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Volumn 17, Issue 9, 1998, Pages 771-777

Mouse cytochrome b561: cDNA cloning and expression in rat brain, mouse embryos, and human glioma cell lines

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMIDATING ENZYME; COMPLEMENTARY DNA; CYTOCHROME B5;

EID: 0031704569     PISSN: 10445498     EISSN: None     Source Type: Journal    
DOI: 10.1089/dna.1998.17.771     Document Type: Article
Times cited : (11)

References (27)
  • 1
    • 0023009792 scopus 로고
    • Evidence for an ascorbate shuttle for the transfer of reducing equivalents across chromaffin granule membranes
    • BEERS, M.F., JOHNSON, R.G., and SCARPA, A. (1986). Evidence for an ascorbate shuttle for the transfer of reducing equivalents across chromaffin granule membranes. J. Biol. Chem. 261, 2529-2535.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2529-2535
    • Beers, M.F.1    Johnson, R.G.2    Scarpa, A.3
  • 2
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • CHOMPCZYNSKI, P., and SACCHI, N. (1987). Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chompczynski, P.1    Sacchi, N.2
  • 3
    • 0344988568 scopus 로고
    • Ontogenic appearance and disappearance of tyrosine hydroxylase and catecholamines in the rat embryo
    • COCHARD, P., GOLDSTEIN, M., and BLACK, I.B. (1978). Ontogenic appearance and disappearance of tyrosine hydroxylase and catecholamines in the rat embryo. Proc. Natl. Acad. Sci. USA 75, 2986-2990.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2986-2990
    • Cochard, P.1    Goldstein, M.2    Black, I.B.3
  • 4
    • 0024423253 scopus 로고
    • Ascorbic acid within chromaffin granules: In situ kinetics of norepinephrine biosynthesis
    • DHARIWAL, K.R., WASHKO, P., HARTZELL, W.O., and LEVINE, M. (1989). Ascorbic acid within chromaffin granules: in situ kinetics of norepinephrine biosynthesis. J. Biol. Chem. 264, 15404-15409.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15404-15409
    • Dhariwal, K.R.1    Washko, P.2    Hartzell, W.O.3    Levine, M.4
  • 5
    • 0002578116 scopus 로고
    • The identification of helical segments in the polypeptide chain of bacteriorhodopsin
    • ENGELMAN, D.M., GOLDMAN, A., and STEITZ, T.A. (1981). The identification of helical segments in the polypeptide chain of bacteriorhodopsin. Methods Enzymol. 88, 81-88.
    • (1981) Methods Enzymol. , vol.88 , pp. 81-88
    • Engelman, D.M.1    Goldman, A.2    Steitz, T.A.3
  • 6
    • 0015214389 scopus 로고
    • Cytochrome b561 of the bovine adrenal chromaffin granules: A high potential b-type cytochrome
    • FLATMARK, T., and TERLAND, O. (1971). Cytochrome b561 of the bovine adrenal chromaffin granules: a high potential b-type cytochrome. Biochem. Biophys. Acta 253, 487-491.
    • (1971) Biochem. Biophys. Acta , vol.253 , pp. 487-491
    • Flatmark, T.1    Terland, O.2
  • 7
    • 0025885657 scopus 로고
    • Cytochrome b561, ascorbic acid, and transmembrane electron transfer
    • FLEMING, P.J., and KENT, U. (1991). Cytochrome b561, ascorbic acid, and transmembrane electron transfer. Am. J. Clin. Nutr. 54, 1173S-1178S.
    • (1991) Am. J. Clin. Nutr. , vol.54
    • Fleming, P.J.1    Kent, U.2
  • 8
    • 0026007190 scopus 로고
    • Activity of membranous dopamine beta monooxygenase within chromaffin granule ghosts
    • HUYGHE, B.G., and KLINMAN, J.P. (1991). Activity of membranous dopamine beta monooxygenase within chromaffin granule ghosts. J. Biol. Chem. 266, 11544-11550.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11544-11550
    • Huyghe, B.G.1    Klinman, J.P.2
  • 9
    • 0023655324 scopus 로고
    • Purified cytochrome b561 catalyzes transmembrane electron transfer for dopamine beta hydroxylase and peptidyl glycine alpha-amidating monooxygenase activities in reconstituted systems
    • KENT, U.M., and FLEMING, P.J. (1987). Purified cytochrome b561 catalyzes transmembrane electron transfer for dopamine beta hydroxylase and peptidyl glycine alpha-amidating monooxygenase activities in reconstituted systems. J. Biol. Chem. 262, 8174-8178.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8174-8178
    • Kent, U.M.1    Fleming, P.J.2
  • 10
    • 0025194169 scopus 로고
    • Cytochrome b561 is fatty acylated and oriented in the chromaffin granule membrane with its carboxy terminus cytoplasmically exposed
    • KENT, U.M., and FLEMING, P.J. (1990). Cytochrome b561 is fatty acylated and oriented in the chromaffin granule membrane with its carboxy terminus cytoplasmically exposed. J. Biol. Chem. 265, 16422-16427.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16422-16427
    • Kent, U.M.1    Fleming, P.J.2
  • 11
    • 0026474840 scopus 로고
    • Cultured astrocytes express mRNA for peptidylglycine-alpha-amidating monooxygenase, a neuropeptide processing enzyme
    • KLEIN, R.S., and FRICKER, L.D. (1992). Cultured astrocytes express mRNA for peptidylglycine-alpha-amidating monooxygenase, a neuropeptide processing enzyme. Brain Res. 596, 202-208.
    • (1992) Brain Res. , vol.596 , pp. 202-208
    • Klein, R.S.1    Fricker, L.D.2
  • 12
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • KOZAK, M. (1986). Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44, 283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 13
    • 0023661361 scopus 로고
    • The primary structure of human dopamine beta hydroxylase: Insights into the relationship between soluble and the membrane-bound forms of the enzyme
    • LAMOUROUX, A., VIGNY, A., FAUCON-BOUGUET, N., DARMON, M.C., FRANK, R., HENRY, J.-P., and MALLET, J. (1987). The primary structure of human dopamine beta hydroxylase: insights into the relationship between soluble and the membrane-bound forms of the enzyme. EMBO J. 6, 3931-3937.
    • (1987) EMBO J. , vol.6 , pp. 3931-3937
    • Lamouroux, A.1    Vigny, A.2    Faucon-Bouguet, N.3    Darmon, M.C.4    Frank, R.5    Henry, J.-P.6    Mallet, J.7
  • 14
    • 0342874462 scopus 로고
    • Sequence of a cDNA clone encoding mouse glial fibrillary acidic protein: Structural conservation of intermediate filaments
    • LEWIS, S.A., BALCAREK, J.M., KREK, V., SHELANSKI, M., and COWAN, N.J. (1984). Sequence of a cDNA clone encoding mouse glial fibrillary acidic protein: structural conservation of intermediate filaments. Proc. Natl. Acad. Sci. 81, 2743-2746.
    • (1984) Proc. Natl. Acad. Sci. , vol.81 , pp. 2743-2746
    • Lewis, S.A.1    Balcarek, J.M.2    Krek, V.3    Shelanski, M.4    Cowan, N.J.5
  • 15
    • 0022972685 scopus 로고
    • Role of ascorbic acid in dopamine beta hydroxylation: The endogeneous enzyme cofactor and putative electron donor for cofactor regeneration
    • MENNITI, F.S., KNOTH, J., and DILIBERTO, E.J. (1986). Role of ascorbic acid in dopamine beta hydroxylation: the endogeneous enzyme cofactor and putative electron donor for cofactor regeneration. J. Biol. Chem. 261, 16901-16908.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16901-16908
    • Menniti, F.S.1    Knoth, J.2    Diliberto, E.J.3
  • 16
    • 0020657388 scopus 로고
    • Electron transfer across the chromaffin granule membrane
    • NJUS, D., KNOTH, J., COOK, C., and KELLEY, P. (1983). Electron transfer across the chromaffin granule membrane. J. Biol. Chem. 258, 27-30.
    • (1983) J. Biol. Chem. , vol.258 , pp. 27-30
    • Njus, D.1    Knoth, J.2    Cook, C.3    Kelley, P.4
  • 17
    • 0024519147 scopus 로고
    • Developmental regulation of peptidylglycine α-amidating monooxygenase (PAM) in rat heart atrium and ventricle
    • QUAFIK, L.H., MAY, V., KEUTMANN, H.T., and EIPPER, B.A. (1989). Developmental regulation of peptidylglycine α-amidating monooxygenase (PAM) in rat heart atrium and ventricle. J. Biol. Chem. 264, 5839-5845.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5839-5845
    • Quafik, L.H.1    May, V.2    Keutmann, H.T.3    Eipper, B.A.4
  • 18
    • 0024077919 scopus 로고
    • The structure of cytochrome b561, a secretory vesicle-specific transport protein
    • PERIN, M.S., FRIED, V.A., SLAUGHTER, C.A., and SUDHOF, T.C. (1988). The structure of cytochrome b561, a secretory vesicle-specific transport protein. EMBO J. 7, 2697-2703.
    • (1988) EMBO J. , vol.7 , pp. 2697-2703
    • Perin, M.S.1    Fried, V.A.2    Slaughter, C.A.3    Sudhof, T.C.4
  • 19
    • 0025140938 scopus 로고
    • Peptidylglycine-alpha-amidating monooxygenase (PAM) in Schwann cells and glia as well as neurons
    • RHODES, C.H., XU, R.-Y., and ANGELETTI, R.H. (1990). Peptidylglycine-alpha-amidating monooxygenase (PAM) in Schwann cells and glia as well as neurons. J. Histochem. Cytochem. 38, 1301-1311.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 1301-1311
    • Rhodes, C.H.1    Xu, R.-Y.2    Angeletti, R.H.3
  • 21
    • 0026591319 scopus 로고
    • Expression of peptidylglycine α-amidating monooxygenase (EC 1.14.17.3) in the rat central nervous system
    • SCHAFER, M., STOFFERS, K.-H., EIPPER, B.A., and WATSON, S.J. (1992). Expression of peptidylglycine α-amidating monooxygenase (EC 1.14.17.3) in the rat central nervous system. J. Neurosci. 12, 222-234.
    • (1992) J. Neurosci. , vol.12 , pp. 222-234
    • Schafer, M.1    Stoffers, K.-H.2    Eipper, B.A.3    Watson, S.J.4
  • 22
    • 0021287589 scopus 로고
    • Cytochrome b561 catalyzes transmembrane electron transfer
    • SRIVASTAVA, M., DUONG, L.T., and FLEMING, P.J. (1984). Cytochrome b561 catalyzes transmembrane electron transfer. J. Biol. Chem. 259, 8072-8075.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8072-8075
    • Srivastava, M.1    Duong, L.T.2    Fleming, P.J.3
  • 23
    • 0028172069 scopus 로고
    • Human cytochrome b561: A revised hypothesis for conformation in membranes which reconciles sequence and functional information
    • SRIVASTAVA, M., GIBSON, K.R., POLLARD, H.B., and FLEMING, P.J. (1994). Human cytochrome b561: a revised hypothesis for conformation in membranes which reconciles sequence and functional information. Biochem. J. 303, 915-921.
    • (1994) Biochem. J. , vol.303 , pp. 915-921
    • Srivastava, M.1    Gibson, K.R.2    Pollard, H.B.3    Fleming, P.J.4
  • 24
    • 0000614022 scopus 로고
    • Alternative mRNA splicing generates multiple forms of peptidyl-glycine alpha-amidating monooxygenase in rat atrium
    • STOFFERS, D.A., GREEN, C.B., and EIPPER, B.A. (1989). Alternative mRNA splicing generates multiple forms of peptidyl-glycine alpha-amidating monooxygenase in rat atrium. Proc. Natl. Acad. Sci. USA 86, 735-739.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 735-739
    • Stoffers, D.A.1    Green, C.B.2    Eipper, B.A.3
  • 25
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • VON HEIJNE, G., and GAVEL, Y. (1988). Topogenic signals in integral membrane proteins. Eur. J. Biochem. 174, 671-678.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 26
    • 0022971533 scopus 로고
    • Functional coupling between enzymes of the chromaffin granule membrane
    • WAKEFIELD, L.M. CASS, A.E.G., and RADDA, G.K. (1986a). Functional coupling between enzymes of the chromaffin granule membrane. J. Biol. Chem. 261, 9739-9745.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9739-9745
    • Wakefield, L.M.1    Cass, A.E.G.2    Radda, G.K.3
  • 27
    • 0023001148 scopus 로고
    • Electron transfer across the chromaffin granule membrane. Use of EPR to demonstrate reduction of intraveiscular ascorbate radical by the extravesicular mitochondrial NADH:ascorbate radical oxidoreductase
    • WAKEFIELD, L.M., CASS, A.E.G., and RADDA, G.K. (1986b). Electron transfer across the chromaffin granule membrane. Use of EPR to demonstrate reduction of intraveiscular ascorbate radical by the extravesicular mitochondrial NADH:ascorbate radical oxidoreductase. J. Biol. Chem. 261, 9746-9752.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9746-9752
    • Wakefield, L.M.1    Cass, A.E.G.2    Radda, G.K.3


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