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Volumn 66, Issue 4, 1999, Pages 609-616

Differentiating agents regulate cathepsin B gene expression in HL-60 cells

Author keywords

Granulocyte; Monocyte; MRNA; Posttranscriptional regulation; Transcriptional regulation

Indexed keywords

ALITRETINOIN; BUTYRIC ACID; CALCITRIOL; CATHEPSIN B; DACTINOMYCIN; MESSENGER RNA; PHORBOL ESTER; RETINOIC ACID;

EID: 0345363292     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1002/jlb.66.4.609     Document Type: Article
Times cited : (25)

References (55)
  • 1
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • Barrett, A. J., Kirschke, H. (1981) Cathepsin B, cathepsin H, and cathepsin L. Meth. Enzymol. 80, 535-561.
    • (1981) Meth. Enzymol. , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 2
    • 0022532266 scopus 로고
    • Differences in cathepsin B mRNA levels in rat tissues suggest specialized functions
    • San Segundo, B., Chan, S. J., Steiner, D. F. (1986) Differences in cathepsin B mRNA levels in rat tissues suggest specialized functions. FEBS Lett. 201, 251-256.
    • (1986) FEBS Lett. , vol.201 , pp. 251-256
    • San Segundo, B.1    Chan, S.J.2    Steiner, D.F.3
  • 3
    • 0024322516 scopus 로고
    • Expression of five cathepsins in murine melanomas of varying metastatic potential and normal tissues
    • Qian, F., Bajkowski, A. S., Steiner, D. F., Chan, S. J., Frankfater, A. (1989) Expression of five cathepsins in murine melanomas of varying metastatic potential and normal tissues. Cancer Res. 49, 4870-4875.
    • (1989) Cancer Res. , vol.49 , pp. 4870-4875
    • Qian, F.1    Bajkowski, A.S.2    Steiner, D.F.3    Chan, S.J.4    Frankfater, A.5
  • 4
    • 0026095328 scopus 로고
    • Cysteine endopeptidase activity levels in normal human tissues, colorectal adenomas and carcinomas
    • Shuja, S., Sheahan, K., Murnane, M. J. (1991) Cysteine endopeptidase activity levels in normal human tissues, colorectal adenomas and carcinomas. Int. J. Cancer 49, 341-346.
    • (1991) Int. J. Cancer , vol.49 , pp. 341-346
    • Shuja, S.1    Sheahan, K.2    Murnane, M.J.3
  • 7
    • 0021797883 scopus 로고
    • Cathepsin B activity in human blood monocytes during differentiation in vitro
    • Morland, B. (1985) Cathepsin B activity in human blood monocytes during differentiation in vitro. Scand. J. Immunol. 22, 9-16.
    • (1985) Scand. J. Immunol. , vol.22 , pp. 9-16
    • Morland, B.1
  • 8
    • 0025772668 scopus 로고
    • Collagenolytic cysteine proteinases of bone tissue. Cathepsin B, (pro)cathepsin L and a cathepsin L-like 70 kDa proteinase
    • Delaisse, J. M., Ledent, P., Vaes, G. (1991) Collagenolytic cysteine proteinases of bone tissue. Cathepsin B, (pro)cathepsin L and a cathepsin L-like 70 kDa proteinase. Biochem. J. 279, 167-174.
    • (1991) Biochem. J. , vol.279 , pp. 167-174
    • Delaisse, J.M.1    Ledent, P.2    Vaes, G.3
  • 9
    • 0027520745 scopus 로고
    • Extracellular-matrix degradation at acid pH. Avian osteoclast acid collagenase isolation and characterization
    • Blair, H. C., Teitelbaum, S. L., Grosso, L. E., Lacey, D. L., Tan, H. L., McCourt, D. W., Jeffrey, J. J. (1993) Extracellular-matrix degradation at acid pH. Avian osteoclast acid collagenase isolation and characterization. Biochem. J. 290, 873-884.
    • (1993) Biochem. J. , vol.290 , pp. 873-884
    • Blair, H.C.1    Teitelbaum, S.L.2    Grosso, L.E.3    Lacey, D.L.4    Tan, H.L.5    McCourt, D.W.6    Jeffrey, J.J.7
  • 11
    • 0029128688 scopus 로고
    • Avian cathepsin B cDNA: Sequence and demonstration that mRNAs of two sizes are produced in cell types producing large quantities of the enzyme
    • Dong, S. S., Stransky, G. I., Whitaker, C. H., Jordan, S. E., Schlesinger, P. H., Edwards, J. C., Blair, H. C. (1995) Avian cathepsin B cDNA: sequence and demonstration that mRNAs of two sizes are produced in cell types producing large quantities of the enzyme. Biochim. Biophys. Acta 1251, 69-73.
    • (1995) Biochim. Biophys. Acta , vol.1251 , pp. 69-73
    • Dong, S.S.1    Stransky, G.I.2    Whitaker, C.H.3    Jordan, S.E.4    Schlesinger, P.H.5    Edwards, J.C.6    Blair, H.C.7
  • 12
    • 0029007093 scopus 로고
    • Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages
    • Reddy, V. Y., Zhang, Q. Y., Weiss, S. J. (1995) Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc. Natl. Acad. Sci. USA 92, 3849-3853.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3849-3853
    • Reddy, V.Y.1    Zhang, Q.Y.2    Weiss, S.J.3
  • 14
    • 0022910965 scopus 로고
    • MRNA levels of cathepsins B and D during myogenesis
    • Colella, R., Roisen, F. J., Bird, J. W. (1986) mRNA levels of cathepsins B and D during myogenesis. Biomed. Biochim. Acta 45, 1413-1419.
    • (1986) Biomed. Biochim. Acta , vol.45 , pp. 1413-1419
    • Colella, R.1    Roisen, F.J.2    Bird, J.W.3
  • 15
    • 0025915530 scopus 로고
    • Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation. Characterization of a cDNA encoding bovine cathepsin B
    • Bechet, D. M., Ferrara, M. J., Mordier, S. B., Roux, M. P., Deval, C. D., Obled, A. (1991) Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation. Characterization of a cDNA encoding bovine cathepsin B. J. Biol. Chem. 266, 14104-14112.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14104-14112
    • Bechet, D.M.1    Ferrara, M.J.2    Mordier, S.B.3    Roux, M.P.4    Deval, C.D.5    Obled, A.6
  • 16
    • 0028475539 scopus 로고
    • Expression and regulation of three lysosomal cysteine protease activities during growth of a differentiating L6 rat myoblast cell line and its nonfusing variant
    • Jane, D. T., Dufresne, M. J. (1994) Expression and regulation of three lysosomal cysteine protease activities during growth of a differentiating L6 rat myoblast cell line and its nonfusing variant. Biochem. Cell Biol. 72, 267-274.
    • (1994) Biochem. Cell Biol. , vol.72 , pp. 267-274
    • Jane, D.T.1    Dufresne, M.J.2
  • 17
    • 0025883570 scopus 로고
    • Isolation of a cathepsin B-encoding cDNA from murine osteogenic cells
    • Freimert, C., Closs, E. I., Silbermann, M., Erfle, V., Strauss, P. G. (1991) Isolation of a cathepsin B-encoding cDNA from murine osteogenic cells. Gene 103, 259-261.
    • (1991) Gene , vol.103 , pp. 259-261
    • Freimert, C.1    Closs, E.I.2    Silbermann, M.3    Erfle, V.4    Strauss, P.G.5
  • 18
    • 0025323360 scopus 로고
    • Changes in the expression of elastase and cathepsin B with differentiation of U937 promonocytes by GMCSF
    • Ward, C. J., Crocker, J., Chan, S. J., Stockley, R. A., Burnett, D. (1990) Changes in the expression of elastase and cathepsin B with differentiation of U937 promonocytes by GMCSF. Biochem. Biophys. Res. Commun. 167, 659-664.
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 659-664
    • Ward, C.J.1    Crocker, J.2    Chan, S.J.3    Stockley, R.A.4    Burnett, D.5
  • 19
    • 0028356053 scopus 로고
    • Latency of cathepsin B secreted by human colon carcinoma cells is not linked to secretion of cystatin C and is relieved by neutrophil elastase
    • Keppler, D., Waridel, P., Abrahamson, M., Bachmann, D., Berdoz, J., Sordat, B. (1994) Latency of cathepsin B secreted by human colon carcinoma cells is not linked to secretion of cystatin C and is relieved by neutrophil elastase. Biochim. Biophys. Acta 1226, 117-125.
    • (1994) Biochim. Biophys. Acta , vol.1226 , pp. 117-125
    • Keppler, D.1    Waridel, P.2    Abrahamson, M.3    Bachmann, D.4    Berdoz, J.5    Sordat, B.6
  • 20
    • 0020576885 scopus 로고
    • Synthesis of cathepsin B by cells derived from the HL60 promyelocytic leukaemia cell line
    • Burnett, D., Crocker, J., Vaughan, A. T. (1983) Synthesis of cathepsin B by cells derived from the HL60 promyelocytic leukaemia cell line. J. Cell Physiol. 115, 249-254.
    • (1983) J. Cell Physiol. , vol.115 , pp. 249-254
    • Burnett, D.1    Crocker, J.2    Vaughan, A.T.3
  • 21
    • 0022520824 scopus 로고
    • Cathepsin B synthesis by the HL60 promyelocytic cell line: Effects of stimulating agents and anti-inflammatory compounds
    • Burnett, D., Crocker, J., Afford, S. C., Bunce, C. M., Brown, G., Stockley, R. A. (1986) Cathepsin B synthesis by the HL60 promyelocytic cell line: effects of stimulating agents and anti-inflammatory compounds. Biochim. Biophys. Acta 887, 283-290.
    • (1986) Biochim. Biophys. Acta , vol.887 , pp. 283-290
    • Burnett, D.1    Crocker, J.2    Afford, S.C.3    Bunce, C.M.4    Brown, G.5    Stockley, R.A.6
  • 22
    • 0023605430 scopus 로고
    • The HL-60 promyelocytic leukemia cell line: Proliferation, differentiation, and cellular oncogene expression
    • Collins, S. J. (1987) The HL-60 promyelocytic leukemia cell line: proliferation, differentiation, and cellular oncogene expression. Blood 70, 1233-1244.
    • (1987) Blood , vol.70 , pp. 1233-1244
    • Collins, S.J.1
  • 23
    • 0025997062 scopus 로고
    • Rapid, small-scale RNA isolation from tissue culture cells
    • Xie, W., Rothblum, L. I. (1991) Rapid, small-scale RNA isolation from tissue culture cells. BioTechniques 11, 325-327.
    • (1991) BioTechniques , vol.11 , pp. 325-327
    • Xie, W.1    Rothblum, L.I.2
  • 24
    • 0028297896 scopus 로고
    • Human gastric adenocarcinoma cathepsin B: Isolation and sequencing of full-length cDNAs and polymorphisms of the gene
    • Cao, L., Taggart, R. T., Berquin, I. M., Moin, K., Fong, D., Sloane, B. F. (1994) Human gastric adenocarcinoma cathepsin B: isolation and sequencing of full-length cDNAs and polymorphisms of the gene. Gene 139, 163-169.
    • (1994) Gene , vol.139 , pp. 163-169
    • Cao, L.1    Taggart, R.T.2    Berquin, I.M.3    Moin, K.4    Fong, D.5    Sloane, B.F.6
  • 25
    • 0021114732 scopus 로고
    • Cloning and sequencing of a deoxyribonucleic acid copy of glyceraldehyde-3-phosphate dehydrogenase messenger ribonucleic acid isolated from chicken muscle
    • Dugaiczyk, A., Haron, J. A., Stone, E. M., Dennison, O. E., Rothblum, K. N., Schwartz, R. J. (1983) Cloning and sequencing of a deoxyribonucleic acid copy of glyceraldehyde-3-phosphate dehydrogenase messenger ribonucleic acid isolated from chicken muscle. Biochemistry 22, 1605-1613.
    • (1983) Biochemistry , vol.22 , pp. 1605-1613
    • Dugaiczyk, A.1    Haron, J.A.2    Stone, E.M.3    Dennison, O.E.4    Rothblum, K.N.5    Schwartz, R.J.6
  • 27
    • 0026518253 scopus 로고
    • Confirmation of the human cathepsin B gene (CTSB) assignment to chromosome 8
    • Fong, D., Chan, M. M., Hsieh, W. T., Menninger, J. C., Ward, D. C. (1992) Confirmation of the human cathepsin B gene (CTSB) assignment to chromosome 8. Hum. Genet. 89, 10-12.
    • (1992) Hum. Genet. , vol.89 , pp. 10-12
    • Fong, D.1    Chan, M.M.2    Hsieh, W.T.3    Menninger, J.C.4    Ward, D.C.5
  • 28
    • 0026042713 scopus 로고
    • Optimization of transient transfection into human myeloid cell lines using a luciferase reporter gene
    • Pahl, H. L., Burn, T. C., Tenen, D. G. (1991) Optimization of transient transfection into human myeloid cell lines using a luciferase reporter gene. Exp. Hematol. 19, 1038-1041.
    • (1991) Exp. Hematol. , vol.19 , pp. 1038-1041
    • Pahl, H.L.1    Burn, T.C.2    Tenen, D.G.3
  • 29
    • 0028881129 scopus 로고
    • Nitric oxide regulates IL-8 expression in melanoma cells at the transcriptional level
    • Andrew, P. J., Harant, H., Lindley, I. J. (1995) Nitric oxide regulates IL-8 expression in melanoma cells at the transcriptional level. Biochem. Biophys. Res. Commun. 214, 949-956.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 949-956
    • Andrew, P.J.1    Harant, H.2    Lindley, I.J.3
  • 30
    • 0031571094 scopus 로고    scopus 로고
    • Stimulation of osteopontin mRNA expression in HL-60 cells is independent of differentiation
    • Atkins, K. B., Simpson, R. U., Somerman, M. J. (1997) Stimulation of osteopontin mRNA expression in HL-60 cells is independent of differentiation. Arch. Biochem. Biophys. 343, 157-163.
    • (1997) Arch. Biochem. Biophys. , vol.343 , pp. 157-163
    • Atkins, K.B.1    Simpson, R.U.2    Somerman, M.J.3
  • 31
    • 0028981753 scopus 로고
    • The peri-κ B site mediates human immunodeficiency virus type 2 enhancer activation in monocytes but not in T cells
    • Clark, N. M., Hannibal, M. C., Markovitz, D. M. (1995) The peri-κ B site mediates human immunodeficiency virus type 2 enhancer activation in monocytes but not in T cells. J. Virol. 69, 4854-4862.
    • (1995) J. Virol. , vol.69 , pp. 4854-4862
    • Clark, N.M.1    Hannibal, M.C.2    Markovitz, D.M.3
  • 32
    • 0027318624 scopus 로고
    • Differential regulation of the human immunodeficiency virus type 2 enhancer in monocytes at various stages of differentiation
    • Hilfinger, J. M., Clark, N., Smith, M., Robinson, K., Markovitz, D. M. (1993) Differential regulation of the human immunodeficiency virus type 2 enhancer in monocytes at various stages of differentiation. J. Virol. 67, 4448-4453.
    • (1993) J. Virol. , vol.67 , pp. 4448-4453
    • Hilfinger, J.M.1    Clark, N.2    Smith, M.3    Robinson, K.4    Markovitz, D.M.5
  • 33
    • 0024385637 scopus 로고
    • Enhanced transfection efficiency and improved cell survival after electroporation of G2/M-synchronized cells and treatment with sodium butyrate
    • Goldstein, S., Fordis, C. M., Howard, B. H. (1989) Enhanced transfection efficiency and improved cell survival after electroporation of G2/M-synchronized cells and treatment with sodium butyrate. Nucleic Acids Res. 17, 3959-3971.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 3959-3971
    • Goldstein, S.1    Fordis, C.M.2    Howard, B.H.3
  • 34
    • 0023893330 scopus 로고
    • +)-ATPase activity expressed in mouse L cells by transfection with DNA encoding the alpha-subunit of an avian sodium pump
    • +)-ATPase activity expressed in mouse L cells by transfection with DNA encoding the alpha-subunit of an avian sodium pump. J. Biol. Chem. 263, 4347-4354.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4347-4354
    • Takeyasu, K.1    Tamkun, M.M.2    Renaud, K.J.3    Fambrough, D.M.4
  • 35
    • 0025185463 scopus 로고
    • Induction of apoptosis (programmed cell death) in human leukemic HL-60 cells by inhibition of RNA or protein synthesis
    • Martin, S. J., Lennon, S. V., Bonham, A. M., Cotter, T. G. (1990) Induction of apoptosis (programmed cell death) in human leukemic HL-60 cells by inhibition of RNA or protein synthesis. J. Immunol. 145, 1859-1867.
    • (1990) J. Immunol. , vol.145 , pp. 1859-1867
    • Martin, S.J.1    Lennon, S.V.2    Bonham, A.M.3    Cotter, T.G.4
  • 36
    • 0027772540 scopus 로고
    • The molecular and genetic dissection of the retinoid signalling pathway
    • Chambon, P. (1993) The molecular and genetic dissection of the retinoid signalling pathway. Gene 135, 223-228.
    • (1993) Gene , vol.135 , pp. 223-228
    • Chambon, P.1
  • 37
    • 0029805717 scopus 로고    scopus 로고
    • 3-and retinoic acid-induced monocytic differentiation: Interactions between the endogenous vitamin retinoid X receptors in U-937 cells
    • 3-and Retinoic acid-induced monocytic differentiation: Interactions between the endogenous vitamin retinoid X receptors in U-937 cells. Cell Growth Diff. 7, 1239-1249.
    • (1996) Cell Growth Diff. , vol.7 , pp. 1239-1249
    • Botling, J.1    Oberg, F.2    Torma, H.3    Tuohimaa, P.4    Blauer, M.5    Nilsson, K.6
  • 38
    • 0030027490 scopus 로고    scopus 로고
    • Selective effects of ligands on vitamin D3 receptor-and retinoid X receptor-mediated gene activation in vivo
    • Lemon, B. D., Freedman, L. P. (1996) Selective effects of ligands on vitamin D3 receptor-and retinoid X receptor-mediated gene activation in vivo. Mol. Cell Biol. 16, 1006-1016.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1006-1016
    • Lemon, B.D.1    Freedman, L.P.2
  • 39
    • 0027319177 scopus 로고
    • Characterization of the cathepsin B gene and multiple mRNAs in human tissues: Evidence for alternative splicing of cathepsin B pre-mRNA
    • Gong, Q., Chan, S. J., Bajkowski, A. S., Steiner, D. F., Frankfater, A. (1993) Characterization of the cathepsin B gene and multiple mRNAs in human tissues: evidence for alternative splicing of cathepsin B pre-mRNA. DNA Cell Biol. 12, 299-309.
    • (1993) DNA Cell Biol. , vol.12 , pp. 299-309
    • Gong, Q.1    Chan, S.J.2    Bajkowski, A.S.3    Steiner, D.F.4    Frankfater, A.5
  • 40
    • 0029831908 scopus 로고    scopus 로고
    • Gamma interferon induced increases in intracellular cathepsin B activity in PMA primed THP-1 cells are blocked by inhibitors of protein kinase C
    • Li, Q., Bever, C. T. (1996) Gamma interferon induced increases in intracellular cathepsin B activity in PMA primed THP-1 cells are blocked by inhibitors of protein kinase C. Immunopharmacol. Immunotoxicol. 18, 375.
    • (1996) Immunopharmacol. Immunotoxicol. , vol.18 , pp. 375
    • Li, Q.1    Bever, C.T.2
  • 41
    • 0029026791 scopus 로고
    • Regulation of cathepsin D gene expression in HL-60 cells by retinoic acid and calcitriol
    • Atkins, K. B., Troen, B. R. (1995) Regulation of cathepsin D gene expression in HL-60 cells by retinoic acid and calcitriol. Cell Growth Diff. 6, 871-877.
    • (1995) Cell Growth Diff. , vol.6 , pp. 871-877
    • Atkins, K.B.1    Troen, B.R.2
  • 42
    • 0025271098 scopus 로고
    • Retinoic acid-induced granulocytic differentiation of HL-60 myeloid leukemia cells is mediated directly through the retinoic acid receptor (RAR-alpha)
    • Collins, S. J., Robertson, K. A., Mueller, L. (1990) Retinoic acid-induced granulocytic differentiation of HL-60 myeloid leukemia cells is mediated directly through the retinoic acid receptor (RAR-alpha). Mol. Cell Biol. 10, 2154-2163.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 2154-2163
    • Collins, S.J.1    Robertson, K.A.2    Mueller, L.3
  • 43
    • 84995851395 scopus 로고
    • Sensitive and specific detection of retinoid receptor subtype proteins in cultured cell and tumor extracts
    • Titcomb, M. W., Gottardis, M. M., Pike, J. W., Allegretto, E. A. (1994) Sensitive and specific detection of retinoid receptor subtype proteins in cultured cell and tumor extracts. Mol. Endocrinol. 8, 870-877.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 870-877
    • Titcomb, M.W.1    Gottardis, M.M.2    Pike, J.W.3    Allegretto, E.A.4
  • 44
    • 0025854175 scopus 로고
    • Differentiation-related regulation of 1,25-dihydroxyvitamin D3 receptor mRNA in human leukaemia cells HL-60
    • Pan, P., Reddy, K., Lee, S., Studzinski, G. P. (1991) Differentiation-related regulation of 1,25-dihydroxyvitamin D3 receptor mRNA in human leukaemia cells HL-60. Cell Prolif. 24, 159-170.
    • (1991) Cell Prolif. , vol.24 , pp. 159-170
    • Pan, P.1    Reddy, K.2    Lee, S.3    Studzinski, G.P.4
  • 45
    • 0020265220 scopus 로고
    • 1 alpha,25-Dihydroxycholecalciferol and a human myeloid leukaemia cell line (HL-60)
    • Tanaka, H., Abe, E., Miyaura, C., Kuribayashi, T., Konno, K., Nishii, Y., Suda, T. (1982) 1 alpha,25-Dihydroxycholecalciferol and a human myeloid leukaemia cell line (HL-60). Biochem. J. 204, 713-719.
    • (1982) Biochem. J. , vol.204 , pp. 713-719
    • Tanaka, H.1    Abe, E.2    Miyaura, C.3    Kuribayashi, T.4    Konno, K.5    Nishii, Y.6    Suda, T.7
  • 46
    • 0031935060 scopus 로고    scopus 로고
    • Truncation of Spl transcription factor by myeloblastin in undifferentiated HL60 cells
    • Rao, J., Zhang, F., Donnelly, R. J., Spector, N. L., Studzinski, G. P. (1998) Truncation of Spl transcription factor by myeloblastin in undifferentiated HL60 cells. J. Cell Physiol. 175, 121-128.
    • (1998) J. Cell Physiol. , vol.175 , pp. 121-128
    • Rao, J.1    Zhang, F.2    Donnelly, R.J.3    Spector, N.L.4    Studzinski, G.P.5
  • 47
    • 0026710374 scopus 로고
    • Two cytotoxic cell proteinase genes are differentially sensitive to sodium butyrate
    • Fregeau, C. J., Helgason, C. D., Bleackley, R. C. (1992) Two cytotoxic cell proteinase genes are differentially sensitive to sodium butyrate. Nucleic Acids Res. 20, 3113-3119.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3113-3119
    • Fregeau, C.J.1    Helgason, C.D.2    Bleackley, R.C.3
  • 48
    • 0028787420 scopus 로고
    • Granulocyte-macrophage colony-stimulating factor, phorbol ester, and sodium butyrate induce the CDllc integrin gene promoter activity during myeloid cell differentiation
    • Rubio, M. A., Lopez-Rodriguez, C., Nueda, A., Aller, P., Armesilla, A. L., Vega, M. A., Corbi, A. L. (1995) Granulocyte-macrophage colony-stimulating factor, phorbol ester, and sodium butyrate induce the CDllc integrin gene promoter activity during myeloid cell differentiation. Blood 86, 3715-3724.
    • (1995) Blood , vol.86 , pp. 3715-3724
    • Rubio, M.A.1    Lopez-Rodriguez, C.2    Nueda, A.3    Aller, P.4    Armesilla, A.L.5    Vega, M.A.6    Corbi, A.L.7
  • 49
    • 0029785689 scopus 로고    scopus 로고
    • Differential expression and butyrate response of human alkaline phosphatase genes are mediated by upstream DNA elements
    • Park, C., Chamberlin, M. E., Pan, C. J., Chou, J. Y. (1996) Differential expression and butyrate response of human alkaline phosphatase genes are mediated by upstream DNA elements. Biochemistry 35, 9807-9814.
    • (1996) Biochemistry , vol.35 , pp. 9807-9814
    • Park, C.1    Chamberlin, M.E.2    Pan, C.J.3    Chou, J.Y.4
  • 50
    • 0017767153 scopus 로고
    • n-Butyrate causes histone modification in HeLa and friend erythroleukaemia cells
    • Riggs, M. G., Whittaker, R. G., Neumann, J. R., Ingram, V. M. (1977) n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells. Nature 268, 462-464.
    • (1977) Nature , vol.268 , pp. 462-464
    • Riggs, M.G.1    Whittaker, R.G.2    Neumann, J.R.3    Ingram, V.M.4
  • 51
    • 0020025385 scopus 로고
    • Effects of sodium butyrate, a new pharmacological agent, on cells in culture
    • Kruh, J. (1982) Effects of sodium butyrate, a new pharmacological agent, on cells in culture. Mol. Cell. Biochem. 42, 65-82.
    • (1982) Mol. Cell. Biochem. , vol.42 , pp. 65-82
    • Kruh, J.1
  • 52
    • 0026697332 scopus 로고
    • Scaffold-attached regions (SAR elements) mediate transcriptional effects due to butyrate
    • Klehr, D., Schlake, T., Maass, K., Bode, J. (1992) Scaffold-attached regions (SAR elements) mediate transcriptional effects due to butyrate. Biochemistry 31, 3222-3229.
    • (1992) Biochemistry , vol.31 , pp. 3222-3229
    • Klehr, D.1    Schlake, T.2    Maass, K.3    Bode, J.4
  • 53
    • 0026515651 scopus 로고
    • Effects of sodium butyrate on 1,25-dihydroxyvitamin D3 receptor activity in primary chick kidney cells
    • Maiyar, A. C., Norman, A. W, (1992) Effects of sodium butyrate on 1,25-dihydroxyvitamin D3 receptor activity in primary chick kidney cells. Mol. Cell. Endocrinol. 84, 99-107.
    • (1992) Mol. Cell. Endocrinol. , vol.84 , pp. 99-107
    • Maiyar, A.C.1    Norman, A.W.2
  • 54
    • 0029829231 scopus 로고    scopus 로고
    • Novel role for Spl in phorbol ester enhancement of human platelet thromboxane receptor gene expression
    • 19%
    • D'Angelo, D. D., Oliver, B. G., Davis, M. G., McCluskey, T. S., Dorn, G. W. (19%) Novel role for Spl in phorbol ester enhancement of human platelet thromboxane receptor gene expression. J. Biol. Chem. 271, 19696-19704.
    • J. Biol. Chem. , vol.271 , pp. 19696-19704
    • D'Angelo, D.D.1    Oliver, B.G.2    Davis, M.G.3    McCluskey, T.S.4    Dorn, G.W.5
  • 55
    • 0025139398 scopus 로고
    • HL-60 cells induced to differentiate towards neutrophils subsequently die via apoptosis
    • Martin, S. J., Bradley, J. G., Cotter, T. G. (1990) HL-60 cells induced to differentiate towards neutrophils subsequently die via apoptosis. Clin. Exp. Immunol. 79, 448-453.
    • (1990) Clin. Exp. Immunol. , vol.79 , pp. 448-453
    • Martin, S.J.1    Bradley, J.G.2    Cotter, T.G.3


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