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Volumn 270, Issue 6, 2003, Pages 1076-1088

Human acid sphingomyelinase: Assignment of the disulfide bond pattern

Author keywords

Disulfide bonds; Enzymatic and chemical cleavage; Human acid sphingomyelinase; MALDI MS; PSD

Indexed keywords

CERAMIDE; PHOSPHORYLCHOLINE; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE; TRYPSIN;

EID: 0344643423     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03435.x     Document Type: Article
Times cited : (43)

References (27)
  • 1
    • 0001745899 scopus 로고
    • Niemann-Pick disease types A and B: Acid sphingomyelinase deficiencies
    • Scriver, C.R., Beaudet, A.L., Sly, W.S. & Valle, D., eds. McGraw Hill, New York
    • Schuchman, E.H. & Desnick, R.J. (1995) Niemann-Pick disease types A and B: Acid sphingomyelinase deficiencies. In The Metabolic and Molecular Bases of Inherited Disease, 7th edn. (Scriver, C.R., Beaudet, A.L., Sly, W.S. & Valle, D., eds), pp. 2601-2624. McGraw Hill, New York.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease, 7th Edn. , pp. 2601-2624
    • Schuchman, E.H.1    Desnick, R.J.2
  • 3
    • 0024423426 scopus 로고
    • Isolation of cDNA clones encoding human acid sphingomyelinase: Occurrence of alternatively processed transcripts
    • Quintern, L.E., Schuchman, E.H., Levran, O., Suchi, M., Ferlinz, K., Reinke, H., Sandhoff, K. & Desnick, R.J. (1989) Isolation of cDNA clones encoding human acid sphingomyelinase: occurrence of alternatively processed transcripts. EMBO J. 8, 2469-2473.
    • (1989) EMBO J. , vol.8 , pp. 2469-2473
    • Quintern, L.E.1    Schuchman, E.H.2    Levran, O.3    Suchi, M.4    Ferlinz, K.5    Reinke, H.6    Sandhoff, K.7    Desnick, R.J.8
  • 4
    • 0025819971 scopus 로고
    • Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs
    • Schuchman, E.H., Suchi, M., Takahashi, T., Sandhoff, K. & Desnick, R.J. (1991) Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs. J. Biol. Chem. 266, 8531-8539.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8531-8539
    • Schuchman, E.H.1    Suchi, M.2    Takahashi, T.3    Sandhoff, K.4    Desnick, R.J.5
  • 5
    • 0027984782 scopus 로고
    • Processing of human acid sphingomyelinase in normal and I-cell fibroblasts
    • Hurwitz, R., Ferlinz, K, Vielhaber, G. & Sandhoff, K. (1994) Processing of human acid sphingomyelinase in normal and I-cell fibroblasts. J. Biol. Chem. 269, 5440-5445.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5440-5445
    • Hurwitz, R.1    Ferlinz, K.2    Vielhaber, G.3    Sandhoff, K.4
  • 6
    • 0030590887 scopus 로고    scopus 로고
    • Purification of acid sphingomyelinase from human placenta: Characterization and N-terminal sequence
    • Lansmann, S., Ferlinz, K., Hurwitz, R., Bartelsen, O., Glombitza, G. & Sandhoff, K. (1996) Purification of acid sphingomyelinase from human placenta: Characterization and N-terminal sequence. FEBS Lett. 399, 227-231.
    • (1996) FEBS Lett. , vol.399 , pp. 227-231
    • Lansmann, S.1    Ferlinz, K.2    Hurwitz, R.3    Bartelsen, O.4    Glombitza, G.5    Sandhoff, K.6
  • 7
    • 0031020869 scopus 로고    scopus 로고
    • Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site directed mutagenesis
    • Ferlinz, K., Hurwitz, R., Mozcall, H., Lansmann, S., Schuchman, E.A. & Sandhoff, K. (1997) Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site directed mutagenesis. Eur. J. Biochem. 243, 511-517.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 511-517
    • Ferlinz, K.1    Hurwitz, R.2    Mozcall, H.3    Lansmann, S.4    Schuchman, E.A.5    Sandhoff, K.6
  • 8
    • 0029996139 scopus 로고    scopus 로고
    • Signal transduction through lipid second messengers
    • Spiegel, S., Foster, D. & Kolesnick, R. (1996) Signal transduction through lipid second messengers. Curr. Opin. Cell Biol. 8, 159-167.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 159-167
    • Spiegel, S.1    Foster, D.2    Kolesnick, R.3
  • 9
    • 0030448021 scopus 로고    scopus 로고
    • Functions of ceramide in coordinating cellular responses to stress
    • Hannun, Y.A. (1996) Functions of ceramide in coordinating cellular responses to stress. Science 274, 1855-1859.
    • (1996) Science , vol.274 , pp. 1855-1859
    • Hannun, Y.A.1
  • 10
    • 0034738011 scopus 로고    scopus 로고
    • Physiology and pathophysiology of sphingolipid metabolism and signaling
    • Huwiler, A., Kolter, T., Pfeilschifter, J. & Sandhoff, K. (2000) Physiology and pathophysiology of sphingolipid metabolism and signaling. Biochim. Biophys. Acta 1485, 63-99.
    • (2000) Biochim. Biophys. Acta , vol.1485 , pp. 63-99
    • Huwiler, A.1    Kolter, T.2    Pfeilschifter, J.3    Sandhoff, K.4
  • 12
    • 0028275240 scopus 로고
    • Sphingolipid activator protein (sap-D) stimulates the lysosomal degradation of ceramide in vivo
    • Klein, A., Henseler, M., Klein, C., Suzuki, K., Harzer, K. & Sandhoff, K. (1994) Sphingolipid activator protein (sap-D) stimulates the lysosomal degradation of ceramide in vivo. Biochem. Biophys. Res. Com. 200, 1440-1448.
    • (1994) Biochem. Biophys. Res. Com. , vol.200 , pp. 1440-1448
    • Klein, A.1    Henseler, M.2    Klein, C.3    Suzuki, K.4    Harzer, K.5    Sandhoff, K.6
  • 13
    • 0028353499 scopus 로고
    • Acid sphingomyelinase posesses a domain homologous to its activator proteins: Saposins B and D
    • Ponting, C.P. (1994) Acid sphingomyelinase posesses a domain homologous to its activator proteins: saposins B and D. Protein Sci. 3, 359-361.
    • (1994) Protein Sci. , vol.3 , pp. 359-361
    • Ponting, C.P.1
  • 16
    • 0344701035 scopus 로고    scopus 로고
    • Expression of recombinant human acid sphingomyelinase in insect Sf21 cells: Purification, processing and enzymatic characterization
    • Bartelsen, O., Lansmann, S., Nettersheim, M., Lemm, T., Ferlinz, K. & Sandhoff, K (1998) Expression of recombinant human acid sphingomyelinase in insect Sf21 cells: purification, processing and enzymatic characterization. J. Biotechnol. 63, 29-40.
    • (1998) J. Biotechnol. , vol.63 , pp. 29-40
    • Bartelsen, O.1    Lansmann, S.2    Nettersheim, M.3    Lemm, T.4    Ferlinz, K.5    Sandhoff, K.6
  • 18
    • 0028544044 scopus 로고
    • Prompt fragmentation of disulfide-linked peptides during matrix-assisted laser desorption ionization mass spectrometry
    • Patterson, S.D. & Katta, V. (1994) Prompt fragmentation of disulfide-linked peptides during matrix-assisted laser desorption ionization mass spectrometry. Anal. Chem. 66, 3727-3732.
    • (1994) Anal. Chem. , vol.66 , pp. 3727-3732
    • Patterson, S.D.1    Katta, V.2
  • 19
    • 0023785840 scopus 로고
    • Oligosaccharide structure and amino acid sequence of the major glycopeptides of mature human beta-hexosaminidase
    • O'Dowd, B.F., Cumming, D.A., Gravel, R.A. & Mahuran, D. (1988) Oligosaccharide structure and amino acid sequence of the major glycopeptides of mature human beta-hexosaminidase. Biochemistry 27, 5216-5226.
    • (1988) Biochemistry , vol.27 , pp. 5216-5226
    • O'Dowd, B.F.1    Cumming, D.A.2    Gravel, R.A.3    Mahuran, D.4
  • 20
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R. & Kornfeld, S. (1985) Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 21
    • 0031050298 scopus 로고    scopus 로고
    • A novel methodology for assignment of disulfide bond pairings in proteins
    • Wu, J. & Watson, J.T. (1997) A novel methodology for assignment of disulfide bond pairings in proteins. Protein Sci. 6, 391-398.
    • (1997) Protein Sci. , vol.6 , pp. 391-398
    • Wu, J.1    Watson, J.T.2
  • 22
    • 0039703311 scopus 로고    scopus 로고
    • Complete localization of disulfide bonds in GM2 activator protein
    • Schuette, C.G., Lemm, T., Glombitza, G.J. & Sandhoff, K. (1998) Complete localization of disulfide bonds in GM2 activator protein. Protein Sci. 7, 1039-1045.
    • (1998) Protein Sci. , vol.7 , pp. 1039-1045
    • Schuette, C.G.1    Lemm, T.2    Glombitza, G.J.3    Sandhoff, K.4
  • 23
    • 43949148860 scopus 로고
    • Sequencing of peptides in a time-of-flight mass spectrometer: Evaluation of post source decay following matrix-assisted laser desorption ionization (MALDI)
    • Kaufmann, R., Hirsch, D. & Sprengler, B. (1994) Sequencing of peptides in a time-of-flight mass spectrometer: Evaluation of post source decay following matrix-assisted laser desorption ionization (MALDI). Int. J. Mass Spectrom. Ion Proc. 86, 137-154.
    • (1994) Int. J. Mass Spectrom. Ion Proc. , vol.86 , pp. 137-154
    • Kaufmann, R.1    Hirsch, D.2    Sprengler, B.3
  • 24
    • 0032974462 scopus 로고    scopus 로고
    • Characterization of human acid sphingo-myelinase purified from the media of overexpressing Chinese hamster ovary cells
    • He, X., Miranda, S.R., Xiong, X., Dagan, A., Gatt, S. & Schuchman, E.H. (1999) Characterization of human acid sphingo-myelinase purified from the media of overexpressing Chinese hamster ovary cells. Biochim. Biophys. Acta 1432, 251-264.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 251-264
    • He, X.1    Miranda, S.R.2    Xiong, X.3    Dagan, A.4    Gatt, S.5    Schuchman, E.H.6
  • 25
    • 0027320393 scopus 로고
    • Cloning of a human acid sphingomyehnase cDNA with a new mutation that renders the enzyme inactive
    • Ida, H., Rennert, O.M., Eto, Y. & Chan, W.Y. (1993) Cloning of a human acid sphingomyehnase cDNA with a new mutation that renders the enzyme inactive. J. Biochem. 114, 15-20.
    • (1993) J. Biochem. , vol.114 , pp. 15-20
    • Ida, H.1    Rennert, O.M.2    Eto, Y.3    Chan, W.Y.4
  • 26
    • 0034655952 scopus 로고    scopus 로고
    • Disulfide connectivity in cerebroside sulfate activator is not necessary for biological activity or alpha-helical content but is necessary for trypsin resistance and strong ligand binding
    • Faull, K.F., Higginson, J., Waring, A.J., Johnson, J., To, T., Whitelegge, J.P., Stevens, R.L., Fluharty, C.B. & Fluharty, A.L. (2000) Disulfide connectivity in cerebroside sulfate activator is not necessary for biological activity or alpha-helical content but is necessary for trypsin resistance and strong ligand binding. Arch. Biochem. Biophys. 376, 266-274.
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 266-274
    • Faull, K.F.1    Higginson, J.2    Waring, A.J.3    Johnson, J.4    To, T.5    Whitelegge, J.P.6    Stevens, R.L.7    Fluharty, C.B.8    Fluharty, A.L.9
  • 27
    • 0028468309 scopus 로고
    • The tricyclic antidepressant desipramine causes proteolytic degradation of lysosomal sphingomyelinase in human fibroblasts
    • Hurwitz, R., Ferlinz, K. & Sandhoff, K. (1994) The tricyclic antidepressant desipramine causes proteolytic degradation of lysosomal sphingomyelinase in human fibroblasts. Biol. Chem. Hoppe Seyler 375, 447-450.
    • (1994) Biol. Chem. Hoppe Seyler , vol.375 , pp. 447-450
    • Hurwitz, R.1    Ferlinz, K.2    Sandhoff, K.3


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