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Volumn 242, Issue 2, 1996, Pages 339-351

Isolation and characterization of a 14.5-kDa trichloroacetic-acid-soluble translational inhibitor protein from human monocytes that is upregulated upon cellular differentiation

Author keywords

Hepatocytes; Monocytes; Renal tubular cells; Translational inhibitor; Trichloroacetic acid soluble protein

Indexed keywords

COMPLEMENTARY DNA; INHIBITOR PROTEIN;

EID: 0029806258     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0339r.x     Document Type: Article
Times cited : (85)

References (45)
  • 1
    • 0027480445 scopus 로고
    • Characterization, purification and cDNA cloning of a rat perchloric-acid-soluble 23 kDa protein present only in liver and kidney
    • Levy-Favatier, F., Cuisset, L., Nedelec, L., Tichonicky, L., Kruh, J. & Delpech, M. (1993) Characterization, purification and cDNA cloning of a rat perchloric-acid-soluble 23 kDa protein present only in liver and kidney, Eur. J. Biochem. 212, 665-673.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 665-673
    • Levy-Favatier, F.1    Cuisset, L.2    Nedelec, L.3    Tichonicky, L.4    Kruh, J.5    Delpech, M.6
  • 2
    • 0029585753 scopus 로고
    • Isolation and Characterization of a novel perchloric acid soluble protein inhibiting cell-free protein synthesis
    • Oka, T., Tsuji, H., Noda, C., Sakai, K., Hong, Y.-m., Suzuki, I., Munoz, S. & Natori, Y. (1995) Isolation and Characterization of a novel perchloric acid soluble protein inhibiting cell-free protein synthesis, J. Biol. Chem. 270, 30060-30067.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30060-30067
    • Oka, T.1    Tsuji, H.2    Noda, C.3    Sakai, K.4    Hong, Y.-M.5    Suzuki, I.6    Munoz, S.7    Natori, Y.8
  • 3
    • 0344441629 scopus 로고
    • Regulation of protein synthesis in rabbit reticulocyte lysates: Characteristics of inhibition of protein synthesis by a translational inhibitor from heme-deficient lysates and its relationship to the initiation factor which binds Met-tRNA
    • Ranu, R. S., Levin, B. H., Delaunay, J., Ernst, V. & London, I. M. (1976) Regulation of protein synthesis in rabbit reticulocyte lysates: Characteristics of inhibition of protein synthesis by a translational inhibitor from heme-deficient lysates and its relationship to the initiation factor which binds Met-tRNA, Proc. Natl Acad. Sci. USA 73, 2720-2724.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 2720-2724
    • Ranu, R.S.1    Levin, B.H.2    Delaunay, J.3    Ernst, V.4    London, I.M.5
  • 4
    • 0028580175 scopus 로고
    • Regulation of heme-regulated eIF-2 alpha kinase and its expression in erythroid cells
    • Chen, J. J., Crosby, J. S. & London, I. M. (1994) Regulation of heme-regulated eIF-2 alpha kinase and its expression in erythroid cells, Biochimie 76, 761-769.
    • (1994) Biochimie , vol.76 , pp. 761-769
    • Chen, J.J.1    Crosby, J.S.2    London, I.M.3
  • 5
    • 0027418321 scopus 로고
    • The eIF-2α protein kinases, regulators of translation in eukaryotes from yeast to humans
    • Samuel, C. E. (1993) The eIF-2α protein kinases, regulators of translation in eukaryotes from yeast to humans, J. Biol. Chem. 268, 7603-7606.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7603-7606
    • Samuel, C.E.1
  • 6
    • 0000002161 scopus 로고
    • Binding of Met-tRNA in translation in eukaryotes
    • (Trachsel, H., ed.) CRC Press, London
    • Jackson, R. J. (1991) Binding of Met-tRNA in translation in eukaryotes, in Translation in eukaryotes (Trachsel, H., ed.) pp. 193-229, CRC Press, London.
    • (1991) Translation in Eukaryotes , pp. 193-229
    • Jackson, R.J.1
  • 7
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey, J. W. B. (1991) Translational control in mammalian cells, Anna. Rev. Biochem. 60, 717-755.
    • (1991) Anna. Rev. Biochem. , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 8
    • 77956925190 scopus 로고
    • Regulation of protein synthesis
    • (Boyer, P. D. & Krebs, E. G., eds) 3rd edn, Academic Press, New York
    • London, I. M., Levin, D. H., Matts, R. L., Thomas, N. S. B., Petryshin, R. & Chen, J. J. (1987) Regulation of protein synthesis, in The enzymes (Boyer, P. D. & Krebs, E. G., eds) 3rd edn, pp. 359-380, Academic Press, New York.
    • (1987) The Enzymes , pp. 359-380
    • London, I.M.1    Levin, D.H.2    Matts, R.L.3    Thomas, N.S.B.4    Petryshin, R.5    Chen, J.J.6
  • 9
    • 0018386538 scopus 로고
    • Separation of and cholesterolsynthesis by human lymphocytes and monocytes
    • Fogelman, A. M., Seager, J., Hokom, M. & Edwards, P. A. (1979) Separation of and cholesterolsynthesis by human lymphocytes and monocytes, J. Lipid Res. 20, 379-388.
    • (1979) J. Lipid Res. , vol.20 , pp. 379-388
    • Fogelman, A.M.1    Seager, J.2    Hokom, M.3    Edwards, P.A.4
  • 10
    • 0016377705 scopus 로고
    • Isolation of rough and smooth microsomes-gene-ral
    • Dallner, G. (1974) Isolation of rough and smooth microsomes-gene-ral, Methods Enzymol. 31, 191-201.
    • (1974) Methods Enzymol. , vol.31 , pp. 191-201
    • Dallner, G.1
  • 11
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, 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, Annl. Biochem. 166, 368-379.
    • (1987) Annl. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 13
    • 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
  • 14
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis, C. & de Jong, P. J. (1990) Ligation-independent cloning of PCR products (LIC-PCR), Nucleic Acids Res. 18, 6060-6074.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6060-6074
    • Aslanidis, C.1    De Jong, P.J.2
  • 15
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin, J. M., Przybyla, R. J. & Rutter, W. J. (1979) Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease, Biochemistry 18, 5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, R.J.2    Rutter, W.J.3
  • 16
    • 0025322067 scopus 로고
    • Simplified northern blot hybridization using 5% sodium dodecyl sulfate
    • Virca, G. D. (1990) Simplified northern blot hybridization using 5% sodium dodecyl sulfate, BioTechniques 8, 370-371.
    • (1990) BioTechniques , vol.8 , pp. 370-371
    • Virca, G.D.1
  • 17
    • 0027295643 scopus 로고
    • Effects of purinergic agents on human mononuclear phagocytes are differentiation dependent. Implications for atherogenesis
    • Müller, G., Kerkhoff, C., Hankowitz, J., Pataki, M., Kovacs, E., Lackner, K. J. & Schmitz, G. (1993) Effects of purinergic agents on human mononuclear phagocytes are differentiation dependent. Implications for atherogenesis, Arterioscler. Thromb. 13, 1317-1326.
    • (1993) Arterioscler. Thromb. , vol.13 , pp. 1317-1326
    • Müller, G.1    Kerkhoff, C.2    Hankowitz, J.3    Pataki, M.4    Kovacs, E.5    Lackner, K.J.6    Schmitz, G.7
  • 18
    • 0016378181 scopus 로고
    • Subcellular fractionation of rat liver
    • Fleischer, S. & Kervina, M. (1974) Subcellular fractionation of rat liver, Methods Enzymol. 31, 6-41.
    • (1974) Methods Enzymol. , vol.31 , pp. 6-41
    • Fleischer, S.1    Kervina, M.2
  • 21
    • 0028175555 scopus 로고
    • Differential expression of scavenger receptor isoforms during monocyte-macrophage differentiation and foam cell formation
    • Geng, Y.-J., Kodama, T. & Hansson, G. K. (1994) Differential expression of scavenger receptor isoforms during monocyte-macrophage differentiation and foam cell formation, Arterioscler. Thromb. 14, 798-806.
    • (1994) Arterioscler. Thromb. , vol.14 , pp. 798-806
    • Geng, Y.-J.1    Kodama, T.2    Hansson, G.K.3
  • 22
    • 0019796014 scopus 로고
    • Acetoacetylated lipoproteins used to distinguish fibroblasts from macrophages in vitro by fluorescence microscopy
    • Pitas, R. E., Innerarity, T. I., Weinstein, J. N. & Mahley, R. W. (1981) Acetoacetylated lipoproteins used to distinguish fibroblasts from macrophages in vitro by fluorescence microscopy, Arteriosclerosis 1, 177-185.
    • (1981) Arteriosclerosis , vol.1 , pp. 177-185
    • Pitas, R.E.1    Innerarity, T.I.2    Weinstein, J.N.3    Mahley, R.W.4
  • 23
    • 0028087593 scopus 로고
    • Assay for scavenger receptors on human monocyte-derived macrophages
    • Gugliucci, A. C. & Stahl, A. J. C. (1994) Assay for scavenger receptors on human monocyte-derived macrophages, J. Immunol. Methods 174, 103-107.
    • (1994) J. Immunol. Methods , vol.174 , pp. 103-107
    • Gugliucci, A.C.1    Stahl, A.J.C.2
  • 24
    • 0022920789 scopus 로고
    • Use of high concentrations of glutaraldehyde for immunocytochemistry of transmitter-synthesizing enzymes in the central nervous system
    • Kosaka, T., Nagatsu, L., Wu, J. Y. & Hama, K. (1986) Use of high concentrations of glutaraldehyde for immunocytochemistry of transmitter-synthesizing enzymes in the central nervous system, Neuroscience 18, 975-990.
    • (1986) Neuroscience , vol.18 , pp. 975-990
    • Kosaka, T.1    Nagatsu, L.2    Wu, J.Y.3    Hama, K.4
  • 25
    • 0027721972 scopus 로고
    • Dopamine is taken up from the circulation by, and released from, local noradrenergic varicose axon terminals in zona glomerulosa of the rat: A neurochemical and immunocytochemical study
    • Vizi, E. S., Tóth, I. E., Orsó, E., Szalay, K. Sz., Szabó, D., Baranyi, M. & Vinson, G. P. (1993) Dopamine is taken up from the circulation by, and released from, local noradrenergic varicose axon terminals in zona glomerulosa of the rat: a neurochemical and immunocytochemical study, J. Endocrinol. 139, 213-226.
    • (1993) J. Endocrinol. , vol.139 , pp. 213-226
    • Vizi, E.S.1    Tóth, I.E.2    Orsó, E.3    Szalay, K.Sz.4    Szabó, D.5    Baranyi, M.6    Vinson, G.P.7
  • 26
    • 0003253048 scopus 로고
    • Fixation, dehydration and embedding of biological specimens
    • (Glauert, A. M., ed.), North-Holland Publishing Company, Amsterdam
    • Glauert, A. M. (1975) Fixation, dehydration and embedding of biological specimens, in Practical methods in electron microscopy, vol. 3, part I (Glauert, A. M., ed.), North-Holland Publishing Company, Amsterdam.
    • (1975) Practical Methods in Electron Microscopy , vol.3 , Issue.1 PART
    • Glauert, A.M.1
  • 27
    • 0019143031 scopus 로고
    • Exons encode functional and structural units of chicken lysozyme
    • Jung, A., Sippel, A. E., Grez, M. & Schutz, G. (1980) Exons encode functional and structural units of chicken lysozyme, Proc. Natl Acad. Sci. USA 77, 5759-5763.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 5759-5763
    • Jung, A.1    Sippel, A.E.2    Grez, M.3    Schutz, G.4
  • 28
    • 0020479238 scopus 로고
    • The complete nucleotide sequence of the chicken-actin gene and its evolutionary relationship to the actin gene family
    • Fornwald, J. A., Kuncio, G., Peng, I. & Ordahl, C. P. (1982) The complete nucleotide sequence of the chicken-actin gene and its evolutionary relationship to the actin gene family, Nucleic Acids Res. 10, 3861-3876.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 3861-3876
    • Fornwald, J.A.1    Kuncio, G.2    Peng, I.3    Ordahl, C.P.4
  • 29
    • 0019972680 scopus 로고
    • Nucleotide sequence of the rat skeletal muscle actin gene
    • Zakut, R., Shani, M., Givol, D., Neuman, S., Yaffe, D. & Nudel, U. (1982) Nucleotide sequence of the rat skeletal muscle actin gene, Nature 298, 857-859.
    • (1982) Nature , vol.298 , pp. 857-859
    • Zakut, R.1    Shani, M.2    Givol, D.3    Neuman, S.4    Yaffe, D.5    Nudel, U.6
  • 30
    • 0025113220 scopus 로고
    • Casein kinase 2: An 'eminence grise' in cellular regulation?
    • Pinna, L. A. (1990) Casein kinase 2: an 'eminence grise' in cellular regulation? Biochim. Biophys. Acta 1054, 267-284.
    • (1990) Biochim. Biophys. Acta , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 31
    • 0022881173 scopus 로고
    • Substrate specifity of protein kinase C. Use of synthetic peptides corresponding to physiological sites as probes for substrate recognition requirements
    • Woodgett, J. R., Gould, K. L. & Hunter, T. (1986) Substrate specifity of protein kinase C. Use of synthetic peptides corresponding to physiological sites as probes for substrate recognition requirements, Eur. J. Biochem. 161, 177-184.
    • (1986) Eur. J. Biochem. , vol.161 , pp. 177-184
    • Woodgett, J.R.1    Gould, K.L.2    Hunter, T.3
  • 32
    • 0022348840 scopus 로고
    • Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3′:5′ monophosphate-dependent protein kinase
    • Kishimoto, A., Nishiyama, K., Nakanishi, H., Uratsuji, Y., Nomura, H., Takeyama, Y. & Nishizuka, Y. (1985) Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3′:5′ monophosphate-dependent protein kinase, J. Biol. Chem. 260, 12492-12499.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12492-12499
    • Kishimoto, A.1    Nishiyama, K.2    Nakanishi, H.3    Uratsuji, Y.4    Nomura, H.5    Takeyama, Y.6    Nishizuka, Y.7
  • 34
    • 0024559375 scopus 로고
    • Acylation of viral and eukaryotic proteins
    • Grand, R. J. (1989) Acylation of viral and eukaryotic proteins, Biochem. J. 258, 625-638.
    • (1989) Biochem. J. , vol.258 , pp. 625-638
    • Grand, R.J.1
  • 35
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. (1986) A new method for predicting signal sequence cleavage sites, Nucleic Acids Res. 14, 4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 36
    • 0024410675 scopus 로고
    • Two nifa-like genes reqiuired for expression of alternative nitrogenase by Azotobacter vinelandii
    • Joerger, R. D., Jacobson, M. R. & Bishop, P. E. (1989) Two nifa-like genes reqiuired for expression of alternative nitrogenase by Azotobacter vinelandii, J. Bacteriol. 171, 3256-3267.
    • (1989) J. Bacteriol. , vol.171 , pp. 3256-3267
    • Joerger, R.D.1    Jacobson, M.R.2    Bishop, P.E.3
  • 37
    • 0029073731 scopus 로고
    • Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes
    • Burland, V. D., Plunkett, G., Sofia, H. J., Daniels, D. L. & Blattner, F. R. (1995) Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes, Nucleic Acids Res. 23, 2105-2119.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2105-2119
    • Burland, V.D.1    Plunkett, G.2    Sofia, H.J.3    Daniels, D.L.4    Blattner, F.R.5
  • 38
    • 0028700721 scopus 로고
    • Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin
    • Ogasawara, N., Nakai, S. & Yoshikawa, H. (1994) Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin, DNA Res. 1, 1-14.
    • (1994) DNA Res. , vol.1 , pp. 1-14
    • Ogasawara, N.1    Nakai, S.2    Yoshikawa, H.3
  • 40
    • 0029278091 scopus 로고
    • The NADP-glutamate dehydrogenase of the cyanobacterium Synechocystis 6803: Cloning, transcriptional analysis and disruption of the gdhA gene
    • Chávez, S., Reyes, J. C., Chauvat, F., Florencio, F. J. & Candau, P. (1995) The NADP-glutamate dehydrogenase of the cyanobacterium Synechocystis 6803: cloning, transcriptional analysis and disruption of the gdhA gene, Plant Mol. Biol. 28, 173-188.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 173-188
    • Chávez, S.1    Reyes, J.C.2    Chauvat, F.3    Florencio, F.J.4    Candau, P.5
  • 41
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • Pause, A., Belsham, G. J., Gingras, A.-C., Donzé, O., Lin, T.-A., Lawrence, J. C. Jr & Sonenberg, N. (1994) Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function, Nature 372, 762-767.
    • (1994) Nature , vol.372 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.-C.3    Donzé, O.4    Lin, T.-A.5    Lawrence Jr., J.C.6    Sonenberg, N.7
  • 42
    • 0028222129 scopus 로고
    • Molecular cloning and tissue distribution of PHAS-I, an intracellular target for insulin an growth factors
    • Hu, C., Pang, S., Kong, X., Velleca, M. & Lawrence, J. C. Jr (1994) Molecular cloning and tissue distribution of PHAS-I, an intracellular target for insulin an growth factors, Proc. Natl Acad. Sci. USA 91, 3730-3734.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3730-3734
    • Hu, C.1    Pang, S.2    Kong, X.3    Velleca, M.4    Lawrence Jr., J.C.5
  • 44
    • 0025323711 scopus 로고
    • Structural features of the HMG chromosomal proteins and their genes
    • Bustin, M., Lehn, D. A. & Landsman, D. (1990) Structural features of the HMG chromosomal proteins and their genes, Biochim. Biophys. Acta 1049, 231-243.
    • (1990) Biochim. Biophys. Acta , vol.1049 , pp. 231-243
    • Bustin, M.1    Lehn, D.A.2    Landsman, D.3
  • 45
    • 0028173897 scopus 로고
    • Structures and functions of multiligand lipoprotein receptors: Macrophage scavenger receptors and LDL receptor-related protein (LRP)
    • Krieger, M. & Herz, J. (1994) Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor-related protein (LRP), Annu. Rev. Biochem. 63, 601-637.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 601-637
    • Krieger, M.1    Herz, J.2


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