: 1964200
    • Laminski NA, Meyers AM, Sonnekus MI, Smyth AE (1990) Prevalence of hypocitraturia and hypopyrophosphaturia in recurrent calcium stone formers: as isolated defects or associated with other metabolic abnormalities. Nephron 56:379–386
    • (1990) Nephron , vol.56 , pp. 379-386
    • Laminski, N.A.1    Meyers, A.M.2    Sonnekus, M.I.3    Smyth, A.E.4
  • 107
    • 0016582707 scopus 로고
    • The effect of 1,25-dihydroxycholecalciferol on renal tubular reabsorption of phosphate, intestinal absorption of calcium and bone histology in hypophosphataemic renal tubular rickets
    • COI: 1:CAS:528:DyaE2MXksFers7k%3D, PID: 163719
    • Russell RG, Smith R, Preston C, Walton RJ, Woods CG, Henderson RG, Norman AW (1975) The effect of 1,25-dihydroxycholecalciferol on renal tubular reabsorption of phosphate, intestinal absorption of calcium and bone histology in hypophosphataemic renal tubular rickets. Clin Sci Mol Med 48:177–186
    • (1975) Clin Sci Mol Med , vol.48 , pp. 177-186
    • Russell, R.G.1    Smith, R.2    Preston, C.3    Walton, R.J.4    Woods, C.G.5    Henderson, R.G.6    Norman, A.W.7
  • 108
    • 84865104399 scopus 로고    scopus 로고
    • Respiratory mechanics in an infant with perinatal lethal hypophosphatasia treated with human recombinant enzyme replacement therapy
    • PID: 22328548
    • Rodriguez E, Bober MB, Davey L, Zamora A, Li Puma AB, Chidekel A, Shaffer TH (2012) Respiratory mechanics in an infant with perinatal lethal hypophosphatasia treated with human recombinant enzyme replacement therapy. Pediatr Pulmonol 47:917–922
    • (2012) Pediatr Pulmonol , vol.47 , pp. 917-922
    • Rodriguez, E.1    Bober, M.B.2    Davey, L.3    Zamora, A.4    Li Puma, A.B.5    Chidekel, A.6    Shaffer, T.H.7
  • 109
    • 0022968773 scopus 로고
    • Management of femoral fractures and pseudofractures in adult hypophosphatasia
    • COI: 1:STN:280:DyaL28zgsVGgsA%3D%3D, PID: 3745261
    • Coe JD, Murphy WA, Whyte MP (1986) Management of femoral fractures and pseudofractures in adult hypophosphatasia. J Bone Joint Surg Am 68:981–990
    • (1986) J Bone Joint Surg Am , vol.68 , pp. 981-990
    • Coe, J.D.1    Murphy, W.A.2    Whyte, M.P.3
  • 110
    • 0019965925 scopus 로고
    • Infantile hypophosphatasia: enzyme replacement therapy by intravenous infusion of alkaline phosphatase-rich plasma from patients with Paget’s bone disease
    • COI: 1:STN:280:DyaL383mvVektQ%3D%3D, PID: 7108657
    • Whyte MP, Valdes R Jr, Ryan LM, McAlister WH (1982) Infantile hypophosphatasia: enzyme replacement therapy by intravenous infusion of alkaline phosphatase-rich plasma from patients with Paget’s bone disease. J Pediatr 101:379–386
    • (1982) J Pediatr , vol.101 , pp. 379-386
    • Whyte, M.P.1    Valdes, R.2    Ryan, L.M.3    McAlister, W.H.4
  • 111
    • 0021719343 scopus 로고
    • Enzyme replacement therapy for infantile hypophosphatasia attempted by intravenous infusions of alkaline phosphatase-rich Paget plasma: results in three additional patients
    • COI: 1:STN:280:DyaL2M%2FlslCmsg%3D%3D, PID: 6502342
    • Whyte MP, McAlister WH, Patton LS, Magill HL, Fallon MD, Lorentz WB Jr, Herrod HG (1984) Enzyme replacement therapy for infantile hypophosphatasia attempted by intravenous infusions of alkaline phosphatase-rich Paget plasma: results in three additional patients. J Pediatr 105:926–933
    • (1984) J Pediatr , vol.105 , pp. 926-933
    • Whyte, M.P.1    McAlister, W.H.2    Patton, L.S.3    Magill, H.L.4    Fallon, M.D.5    Lorentz, W.B.6    Herrod, H.G.7
  • 112
    • 0024810414 scopus 로고
    • Biochemical and morphological effects of human hepatic alkaline phosphatase in a neonate with hypophosphatasia
    • COI: 1:STN:280:DyaK3czosF2iug%3D%3D, PID: 2642253
    • Weninger M, Stinson RA, Plenk H Jr, Bock P, Pollak A (1989) Biochemical and morphological effects of human hepatic alkaline phosphatase in a neonate with hypophosphatasia. Acta Paediatr Scand Suppl 360:154–160
    • (1989) Acta Paediatr Scand Suppl , vol.360 , pp. 154-160
    • Weninger, M.1    Stinson, R.A.2    Plenk, H.3    Bock, P.4    Pollak, A.5
  • 113
    • 0009761007 scopus 로고
    • Failure of hyperphosphatasemia by intravenous infusion of purified placental alkaline phosphatase (ALP) to correct severe hypophosphatasia: evidence against a role for circulating ALP in skeletal mineralization
    • Whyte MP, Habib D, Coburn SP, Tecklenburg F, Ryan L, Fedde KN, Stinson RA (1992) Failure of hyperphosphatasemia by intravenous infusion of purified placental alkaline phosphatase (ALP) to correct severe hypophosphatasia: evidence against a role for circulating ALP in skeletal mineralization (abstract). J Bone Miner Res 7:S155
    • (1992) J Bone Miner Res , vol.7 , pp. S155
    • Whyte, M.P.1    Habib, D.2    Coburn, S.P.3    Tecklenburg, F.4    Ryan, L.5    Fedde, K.N.6    Stinson, R.A.7
  • 116
    • 34147099203 scopus 로고    scopus 로고
    • Adult hypophosphatasia treated with teriparatide
    • COI: 1:CAS:528:DC%2BD2sXksVSrsL8%3D, PID: 17213282
    • Whyte MP, Mumm S, Deal C (2007) Adult hypophosphatasia treated with teriparatide. J Clin Endocrinol Metab 92:1203–1208
    • (2007) J Clin Endocrinol Metab , vol.92 , pp. 1203-1208
    • Whyte, M.P.1    Mumm, S.2    Deal, C.3
  • 117
    • 45849148915 scopus 로고    scopus 로고
    • Treatment of adult hypophosphatasia with teriparatide
    • PID: 18308659
    • Camacho PM, Painter S, Kadanoff R (2008) Treatment of adult hypophosphatasia with teriparatide. Endocr Pract 14:204–208
    • (2008) Endocr Pract , vol.14 , pp. 204-208
    • Camacho, P.M.1    Painter, S.2    Kadanoff, R.3
  • 118
    • 76749102085 scopus 로고    scopus 로고
    • Teriparatide treatment in adult hypophosphatasia in a patient exposed to bisphosphonate: a case report
    • PID: 22461258
    • Doshi KB, Hamrahian AH, Licata AA (2009) Teriparatide treatment in adult hypophosphatasia in a patient exposed to bisphosphonate: a case report. Clin Cases Miner Bone Metab 6:266–269
    • (2009) Clin Cases Miner Bone Metab , vol.6 , pp. 266-269
    • Doshi, K.B.1    Hamrahian, A.H.2    Licata, A.A.3
  • 119
    • 78650046620 scopus 로고    scopus 로고
    • Parathyroid hormone treatment improves pain and fracture healing in adult hypophosphatasia
    • COI: 1:CAS:528:DC%2BC3cXhs1arsLrN, PID: 20739387
    • Schalin-Jantti C, Mornet E, Lamminen A, Valimaki MJ (2010) Parathyroid hormone treatment improves pain and fracture healing in adult hypophosphatasia. J Clin Endocrinol Metab 95:5174–5179
    • (2010) J Clin Endocrinol Metab , vol.95 , pp. 5174-5179
    • Schalin-Jantti, C.1    Mornet, E.2    Lamminen, A.3    Valimaki, M.J.4
  • 121
    • 84868318153 scopus 로고    scopus 로고
    • Failure of teriparatide in treatment of bone complications of adult hypophosphatasia
    • COI: 1:CAS:528:DC%2BC38XisFGrtr4%3D, PID: 22218563
    • Laroche M (2012) Failure of teriparatide in treatment of bone complications of adult hypophosphatasia. Calcif Tissue Int 90:250
    • (2012) Calcif Tissue Int , vol.90 , pp. 250
    • Laroche, M.1
  • 122
    • 3242887547 scopus 로고    scopus 로고
    • Bone neoplasms in F344 rats given teriparatide [rhPTH(1-34)] are dependent on duration of treatment and dose
    • COI: 1:CAS:528:DC%2BD2cXlslSgtro%3D, PID: 15204966
    • Vahle JL, Long GG, Sandusky G, Westmore M, Ma YL, Sato M (2004) Bone neoplasms in F344 rats given teriparatide [rhPTH(1-34)] are dependent on duration of treatment and dose. Toxicol Pathol 32:426–438
    • (2004) Toxicol Pathol , vol.32 , pp. 426-438
    • Vahle, J.L.1    Long, G.G.2    Sandusky, G.3    Westmore, M.4    Ma, Y.L.5    Sato, M.6
  • 123
    • 84897586287 scopus 로고    scopus 로고
    • Single- and multiple-dose randomized studies of blosozumab, a monoclonal antibody against sclerostin, in healthy postmenopausal women
    • COI: 1:CAS:528:DC%2BC2cXkslCrs70%3D, PID: 23996473
    • McColm J, Hu L, Womack T, Tang CC, Chiang AY (2014) Single- and multiple-dose randomized studies of blosozumab, a monoclonal antibody against sclerostin, in healthy postmenopausal women. J Bone Miner Res 29:935–943
    • (2014) J Bone Miner Res , vol.29 , pp. 935-943
    • McColm, J.1    Hu, L.2    Womack, T.3    Tang, C.C.4    Chiang, A.Y.5
  • 124
    • 0034056847 scopus 로고    scopus 로고
    • Selective drug delivery system to bone: small peptide (Asp)6 conjugation
    • COI: 1:CAS:528:DC%2BD3cXjt1CrsLw%3D, PID: 10804024
    • Kasugai S, Fujisawa R, Waki Y, Miyamoto K, Ohya K (2000) Selective drug delivery system to bone: small peptide (Asp)6 conjugation. J Bone Miner Res 15:936–943
    • (2000) J Bone Miner Res , vol.15 , pp. 936-943
    • Kasugai, S.1    Fujisawa, R.2    Waki, Y.3    Miyamoto, K.4    Ohya, K.5
  • 132
    • 84962724838 scopus 로고    scopus 로고
    • Whyte MP, Madson KL, Phillips KL, Reeves A, McAlister WH, Yakimoski A, Mack KE, Hamilton K, Kagan K, Fugita K, Thompson D, Moseley S, Odrljin T, Greenberg CR Asfotase alfa therapy for children with hypophosphatasia (submitted)
    • Whyte MP, Madson KL, Phillips KL, Reeves A, McAlister WH, Yakimoski A, Mack KE, Hamilton K, Kagan K, Fugita K, Thompson D, Moseley S, Odrljin T, Greenberg CR Asfotase alfa therapy for children with hypophosphatasia (submitted)


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