메뉴 건너뛰기




Volumn 134, Issue 1, 2003, Pages 63-70

Tissue-nonspecific alkaline phosphatase with an Asp289→Val mutation fails to reach the cell surface and undergoes proteasome-mediated degradation

Author keywords

Alkaline phosphatase; Calcium; Hypophosphatasia; Proteasome; Ubiquitination

Indexed keywords

ALKALINE PHOSPHATASE; ASPARTIC ACID; CALCIUM ION; GLUTAMINE; GLYCINE; PROTEASOME; TISSUE NONSPECIFIC ALKALINE PHOSPHATASE; UBIQUITIN; UNCLASSIFIED DRUG; VALINE;

EID: 0041318958     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvg114     Document Type: Article
Times cited : (42)

References (29)
  • 1
    • 0000985304 scopus 로고
    • The possible significance of hexosephosphoric esters in ossification
    • Robison, J.C. (1923) The possible significance of hexosephosphoric esters in ossification. Biochem. J. 17, 286-293
    • (1923) Biochem. J. , vol.17 , pp. 286-293
    • Robison, J.C.1
  • 2
    • 0025021039 scopus 로고
    • The human alkaline phosphatases: What we know and what we don't know
    • Harris, H. (1989) The human alkaline phosphatases: what we know and what we don't know. Clin. Chim. Acta. 186, 133-150
    • (1989) Clin. Chim. Acta , vol.186 , pp. 133-150
    • Harris, H.1
  • 3
    • 0000034593 scopus 로고
    • Hypophosphatasia: A new developmental anomaly
    • Rathbun, J.C. (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
  • 4
    • 0001551832 scopus 로고    scopus 로고
    • Hypophosphatasia
    • (Scriver, C.R., Beaudet, A.L., Sly, W.S., Valle, D., Childs, B., Kinzler, K.W., and Vogelstein, B., eds.) 8th ed., McGraw-Hill, New York, NY
    • Whyte, M.P. (2001) Hypophosphatasia in The Metabolic and Molecular Basis of Inherited Disease (Scriver, C.R., Beaudet, A.L., Sly, W.S., Valle, D., Childs, B., Kinzler, K.W., and Vogelstein, B., eds.) 8th ed., Vol. 4, pp. 5313-5329, McGraw-Hill, New York, NY
    • (2001) The Metabolic and Molecular Basis of Inherited Disease , vol.4 , pp. 5313-5329
    • Whyte, M.P.1
  • 5
    • 0034113511 scopus 로고    scopus 로고
    • Hypophosphatasia: The mutations in the tissue-nonspecific alkaline phosphatase gene
    • Mornet, E. (2000) Hypophosphatasia: The mutations in the tissue-nonspecific alkaline phosphatase gene. Hum. Mutat. 15, 309-315
    • (2000) Hum. Mutat. , vol.15 , pp. 309-315
    • Mornet, E.1
  • 6
    • 0029115393 scopus 로고
    • Mice lacking tissue non-specific alkaline phosphatase die from seizures due to defective metabolism of vitamin B-6
    • Waymire, K.G., Mahuren, J.D., Jaje, J.M., Guilarte, T.R., Coburn, S.P., and Macgregor, G.R. (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
  • 7
    • 1842409589 scopus 로고    scopus 로고
    • Inactivation of two mouse alkaline phosphatase genes and establishment of a model of infantile hypophosphatasia
    • Narisawa, S., Frohlander, N., and Millán, J.L. (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    Millán, J.L.3
  • 9
    • 0000901269 scopus 로고
    • Mechanisms of calcification: Role of collagen, polyphosphates, and phosphatase
    • Fleisch, H. and Neuman, W.F. (1961) Mechanisms of calcification: role of collagen, polyphosphates, and phosphatase. Amer. J. Physiol. 200, 94-1300
    • (1961) Amer. J. Physiol. , vol.200 , pp. 94-1300
    • Fleisch, H.1    Neuman, W.F.2
  • 10
    • 0037047051 scopus 로고    scopus 로고
    • Tissue-nonspecific alkaline phosphatase and plasma cell membrane glycoprotein-1 are central antagonistic regulators of bone mineralization
    • Hessle, L., Johnson, K.A., Anderson, H.C., Narisawa, S., Sali, A., Goding, J.W., Terkeltaub, R., and Millán, J.L. (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    Millán, J.L.8
  • 11
    • 0035903096 scopus 로고    scopus 로고
    • Structural evidence for a functional role of human tissue nonspecific alkaline phosphatase in bone mineralization
    • Mornet, E., Stura, E., Lia-Baldin, A-S., Stigbrand, T., Menez, A., and Le Du, M-H. (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-Baldin, A.-S.3    Stigbrand, T.4    Menez, A.5    Le Du, M.-H.6
  • 12
    • 0035937857 scopus 로고    scopus 로고
    • Crystal structure of alkaline phosphatase from human placenta at 1.8 Å resolution
    • Le Du, M.H., Stigbrand, T., Taussig, M.J., Menez, A., and Stura, E.A. (2001) Crystal structure of alkaline phosphatase from human placenta at 1.8 Å resolution. 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
  • 13
    • 0032604016 scopus 로고    scopus 로고
    • Characterization of eleven novel mutations (M45L, R119H, 544delG, G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with severe hypophosphatasia
    • Taillandier, A., Zurutuza, L., Muller, F., Simon-Bouy, B., Serre, J.L., Bird, L., Brenner, R., Boute, O., Cousin, J., Gillard, D., Heidemann, P.H., Steinmann, B., Wallot, M., and Mornet, E (1999) Characterization of eleven novel mutations (M45L, R119H, 544delG, G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with severe hypophosphatasia. Hum. Mutat. 13, 171-172
    • (1999) Hum. Mutat. , vol.13 , pp. 171-172
    • Taillandier, A.1    Zurutuza, L.2    Muller, F.3    Simon-Bouy, B.4    Serre, J.L.5    Bird, L.6    Brenner, R.7    Boute, O.8    Cousin, J.9    Gillard, D.10    Heidemann, P.H.11    Steinmann, B.12    Wallot, M.13    Mornet, E.14
  • 17
    • 0036471397 scopus 로고    scopus 로고
    • 153→Asp substitution, a cause of perinatal hypophosphatasia
    • 153→Asp substitution, a cause of perinatal hypophosphatasia. Biochem. J. 361, 473-480
    • (2002) Biochem. J. , vol.361 , pp. 473-480
    • Ito, M.1    Amizuka, N.2    Ozawa, H.3    Oda, K.4
  • 18
    • 0032706573 scopus 로고    scopus 로고
    • A general method for rapid purification of soluble versions of glycosylphosphatidylinositol-anchored proteins expressed in insect cells: An application for human tissue-nonspecific alkaline phosphatase
    • Oda, K., Amaya, Y., Fukushi-Irie, M., Kinameri, Y., Ohsuye, K., Kubota, I., Fujimura, S., and Kobayashi, J. (1999) A general method for rapid purification of soluble versions of glycosylphosphatidylinositol-anchored proteins expressed in insect cells: An application for human tissue-nonspecific alkaline phosphatase. J. Biochem. 126, 694-699
    • (1999) J. Biochem. , vol.126 , pp. 694-699
    • Oda, K.1    Amaya, Y.2    Fukushi-Irie, M.3    Kinameri, Y.4    Ohsuye, K.5    Kubota, I.6    Fujimura, S.7    Kobayashi, J.8
  • 19
    • 0019328958 scopus 로고
    • Role of phosphatidylinositol in attachment of alkaline phosphatase to membranes
    • Low, M.G. and Zilversmit, D.B. (1980) Role of phosphatidylinositol in attachment of alkaline phosphatase to membranes. Biochemistry 19, 3913-3918
    • (1980) Biochemistry , vol.19 , pp. 3913-3918
    • Low, M.G.1    Zilversmit, D.B.2
  • 21
    • 0023696449 scopus 로고
    • Structure of the human liver/bone/kidney alkaline phosphatase gene
    • Weiss, M.J., Ray, K., Henthorn, P.S., Lamb, B., Kadesch, T., and Harris, H. (1988) Structure of the human liver/bone/kidney alkaline phosphatase gene. J. Biol. Chem. 263, 12002-12010
    • (1988) J. Biol. Chem. , vol.263 , pp. 12002-12010
    • Weiss, M.J.1    Ray, K.2    Henthorn, P.S.3    Lamb, B.4    Kadesch, T.5    Harris, H.6
  • 24
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality-control in the secretory pathway
    • Ellgaard, L., Molinari, M., and Helenius, A. (1999) Setting the standards: quality-control in the secretory pathway. Science 286, 1882-1888
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 25
    • 0033208984 scopus 로고    scopus 로고
    • ER protein quality control and proteasome-mediated protein degradation
    • Brodsky, J.L. and McCracken, A.A. (1999) ER protein quality control and proteasome-mediated protein degradation. Semin. Cell Dev. Biol. 10, 507-513
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 507-513
    • Brodsky, J.L.1    McCracken, A.A.2
  • 26
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B., Ye, Y., and Rapoport, T.A. (2002) Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol. 3, 246-255
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 27
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays, N.W., Gardner, R.G., Seelig, L.P., Joaziero, C.A., and Hampton, R.Y. (2001) Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat. Cell Biol. 3, 24-29
    • (2001) Nat. Cell Biol. , vol.3 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3    Joaziero, C.A.4    Hampton, R.Y.5
  • 29
    • 0037043340 scopus 로고    scopus 로고
    • An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport
    • Haynes, C.M., Caldwell, S., and Cooper, A.A. (2002) An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. J. Cell Biol. 158, 91-101
    • (2002) J. Cell Biol. , vol.158 , pp. 91-101
    • Haynes, C.M.1    Caldwell, S.2    Cooper, A.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.