메뉴 건너뛰기




Volumn 79, Issue 3, 2000, Pages 208-217

CALNUC (nucleobindin) is localized in the Golgi apparatus in insect cells

Author keywords

CALNUC; Golgi; Insect; Nucleobindin; Sf21 cell

Indexed keywords

COMPLEMENTARY DNA; MEMBRANE PROTEIN; MONOCLONAL ANTIBODY; PEROXIDASE; PROTEINASE K;

EID: 18844475151     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1078/S0171-9335(04)70024-2     Document Type: Article
Times cited : (22)

References (36)
  • 1
    • 0030857326 scopus 로고    scopus 로고
    • More than silk and honey - Or, can insect cells serve in the production of therapeutic glycoproteins?
    • Altmann, F. (1997): More than silk and honey - or, can insect cells serve in the production of therapeutic glycoproteins? Glycoconj. J. 14, 643-646.
    • (1997) Glycoconj. J. , vol.14 , pp. 643-646
    • Altmann, F.1
  • 2
    • 0028909554 scopus 로고
    • Processing of asparagine-linked oligosaccharides in insect cells: Evidence for α-mannosidase II
    • Altmann, F., März, L. (1995): Processing of asparagine-linked oligosaccharides in insect cells: evidence for α-mannosidase II. Glycoconj. J. 12, 150-155.
    • (1995) Glycoconj. J. , vol.12 , pp. 150-155
    • Altmann, F.1    März, L.2
  • 3
    • 0029085691 scopus 로고
    • Insect cells contain an unusual, membrane-bound ß-N-acetylglucosaminidase probably involved in the processing of protein N-glycans
    • Altmann, F., Schwihla, H., Staudacher, E., Glössl, J., März, L. (1995): Insect cells contain an unusual, membrane-bound ß-N-acetylglucosaminidase probably involved in the processing of protein N-glycans. J. Biol. Chem. 270, 17344-17349.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17344-17349
    • Altmann, F.1    Schwihla, H.2    Staudacher, E.3    Glössl, J.4    März, L.5
  • 4
    • 0028485781 scopus 로고
    • Human protein NEFA, a novel DNa binding/EF-hand/leucine zipper protein. Molecular cloning and sequence analysis of the cDNA, isolation and characterization of the protein
    • Barnikol-Watanabe, S., Groß, N. A., Götz, H., Henkel, T., Karabinos, A., Kratzin, H., Barnikol, H. U., Hilschmann, N. (1994): Human protein NEFA, a novel DNA binding/EF-hand/leucine zipper protein. Molecular cloning and sequence analysis of the cDNA, isolation and characterization of the protein. Biol. Chem. Hoppe Seyler 375, 497-512.
    • (1994) Biol. Chem. Hoppe Seyler , vol.375 , pp. 497-512
    • Barnikol-Watanabe, S.1    Groß, N.A.2    Götz, H.3    Henkel, T.4    Karabinos, A.5    Kratzin, H.6    Barnikol, H.U.7    Hilschmann, N.8
  • 5
    • 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. (1976): A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0026335806 scopus 로고
    • Calcium sequestration in the Golgi apparatus of cultured mammalian cells revealed by laser scanning confocal microscopy and ion microscopy
    • Chandra, S., Kable, E. P. W., Morrison, G. H., Webb, W. W. (1991): Calcium sequestration in the Golgi apparatus of cultured mammalian cells revealed by laser scanning confocal microscopy and ion microscopy. J. Cell Sci. 100, 747-752.
    • (1991) J. Cell Sci. , vol.100 , pp. 747-752
    • Chandra, S.1    Kable, E.P.W.2    Morrison, G.H.3    Webb, W.W.4
  • 7
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • Cleveland, D. W., Fischer, S. G., Kirschner, M. W., Laemmli, U. K. (1977): Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252, 1102-1106.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1102-1106
    • Cleveland, D.W.1    Fischer, S.G.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 8
    • 0027055402 scopus 로고
    • Adhesion of Golgi cisternae by proteinaceous interactions: Intercisternal bridges as putative adhesive structures
    • Cluett, E. B., Brown, W. J. (1992): Adhesion of Golgi cisternae by proteinaceous interactions: intercisternal bridges as putative adhesive structures. J. Cell Sci. 103, 773-784.
    • (1992) J. Cell Sci. , vol.103 , pp. 773-784
    • Cluett, E.B.1    Brown, W.J.2
  • 9
    • 0020071663 scopus 로고
    • Hepatic Golgi fractions resolved into membrane and content subtractions
    • Howell, K. E., Palade, G. E. (1982): Hepatic Golgi fractions resolved into membrane and content subtractions. J. Cell Biol. 92, 822-832.
    • (1982) J. Cell Biol. , vol.92 , pp. 822-832
    • Howell, K.E.1    Palade, G.E.2
  • 10
    • 0022541887 scopus 로고
    • An established MRL/Mp-lpr/lpr cell line with null cell properties produces a B cell differentiation factor(s) that promotes anti-single-stranded DNA antibody production in MRL spleen cell culture
    • Kanai, Y., Katagiri, T., Mori, S., Kubota, T. (1986): An established MRL/Mp-lpr/lpr cell line with null cell properties produces a B cell differentiation factor(s) that promotes anti-single-stranded DNA antibody production in MRL spleen cell culture. Int. Arch. Allergy Appl. Immunol. 81, 92-94.
    • (1986) Int. Arch. Allergy Appl. Immunol. , vol.81 , pp. 92-94
    • Kanai, Y.1    Katagiri, T.2    Mori, S.3    Kubota, T.4
  • 13
    • 0028123669 scopus 로고
    • A protein-specific monoclonal antibody to rat liver ß1 → 4 galactosyltransferase and its application to immunohistochemistry
    • Kawano, J., Ide, S., Oinuma, T., Suganuma, T. (1994): A protein-specific monoclonal antibody to rat liver ß1 → 4 galactosyltransferase and its application to immunohistochemistry. J. Histochem. Cytochem. 42, 363-369.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 363-369
    • Kawano, J.1    Ide, S.2    Oinuma, T.3    Suganuma, T.4
  • 14
    • 0026523755 scopus 로고
    • Characterization of ß1 → 4 galactosyltransferase purified from rat liver microsomes
    • Kawano, J., Oinuma, T., Nakayama, T., Suganuma, T. (1992): Characterization of ß1 → 4 galactosyltransferase purified from rat liver microsomes. J. Biochem. 111, 568-572.
    • (1992) J. Biochem. , vol.111 , pp. 568-572
    • Kawano, J.1    Oinuma, T.2    Nakayama, T.3    Suganuma, T.4
  • 15
    • 0031427672 scopus 로고    scopus 로고
    • Regional distribution of ß1 → 4 galactosyltransferase in rat epididymis
    • Kawano, J., Ide, S., Oinuma, T., Suganuma, T. (1997): Regional distribution of ß1 → 4 galactosyltransferase in rat epididymis. Acta Histochem. Cytochem. 30, 491-495.
    • (1997) Acta Histochem. Cytochem. , vol.30 , pp. 491-495
    • Kawano, J.1    Ide, S.2    Oinuma, T.3    Suganuma, T.4
  • 16
    • 0033594080 scopus 로고    scopus 로고
    • Golgi structure in three dimensions: Functional insights from the normal rat kidney cell
    • Ladinsky, M. S., Mastronarde, D. N., McIntosh, J. R., Howell, K. E., Staehelin, L. A. (1999): Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J. Cell Biol. 144, 1135-1149.
    • (1999) J. Cell Biol. , vol.144 , pp. 1135-1149
    • Ladinsky, M.S.1    Mastronarde, D.N.2    McIntosh, J.R.3    Howell, K.E.4    Staehelin, L.A.5
  • 17
    • 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
    • 0021379023 scopus 로고
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis. J. Biochem. 95, 511-519.
    • (1984) J. Biochem. , vol.95 , pp. 511-519
    • Maruyama, K.1    Mikawa, T.2    Ebashi, S.3
  • 22
    • 0028357838 scopus 로고
    • Calcium-binding activity of nucleobindin mediated by an EF hand moiety
    • Miura, K., Kurosawa, Y., Kanai, Y. (1994): Calcium-binding activity of nucleobindin mediated by an EF hand moiety. Biochem. Biophys. Res. Commun. 199, 1388-1393.
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 1388-1393
    • Miura, K.1    Kurosawa, Y.2    Kanai, Y.3
  • 23
    • 0026657729 scopus 로고
    • Molecular cloning of nucleobindin, a novel DNA-binding protein that contains both a signal peptide and a leucine zipper structure
    • Miura, K., Titani, K., Kurosawa, Y., Kanai, Y. (1992): Molecular cloning of nucleobindin, a novel DNA-binding protein that contains both a signal peptide and a leucine zipper structure. Biochem. Biophys. Res. Commun. 187, 375-380.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 375-380
    • Miura, K.1    Titani, K.2    Kurosawa, Y.3    Kanai, Y.4
  • 24
    • 0021813042 scopus 로고
    • Characterization of a monoclonal antibody to hog thyroid peroxidase and its use for immunohistochemical localization of the peroxidase in the thyroid gland
    • Nakagawa, H., Kotani, T., Ohtaki, S., Kawano, J., Aikawa, E., Imagawa, M., Hashida, S., Ishikawa, E. (1985): Characterization of a monoclonal antibody to hog thyroid peroxidase and its use for immunohistochemical localization of the peroxidase in the thyroid gland. J. Biochem. 97, 1709-1718.
    • (1985) J. Biochem. , vol.97 , pp. 1709-1718
    • Nakagawa, H.1    Kotani, T.2    Ohtaki, S.3    Kawano, J.4    Aikawa, E.5    Imagawa, M.6    Hashida, S.7    Ishikawa, E.8
  • 25
    • 0030982434 scopus 로고    scopus 로고
    • High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells
    • Pezzati, R., Bossi, M., Podini, P., Meldolesi, J., Grohovaz, F. (1997): High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells. Mol. Biol. Cell 8, 1501-1512.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1501-1512
    • Pezzati, R.1    Bossi, M.2    Podini, P.3    Meldolesi, J.4    Grohovaz, F.5
  • 26
    • 0032530396 scopus 로고    scopus 로고
    • 2+ store, with functional properties distinct from those of the endoplasmic reticulum
    • 2+ store, with functional properties distinct from those of the endoplasmic reticulum. EMBO J. 17, 5298-5308.
    • (1998) EMBO J. , vol.17 , pp. 5298-5308
    • Pinton, P.1    Pozzan, T.2    Rizzuto, R.3
  • 27
    • 0030700315 scopus 로고    scopus 로고
    • Baculoviruses as expression vectors
    • Possee, R. D. (1997): Baculoviruses as expression vectors. Curr. Opin. Biotechnol. 8, 569-572.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 569-572
    • Possee, R.D.1
  • 28
    • 0030747549 scopus 로고    scopus 로고
    • Purification and properties of α-mannosidase II from Golgi-like membranes of baculovirus-infected Spodoptera frugiperda (IPLB-SF-21AE) cells
    • Ren, J., Castellino, F. J., Bretthauer, R. K. (1997): Purification and properties of α-mannosidase II from Golgi-like membranes of baculovirus-infected Spodoptera frugiperda (IPLB-SF-21AE) cells. Biochem. J. 324, 951-956.
    • (1997) Biochem. J. , vol.324 , pp. 951-956
    • Ren, J.1    Castellino, F.J.2    Bretthauer, R.K.3
  • 29
    • 0030731272 scopus 로고    scopus 로고
    • Cholesterol-independent targeting of Golgi membrane proteins in insect cells
    • Rolls, M. M., Marquardt, M. T., Kielian, M., Machamer, C. E. (1997): Cholesterol-independent targeting of Golgi membrane proteins in insect cells. Mol. Biol. Cell 8, 2111-2118.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2111-2118
    • Rolls, M.M.1    Marquardt, M.T.2    Kielian, M.3    Machamer, C.E.4
  • 30
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., von Jagow, G. (1987): Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 31
    • 0025760015 scopus 로고
    • The isolated ER-Golgi intermediate compartment exhibits properties that are different from ER and cis-Golgi
    • Schweizer, A., Matter, K., Ketcham, C. M., Hauri, H.-P. (1991): The isolated ER-Golgi intermediate compartment exhibits properties that are different from ER and cis-Golgi. J. Cell Biol. 113, 45-54.
    • (1991) J. Cell Biol. , vol.113 , pp. 45-54
    • Schweizer, A.1    Matter, K.2    Ketcham, C.M.3    Hauri, H.-P.4
  • 32
    • 0023783855 scopus 로고
    • A simple in situ cyanogen bromide cleavage method to obtain internal amino acid sequence of proteins electroblotted to polyvinyldifluoride membranes
    • Scott, M. G., Crimmins, D. L., McCourt, D. W., Tarrand, J. J., Eyerman, M. C., Nahm, M. H. (1988): A simple in situ cyanogen bromide cleavage method to obtain internal amino acid sequence of proteins electroblotted to polyvinyldifluoride membranes. Biochem. Biophys. Res. Commun. 155, 1353-1359.
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 1353-1359
    • Scott, M.G.1    Crimmins, D.L.2    McCourt, D.W.3    Tarrand, J.J.4    Eyerman, M.C.5    Nahm, M.H.6
  • 33
    • 0006894539 scopus 로고
    • Rat-kidney lysosomes: Isolation and properties
    • Shibko, S., Tappel, A. L. (1965): Rat-kidney lysosomes: isolation and properties. Biochem. J. 95, 731-741.
    • (1965) Biochem. J. , vol.95 , pp. 731-741
    • Shibko, S.1    Tappel, A.L.2
  • 34
    • 0031460148 scopus 로고    scopus 로고
    • The mechanism of Golgi segregation during mitosis is cell type-specific
    • Stanley, H., Botas, J., Malhotra, V. (1997): The mechanism of Golgi segregation during mitosis is cell type-specific. Proc. Natl. Acad. Sci. USA 94, 14467-14470.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14467-14470
    • Stanley, H.1    Botas, J.2    Malhotra, V.3
  • 36
    • 0028965878 scopus 로고
    • Isolation, characterization, and primary structure of a calcium-binding 63-kDa bone protein
    • Wendel, M., Sommarin, Y., Bergman, T., Heinegård, D. (1995): Isolation, characterization, and primary structure of a calcium-binding 63-kDa bone protein. J. Biol. Chem. 270, 6125-6133.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6125-6133
    • Wendel, M.1    Sommarin, Y.2    Bergman, T.3    Heinegård, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.