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Volumn 143, Issue 1, 2008, Pages 117-122

Identification and characterization of cathepsin D in a highly purified sialidase from starfish A. pectinifera

Author keywords

Asterina pectinifera; Cathepsin D; Enzymatic properties; Ovary of starfish; Sialidase

Indexed keywords

CATHEPSIN D; PEPSTATIN; SIALIDASE;

EID: 38849158474     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm199     Document Type: Article
Times cited : (3)

References (29)
  • 1
    • 38849112208 scopus 로고    scopus 로고
    • Rosenberg, A. (1995) Biochemistry and role of sialic acids in Biology of the Sialic Acids (Schauer, R., Kelm, S., Reuter, G., Roggentin, P., and Shaw, L., eds) pp. 31, Plenum Press, New York and London
    • Rosenberg, A. (1995) Biochemistry and role of sialic acids in Biology of the Sialic Acids (Schauer, R., Kelm, S., Reuter, G., Roggentin, P., and Shaw, L., eds) pp. 31, Plenum Press, New York and London
  • 2
    • 38849200721 scopus 로고    scopus 로고
    • Rosenberg, A. (1995) Biochemistry and function of Sialidases in Biology of the Sialic Acids (Saito, M., and Yu, R.K., eds) pp. 261-277, Plenum Press, New York and London
    • Rosenberg, A. (1995) Biochemistry and function of Sialidases in Biology of the Sialic Acids (Saito, M., and Yu, R.K., eds) pp. 261-277, Plenum Press, New York and London
  • 3
    • 38849194999 scopus 로고    scopus 로고
    • Schauer, R. (1982) Introduction in Sialic Acids-Chemistry, Metabolism and Function (Schauer, R. and Vliegenthart, J.F.G., eds) pp. 1-3, Springer, New York.
    • Schauer, R. (1982) Introduction in Sialic Acids-Chemistry, Metabolism and Function (Schauer, R. and Vliegenthart, J.F.G., eds) pp. 1-3, Springer, New York.
  • 4
    • 0026619682 scopus 로고
    • Bacterial sialidases-roles in pathogenicity and nutrition
    • Corfield, T. (1992) Bacterial sialidases-roles in pathogenicity and nutrition. Glycobiology 2, 509-521
    • (1992) Glycobiology , vol.2 , pp. 509-521
    • Corfield, T.1
  • 5
    • 0014939395 scopus 로고
    • Studies on the soluble and lysosomal neuraminidases of rat liver
    • Tulsiani, D.R. and Carubelli, R. (1970) Studies on the soluble and lysosomal neuraminidases of rat liver. J. Biol. Chem. 245, 1821-1827
    • (1970) J. Biol. Chem , vol.245 , pp. 1821-1827
    • Tulsiani, D.R.1    Carubelli, R.2
  • 6
    • 0021808696 scopus 로고
    • Purification and characterization of cytosolic sialidase from rat liver
    • Miyagi, T. and Tsuiki, S. (1985) Purification and characterization of cytosolic sialidase from rat liver. J. Biol. Chem. 260, 6710-6716
    • (1985) J. Biol. Chem , vol.260 , pp. 6710-6716
    • Miyagi, T.1    Tsuiki, S.2
  • 7
    • 0033582517 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides
    • Miyagi, T., Wada, T., Iwamatsu, A., Hata, K., Yoshikawa, Y., Tokuyama, S., and Sawada, M. (1999) Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides. J. Biol. Chem. 274, 5004-5011
    • (1999) J. Biol. Chem , vol.274 , pp. 5004-5011
    • Miyagi, T.1    Wada, T.2    Iwamatsu, A.3    Hata, K.4    Yoshikawa, Y.5    Tokuyama, S.6    Sawada, M.7
  • 8
    • 0021279238 scopus 로고
    • Rat-liver lysosomal sialidase. Solubilization, substrate specificity and comparison with the cytosolic sialidase
    • Miyagi, T. and Tsuiki, S. (1984) Rat-liver lysosomal sialidase. Solubilization, substrate specificity and comparison with the cytosolic sialidase. Eur. J. Biochem. 141, 75-81
    • (1984) Eur. J. Biochem , vol.141 , pp. 75-81
    • Miyagi, T.1    Tsuiki, S.2
  • 9
    • 18944385187 scopus 로고    scopus 로고
    • Differential expression of endogenous sialidases of human monocytes during cellular differentiation into macrophages
    • Stamatos, N.M., Liang, F., Nan, X., Landry, K., Cross, A.S., Wang, L.X., and Pshezhetsky, A.V. (2005) Differential expression of endogenous sialidases of human monocytes during cellular differentiation into macrophages. FEBS J. 272, 2545-2556
    • (2005) FEBS J , vol.272 , pp. 2545-2556
    • Stamatos, N.M.1    Liang, F.2    Nan, X.3    Landry, K.4    Cross, A.S.5    Wang, L.X.6    Pshezhetsky, A.V.7
  • 10
    • 0029920035 scopus 로고    scopus 로고
    • Involvement of an endogenous sialidase in skeletal muscle cell differentiation
    • Sato, K. and Miyagi, T. (1996) Involvement of an endogenous sialidase in skeletal muscle cell differentiation. Biochem. Biophys. Res. Commun. 221, 826-830
    • (1996) Biochem. Biophys. Res. Commun , vol.221 , pp. 826-830
    • Sato, K.1    Miyagi, T.2
  • 12
    • 0034326899 scopus 로고    scopus 로고
    • Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis
    • Bonten, E.J., Arts, W.F., Beck, M., Covanis, A., Donati, M.A., Parini, R., Zammarchi, E., and d'Azzo, A. (2000) Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis. Hum. Mol. Genet. 9, 2715-2725
    • (2000) Hum. Mol. Genet , vol.9 , pp. 2715-2725
    • Bonten, E.J.1    Arts, W.F.2    Beck, M.3    Covanis, A.4    Donati, M.A.5    Parini, R.6    Zammarchi, E.7    d'Azzo, A.8
  • 14
    • 0024495357 scopus 로고
    • Identification and in vitro reconstitution of lysosomal neuraminidase from human placenta
    • van der Horst, G.T., Galjart, N.J., d'Azzo, A., Galjaard, H., and Verheijen, F.W. (1989) Identification and in vitro reconstitution of lysosomal neuraminidase from human placenta. J. Biol. Chem. 264, 1317-1322
    • (1989) J. Biol. Chem , vol.264 , pp. 1317-1322
    • van der Horst, G.T.1    Galjart, N.J.2    d'Azzo, A.3    Galjaard, H.4    Verheijen, F.W.5
  • 15
    • 0021837357 scopus 로고
    • Human placental neuraminidase. Activation, stabilization and association with beta-galactosidase and its protective protein
    • Verheijen, F.W., Palmeri, S., Hoogeveen, A.T., and Galjaard, H. (1985) Human placental neuraminidase. Activation, stabilization and association with beta-galactosidase and its protective protein. Eur. J. Biochem. 149, 315-321
    • (1985) Eur. J. Biochem , vol.149 , pp. 315-321
    • Verheijen, F.W.1    Palmeri, S.2    Hoogeveen, A.T.3    Galjaard, H.4
  • 18
    • 0023783875 scopus 로고
    • Expression of cDNA encoding the human "protective protein" associated with lysosomal beta-galactosidase and neuraminidase: Homology to yeast proteases
    • Galjart, N.J., Gillemans, N., Harris, A., van der Horst, G.T., Verheijen, F.W., Galjaard, H., and d'Azzo, A. (1988) Expression of cDNA encoding the human "protective protein" associated with lysosomal beta-galactosidase and neuraminidase: homology to yeast proteases. Cell 54, 755-764
    • (1988) Cell , vol.54 , pp. 755-764
    • Galjart, N.J.1    Gillemans, N.2    Harris, A.3    van der Horst, G.T.4    Verheijen, F.W.5    Galjaard, H.6    d'Azzo, A.7
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0018421350 scopus 로고
    • Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl- alpha-D-N-acetylneuraminate) substrate
    • Potier, M., Mameli, L., Belisle, M., Dallaire, L., and Melancon, S.B. (1979) Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl- alpha-D-N-acetylneuraminate) substrate. Anal. Biochem. 94, 287-296
    • (1979) Anal. Biochem , vol.94 , pp. 287-296
    • Potier, M.1    Mameli, L.2    Belisle, M.3    Dallaire, L.4    Melancon, S.B.5
  • 22
    • 0032790483 scopus 로고    scopus 로고
    • Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin E and cathepsin D
    • Yasuda, Y., Kageyama, T., Akamine, A., Shibata, M., Kominami, E., Uchiyama, Y., and Yamamoto, K. (1999) Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin E and cathepsin D. J. Biochem. (Tokyo). 125, 1137-1143
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 1137-1143
    • Yasuda, Y.1    Kageyama, T.2    Akamine, A.3    Shibata, M.4    Kominami, E.5    Uchiyama, Y.6    Yamamoto, K.7
  • 24
    • 0030012760 scopus 로고    scopus 로고
    • Purification and characterization of tomatinase from Fusarium oxysporum f. sp. lycopersici
    • Lairini, K., Perez-Espinosa, A., Pineda, M., and Ruiz-Rubio, M. (1996) Purification and characterization of tomatinase from Fusarium oxysporum f. sp. lycopersici. Appl. Environ. Microbiol. 62, 1604-1609
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 1604-1609
    • Lairini, K.1    Perez-Espinosa, A.2    Pineda, M.3    Ruiz-Rubio, M.4
  • 25
    • 0024234582 scopus 로고
    • In vitro activation of neuraminidase in the [beta]-galactosidase-neuraminidase-protective protein complex by cathepsin C
    • D'Agrosa, R.M. and Callahan, J.W. (1988) In vitro activation of neuraminidase in the [beta]-galactosidase-neuraminidase-protective protein complex by cathepsin C. Biochem. Biophys. Res. Commun. 157, 770-775
    • (1988) Biochem. Biophys. Res. Commun , vol.157 , pp. 770-775
    • D'Agrosa, R.M.1    Callahan, J.W.2
  • 26
    • 0021048523 scopus 로고
    • Cathepsin D from human brain: Purification and multiple forms
    • Azaryan, A., Akopyan, T., and Buniatian, H. (1983) Cathepsin D from human brain: purification and multiple forms. Biomed. Biochim. Acta 42, 1237-1246
    • (1983) Biomed. Biochim. Acta , vol.42 , pp. 1237-1246
    • Azaryan, A.1    Akopyan, T.2    Buniatian, H.3
  • 27
    • 0018801568 scopus 로고
    • Cathepsin D isozymes from porcine spleens. Large scale purification and polypeptide chain arrangements
    • Huang, J.S., Huang, S.S., and Tang, J. (1979) Cathepsin D isozymes from porcine spleens. Large scale purification and polypeptide chain arrangements. J. Biol. Chem. 254, 11405-11417
    • (1979) J. Biol. Chem , vol.254 , pp. 11405-11417
    • Huang, J.S.1    Huang, S.S.2    Tang, J.3
  • 28
    • 0019604913 scopus 로고
    • Two-step affinity-chromatographic purification of cathepsin D from pig myometrium with high yield
    • Afting, E.G. and Recker, M.L. (1981) Two-step affinity-chromatographic purification of cathepsin D from pig myometrium with high yield. Biochem. J. 197, 519-522
    • (1981) Biochem. J , vol.197 , pp. 519-522
    • Afting, E.G.1    Recker, M.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.