메뉴 건너뛰기




Volumn 43, Issue 1, 2002, Pages 90-102

Induction of histone acetylation and inhibition of growth of mouse erythroleukemia cells by S-allylmercaptocysteine

Author keywords

[No Author keywords available]

Indexed keywords

ALLICIN; ALLYL ISOTHIOCYANATE; BUTYRIC ACID DERIVATIVE; CYSTEINE DERIVATIVE; ENZYME INHIBITOR; HISTONE; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; PROTEASOME INHIBITOR; S ALLYLCYSTEINE; S ALLYLMERCAPTOCYSTEINE; SULFONE DERIVATIVE; THIOL DERIVATIVE; UNCLASSIFIED DRUG; ACYLTRANSFERASE; ALLYL COMPOUND; ANTINEOPLASTIC AGENT; BENZYLOXYCARBONYLLEUCYL LEUCYL LEUCINE ALDEHYDE; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CYSTEINE; DRUG DERIVATIVE; LEUPEPTIN; S-ALLYLCYSTEINE; S-ALLYLMERCAPTOCYSTEINE; SACCHAROMYCES CEREVISIAE PROTEIN; SULFINIC ACID DERIVATIVE;

EID: 0036437194     PISSN: 01635581     EISSN: None     Source Type: Journal    
DOI: 10.1207/S15327914NC431_11     Document Type: Article
Times cited : (82)

References (36)
  • 1
    • 0032702598 scopus 로고    scopus 로고
    • Role of covalent modifications of histones in regulating gene expression
    • Spencer VA and Davie JR: Role of covalent modifications of histones in regulating gene expression. Gene 240, 1-12, 1999.
    • (1999) Gene , vol.240 , pp. 1-12
    • Spencer, V.A.1    Davie, J.R.2
  • 2
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD and Allis CD: The language of covalent histone modifications. Nature 403, 41-45, 2000.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 3
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner BM: Histone acetylation and an epigenetic code. Bioessays 22, 836-845, 2000.
    • (2000) Bioessays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 4
    • 0030744052 scopus 로고    scopus 로고
    • Differentiating and growth inhibitory effects of diallyl disulfide on cancer cells
    • Lea MA and Ayyala US: Differentiating and growth inhibitory effects of diallyl disulfide on cancer cells. Int J Oncol 11, 181-186, 1997.
    • (1997) Int J Oncol , vol.11 , pp. 181-186
    • Lea, M.A.1    Ayyala, U.S.2
  • 5
    • 0033173102 scopus 로고    scopus 로고
    • Increased acetylation of histones induced by diallyl disulfide and structurally related molecules
    • Lea MA, Randolph VM, and Patel M: Increased acetylation of histones induced by diallyl disulfide and structurally related molecules. Int J Oncol 15, 347-352, 1999.
    • (1999) Int J Oncol , vol.15 , pp. 347-352
    • Lea, M.A.1    Randolph, V.M.2    Patel, M.3
  • 6
    • 0035876964 scopus 로고    scopus 로고
    • Induction of histone acetylation in mouse erythroleukemia cells by some organosulfur compounds including allyl isothiocyanate
    • Lea MA, Randolph VM, Lee JE, and DesBordes C: Induction of histone acetylation in mouse erythroleukemia cells by some organosulfur compounds including allyl isothiocyanate. Int J Cancer 92, 784-789, 2001.
    • (2001) Int J Cancer , vol.92 , pp. 784-789
    • Lea, M.A.1    Randolph, V.M.2    Lee, J.E.3    DesBordes, C.4
  • 7
    • 0022039421 scopus 로고
    • The chemistry of garlic and onions
    • Block E: The chemistry of garlic and onions. Sci Am 252, 114-119, 1985.
    • (1985) Sci Am , vol.252 , pp. 114-119
    • Block, E.1
  • 8
    • 0026756541 scopus 로고
    • The organosulfur chemistry of the genus Allium - Implications for the organic chemistry of sulfur
    • Block E: The organosulfur chemistry of the genus Allium - Implications for the organic chemistry of sulfur. Angew Chem Int Ed Engl 31, 1135-1178, 1992.
    • (1992) Angew Chem Int Ed Engl , vol.31 , pp. 1135-1178
    • Block, E.1
  • 9
    • 0017898940 scopus 로고
    • Suppression of histone deacetylation in vivo and in vitro by sodium butyrate
    • Boffa L, Vidali G, Mann RS, and Allfrey VG: Suppression of histone deacetylation in vivo and in vitro by sodium butyrate. J Biol Chem 253, 3364-3366, 1978.
    • (1978) J Biol Chem , vol.253 , pp. 3364-3366
    • Boffa, L.1    Vidali, G.2    Mann, R.S.3    Allfrey, V.G.4
  • 10
    • 0017809719 scopus 로고
    • Turnover of histone acetyl groups in cultured cells is inhibited by sodium butyrate
    • Reeves R and Candido EPM: Turnover of histone acetyl groups in cultured cells is inhibited by sodium butyrate. FEBS Lett 91, 117-120, 1978.
    • (1978) FEBS Lett , vol.91 , pp. 117-120
    • Reeves, R.1    Candido, E.P.M.2
  • 11
    • 0017864644 scopus 로고
    • The effect of sodium butyrate on histone modification
    • Sealy L and Chalkley R: The effect of sodium butyrate on histone modification. Cell 14, 115-121, 1978.
    • (1978) Cell , vol.14 , pp. 115-121
    • Sealy, L.1    Chalkley, R.2
  • 12
    • 0025872079 scopus 로고
    • Inhibition of cytochrome P450 2E1 by diallyl sulfide and its metabolites
    • Brady JF, Ishizaki H, Fukuto JM, Lin MC, Fadel A, et al.: Inhibition of cytochrome P450 2E1 by diallyl sulfide and its metabolites. Chem Res Toxicol 4, 642-647, 1991.
    • (1991) Chem Res Toxicol , vol.4 , pp. 642-647
    • Brady, J.F.1    Ishizaki, H.2    Fukuto, J.M.3    Lin, M.C.4    Fadel, A.5
  • 13
    • 0030992920 scopus 로고    scopus 로고
    • Metabolism of the chemopreventive agent diallyl sulfide to glutathione conjugates in rats
    • Jin L and Baillie TA: Metabolism of the chemopreventive agent diallyl sulfide to glutathione conjugates in rats. Chem Res Toxicol 10, 318-327, 1997.
    • (1997) Chem Res Toxicol , vol.10 , pp. 318-327
    • Jin, L.1    Baillie, T.A.2
  • 14
    • 0026517057 scopus 로고
    • Antiproliferative effect of the garlic compound S-allyl cysteine on human neuroblastoma cells in vitro
    • Welch C, Wuarin L, and Sidell N: Antiproliferative effect of the garlic compound S-allyl cysteine on human neuroblastoma cells in vitro. Cancer Lett 63, 211-219, 1992.
    • (1992) Cancer Lett , vol.63 , pp. 211-219
    • Welch, C.1    Wuarin, L.2    Sidell, N.3
  • 15
    • 0027392852 scopus 로고
    • Growth inhibition and modulation of cell markers of melanoma by S-allyl cysteine
    • Takeyama H, Hoon DSB, Saxton RE, Morton DL, and Irie RF: Growth inhibition and modulation of cell markers of melanoma by S-allyl cysteine. Oncology 50, 63-69, 1993.
    • (1993) Oncology , vol.50 , pp. 63-69
    • Takeyama, H.1    Hoon, D.S.B.2    Saxton, R.E.3    Morton, D.L.4    Irie, R.F.5
  • 16
    • 0028213389 scopus 로고
    • Thioallyl compounds: Potent inhibitors of cell proliferation
    • Lee ES, Steiner M, and Lin R: Thioallyl compounds: Potent inhibitors of cell proliferation. Biochim Biophys Acta 1221, 73-77, 1994.
    • (1994) Biochim Biophys Acta , vol.1221 , pp. 73-77
    • Lee, E.S.1    Steiner, M.2    Lin, R.3
  • 17
    • 0031057489 scopus 로고    scopus 로고
    • S-allylmercaptocysteine inhibits cell proliferation and reduces the viability of erythroleukemia, breast, and prostate cancer cell lines
    • Sigounas G, Hooker JL, Anagnostou A, and Steiner M: S-allylmercaptocysteine inhibits cell proliferation and reduces the viability of erythroleukemia, breast, and prostate cancer cell lines. Nutr Cancer 27, 186-191, 1997.
    • (1997) Nutr Cancer , vol.27 , pp. 186-191
    • Sigounas, G.1    Hooker, J.L.2    Anagnostou, A.3    Steiner, M.4
  • 18
    • 0030826223 scopus 로고    scopus 로고
    • Sallylmercaptocysteine, a stable thioallyl compound, induces apoptosis in erythroleukemia cell lines
    • Sigounas G, Hooker JL, Li W, Anagnostou A, and Steiner M: Sallylmercaptocysteine, a stable thioallyl compound, induces apoptosis in erythroleukemia cell lines. Nutr Cancer 28, 153-159, 1997.
    • (1997) Nutr Cancer , vol.28 , pp. 153-159
    • Sigounas, G.1    Hooker, J.L.2    Li, W.3    Anagnostou, A.4    Steiner, M.5
  • 19
    • 0012679602 scopus 로고    scopus 로고
    • Effects of garlic thioallyl derivatives on growth, glutathione concentration, and polyamine formation of human prostate carcinoma cells in culture
    • Pinto JT, Qiao C, Xing J, Rivlin RS, Protomastro ML, et al.: Effects of garlic thioallyl derivatives on growth, glutathione concentration, and polyamine formation of human prostate carcinoma cells in culture. Am J Clin Nutr 66, 398-405, 1997.
    • (1997) Am J Clin Nutr , vol.66 , pp. 398-405
    • Pinto, J.T.1    Qiao, C.2    Xing, J.3    Rivlin, R.S.4    Protomastro, M.L.5
  • 20
    • 0035863512 scopus 로고    scopus 로고
    • Anti-proliferative effects of S-allylmercaptocysteine on colon cancer cells when tested alone or in combination with sulindac sulfide
    • Shirin H, Pinto JT, Kawabata Y, Soh J-W, Delohery T, et al.: Anti-proliferative effects of S-allylmercaptocysteine on colon cancer cells when tested alone or in combination with sulindac sulfide. Cancer Res 61, 725-731, 2001.
    • (2001) Cancer Res , vol.61 , pp. 725-731
    • Shirin, H.1    Pinto, J.T.2    Kawabata, Y.3    Soh, J.-W.4    Delohery, T.5
  • 21
    • 0000116588 scopus 로고
    • The effect of allicin from garlic on tumor growth
    • DiPaolo JA and Carruthers C: The effect of allicin from garlic on tumor growth. Cancer Res 20, 431-434, 1960.
    • (1960) Cancer Res , vol.20 , pp. 431-434
    • DiPaolo, J.A.1    Carruthers, C.2
  • 22
    • 0003089632 scopus 로고    scopus 로고
    • The composition and chemistry of garlic cloves and processed garlic
    • Koch HP and Lawson LD (eds). Baltimore, MD: Williams & Wilkins
    • Lawson LD: The composition and chemistry of garlic cloves and processed garlic. In Garlic. The Science and Therapeutic Application of Allium Sativum L. and Related Species, Koch HP and Lawson LD (eds). Baltimore, MD: Williams & Wilkins, 1996, pp 37-107.
    • (1996) Garlic. The Science and Therapeutic Application of Allium Sativum L. and Related Species , pp. 37-107
    • Lawson, L.D.1
  • 23
    • 0028819490 scopus 로고
    • A spectrophotometric method for quantitative determination of allicin and total garlic thiosulfinates
    • Han J, Lawson L, Han G, and Han P: A spectrophotometric method for quantitative determination of allicin and total garlic thiosulfinates. Anal Biochem 225, 157-160, 1995.
    • (1995) Anal Biochem , vol.225 , pp. 157-160
    • Han, J.1    Lawson, L.2    Han, G.3    Han, P.4
  • 24
    • 0031865432 scopus 로고    scopus 로고
    • Induction of reporter gene expression by inhibitors of histone deacetylase
    • Lea MA and Randolph VM: Induction of reporter gene expression by inhibitors of histone deacetylase. Anticancer Res 18, 2717-2722, 1998.
    • (1998) Anticancer Res , vol.18 , pp. 2717-2722
    • Lea, M.A.1    Randolph, V.M.2
  • 25
    • 0028983190 scopus 로고
    • Discordant effects of butyrate analogues on erythroleukemia cell proliferation, differentiation and histone deacetylase
    • Lea MA and Tulsyan N: Discordant effects of butyrate analogues on erythroleukemia cell proliferation, differentiation and histone deacetylase. Anticancer Res 15, 879-884, 1995.
    • (1995) Anticancer Res , vol.15 , pp. 879-884
    • Lea, M.A.1    Tulsyan, N.2
  • 26
    • 0034634635 scopus 로고    scopus 로고
    • Rapid induction of histone hyperacetylation and cellular differentiation in human breast tumor cell lines following degradation of histone deacetylase-1
    • Zhou Q, Melkoumian ZK, Lucktong A, Moniwa M, Davie JR, et al.: Rapid induction of histone hyperacetylation and cellular differentiation in human breast tumor cell lines following degradation of histone deacetylase-1. J Biol Chem 275, 35256-35263, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 35256-35263
    • Zhou, Q.1    Melkoumian, Z.K.2    Lucktong, A.3    Moniwa, M.4    Davie, J.R.5
  • 27
    • 0342871691 scopus 로고    scopus 로고
    • Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: Effects on replication, transcription, translation, and the cellular stress response
    • Mimnaugh EG, Chen HY, Davie JR, Celis JE, and Neckers L: Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: Effects on replication, transcription, translation, and the cellular stress response. Biochemistry 36, 14418-14429, 1997.
    • (1997) Biochemistry , vol.36 , pp. 14418-14429
    • Mimnaugh, E.G.1    Chen, H.Y.2    Davie, J.R.3    Celis, J.E.4    Neckers, L.5
  • 30
    • 0035127032 scopus 로고    scopus 로고
    • A historical perspective on garlic and cancer
    • Milner JA: A historical perspective on garlic and cancer. J Nutr 131, 1027S-1031S, 2001.
    • (2001) J Nutr , vol.131
    • Milner, J.A.1
  • 31
    • 0034639280 scopus 로고    scopus 로고
    • Sallylmercaptoglutathione: The reaction product of allicin with glutathione possesses SH-modifying and antioxidant properties
    • Rabinkov A, Miron T, Mirelman D, Wilchek M, Glozman S, et al.: Sallylmercaptoglutathione: The reaction product of allicin with glutathione possesses SH-modifying and antioxidant properties. Biochim Biophys Acta 1499, 144-153, 2000.
    • (2000) Biochim Biophys Acta , vol.1499 , pp. 144-153
    • Rabinkov, A.1    Miron, T.2    Mirelman, D.3    Wilchek, M.4    Glozman, S.5
  • 33
    • 0035933731 scopus 로고    scopus 로고
    • Histone hyperacetylation induced by histone deacetylase inhibitors is not sufficient to cause growth inhibition in human dermal fibroblasts
    • Brinkmann H, Dahler AL, Popa C, Serewko MM, Parsons PG, et al.: Histone hyperacetylation induced by histone deacetylase inhibitors is not sufficient to cause growth inhibition in human dermal fibroblasts. J Biol Chem 276, 22491-22499, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 22491-22499
    • Brinkmann, H.1    Dahler, A.L.2    Popa, C.3    Serewko, M.M.4    Parsons, P.G.5
  • 34
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung P, Tanner G, Cheung WL, Sassone-Corsi P, Denu JM, et al.: Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol Cell 5, 905-915, 2000.
    • (2000) Mol Cell , vol.5 , pp. 905-915
    • Cheung, P.1    Tanner, G.2    Cheung, W.L.3    Sassone-Corsi, P.4    Denu, J.M.5
  • 35
    • 0033638105 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14
    • Lo W-S, Trievel RC, Rojas JR, Duggan L, Hsu J-Y, et al.: Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Mol Cell 5, 917-926, 2000.
    • (2000) Mol Cell , vol.5 , pp. 917-926
    • Lo, W.-S.1    Trievel, R.C.2    Rojas, J.R.3    Duggan, L.4    Hsu, J.-Y.5
  • 36
    • 0034730523 scopus 로고    scopus 로고
    • Rapid dephosphorylation of H1 histones after apoptosis induction
    • Kratzmeier M, Albig W, Hanecke K, and Doenecke D: Rapid dephosphorylation of H1 histones after apoptosis induction. J Biol Chem 275, 30478-30486, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 30478-30486
    • Kratzmeier, M.1    Albig, W.2    Hanecke, K.3    Doenecke, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.