메뉴 건너뛰기




Volumn 325, Issue 1-2, 2002, Pages 59-70

Different distributions of human bone alkaline phosphatase isoforms in serum and bone tissue extracts

Author keywords

Alkaline phosphatase; Biochemical markers; Bone turnover; Glycosylphosphatidylinositol specific phospholipase D; Musculoskeletal diseases; Osteoblasts

Indexed keywords

ALKALINE PHOSPHATASE; GLYCOSYLPHOSPHATIDYLINOSITOL; PHOSPHOLIPASE D; TRITON X 100;

EID: 0036843257     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-8981(02)00248-6     Document Type: Article
Times cited : (41)

References (49)
  • 1
    • 0028918706 scopus 로고
    • Biology of human alkaline phosphatases with special reference to cancer
    • Millán J.L., Fishman W.H. Biology of human alkaline phosphatases with special reference to cancer. Crit. Rev. Clin. Lab. Sci. 32:1995;1-39.
    • (1995) Crit. Rev. Clin. Lab. Sci. , vol.32 , pp. 1-39
    • Millán, J.L.1    Fishman, W.H.2
  • 2
    • 0031020048 scopus 로고    scopus 로고
    • Different responses of bone alkaline phosphatase isoforms during recombinant insulin-like growth factor-I (IGF-I) and during growth hormone therapy in adults with growth hormone deficiency
    • Magnusson P., Degerblad M., Sääf M., Larsson L., Thorén M. Different responses of bone alkaline phosphatase isoforms during recombinant insulin-like growth factor-I (IGF-I) and during growth hormone therapy in adults with growth hormone deficiency. J. Bone Miner. Res. 12:1997;210-220.
    • (1997) J. Bone Miner. Res. , vol.12 , pp. 210-220
    • Magnusson, P.1    Degerblad, M.2    Sääf, M.3    Larsson, L.4    Thorén, M.5
  • 3
    • 0023724387 scopus 로고
    • Alkaline phosphatase is an ectoenzyme that acts on micromolar concentrations of natural substrates at physiologic pH in human osteosarcoma cells
    • Fedde K.N., Lane C.C., Whyte M.P. Alkaline phosphatase is an ectoenzyme that acts on micromolar concentrations of natural substrates at physiologic pH in human osteosarcoma cells. Arch. Biochem. Biophys. 264:1988;400-409.
    • (1988) Arch. Biochem. Biophys. , vol.264 , pp. 400-409
    • Fedde, K.N.1    Lane, C.C.2    Whyte, M.P.3
  • 4
    • 0030781023 scopus 로고    scopus 로고
    • Glycosyl-phosphatidylinositol anchored membrane enzymes
    • Hooper N.M. Glycosyl-phosphatidylinositol anchored membrane enzymes. Clin. Chim. Acta. 266:1997;3-12.
    • (1997) Clin. Chim. Acta , vol.266 , pp. 3-12
    • Hooper, N.M.1
  • 5
    • 0023555024 scopus 로고
    • Levamisole and inorganic pyrophosphate inhibit β-glycerophosphate induced mineralization of bone formed in vitro
    • Tenenbaum H.C. Levamisole and inorganic pyrophosphate inhibit β-glycerophosphate induced mineralization of bone formed in vitro. Bone Miner. 3:1987;13-26.
    • (1987) Bone Miner. , vol.3 , pp. 13-26
    • Tenenbaum, H.C.1
  • 6
    • 0025845372 scopus 로고
    • Initiation and progression of mineralization of bone nodules formed in vitro: The role of alkaline phosphatase and organic phosphate
    • Bellows C.G., Aubin J.E., Heersche J.N.M. Initiation and progression of mineralization of bone nodules formed in vitro: the role of alkaline phosphatase and organic phosphate. Bone Miner. 14:1991;27-40.
    • (1991) Bone Miner. , vol.14 , pp. 27-40
    • Bellows, C.G.1    Aubin, J.E.2    Heersche, J.N.M.3
  • 7
    • 0032717156 scopus 로고    scopus 로고
    • Involvement of phosphodiesterase I in mineralization: Histochemical studies using antler from red deer (Cervus elaphus) as a model
    • Barling P.M., Gupta D.K., Lim C.E.L. Involvement of phosphodiesterase I in mineralization: histochemical studies using antler from red deer (Cervus elaphus) as a model. Calcif. Tissue Int. 65:1999;384-389.
    • (1999) Calcif. Tissue Int. , vol.65 , pp. 384-389
    • Barling, P.M.1    Gupta, D.K.2    Lim, C.E.L.3
  • 8
    • 0033815250 scopus 로고    scopus 로고
    • Functional characterization of osteoblasts and osteoclasts from alkaline phosphatase knockout mice
    • Wennberg C., Hessle L., Lundberg P.et al. Functional characterization of osteoblasts and osteoclasts from alkaline phosphatase knockout mice. J. Bone Miner. Res. 15:2000;1879-1888.
    • (2000) J. Bone Miner. Res. , vol.15 , pp. 1879-1888
    • Wennberg, C.1    Hessle, L.2    Lundberg, P.3
  • 9
    • 0022572056 scopus 로고
    • Skeletal alkaline phosphatase activity as a bone formation index in vitro
    • Farley J.R., Baylink D.J. Skeletal alkaline phosphatase activity as a bone formation index in vitro. Metabolism. 35:1986;563-571.
    • (1986) Metabolism , vol.35 , pp. 563-571
    • Farley, J.R.1    Baylink, D.J.2
  • 11
    • 0026521313 scopus 로고
    • Human osteosarcoma cells spontaneously release matrix-vesicle-like structures with the capacity to mineralize
    • Fedde K.N. Human osteosarcoma cells spontaneously release matrix-vesicle-like structures with the capacity to mineralize. Bone Miner. 17:1992;145-151.
    • (1992) Bone Miner. , vol.17 , pp. 145-151
    • Fedde, K.N.1
  • 12
    • 0031909296 scopus 로고    scopus 로고
    • Skeletal alkaline phosphatase activity is primarily released from human osteoblasts in an insoluble form, and the net release is inhibited by calcium and skeletal growth factors
    • Anh D.J., Dimai H.P., Hall S.L., Farley J.R. Skeletal alkaline phosphatase activity is primarily released from human osteoblasts in an insoluble form, and the net release is inhibited by calcium and skeletal growth factors. Calcif. Tissue Int. 62:1998;332-340.
    • (1998) Calcif. Tissue Int. , vol.62 , pp. 332-340
    • Anh, D.J.1    Dimai, H.P.2    Hall, S.L.3    Farley, J.R.4
  • 13
    • 0029061758 scopus 로고
    • Molecular biology of matrix vesicles
    • Anderson H.C. Molecular biology of matrix vesicles. Clin. Orthop. 314:1995;266-280.
    • (1995) Clin. Orthop. , vol.314 , pp. 266-280
    • Anderson, H.C.1
  • 14
    • 0011247706 scopus 로고    scopus 로고
    • Apoptosis may determine the release of skeletal alkaline phosphatase activity from human osteoblast-line cells
    • Farley J.R., Stilt-Coffing B. Apoptosis may determine the release of skeletal alkaline phosphatase activity from human osteoblast-line cells. Calcif. Tissue Int. 68:2001;43-52.
    • (2001) Calcif. Tissue Int. , vol.68 , pp. 43-52
    • Farley, J.R.1    Stilt-Coffing, B.2
  • 15
    • 0022459882 scopus 로고
    • Characterization of multiple forms of phosphoinositide-specific phospholipase C purified from human platelets
    • Low M.G., Carroll R.C., Cox A.C. Characterization of multiple forms of phosphoinositide-specific phospholipase C purified from human platelets. Biochem. J. 237:1986;139-145.
    • (1986) Biochem. J. , vol.237 , pp. 139-145
    • Low, M.G.1    Carroll, R.C.2    Cox, A.C.3
  • 17
    • 0023872334 scopus 로고
    • A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma
    • Low M.G., Prasad A.R.S. A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma. Proc. Natl. Acad. Sci. U. S. A. 85:1988;980-984.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 980-984
    • Low, M.G.1    Prasad, A.R.S.2
  • 18
    • 0032006630 scopus 로고    scopus 로고
    • Release and extracellular transit of glycosylphosphatidylinositol proteins
    • Miller J.L. Release and extracellular transit of glycosylphosphatidylinositol proteins. J. Lab. Clin. Med. 131:1998;115-123.
    • (1998) J. Lab. Clin. Med. , vol.131 , pp. 115-123
    • Miller, J.L.1
  • 19
    • 0025998739 scopus 로고
    • Factors affecting the ability of glycosylphosphatidylinositol-specific phospholipase D to degrade the membrane anchors of cell surface proteins
    • Low M.G., Huang K.-S. Factors affecting the ability of glycosylphosphatidylinositol-specific phospholipase D to degrade the membrane anchors of cell surface proteins. Biochem. J. 279:1991;483-493.
    • (1991) Biochem. J. , vol.279 , pp. 483-493
    • Low, M.G.1    Huang, K.-S.2
  • 20
    • 0030885251 scopus 로고    scopus 로고
    • Mammalian GPI proteins: Sorting, membrane residence and functions
    • Nosjean O., Briolay A., Roux B. Mammalian GPI proteins: sorting, membrane residence and functions. Biochim. Biophys. Acta. 1331:1997;153-186.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 153-186
    • Nosjean, O.1    Briolay, A.2    Roux, B.3
  • 21
    • 0033934808 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-specific phospholipase D of human serum-activity modulation by naturally occurring amphiphiles
    • Rhode H., Schulze M., Cumme G.A.et al. Glycosylphosphatidylinositol-specific phospholipase D of human serum-activity modulation by naturally occurring amphiphiles. Biol. Chem. 381:2000;471-485.
    • (2000) Biol. Chem. , vol.381 , pp. 471-485
    • Rhode, H.1    Schulze, M.2    Cumme, G.A.3
  • 22
    • 0033172822 scopus 로고    scopus 로고
    • Solubilization of liver alkaline phosphatase isoenzyme during cholestasis in dogs
    • Solter P.F., Hoffmann W.E. Solubilization of liver alkaline phosphatase isoenzyme during cholestasis in dogs. Am. J. Vet. Res. 60:1999;1010-1015.
    • (1999) Am. J. Vet. Res. , vol.60 , pp. 1010-1015
    • Solter, P.F.1    Hoffmann, W.E.2
  • 23
    • 0026578459 scopus 로고
    • Determination of alkaline phosphatase isoenzymes in serum by high-performance liquid chromatography with post-column reaction detection
    • Magnusson P., Löfman O., Larsson L. Determination of alkaline phosphatase isoenzymes in serum by high-performance liquid chromatography with post-column reaction detection. J. Chromatogr. 576:1992;79-86.
    • (1992) J. Chromatogr. , vol.576 , pp. 79-86
    • Magnusson, P.1    Löfman, O.2    Larsson, L.3
  • 24
    • 0027263794 scopus 로고
    • Methodological aspects on separation and reaction conditions of bone and liver alkaline phosphatase isoform analysis by high-performance liquid chromatography
    • Magnusson P., Löfman O., Larsson L. Methodological aspects on separation and reaction conditions of bone and liver alkaline phosphatase isoform analysis by high-performance liquid chromatography. Anal. Biochem. 211:1993;156-163.
    • (1993) Anal. Biochem. , vol.211 , pp. 156-163
    • Magnusson, P.1    Löfman, O.2    Larsson, L.3
  • 25
    • 0028820633 scopus 로고
    • Serum osteocalcin and bone and liver alkaline phosphatase isoforms in healthy children and adolescents
    • Magnusson P., Häger A., Larsson L. Serum osteocalcin and bone and liver alkaline phosphatase isoforms in healthy children and adolescents. Pediatr. Res. 38:1995;955-961.
    • (1995) Pediatr. Res. , vol.38 , pp. 955-961
    • Magnusson, P.1    Häger, A.2    Larsson, L.3
  • 26
    • 0029583933 scopus 로고
    • Determination of bone alkaline phosphatase isoforms in serum by a new high-performance liquid chromatography assay in patients with metabolic bone disease
    • Magnusson P., Löfman O., Toss G., Larsson L. Determination of bone alkaline phosphatase isoforms in serum by a new high-performance liquid chromatography assay in patients with metabolic bone disease. Acta Orthop. Scand. 66(Suppl. 266):1995;203-204.
    • (1995) Acta Orthop. Scand. , vol.66 , Issue.SUPPL. 266 , pp. 203-204
    • Magnusson, P.1    Löfman, O.2    Toss, G.3    Larsson, L.4
  • 27
    • 0031875137 scopus 로고    scopus 로고
    • Differences of bone alkaline phosphatase isoforms in metastatic bone disease and discrepant effects of clodronate on different skeletal sites indicated by the location of pain
    • Magnusson P., Larsson L., Englund G., Larsson B., Strang P., Selin-Sjögren L. Differences of bone alkaline phosphatase isoforms in metastatic bone disease and discrepant effects of clodronate on different skeletal sites indicated by the location of pain. Clin. Chem. 44:1998;1621-1628.
    • (1998) Clin. Chem. , vol.44 , pp. 1621-1628
    • Magnusson, P.1    Larsson, L.2    Englund, G.3    Larsson, B.4    Strang, P.5    Selin-Sjögren, L.6
  • 28
    • 0032712430 scopus 로고    scopus 로고
    • Isoforms of bone alkaline phosphatase: Characterization and origin in human trabecular and cortical bone
    • Magnusson P., Larsson L., Magnusson M., Davie M.W.J., Sharp C.A. Isoforms of bone alkaline phosphatase: characterization and origin in human trabecular and cortical bone. J. Bone Miner. Res. 14:1999;1926-1933.
    • (1999) J. Bone Miner. Res. , vol.14 , pp. 1926-1933
    • Magnusson, P.1    Larsson, L.2    Magnusson, M.3    Davie, M.W.J.4    Sharp, C.A.5
  • 29
    • 0035035358 scopus 로고    scopus 로고
    • The decrease of IGF-I, IGF-binding protein-3 and bone alkaline phosphatase isoforms during gluten challenge correlates with small intestinal inflammation in children with coeliac disease
    • Jansson U.H.G., Kristiansson B., Magnusson P., Larsson L., Albertsson-Wikland K., Bjarnason R. The decrease of IGF-I, IGF-binding protein-3 and bone alkaline phosphatase isoforms during gluten challenge correlates with small intestinal inflammation in children with coeliac disease. Eur. J. Endocrinol. 144:2001;417-423.
    • (2001) Eur. J. Endocrinol. , vol.144 , pp. 417-423
    • Jansson, U.H.G.1    Kristiansson, B.2    Magnusson, P.3    Larsson, L.4    Albertsson-Wikland, K.5    Bjarnason, R.6
  • 30
  • 31
    • 0029876547 scopus 로고    scopus 로고
    • Differential solubilization of osteoblastic alkaline phosphatase from human primary bone cell cultures
    • Radisson J., Angrand M., Chavassieux P., Roux B., Azzar G. Differential solubilization of osteoblastic alkaline phosphatase from human primary bone cell cultures. Int. J. Biochem. Cell Biol. 28:1996;421-430.
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 421-430
    • Radisson, J.1    Angrand, M.2    Chavassieux, P.3    Roux, B.4    Azzar, G.5
  • 32
    • 0033407479 scopus 로고    scopus 로고
    • Activity increase after extraction of alkaline phosphatase from human osteoblastic membranes by nonionic detergents: Influence of age and sex
    • Bourrat C., Radisson J., Chavassieux P., Azzar G., Roux B., Meunier P.J. Activity increase after extraction of alkaline phosphatase from human osteoblastic membranes by nonionic detergents: influence of age and sex. Calcif. Tissue Int. 66:2000;22-28.
    • (2000) Calcif. Tissue Int. , vol.66 , pp. 22-28
    • Bourrat, C.1    Radisson, J.2    Chavassieux, P.3    Azzar, G.4    Roux, B.5    Meunier, P.J.6
  • 33
    • 0031965447 scopus 로고    scopus 로고
    • Purification and characterization of bone-specific alkaline phosphatase from a human osteosarcoma cell line
    • Nakayama M., Gorai I., Minaguchi H., Rosenquist C., Qvist P. Purification and characterization of bone-specific alkaline phosphatase from a human osteosarcoma cell line. Calcif. Tissue Int. 62:1998;67-73.
    • (1998) Calcif. Tissue Int. , vol.62 , pp. 67-73
    • Nakayama, M.1    Gorai, I.2    Minaguchi, H.3    Rosenquist, C.4    Qvist, P.5
  • 34
    • 0025036837 scopus 로고
    • Purification and characterization of glycosyl-phosphatidylinositol-specific phospholipase D
    • Huang K.-S., Li S., Fung W.-J.C.et al. Purification and characterization of glycosyl-phosphatidylinositol-specific phospholipase D. J. Biol. Chem. 265:1990;17738-17745.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17738-17745
    • Huang, K.-S.1    Li, S.2    Fung, W.-J.C.3
  • 35
    • 0025895597 scopus 로고
    • Skeletal alkaline phosphatase specific activity is an index of the osteoblastic phenotype in subpopulations of the human osteosarcoma cell line SaOS-2
    • Farley J.R., Hall S.L., Herring S., Tarbaux N.M., Matsuyama T., Wergedal J.E. Skeletal alkaline phosphatase specific activity is an index of the osteoblastic phenotype in subpopulations of the human osteosarcoma cell line SaOS-2. Metabolism. 40:1991;664-671.
    • (1991) Metabolism , vol.40 , pp. 664-671
    • Farley, J.R.1    Hall, S.L.2    Herring, S.3    Tarbaux, N.M.4    Matsuyama, T.5    Wergedal, J.E.6
  • 36
    • 0024577074 scopus 로고
    • Alkaline phosphatase activity from human osteosarcoma cell line SaOS-2: An isoenzyme standard for quantifying skeletal alkaline phosphatase activity in serum
    • Farley J.R., Kyeyune-Nyombi E., Tarbaux N.M., Hall S.L., Strong D.D. Alkaline phosphatase activity from human osteosarcoma cell line SaOS-2: an isoenzyme standard for quantifying skeletal alkaline phosphatase activity in serum. Clin. Chem. 35:1989;223-229.
    • (1989) Clin. Chem. , vol.35 , pp. 223-229
    • Farley, J.R.1    Kyeyune-Nyombi, E.2    Tarbaux, N.M.3    Hall, S.L.4    Strong, D.D.5
  • 37
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 38
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier C. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256:1981;1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 39
    • 0036956634 scopus 로고    scopus 로고
    • Monoclonal antibodies against tissue non-specific (liver/bone/kidney) alkaline phosphatase: The ISOBM TD-9 workshop
    • in press
    • Magnusson P., Ärlestig L., Paus E.et al. Monoclonal antibodies against tissue non-specific (liver/bone/kidney) alkaline phosphatase: the ISOBM TD-9 workshop. Tumour Biol. 23:2002;. [in press].
    • (2002) Tumour Biol. , vol.23
    • Magnusson, P.1    Ärlestig, L.2    Paus, E.3
  • 40
    • 0016322758 scopus 로고
    • The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins
    • Ashwell G., Morell A.G. The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins. Adv. Enzymol. Relat. Areas Mol. Biol. 41:1974;99-128.
    • (1974) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.41 , pp. 99-128
    • Ashwell, G.1    Morell, A.G.2
  • 41
    • 0020021127 scopus 로고
    • Carbohydrate-specific receptors of the liver
    • Ashwell G., Harford J. Carbohydrate-specific receptors of the liver. Ann. Rev. Biochem. 51:1982;531-554.
    • (1982) Ann. Rev. Biochem. , vol.51 , pp. 531-554
    • Ashwell, G.1    Harford, J.2
  • 42
    • 0020490742 scopus 로고
    • The role of the liver in clearance of glycoproteins from the general circulation, with special reference to intestinal alkaline phosphatase
    • Meijer D.K.F., Scholtens H.B., Hardonk M.J. The role of the liver in clearance of glycoproteins from the general circulation, with special reference to intestinal alkaline phosphatase. Pharm. Weekbl., Sci. 4:1982;57-70.
    • (1982) Pharm. Weekbl., Sci. , vol.4 , pp. 57-70
    • Meijer, D.K.F.1    Scholtens, H.B.2    Hardonk, M.J.3
  • 44
    • 0032559577 scopus 로고    scopus 로고
    • Elimination of alkaline phosphatases from circulation by the galactose receptor. Different isoforms are cleared at various rates
    • Blom E., Ali M.M., Mortensen B., Huseby N.-E. Elimination of alkaline phosphatases from circulation by the galactose receptor. Different isoforms are cleared at various rates. Clin. Chim. Acta. 270:1998;125-137.
    • (1998) Clin. Chim. Acta , vol.270 , pp. 125-137
    • Blom, E.1    Ali, M.M.2    Mortensen, B.3    Huseby, N.-E.4
  • 45
    • 0000844885 scopus 로고
    • Differential action of neuraminidase on human serum alkaline phosphatases
    • Robinson J.C., Pierce J.E. Differential action of neuraminidase on human serum alkaline phosphatases. Nature. 204:1964;472-473.
    • (1964) Nature , vol.204 , pp. 472-473
    • Robinson, J.C.1    Pierce, J.E.2
  • 46
    • 3643094131 scopus 로고
    • The behavior of infused human placental alkaline phosphatase in human subjects
    • Clubb J.S., Neale F.C., Posen S. The behavior of infused human placental alkaline phosphatase in human subjects. J. Lab. Clin. Med. 66:1965;493-507.
    • (1965) J. Lab. Clin. Med. , vol.66 , pp. 493-507
    • Clubb, J.S.1    Neale, F.C.2    Posen, S.3
  • 47
    • 0017797536 scopus 로고
    • The function of carbohydrate moiety and alteration of carbohydrate composition in human alkaline phosphatase isoenzymes
    • Komoda T., Sakagishi Y. The function of carbohydrate moiety and alteration of carbohydrate composition in human alkaline phosphatase isoenzymes. Biochim. Biophys. Acta. 523:1978;395-406.
    • (1978) Biochim. Biophys. Acta , vol.523 , pp. 395-406
    • Komoda, T.1    Sakagishi, Y.2
  • 48
    • 0003238947 scopus 로고    scopus 로고
    • Differences in sialic acid residues among bone alkaline phosphatase isoforms: A physical, biochemical, and immunological characterization
    • in press
    • Magnusson P., Farley J.R. Differences in sialic acid residues among bone alkaline phosphatase isoforms: a physical, biochemical, and immunological characterization. Calcif. Tissue Int. 71:2002;. [in press].
    • (2002) Calcif. Tissue Int. , vol.71
    • Magnusson, P.1    Farley, J.R.2
  • 49
    • 0029066224 scopus 로고
    • An age-related decrease in the concentration of insulin-like growth factor binding protein-5 in human cortical bone
    • Nicolas V., Mohan S., Honda Y.et al. An age-related decrease in the concentration of insulin-like growth factor binding protein-5 in human cortical bone. Calcif. Tissue Int. 57:1995;206-212.
    • (1995) Calcif. Tissue Int. , vol.57 , pp. 206-212
    • Nicolas, V.1    Mohan, S.2    Honda, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.