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Volumn 59, Issue 5, 1999, Pages 315-324

Retinoylation of proteins in rat hepatocytes following uptake of chylomicron remnant retinyl ester

Author keywords

Covalent protein modification; Lipoproteins; Parenchymal liver cells; Vitamin A

Indexed keywords

ALCOHOL; CHYLOMICRON; CITRAL; PROTEIN; RETINOIC ACID; RETINOID; RETINOL; RETINOL ESTER; TRITIUM;

EID: 0032833632     PISSN: 00365513     EISSN: None     Source Type: Journal    
DOI: 10.1080/00365519950185508     Document Type: Article
Times cited : (2)

References (38)
  • 2
    • 0000783611 scopus 로고
    • Role of nuclear retinoic acid receptors in the regulation of gene expression
    • Blomhoff R, editor. New York: Marcel Dekker Inc.
    • Kastner P, Chambon P, Leid M. Role of nuclear retinoic acid receptors in the regulation of gene expression. In: Blomhoff R, editor. Vitamin A in health and disease. New York: Marcel Dekker Inc., 1994: 189-238.
    • (1994) Vitamin A in Health and Disease , pp. 189-238
    • Kastner, P.1    Chambon, P.2    Leid, M.3
  • 3
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf DJ, Evans RM. The RXR heterodimers and orphan receptors. Cell 1995; 83: 841-50.
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 5
    • 0000874137 scopus 로고
    • Vision
    • Blomhoff R, editor. New York: Marcel Dekker Inc.
    • Rando RR. Vision. In: Blomhoff R, editor. Vitamin A in health and disease. New York: Marcel Dekker Inc., 1994: 503-29.
    • (1994) Vitamin A in Health and Disease , pp. 503-529
    • Rando, R.R.1
  • 6
    • 0024314622 scopus 로고
    • The stereospecific suicide inhibition of human melanoma thioredoxin reductase by 13-cis-retinoic acid
    • Schallreuter KU, Wood JM. The stereospecific suicide inhibition of human melanoma thioredoxin reductase by 13-cis-retinoic acid. Biochem Biophys Res Commun 1989; 160: 573-9.
    • (1989) Biochem Biophys Res Commun , vol.160 , pp. 573-579
    • Schallreuter, K.U.1    Wood, J.M.2
  • 7
    • 0024492833 scopus 로고
    • Retinoic acid is a modulator of thyroid hormone activation of Ca2+-ATPase in the human erythrocyte membrane
    • Smith TJ, Davis FB, Davis PJ. Retinoic acid is a modulator of thyroid hormone activation of Ca2+-ATPase in the human erythrocyte membrane. J Biol Chem 1989; 264: 687-9.
    • (1989) J Biol Chem , vol.264 , pp. 687-689
    • Smith, T.J.1    Davis, F.B.2    Davis, P.J.3
  • 8
    • 0026755156 scopus 로고
    • Stereochemical requirements for the modulation by retinoic acid of thyroid hormone activation of Ca(2+)-ATPase and binding at the human erythrocyte membrane
    • Smith TJ, Davis FB, Davis PJ. Stereochemical requirements for the modulation by retinoic acid of thyroid hormone activation of Ca(2+)-ATPase and binding at the human erythrocyte membrane. Biochem J 1992; 284: 583-7.
    • (1992) Biochem J , vol.284 , pp. 583-587
    • Smith, T.J.1    Davis, F.B.2    Davis, P.J.3
  • 9
    • 0024523883 scopus 로고
    • Retinoic acid acylation (retinoylation) of a nuclear protein in the human acute myeloid leukemia cell line HL60
    • Takahashi N, Breitman TR. Retinoic acid acylation (retinoylation) of a nuclear protein in the human acute myeloid leukemia cell line HL60. J Biol Chem 1989; 264: 5159-63.
    • (1989) J Biol Chem , vol.264 , pp. 5159-5163
    • Takahashi, N.1    Breitman, T.R.2
  • 10
    • 0024803738 scopus 로고
    • Covalent binding of 17 beta-estradiol and retinoic acid to proteins in the human breast cancer cell line MCF-7
    • Takahashi N, Breitman TR. Covalent binding of 17 beta-estradiol and retinoic acid to proteins in the human breast cancer cell line MCF-7. In Vitro Cell Dev Biol 1989; 25: 1199-200.
    • (1989) In Vitro Cell Dev Biol , vol.25 , pp. 1199-1200
    • Takahashi, N.1    Breitman, T.R.2
  • 11
    • 0025981994 scopus 로고
    • Retinoylation of proteins in leukemia, embryonal carcinoma, and normal kidney cell lines: Differences associated with differential responses to retinoic acid
    • Takahashi N, Breitman TR. Retinoylation of proteins in leukemia, embryonal carcinoma, and normal kidney cell lines: differences associated with differential responses to retinoic acid. Arch Biochem Biophys 1991; 285: 105-10.
    • (1991) Arch Biochem Biophys , vol.285 , pp. 105-110
    • Takahashi, N.1    Breitman, T.R.2
  • 12
    • 0026480957 scopus 로고
    • The covalent labeling of proteins by 17 beta-estradiol, retinoic acid, and progesterone in the human breast cancer cell lines MCF-7 and MCF-7/AdrR
    • Takahashi N, Breitman TR. The covalent labeling of proteins by 17 beta-estradiol, retinoic acid, and progesterone in the human breast cancer cell lines MCF-7 and MCF-7/AdrR. J Steroid Biochem Mol Biol 1992; 43: 489-97.
    • (1992) J Steroid Biochem Mol Biol , vol.43 , pp. 489-497
    • Takahashi, N.1    Breitman, T.R.2
  • 13
    • 0028021692 scopus 로고
    • Retinoylation of vimentin in the human myeloid leukemia cell line HL60
    • Takahashi N, Breitman TR. Retinoylation of vimentin in the human myeloid leukemia cell line HL60. J Biol Chem 1994; 269: 5913-7.
    • (1994) J Biol Chem , vol.269 , pp. 5913-5917
    • Takahashi, N.1    Breitman, T.R.2
  • 14
    • 0001291406 scopus 로고
    • Retinoylation of proteins in mammalian cells
    • Blomhoff R, editor. New York: Marcel Dekker Inc.
    • Takahashi N, Breitman TR. Retinoylation of proteins in mammalian cells. In: Blomhoff R, editor. Vitamin A in health and disease. New York: Marcel Dekker Inc., 1994: 257-73.
    • (1994) Vitamin A in Health and Disease , pp. 257-273
    • Takahashi, N.1    Breitman, T.R.2
  • 15
    • 0026042915 scopus 로고
    • Retinoylation of cytokeratins in normal human epidermal keratinocytes
    • Takahashi N, Jetten AM, Breitman TR. Retinoylation of cytokeratins in normal human epidermal keratinocytes. Biochem Biophys Res Commun 1991; 180: 393-400.
    • (1991) Biochem Biophys Res Commun , vol.180 , pp. 393-400
    • Takahashi, N.1    Jetten, A.M.2    Breitman, T.R.3
  • 16
    • 0026004738 scopus 로고
    • Retinoylation of the cAMP-binding regulatory subunits of type I and type II cAMP-dependent protein kinases in HL60 cells
    • Takahashi N, Liapi C, Anderson WB, Breitman TR. Retinoylation of the cAMP-binding regulatory subunits of type I and type II cAMP-dependent protein kinases in HL60 cells. Arch Biochem Biophys 1991; 290: 293-302.
    • (1991) Arch Biochem Biophys , vol.290 , pp. 293-302
    • Takahashi, N.1    Liapi, C.2    Anderson, W.B.3    Breitman, T.R.4
  • 18
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • Casey PJ. Protein lipidation in cell signaling. Science 1995; 268: 221-5.
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 19
    • 0029926257 scopus 로고    scopus 로고
    • Retinoylation of the type II cAMP-binding regulatory subunit of cAMP-dependent protein kinase is increased in psoriatic human fibroblasts
    • Tournier S, Raynaud F, Gerbaud P, Lohmann SM, Anderson WB, Evain-Brion D. Retinoylation of the type II cAMP-binding regulatory subunit of cAMP-dependent protein kinase is increased in psoriatic human fibroblasts. J Cell Physiol. 1996; 167: 196-203.
    • (1996) J Cell Physiol , vol.167 , pp. 196-203
    • Tournier, S.1    Raynaud, F.2    Gerbaud, P.3    Lohmann, S.M.4    Anderson, W.B.5    Evain-Brion, D.6
  • 21
    • 0029904181 scopus 로고    scopus 로고
    • Retinoids increase human apolipoprotein A-II expression through activation of the retinoid X receptor but not the retinoic acid receptor
    • Vu-Dac N, Schoonjans K, Kosykh V, Dallongeville J, Heyman RA, Staels B, Auwerx J. Retinoids increase human apolipoprotein A-II expression through activation of the retinoid X receptor but not the retinoic acid receptor. Mol Cell Biol 1996; 16: 3350-60.
    • (1996) Mol Cell Biol , vol.16 , pp. 3350-3360
    • Vu-Dac, N.1    Schoonjans, K.2    Kosykh, V.3    Dallongeville, J.4    Heyman, R.A.5    Staels, B.6    Auwerx, J.7
  • 22
    • 0029074474 scopus 로고
    • Regulation of human apolipoprotein A-I expression in Caco-2 and HepG2 cells by all-trans and 9-cis retinoic acids
    • Giller T, Hennes U, Kempen HJ. Regulation of human apolipoprotein A-I expression in Caco-2 and HepG2 cells by all-trans and 9-cis retinoic acids. J Lipid Res 1995; 36: 1021-8.
    • (1995) J Lipid Res , vol.36 , pp. 1021-1028
    • Giller, T.1    Hennes, U.2    Kempen, H.J.3
  • 23
    • 0028960119 scopus 로고
    • 9-cis-retinoic acid is more effective than all-trans-retinoic acid in upregulating expression of the alpha-fetoprotein gene
    • Wan YJ, Pan T, Wang L, Locker J, Wu TC. 9-cis-retinoic acid is more effective than all-trans-retinoic acid in upregulating expression of the alpha-fetoprotein gene. J Mol Endocrinol 1995; 14: 101-8.
    • (1995) J Mol Endocrinol , vol.14 , pp. 101-108
    • Wan, Y.J.1    Pan, T.2    Wang, L.3    Locker, J.4    Wu, T.C.5
  • 24
    • 0029098696 scopus 로고
    • Retinoids stimulate fibrinogen production both in vitro (hepatocytes) and in vivo. Induction requires activation of the retinoid X receptor
    • Nicodeme E, Nicaud M, Issandou M. Retinoids stimulate fibrinogen production both in vitro (hepatocytes) and in vivo. Induction requires activation of the retinoid X receptor. Arterioscler Thromb Vasc Biol 1995; 15: 1660-7.
    • (1995) Arterioscler Thromb Vasc Biol , vol.15 , pp. 1660-1667
    • Nicodeme, E.1    Nicaud, M.2    Issandou, M.3
  • 25
    • 0026688249 scopus 로고
    • Effect of retinoid status on alpha, beta and gamma retinoic acid receptor mRNA levels in various rat tissues
    • Kato S, Mano H, Kumazawa T, Yoshizawa Y, Kojima R, Masushige S. Effect of retinoid status on alpha, beta and gamma retinoic acid receptor mRNA levels in various rat tissues. Biochem J 1992; 286: 755-60.
    • (1992) Biochem J , vol.286 , pp. 755-760
    • Kato, S.1    Mano, H.2    Kumazawa, T.3    Yoshizawa, Y.4    Kojima, R.5    Masushige, S.6
  • 26
    • 0025935588 scopus 로고
    • Vitamin A metabolism: New perspectives on absorption, transport, and storage
    • Blomhoff R, Green MH, Green JB, Berg T, Norum KR. Vitamin A metabolism: new perspectives on absorption, transport, and storage. Physiol Rev 1991; 71: 951-90.
    • (1991) Physiol Rev , vol.71 , pp. 951-990
    • Blomhoff, R.1    Green, M.H.2    Green, J.B.3    Berg, T.4    Norum, K.R.5
  • 27
    • 0015257670 scopus 로고
    • A simplified method of cannulating the intestinal lymphatic of the rat
    • Warshaw AL. A simplified method of cannulating the intestinal lymphatic of the rat. Gut 1972; 13: 66-7.
    • (1972) Gut , vol.13 , pp. 66-67
    • Warshaw, A.L.1
  • 28
    • 0024528865 scopus 로고
    • Uptake of retinyl ester in HL-60 cells via the low-density-lipoprotein-receptor pathway
    • Wathne KO, Carlander B, Norum KR, Blomhoff R. Uptake of retinyl ester in HL-60 cells via the low-density-lipoprotein-receptor pathway. Biochem J 1989; 257: 239-44.
    • (1989) Biochem J , vol.257 , pp. 239-244
    • Wathne, K.O.1    Carlander, B.2    Norum, K.R.3    Blomhoff, R.4
  • 29
    • 0015847114 scopus 로고
    • Quantitative determination of serum triglycerides by the use of enzymes
    • Bucolo G, David H. Quantitative determination of serum triglycerides by the use of enzymes. Clin Chem 1973; 19: 476-482.
    • (1973) Clin Chem , vol.19 , pp. 476-482
    • Bucolo, G.1    David, H.2
  • 30
    • 0025690712 scopus 로고
    • Isolation and cultivation of rat liver stellate cells
    • Blomhoff R, Berg T. Isolation and cultivation of rat liver stellate cells. Methods Enzymol 1990; 190: 58-71.
    • (1990) Methods Enzymol , vol.190 , pp. 58-71
    • Blomhoff, R.1    Berg, T.2
  • 31
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG, Dyer WJ. A rapid method of total lipid extraction and purification. Can J Biochem Physiol 1959; 37: 911-17.
    • (1959) Can J Biochem Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 32
    • 0025598326 scopus 로고
    • Retinoic acid acylation: Retinoylation
    • Takahashi N, Breitman TR. Retinoic acid acylation: retinoylation. Methods Enzymol 1990; 189: 233-8.
    • (1990) Methods Enzymol , vol.189 , pp. 233-238
    • Takahashi, N.1    Breitman, T.R.2
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0023218322 scopus 로고
    • Terminal-group oxidation of retinol by mouse epidermis. Inhibition in vitro and in vivo
    • Connor MJ, Smit MH. Terminal-group oxidation of retinol by mouse epidermis. Inhibition in vitro and in vivo. Biochem J 1987; 244: 489-92.
    • (1987) Biochem J , vol.244 , pp. 489-492
    • Connor, M.J.1    Smit, M.H.2
  • 35
    • 0030062208 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia coli. Recognition of retinol as substate
    • Wang X, Penzes P, Napoli JL. Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia coli. Recognition of retinol as substate. J Biol Chem 1996; 271: 16288-93.
    • (1996) J Biol Chem , vol.271 , pp. 16288-16293
    • Wang, X.1    Penzes, P.2    Napoli, J.L.3
  • 36
    • 0023877571 scopus 로고
    • Retinol bound to physiological carrier molecules regulates growth and differentiation of myeloid leukemic cells
    • Wathne KO, Norum KR, Smeland E, Blomhoff R. Retinol bound to physiological carrier molecules regulates growth and differentiation of myeloid leukemic cells. J Biol Chem 1988; 263: 8691-5.
    • (1988) J Biol Chem , vol.263 , pp. 8691-8695
    • Wathne, K.O.1    Norum, K.R.2    Smeland, E.3    Blomhoff, R.4
  • 37
    • 0028920237 scopus 로고
    • Endogenous distribution of retinoids during normal development and teratogenesis in the mouse embryo
    • Horton C, Maden M. Endogenous distribution of retinoids during normal development and teratogenesis in the mouse embryo. Dev Dyn 1995; 202: 312-23.
    • (1995) Dev Dyn , vol.202 , pp. 312-323
    • Horton, C.1    Maden, M.2


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