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Volumn 55, Issue 2, 2004, Pages 179-191

Lecithin-cholesterol acyltransferase (LCAT) as a plasma glycoprotein: An overview

Author keywords

Cholesterol; Lipoproteins; N glycosylation; Serum glycoprotein; Site directed mutagenesis

Indexed keywords

CHOLESTEROL; DISEASES; ENZYMES; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; OLIGOMERS; PROTEINS; X RAY DIFFRACTION ANALYSIS;

EID: 0347270353     PISSN: 01448617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carbpol.2003.09.005     Document Type: Article
Times cited : (16)

References (151)
  • 1
    • 0032484133 scopus 로고    scopus 로고
    • Structural and functional properties of two mutants of lecithin-cholesterol acyltransferase (T123I and N228K)
    • Adimoolam S., Jin L., Grabbe E., Shieh J.J., Jonas A. Structural and functional properties of two mutants of lecithin-cholesterol acyltransferase (T123I and N228K). Journal of Biological Chemistry. 273:1998;32561-32567.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 32561-32567
    • Adimoolam, S.1    Jin, L.2    Grabbe, E.3    Shieh, J.J.4    Jonas, A.5
  • 3
  • 4
    • 0022573889 scopus 로고
    • Maturation and secretion of lipoprotein lipase in cultured adipose cells. II. Effects of tunicamycin on activation and secretion of the enzyme
    • Amri E.Z., Vannier C., Etienne J., Ailhaud G. Maturation and secretion of lipoprotein lipase in cultured adipose cells. II. Effects of tunicamycin on activation and secretion of the enzyme. Biochimica et Biophysica Acta. 875:1986;334-343.
    • (1986) Biochimica et Biophysica Acta , vol.875 , pp. 334-343
    • Amri, E.Z.1    Vannier, C.2    Etienne, J.3    Ailhaud, G.4
  • 5
    • 0018120222 scopus 로고
    • Human plasma lecithin: Cholesterol acyltransferase (characterization of cofactor-dependent phospholipase activity)
    • Aron L., Jones S., Fielding C.J. Human plasma lecithin: cholesterol acyltransferase (characterization of cofactor-dependent phospholipase activity). Journal of Biological Chemistry. 253:1978;7220-7226.
    • (1978) Journal of Biological Chemistry , vol.253 , pp. 7220-7226
    • Aron, L.1    Jones, S.2    Fielding, C.J.3
  • 6
    • 0025734840 scopus 로고
    • Lecithin:cholesterol acyltransferase deficiency and fish-eye disease
    • Assmann G., Eckardstein A., Funke H. Lecithin:cholesterol acyltransferase deficiency and fish-eye disease. Current Opinion in Lipidology. 2:1991;110-117.
    • (1991) Current Opinion in Lipidology , vol.2 , pp. 110-117
    • Assmann, G.1    Eckardstein, A.2    Funke, H.3
  • 7
    • 0033953321 scopus 로고    scopus 로고
    • Biochemical and compositional analyses of recombinant lecithin:cholesterol acyltransferase (LCAT) obtained from a hepatic source
    • Ayyobi A.F., Lacko A.G., Murray K., Nair M., Li M., Molhuizen H.O., Pritchard P.H. Biochemical and compositional analyses of recombinant lecithin:cholesterol acyltransferase (LCAT) obtained from a hepatic source. Biochimica et Biophysica Acta. 1484:2000;1-13.
    • (2000) Biochimica et Biophysica Acta , vol.1484 , pp. 1-13
    • Ayyobi, A.F.1    Lacko, A.G.2    Murray, K.3    Nair, M.4    Li, M.5    Molhuizen, H.O.6    Pritchard, P.H.7
  • 8
    • 0028909558 scopus 로고
    • Accelerated cholesteryl ester transfer and altered lipoprotein composition in diabetic cynomolgus monkeys
    • Bagdade J.D., Wagner J.D., Rudel L.L., Clarkson T.B. Accelerated cholesteryl ester transfer and altered lipoprotein composition in diabetic cynomolgus monkeys. Journal of Lipid Research. 36:1995;759-766.
    • (1995) Journal of Lipid Research , vol.36 , pp. 759-766
    • Bagdade, J.D.1    Wagner, J.D.2    Rudel, L.L.3    Clarkson, T.B.4
  • 9
    • 0021683698 scopus 로고
    • Effect of tunicamycin and monensin on secretion of thyroxine-binding globulin by cultured human hepatoma (Hep G2) cells
    • Bartalena L., Robbins J. Effect of tunicamycin and monensin on secretion of thyroxine-binding globulin by cultured human hepatoma (Hep G2) cells. Journal of Biological Chemistry. 259:1984;13610-13614.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 13610-13614
    • Bartalena, L.1    Robbins, J.2
  • 10
    • 0021367324 scopus 로고
    • Comparison of human plasma low and high-density lipoproteins as substrates for lecithin:cholesterol acyltransferase
    • Barter P.J., Hopkins G.J., Gorjatschko L. Comparison of human plasma low and high-density lipoproteins as substrates for lecithin:cholesterol acyltransferase. Biochimica et Biophysica Acta. 792:1984;1-5.
    • (1984) Biochimica et Biophysica Acta , vol.792 , pp. 1-5
    • Barter, P.J.1    Hopkins, G.J.2    Gorjatschko, L.3
  • 12
    • 0032920929 scopus 로고    scopus 로고
    • Evidence that lipid hydroperoxides inhibit plasma lecithin:cholesterol acyltransferase activity
    • Bielicki J.K., Forte T.M. Evidence that lipid hydroperoxides inhibit plasma lecithin:cholesterol acyltransferase activity. Journal of Lipid Research. 40:1999;948-954.
    • (1999) Journal of Lipid Research , vol.40 , pp. 948-954
    • Bielicki, J.K.1    Forte, T.M.2
  • 13
    • 0026487873 scopus 로고
    • Analysis of the binding and association of human intermediate density lipoproteins to HepG2 cells
    • Brissette L., Falstrault L. Analysis of the binding and association of human intermediate density lipoproteins to HepG2 cells. Biochimica et Biophysica Acta. 1165:1992;84-92.
    • (1992) Biochimica et Biophysica Acta , vol.1165 , pp. 84-92
    • Brissette, L.1    Falstrault, L.2
  • 14
    • 0029013289 scopus 로고
    • Absence of N-glycosylation at asparagine 43 in human lipoprotein lipase induces its accumulation in the rough endoplasmic reticulum and alters this cellular compartment
    • Buscá R., Pujana M.A., Pognonec P., Auwerx J., Deeb S.S., Reina M., Vilaró S. Absence of N-glycosylation at asparagine 43 in human lipoprotein lipase induces its accumulation in the rough endoplasmic reticulum and alters this cellular compartment. Journal of Lipid Research. 36:1995;939-951.
    • (1995) Journal of Lipid Research , vol.36 , pp. 939-951
    • Buscá, R.1    Pujana, M.A.2    Pognonec, P.3    Auwerx, J.4    Deeb, S.S.5    Reina, M.6    Vilaró, S.7
  • 16
    • 0031107560 scopus 로고    scopus 로고
    • Non-enzymatic glycosylation of lipoproteins in the pathogenesis of atherosclerosis in diabetics
    • Calvo C. Non-enzymatic glycosylation of lipoproteins in the pathogenesis of atherosclerosis in diabetics. Revista Medica de Chile. 125:1997;460-465.
    • (1997) Revista Medica de Chile , vol.125 , pp. 460-465
    • Calvo, C.1
  • 17
    • 0020065476 scopus 로고
    • Fish eye disease: A new familial condition with massive corneal opacities and dyslipoproteinaemia
    • Carlson L.A. Fish eye disease: a new familial condition with massive corneal opacities and dyslipoproteinaemia. European Journal of Clinical Investigation. 12:1982;41-53.
    • (1982) European Journal of Clinical Investigation , vol.12 , pp. 41-53
    • Carlson, L.A.1
  • 18
    • 0022347171 scopus 로고
    • Evidence for the presence in human plasma of lecithin: Cholesterol acyltransferase activity (beta-LCAT) specifically esterifying free cholesterol of combined pre-beta- and beta-lipoproteins. Studies of fish eye disease patients and control subjects
    • Carlson L.A., Holmquist L. Evidence for the presence in human plasma of lecithin: cholesterol acyltransferase activity (beta-LCAT) specifically esterifying free cholesterol of combined pre-beta- and beta-lipoproteins. Studies of fish eye disease patients and control subjects. Acta Medica Scandinavica. 218:1985;197-205.
    • (1985) Acta Medica Scandinavica , vol.218 , pp. 197-205
    • Carlson, L.A.1    Holmquist, L.2
  • 19
    • 84888960957 scopus 로고
    • Importance of the different steps of glycosylation for the activity and secretion of lipoprotein lipase in rat preadipocytes studied with monensin and tunicamycin
    • Chajek-Shaul T., Friedman G., Knobler H., Stein O., Etienne J., Stein Y. Importance of the different steps of glycosylation for the activity and secretion of lipoprotein lipase in rat preadipocytes studied with monensin and tunicamycin. Biochemical and Biophysical Research Communications. 837:1985;121-134.
    • (1985) Biochemical and Biophysical Research Communications , vol.837 , pp. 121-134
    • Chajek-Shaul, T.1    Friedman, G.2    Knobler, H.3    Stein, O.4    Etienne, J.5    Stein, Y.6
  • 20
    • 0029008887 scopus 로고
    • Secretion of active human lecithin-cholesterol acyltransferase by insect cells infected with a recombinant baculovirus
    • Chawla D., Owen J.S. Secretion of active human lecithin-cholesterol acyltransferase by insect cells infected with a recombinant baculovirus. Biochemical Journal. 309:1995;249-253.
    • (1995) Biochemical Journal , vol.309 , pp. 249-253
    • Chawla, D.1    Owen, J.S.2
  • 21
    • 0020564749 scopus 로고
    • Interspecies activation of lecithin-cholesterol acyltransferase by apolipoprotein A-I isolated from the plasma of humans, horses, sheep, goats and rabbits
    • Chen C.-H., Albers J.J. Interspecies activation of lecithin-cholesterol acyltransferase by apolipoprotein A-I isolated from the plasma of humans, horses, sheep, goats and rabbits. Biochimica et Biophysica Acta. 753:1983;40-46.
    • (1983) Biochimica et Biophysica Acta , vol.753 , pp. 40-46
    • Chen, C.-H.1    Albers, J.J.2
  • 22
    • 0021812168 scopus 로고
    • A rapid large-scale procedure for purification of lecithin-cholesterol acyltransferase from human and animal plasma
    • Chen C.-H., Albers J.J. A rapid large-scale procedure for purification of lecithin-cholesterol acyltransferase from human and animal plasma. Biochimica et Biophysica Acta. 834:1985;188-195.
    • (1985) Biochimica et Biophysica Acta , vol.834 , pp. 188-195
    • Chen, C.-H.1    Albers, J.J.2
  • 23
    • 0022462002 scopus 로고
    • Synthesis and secretion of lecithin:cholesterol acyltransferase by the human hepatoma cell line Hep-G2
    • Chen C.-H., Forte T.H., Cahoon B.E., Thrift R.N., Albers J.J. Synthesis and secretion of lecithin:cholesterol acyltransferase by the human hepatoma cell line Hep-G2. Biochimica et Biophysica Acta. 877:1986;433-439.
    • (1986) Biochimica et Biophysica Acta , vol.877 , pp. 433-439
    • Chen, C.-H.1    Forte, T.H.2    Cahoon, B.E.3    Thrift, R.N.4    Albers, J.J.5
  • 24
    • 0020526487 scopus 로고
    • Characterization of lecithin:cholesterol acyltransferase from human plasma. II. Physical properties of the enzyme
    • Chong K.-S., Hara S., Thompson R.E., Lacko A.G. Characterization of lecithin:cholesterol acyltransferase from human plasma. II. Physical properties of the enzyme. Biochimica et Biophysica Acta. 222:1983;553-560.
    • (1983) Biochimica et Biophysica Acta , vol.222 , pp. 553-560
    • Chong, K.-S.1    Hara, S.2    Thompson, R.E.3    Lacko, A.G.4
  • 25
    • 0035065367 scopus 로고    scopus 로고
    • Role of individual amino acids of apolipoprotein A-I in the activation of lecithin: Cholestrol acyltransferase and in HDL rearrangements
    • Cho K.H., Durbin D.M., Jonas A. Role of individual amino acids of apolipoprotein A-I in the activation of lecithin: cholestrol acyltransferase and in HDL rearrangements. Journal of Lipid Research. 42:2001;379-389.
    • (2001) Journal of Lipid Research , vol.42 , pp. 379-389
    • Cho, K.H.1    Durbin, D.M.2    Jonas, A.3
  • 26
    • 0018246098 scopus 로고
    • The effect of carbohydrate depletion on the properties of yeast external invertase
    • Chu F.K., Trimble R.B., Maley F. The effect of carbohydrate depletion on the properties of yeast external invertase. Journal of Biological Chemistry. 253:1978;8691-8693.
    • (1978) Journal of Biological Chemistry , vol.253 , pp. 8691-8693
    • Chu, F.K.1    Trimble, R.B.2    Maley, F.3
  • 27
    • 0018654389 scopus 로고
    • Isolation, properties and mechanism of in vitro action of lecithin:cholesterol acyltransferase from human plasma
    • Chung J., Abano D.A., Fless G.M., Scanu A.M. Isolation, properties and mechanism of in vitro action of lecithin:cholesterol acyltransferase from human plasma. Journal of Biological Chemistry. 254:1979;7456-7464.
    • (1979) Journal of Biological Chemistry , vol.254 , pp. 7456-7464
    • Chung, J.1    Abano, D.A.2    Fless, G.M.3    Scanu, A.M.4
  • 28
    • 0021276357 scopus 로고
    • Effects of compactin, mevalonate and low-density lipoprotein on 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity and low-density-lipoprotein-receptor activity in the human hepatoma cell line Hep G2
    • Cohen L.H., Griffoen M., Havekes L., Schouten D., Van-Hinsberg V., Kempen H.J. Effects of compactin, mevalonate and low-density lipoprotein on 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity and low-density-lipoprotein-receptor activity in the human hepatoma cell line Hep G2. Biochemical Journal. 222:1984;35-39.
    • (1984) Biochemical Journal , vol.222 , pp. 35-39
    • Cohen, L.H.1    Griffoen, M.2    Havekes, L.3    Schouten, D.4    Van-Hinsberg, V.5    Kempen, H.J.6
  • 29
    • 0025736106 scopus 로고
    • Effects of inhibitors of N-linked oligosaccharide processing on the secretion, and stability of lecithin: Cholesterol acyltransferase
    • Collet X., Fielding C.J. Effects of inhibitors of N-linked oligosaccharide processing on the secretion, and stability of lecithin: cholesterol acyltransferase. Biochemistry. 30:1991;3228-3234.
    • (1991) Biochemistry , vol.30 , pp. 3228-3234
    • Collet, X.1    Fielding, C.J.2
  • 30
    • 0027510950 scopus 로고
    • The effect of compounds associated with cigarette smoking on the secretion of lipoprotein lipid by HepG2 cells
    • Craig W.Y. The effect of compounds associated with cigarette smoking on the secretion of lipoprotein lipid by HepG2 cells. Biochimica et Biophysica Acta. 1165:1993;249-258.
    • (1993) Biochimica et Biophysica Acta , vol.1165 , pp. 249-258
    • Craig, W.Y.1
  • 31
    • 0021232897 scopus 로고
    • Lecithin:cholesterol acyltransferase and cholesteryl ester transfer activity from the isolated perfused rabbit liver
    • De Parscau L., Fielding P.E. Lecithin:cholesterol acyltransferase and cholesteryl ester transfer activity from the isolated perfused rabbit liver. Journal of Lipid Research. 25:1984;721-728.
    • (1984) Journal of Lipid Research , vol.25 , pp. 721-728
    • De Parscau, L.1    Fielding, P.E.2
  • 32
    • 0019345949 scopus 로고
    • Lecithin-cholesterol acyltransferase from human plasma
    • Doi Y., Nishida T. Lecithin-cholesterol acyltransferase from human plasma. Methods in Enzymololgy. 71:1981;753-767.
    • (1981) Methods in Enzymololgy , vol.71 , pp. 753-767
    • Doi, Y.1    Nishida, T.2
  • 33
    • 0020519746 scopus 로고
    • Microheterogeneity and physical properties of human lecithin:cholesterol acyltransferase
    • Doi Y., Nishida T. Microheterogeneity and physical properties of human lecithin:cholesterol acyltransferase. Journal of Biological Chemistry. 258:1983;5840-5846.
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 5840-5846
    • Doi, Y.1    Nishida, T.2
  • 34
    • 0002473020 scopus 로고
    • Lipolytic enzymes and the role of apolipoproteins in the regulation of their activity
    • M. Rosseneu. Boca Raton, FL: CRC Press
    • Dolphin P.J. Lipolytic enzymes and the role of apolipoproteins in the regulation of their activity. Rosseneu M. Structure and function of lipoproteins. 1992;295-362 CRC Press, Boca Raton, FL.
    • (1992) Structure and Function of Lipoproteins , pp. 295-362
    • Dolphin, P.J.1
  • 35
    • 0028946013 scopus 로고
    • Glycobiology: Towards understanding the function of sugars
    • Dwek R.A. Glycobiology: towards understanding the function of sugars. Biochemical Society Transactions. 23:1995;1-25.
    • (1995) Biochemical Society Transactions , vol.23 , pp. 1-25
    • Dwek, R.A.1
  • 36
    • 0023159808 scopus 로고
    • Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains
    • Elbein A.D. Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains. Annual Reviews in Biochemistry. 56:1987;497-534.
    • (1987) Annual Reviews in Biochemistry , vol.56 , pp. 497-534
    • Elbein, A.D.1
  • 37
    • 0022544210 scopus 로고
    • Parameters of cholesterol metabolism in the human hepatoma cell line, Hep-G2
    • Erickson S.K., Fielding P.E. Parameters of cholesterol metabolism in the human hepatoma cell line, Hep-G2. Journal of Lipid Research. 27:1986;875-883.
    • (1986) Journal of Lipid Research , vol.27 , pp. 875-883
    • Erickson, S.K.1    Fielding, P.E.2
  • 39
    • 0028887870 scopus 로고
    • Molecular physiology of reverse cholesterol transport
    • Fielding C.J., Fielding P.E. Molecular physiology of reverse cholesterol transport. Journal of Lipid Research. 36:1995;211-228.
    • (1995) Journal of Lipid Research , vol.36 , pp. 211-228
    • Fielding, C.J.1    Fielding, P.E.2
  • 41
    • 0027499376 scopus 로고
    • Lecithin-cholesterol acyltransferase: Effects of mutagenesis at N-linked oligosaccharide attachment sites on acyl acceptor activity
    • Francone O.L., Evangelista L., Fielding C.J. Lecithin-cholesterol acyltransferase: effects of mutagenesis at N-linked oligosaccharide attachment sites on acyl acceptor activity. Biochimica et Biophysica Acta. 1166:1993;301-304.
    • (1993) Biochimica et Biophysica Acta , vol.1166 , pp. 301-304
    • Francone, O.L.1    Evangelista, L.2    Fielding, C.J.3
  • 42
    • 0029953078 scopus 로고    scopus 로고
    • Effects of carboxy-terminal truncation on human lecithin: Cholesterol acyltransferase activity
    • Francone O.L., Evangelista L., Fielding C.J. Effects of carboxy-terminal truncation on human lecithin: cholesterol acyltransferase activity. Journal of Lipid Research. 37:1996;1609-1615.
    • (1996) Journal of Lipid Research , vol.37 , pp. 1609-1615
    • Francone, O.L.1    Evangelista, L.2    Fielding, C.J.3
  • 43
    • 0025836742 scopus 로고
    • Structure-function relationships in human lecithin:cholesterol acyltransferase. Site-directed mutagenesis at serine residues 181 and 216
    • Francone O.L., Fielding C.J. Structure-function relationships in human lecithin:cholesterol acyltransferase. Site-directed mutagenesis at serine residues 181 and 216. Biochemistry. 30:1991;10074-10077.
    • (1991) Biochemistry , vol.30 , pp. 10074-10077
    • Francone, O.L.1    Fielding, C.J.2
  • 44
    • 0024537390 scopus 로고
    • Distribution and functions of lecithin:cholesterol acyltransferase and cholesteryl ester transfer protein in plasma lipoproteins. Evidence for a functional unit containing these activities together with apolipoproteins A-I and D that catalyzes the esterification and transfer of cell-derived cholesterol
    • Francone O.L., Gurakar A., Fielding C.J. Distribution and functions of lecithin:cholesterol acyltransferase and cholesteryl ester transfer protein in plasma lipoproteins. Evidence for a functional unit containing these activities together with apolipoproteins A-I and D that catalyzes the esterification and transfer of cell-derived cholesterol. Journal of Biological Chemistry. 264:1989;7066-7072.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 7066-7072
    • Francone, O.L.1    Gurakar, A.2    Fielding, C.J.3
  • 45
    • 0031608917 scopus 로고    scopus 로고
    • Reverse cholesterol transport and use of transgenic mice and rabbits to reveal candidate genes for protection against atherosclerosis
    • Fruchart J.C., Duriez P. Reverse cholesterol transport and use of transgenic mice and rabbits to reveal candidate genes for protection against atherosclerosis. Bulletin de l'Academie Nationale de Medecine. 182:1998;233-247.
    • (1998) Bulletin de l'Academie Nationale de Medecine , vol.182 , pp. 233-247
    • Fruchart, J.C.1    Duriez, P.2
  • 46
    • 0021281941 scopus 로고
    • Novel mannosidase inhibitor blocking conversion of high mannose to complex oligosaccharides
    • Fuhrmann U., Bause E., Legler G., Ploegh H. Novel mannosidase inhibitor blocking conversion of high mannose to complex oligosaccharides. Nature. 307:1984;755-758.
    • (1984) Nature , vol.307 , pp. 755-758
    • Fuhrmann, U.1    Bause, E.2    Legler, G.3    Ploegh, H.4
  • 47
    • 0002013251 scopus 로고
    • Cell surface carbohydrates: Cell-type specific expression
    • M. Fukuda, & O. Hindsgaul. New York: IRL Press
    • Fukuda M. Cell surface carbohydrates: Cell-type specific expression. Fukuda M., Hindsgaul O. Molecular glycobiology. 1994;1-52 IRL Press, New York.
    • (1994) Molecular Glycobiology , pp. 1-52
    • Fukuda, M.1
  • 49
    • 0022719315 scopus 로고
    • What regulates secretion of non-stored proteins by eukaryotic cells?
    • Gebhart A.M., Ruddon R.W. What regulates secretion of non-stored proteins by eukaryotic cells? Bioessays. 4:1986;213-218.
    • (1986) Bioessays , vol.4 , pp. 213-218
    • Gebhart, A.M.1    Ruddon, R.W.2
  • 51
    • 0018244303 scopus 로고
    • Comparative studies of the lecithin:cholesterol acyltransferase reaction in the plasma of reptiles and amphibians
    • Gillett M.P.T. Comparative studies of the lecithin:cholesterol acyltransferase reaction in the plasma of reptiles and amphibians. Scandinavian Journal of Clinical and Laboratory Investigation. 38:(Suppl 150):1978;32-39.
    • (1978) Scandinavian Journal of Clinical and Laboratory Investigation , vol.38 , Issue.SUPPL. 150 , pp. 32-39
    • Gillett, M.P.T.1
  • 53
    • 84888973439 scopus 로고
    • Relationship between plasma lipid and lipoprotein levels and lecithin:cholesterol acyltransferase activity in non-laying domestic hens. Gallus domesticus
    • Gillett M.P.T., Lima-Filho A.B., Lima-Filho J.L., Lima V.L.M. Relationship between plasma lipid and lipoprotein levels and lecithin:cholesterol acyltransferase activity in non-laying domestic hens. Gallus domesticus. Arquivos do Instituto Biologico. 27:1984;329-337.
    • (1984) Arquivos do Instituto Biologico , vol.27 , pp. 329-337
    • Gillett, M.P.T.1    Lima-Filho, A.B.2    Lima-Filho, J.L.3    Lima, V.L.M.4
  • 54
    • 0000629906 scopus 로고
    • The mechanism of the plasma cholesterol esterification reaction: Plasma fatty acid transferase
    • Glomset J.A. The mechanism of the plasma cholesterol esterification reaction: plasma fatty acid transferase. Biochimica et Biophysica Acta. 65:1962;128-135.
    • (1962) Biochimica et Biophysica Acta , vol.65 , pp. 128-135
    • Glomset, J.A.1
  • 55
    • 0014264541 scopus 로고
    • The plasma lecithin:cholesterol acyltransferase reaction
    • Glomset J.A. The plasma lecithin:cholesterol acyltransferase reaction. Journal of Lipid Research. 9:1968;155-167.
    • (1968) Journal of Lipid Research , vol.9 , pp. 155-167
    • Glomset, J.A.1
  • 56
    • 0000578727 scopus 로고
    • Lecithin:cholesterol acyltransferase deficiency and fish eye disease
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, & D. Valle. New York: McGraw-Hill
    • Glomset J.A., Assmann E.G., Gjone E., Norum K.R. Lecithin:cholesterol acyltransferase deficiency and fish eye disease. Scriver C.R., Beaudet A.L., Sly W.S., Valle D. The metabolic and molecular bases of inherited disease. 1995;1933-1951 McGraw-Hill, New York.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 1933-1951
    • Glomset, J.A.1    Assmann, E.G.2    Gjone, E.3    Norum, K.R.4
  • 58
    • 0030950999 scopus 로고    scopus 로고
    • Familial lecithin:cholesterol acyltransferase deficiency: Molecular analysis of a compound heterozygote: LCAT (Arg147 → Trp) and LCAT (Tyr171 → Stop)
    • Guérin M., Dachet C., Goulinet S., Chevet D., Dolphin P.J., Chapman M.J., Rouis M. Familial lecithin:cholesterol acyltransferase deficiency: molecular analysis of a compound heterozygote: LCAT (Arg147→Trp) and LCAT (Tyr171→Stop). Atherosclerosis. 131:1997;85-95.
    • (1997) Atherosclerosis , vol.131 , pp. 85-95
    • Guérin, M.1    Dachet, C.2    Goulinet, S.3    Chevet, D.4    Dolphin, P.J.5    Chapman, M.J.6    Rouis, M.7
  • 59
    • 0028181691 scopus 로고
    • A new in vitro method for the simultaneous evaluation of cholesteryl ester exchange and mass transfer between HDL and apoB-containing lipoprotein subspecies. Identification of preferential cholesteryl ester acceptors in human plasma
    • Guérin M., Dolphin P.J., Chapman M.J. A new in vitro method for the simultaneous evaluation of cholesteryl ester exchange and mass transfer between HDL and apoB-containing lipoprotein subspecies. Identification of preferential cholesteryl ester acceptors in human plasma. Arteriosclerosis and Thrombosis. 14:1994;199-206.
    • (1994) Arteriosclerosis and Thrombosis , vol.14 , pp. 199-206
    • Guérin, M.1    Dolphin, P.J.2    Chapman, M.J.3
  • 60
    • 0027403267 scopus 로고
    • Effect of fluvastatin sodium (XU62-320), a new inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase, on the induction of low-density lipoprotein receptor in HepG2 cells
    • Hayashi K., Kurokawa J.-I., Nomura S., Kuga Y., Ohkura Y., Kajiyama G. Effect of fluvastatin sodium (XU62-320), a new inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase, on the induction of low-density lipoprotein receptor in HepG2 cells. Biochimica et Biophysica Acta. 1167:1993;223-225.
    • (1993) Biochimica et Biophysica Acta , vol.1167 , pp. 223-225
    • Hayashi, K.1    Kurokawa, J.-I.2    Nomura, S.3    Kuga, Y.4    Ohkura, Y.5    Kajiyama, G.6
  • 61
    • 0028840281 scopus 로고
    • Chicken lecithin-cholesterol acyltransferase. Molecular characterization reveals unusual structure and expression pattern
    • Hengstschlager-Ottnad E., Kuchler K., Schneider W.J. Chicken lecithin-cholesterol acyltransferase. Molecular characterization reveals unusual structure and expression pattern. Journal of Biological Chemistry. 270:1995;26139-26145.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 26139-26145
    • Hengstschlager-Ottnad, E.1    Kuchler, K.2    Schneider, W.J.3
  • 62
    • 0017646948 scopus 로고
    • Studies of the mechanism of tunicamycin inhibition of IgA and IgE secretion by plasma cells
    • Hickman S., Kulczycki A. Jr., Lynch R.G., Kornfeld S. Studies of the mechanism of tunicamycin inhibition of IgA and IgE secretion by plasma cells. Journal of Biological Chemistry. 252:1977;4402-4408.
    • (1977) Journal of Biological Chemistry , vol.252 , pp. 4402-4408
    • Hickman, S.1    Kulczycki Jr., A.2    Lynch, R.G.3    Kornfeld, S.4
  • 64
    • 0027275914 scopus 로고
    • Lecithin:cholesterol acyltransferase deficiency: Identification of a causative gene mutation and a co-inherited protein polymorphism
    • Hill J.S., O K., Wang X., Pritchard P.H. Lecithin:cholesterol acyltransferase deficiency: identification of a causative gene mutation and a co-inherited protein polymorphism. Biochimica et Biophysica Acta. 1181:1993;321-323.
    • (1993) Biochimica et Biophysica Acta , vol.1181 , pp. 321-323
    • Hill, J.S.1    O, K.2    Wang, X.3    Pritchard, P.H.4
  • 65
    • 0027195791 scopus 로고
    • Baboon lecithin cholesterol acyltransferase (LCAT): CDNA sequences of two alleles, evolution, and gene expression
    • Hixson J.E., Driscoll D.M., Birnbaum S., Britten M.L. Baboon lecithin cholesterol acyltransferase (LCAT): cDNA sequences of two alleles, evolution, and gene expression. Gene. 128:1993;259-299.
    • (1993) Gene , vol.128 , pp. 259-299
    • Hixson, J.E.1    Driscoll, D.M.2    Birnbaum, S.3    Britten, M.L.4
  • 66
    • 0023715504 scopus 로고
    • Microheterogeneity of human plasma lecithin:cholesterol acyltransferase examined by isoelectric focusing in immobilized pH gradients
    • Holmquist L., Bjellqvist B. Microheterogeneity of human plasma lecithin:cholesterol acyltransferase examined by isoelectric focusing in immobilized pH gradients. Electrophoresis. 9:1988;580-582.
    • (1988) Electrophoresis , vol.9 , pp. 580-582
    • Holmquist, L.1    Bjellqvist, B.2
  • 67
    • 0027173482 scopus 로고
    • An inhibitor of squalene epoxidase, NB-598, suppresses the secretion of cholesterol and triacylglycerol an simultaneously reduces apolipoprotein B in HepG2 cells
    • Horie M., Hayashi M., Satoh T., Hotta S., Nagata Y., Ishida F., Kamei T. An inhibitor of squalene epoxidase, NB-598, suppresses the secretion of cholesterol and triacylglycerol an simultaneously reduces apolipoprotein B in HepG2 cells. Biochimica et Biophysica Acta. 1168:1993;45-51.
    • (1993) Biochimica et Biophysica Acta , vol.1168 , pp. 45-51
    • Horie, M.1    Hayashi, M.2    Satoh, T.3    Hotta, S.4    Nagata, Y.5    Ishida, F.6    Kamei, T.7
  • 68
    • 0025346154 scopus 로고
    • LCAT activity as a prognostic liver function test
    • Horton R.C., Owen J.S. LCAT activity as a prognostic liver function test. Lancet. 336:1990;249-250.
    • (1990) Lancet , vol.336 , pp. 249-250
    • Horton, R.C.1    Owen, J.S.2
  • 70
    • 0022839162 scopus 로고
    • Human plasma lecithin-cholesterol acyltransferase. An elucidation of the catalytic mechanism
    • Jauhiainen M., Dolphin P.J. Human plasma lecithin-cholesterol acyltransferase. An elucidation of the catalytic mechanism. Journal of Biological Chemistry. 261:1986;7032-7043.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 7032-7043
    • Jauhiainen, M.1    Dolphin, P.J.2
  • 71
    • 0026324559 scopus 로고
    • Human plasma lecithin:cholesterol acyltransferase (LCAT). On the role of essential carboxyl groups in catalysis
    • Jauhiainen M., Dolphin P.J. Human plasma lecithin:cholesterol acyltransferase (LCAT). On the role of essential carboxyl groups in catalysis. Advances in Experimental Medicine and Biology. 285:1990;71-75.
    • (1990) Advances in Experimental Medicine and Biology , vol.285 , pp. 71-75
    • Jauhiainen, M.1    Dolphin, P.J.2
  • 72
    • 0023144454 scopus 로고
    • Aromatic boronic acids as probes of the catalytic site of human plasma lecithin-cholesterol acyltransferase
    • Jauhiainen M., Ridgway N.D., Dolphin P.J. Aromatic boronic acids as probes of the catalytic site of human plasma lecithin-cholesterol acyltransferase. Biochimica et Biophysica Acta. 918:1987;175-188.
    • (1987) Biochimica et Biophysica Acta , vol.918 , pp. 175-188
    • Jauhiainen, M.1    Ridgway, N.D.2    Dolphin, P.J.3
  • 73
    • 0029837484 scopus 로고    scopus 로고
    • Getting the glycosylation right: Implications for the biotechnology industry
    • Jenkins N., Parekh R.B., James D.C. Getting the glycosylation right: implications for the biotechnology industry. Nature Biotechnology. 14:1996;975-981.
    • (1996) Nature Biotechnology , vol.14 , pp. 975-981
    • Jenkins, N.1    Parekh, R.B.2    James, D.C.3
  • 75
    • 0022870107 scopus 로고
    • Studies on the substrate specificity of human and pig lecithin: Cholesterol acyltransferase: Role of low-density lipoproteins
    • Knipping G., Birchbauer A., Stevrer E., Groener J., Zechner R., Kostner G.M. Studies on the substrate specificity of human and pig lecithin: cholesterol acyltransferase: role of low-density lipoproteins. Biochemistry. 25:1986;5242-5249.
    • (1986) Biochemistry , vol.25 , pp. 5242-5249
    • Knipping, G.1    Birchbauer, A.2    Stevrer, E.3    Groener, J.4    Zechner, R.5    Kostner, G.M.6
  • 76
    • 84888943895 scopus 로고
    • Structure of glycoprotein oligosaccharides
    • H. Popper, W. Rutter, F. Gudat, & E. Kottgen. Lancaster: MTP Press
    • Kornfeld R. Structure of glycoprotein oligosaccharides. Popper H., Rutter W., Gudat F., Kottgen E. Structural carbohydrates in the liver. 1983;13-22 MTP Press, Lancaster.
    • (1983) Structural Carbohydrates in the Liver , pp. 13-22
    • Kornfeld, R.1
  • 77
    • 0035813211 scopus 로고    scopus 로고
    • Deletion of specific glycan chains affects differentially the stability, local structures, and activity of lecithin-cholestrol acyltransferase
    • Kosman J., Jonas A. Deletion of specific glycan chains affects differentially the stability, local structures, and activity of lecithin-cholestrol acyltransferase. Journal of Biological Chemistry, 276. 2001.
    • (2001) Journal of Biological Chemistry , vol.276
    • Kosman, J.1    Jonas, A.2
  • 79
    • 0029085605 scopus 로고
    • Retention of glucose units added by the UDP-GLC:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum
    • Labiola C., Cazzulo J.J., Parodi A.J. Retention of glucose units added by the UDP-GLC:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum. Journal of Cell Biology. 130:1995;771-779.
    • (1995) Journal of Cell Biology , vol.130 , pp. 771-779
    • Labiola, C.1    Cazzulo, J.J.2    Parodi, A.J.3
  • 81
    • 0015983464 scopus 로고
    • Serum cholesterol esterification in species resistant and susceptible to atherosclerosis
    • Lacko A.G., Rutenberg H.L., Soloff L.A. Serum cholesterol esterification in species resistant and susceptible to atherosclerosis. Atherosclerosis. 19:1974;297-305.
    • (1974) Atherosclerosis , vol.19 , pp. 297-305
    • Lacko, A.G.1    Rutenberg, H.L.2    Soloff, L.A.3
  • 82
    • 0020984828 scopus 로고
    • Role of intracellular membrane systems in glycosylation of proteins
    • Lennarz W. Role of intracellular membrane systems in glycosylation of proteins. Methods in Enzymology. 98:1983;91-97.
    • (1983) Methods in Enzymology , vol.98 , pp. 91-97
    • Lennarz, W.1
  • 84
    • 0344760521 scopus 로고    scopus 로고
    • Isolation and preliminary microheterogeneity studies of lecithin-cholesterol acyltransferase in plasma from individual patients infected with Schistosoma mansoni
    • Lima V.L.M., Cannizzaro H.M., Owen J.S. Isolation and preliminary microheterogeneity studies of lecithin-cholesterol acyltransferase in plasma from individual patients infected with Schistosoma mansoni. International Hepatology Communications. 6:1997;300-305.
    • (1997) International Hepatology Communications , vol.6 , pp. 300-305
    • Lima, V.L.M.1    Cannizzaro, H.M.2    Owen, J.S.3
  • 85
    • 0031144784 scopus 로고    scopus 로고
    • Immobilized Cratylia mollis lectin as a potential matrix to isolate plasma glycoproteins, including lecithin-cholesterol acyltransferase
    • Lima V.L.M., Correia M.T.S., Cechinel Y.M.N., Sampaio C.A.M., Owen J.S., Coelho L.C.B.B. Immobilized Cratylia mollis lectin as a potential matrix to isolate plasma glycoproteins, including lecithin-cholesterol acyltransferase. Carbohydrate Polymers. 33:1997;27-32.
    • (1997) Carbohydrate Polymers , vol.33 , pp. 27-32
    • Lima, V.L.M.1    Correia, M.T.S.2    Cechinel, Y.M.N.3    Sampaio, C.A.M.4    Owen, J.S.5    Coelho, L.C.B.B.6
  • 88
    • 0023882808 scopus 로고
    • Secretion of lecithin:cholesterol acyltransferase (LCAT) by the human hepatoma cell line, HepG-2
    • Lima V.L.M., McIntyre N., Owen J.S. Secretion of lecithin:cholesterol acyltransferase (LCAT) by the human hepatoma cell line, HepG-2. Biochemical Society Transactions. 16:1988;155-156.
    • (1988) Biochemical Society Transactions , vol.16 , pp. 155-156
    • Lima, V.L.M.1    McIntyre, N.2    Owen, J.S.3
  • 89
    • 84888940148 scopus 로고
    • Secretion of lecithin:cholesterol acyltransferase (LCAT) by cultured human hepatoblastoma cell lines
    • Lima V.L.M., McIntyre N., Owen J.S. Secretion of lecithin:cholesterol acyltransferase (LCAT) by cultured human hepatoblastoma cell lines. Journal of Hepatology. 7:1988;S52.
    • (1988) Journal of Hepatology , vol.7 , pp. 52
    • Lima, V.L.M.1    McIntyre, N.2    Owen, J.S.3
  • 90
    • 0031666963 scopus 로고    scopus 로고
    • An evaluation of the marmoset Callithrix jacchus (sagüi) as an experimental model for the dyslipoproteinemia of human Schistosomiasis mansoni
    • Lima V.L.M., Sena V.L.M., Stewart B., Owen J.S., Dolphin P.J. An evaluation of the marmoset Callithrix jacchus (sagüi) as an experimental model for the dyslipoproteinemia of human Schistosomiasis mansoni. Biochimica et Biophysica Acta. 1393:1998;235-243.
    • (1998) Biochimica et Biophysica Acta , vol.1393 , pp. 235-243
    • Lima, V.L.M.1    Sena, V.L.M.2    Stewart, B.3    Owen, J.S.4    Dolphin, P.J.5
  • 91
    • 0020595853 scopus 로고
    • Hepatoma secretory proteins migrate from rough endoplasmic reticulum to golgi at characteristic rates
    • Lodish H.F., Kong N., Snider M., Strous G.J.A.M. Hepatoma secretory proteins migrate from rough endoplasmic reticulum to golgi at characteristic rates. Nature. 304:1983;80-83.
    • (1983) Nature , vol.304 , pp. 80-83
    • Lodish, H.F.1    Kong, N.2    Snider, M.3    Strous, G.J.A.M.4
  • 93
    • 0025777285 scopus 로고
    • Glycosylation, activity and secretion of lipoprotein lipase in cultured brown adipocytes of newborn mice. Effect of tunicamycin, monensin, 1-deoxymannojirimycin and swainsonine
    • Masuno H., Schultz G.J., Park J.-W., Blanchette-Mackie E.J., Mateo C., Scow R.O. Glycosylation, activity and secretion of lipoprotein lipase in cultured brown adipocytes of newborn mice. Effect of tunicamycin, monensin, 1-deoxymannojirimycin and swainsonine. Biochemical Journal. 277:1991;801-809.
    • (1991) Biochemical Journal , vol.277 , pp. 801-809
    • Masuno, H.1    Schultz, G.J.2    Park, J.-W.3    Blanchette-Mackie, E.J.4    Mateo, C.5    Scow, R.O.6
  • 94
    • 0022597432 scopus 로고
    • Early kinetics of human macrophage apolipoprotein E synthesis and incorporation of carbohydrate precursors
    • Mazzone T., Papagiannes E., Magner T. Early kinetics of human macrophage apolipoprotein E synthesis and incorporation of carbohydrate precursors. Biochimica et Biophysica Acta. 875:1986;393-396.
    • (1986) Biochimica et Biophysica Acta , vol.875 , pp. 393-396
    • Mazzone, T.1    Papagiannes, E.2    Magner, T.3
  • 97
    • 0025142711 scopus 로고
    • Nucleotide sequence of the cDNA for lecithin:cholesterol acyltransferase (LCAT) from rat
    • Meroni G., Malgaretti N., Magnaghi P., Taramelli R. Nucleotide sequence of the cDNA for lecithin:cholesterol acyltransferase (LCAT) from rat. Nucleic Acids Research. 18:1990;5308.
    • (1990) Nucleic Acids Research , vol.18 , pp. 5308
    • Meroni, G.1    Malgaretti, N.2    Magnaghi, P.3    Taramelli, R.4
  • 99
    • 0029976437 scopus 로고    scopus 로고
    • Glycosylation structure and enzyme activity of lecithin:cholesterol acyltransferase from human plasma, HepG2 cells, and baculoviral and Chinese hamster ovary cell expression systems
    • Miller K.R., Wang J., Sorci-Thomas M., Anderson R.A., Parks J.S. Glycosylation structure and enzyme activity of lecithin:cholesterol acyltransferase from human plasma, HepG2 cells, and baculoviral and Chinese hamster ovary cell expression systems. Journal of Lipid Research. 37:1996;551-561.
    • (1996) Journal of Lipid Research , vol.37 , pp. 551-561
    • Miller, K.R.1    Wang, J.2    Sorci-Thomas, M.3    Anderson, R.A.4    Parks, J.S.5
  • 102
    • 0030016524 scopus 로고    scopus 로고
    • Cloning of rabbit LCAT cDNA: Increase in LCAT mRNA abundance in the liver of cholesterol-fed rabbits
    • Murata Y., Maeda E., Yoshino G., Kasuga M. Cloning of rabbit LCAT cDNA: increase in LCAT mRNA abundance in the liver of cholesterol-fed rabbits. Journal of Lipid Research. 37:1996;1616-1622.
    • (1996) Journal of Lipid Research , vol.37 , pp. 1616-1622
    • Murata, Y.1    Maeda, E.2    Yoshino, G.3    Kasuga, M.4
  • 103
    • 0025265056 scopus 로고
    • Affinity of lipid transfer protein for lipid and lipoprotein particles as influenced by lecithin: Cholesterol acyltransferase
    • Nishida H.I., Kato H., Nishida T. Affinity of lipid transfer protein for lipid and lipoprotein particles as influenced by lecithin: cholesterol acyltransferase. Journal of Biological Chemistry. 265:1990;4876-4883.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 4876-4883
    • Nishida, H.I.1    Kato, H.2    Nishida, T.3
  • 104
    • 0017104873 scopus 로고
    • Secretion of lecithin:cholesterol acyltransferase from isolated rat hepatocytes
    • Nordby G., Berg T., Nilsson M., Norum K.R. Secretion of lecithin:cholesterol acyltransferase from isolated rat hepatocytes. Biochimica et Biophysica Acta. 450:1976;69-77.
    • (1976) Biochimica et Biophysica Acta , vol.450 , pp. 69-77
    • Nordby, G.1    Berg, T.2    Nilsson, M.3    Norum, K.R.4
  • 105
    • 0028854573 scopus 로고
    • Role of N-linked glycosylation of lecithin:cholesterol acyltransferase in lipoprotein substrate specificity
    • O K., Hill T.S., Pritchard P.H. Role of N-linked glycosylation of lecithin:cholesterol acyltransferase in lipoprotein substrate specificity. Biochimica et Biophysica Acta. 1254:1995;193-197.
    • (1995) Biochimica et Biophysica Acta , vol.1254 , pp. 193-197
    • O, K.1    Hill, T.S.2    Pritchard, P.H.3
  • 106
    • 0027369786 scopus 로고
    • Lecithin:cholesterol acyltransferase: Role of N-linked glycosylation in enzyme function
    • O K., Hill J.S., Wang X., McLeod R., Pritchard P.H. Lecithin:cholesterol acyltransferase: role of N-linked glycosylation in enzyme function. Biochemical Journal. 294:1993;879-884.
    • (1993) Biochemical Journal , vol.294 , pp. 879-884
    • O, K.1    Hill, J.S.2    Wang, X.3    McLeod, R.4    Pritchard, P.H.5
  • 108
    • 0017944868 scopus 로고
    • Role of carbohydrates in protein secretion and turnover: Effects of tunicamycin on the major cell surface glycoprotein of chick embryo fibroblasts
    • Olden K., Pratt R.M., Yamada K.M. Role of carbohydrates in protein secretion and turnover: effects of tunicamycin on the major cell surface glycoprotein of chick embryo fibroblasts. Cell. 13:1978;461-473.
    • (1978) Cell , vol.13 , pp. 461-473
    • Olden, K.1    Pratt, R.M.2    Yamada, K.M.3
  • 109
    • 0023645273 scopus 로고
    • Synthesis and secretion of lipoprotein lipase in 3T3-L1 adipocytes. Demonstration of inactive forms of lipase in cells
    • Olivecrona T., Chernick S.S., Bengtsson-Olivecrona G., Garrison M., Scow R.O. Synthesis and secretion of lipoprotein lipase in 3T3-L1 adipocytes. Demonstration of inactive forms of lipase in cells. Journal of Biological Chemistry. 262:1987;10748-10759.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 10748-10759
    • Olivecrona, T.1    Chernick, S.S.2    Bengtsson-Olivecrona, G.3    Garrison, M.4    Scow, R.O.5
  • 110
    • 0015023024 scopus 로고
    • Origin and disappearance of plasma lecithin:cholesterol acyltransferase
    • Osuga T., Portman O.W. Origin and disappearance of plasma lecithin:cholesterol acyltransferase. American Journal of Physiology. 220:1971;735-741.
    • (1971) American Journal of Physiology , vol.220 , pp. 735-741
    • Osuga, T.1    Portman, O.W.2
  • 111
    • 84888975000 scopus 로고
    • Plasma lipoproteins and the regulation of cellular function
    • E. Reid, G.M.W. Cook, & D.J. Moore. Investigation of membrane-located receptors, New York: Plenum Press
    • Owen J.S. Plasma lipoproteins and the regulation of cellular function. Reid E., Cook G.M.W., Moore D.J. Methodological surveys in biochemistry and analysis. Investigation of membrane-located receptors. Vol. 13:1984;311-316 Plenum Press, New York.
    • (1984) Methodological Surveys in Biochemistry and Analysis , vol.13 , pp. 311-316
    • Owen, J.S.1
  • 112
  • 113
    • 0029937074 scopus 로고    scopus 로고
    • Complete deficiency of plasma lecithin-cholesterol acyltransferase (LCAT) activity due to a novel homozygous mutation (Gly-30-Ser) in LCAT gene
    • Owen J.S., Wiebusch H., Cullen P., Watts G.F., Lima V.L.M., Funke H., Assmann G. Complete deficiency of plasma lecithin-cholesterol acyltransferase (LCAT) activity due to a novel homozygous mutation (Gly-30-Ser) in LCAT gene. Human Mutations. 8:1996;79-82.
    • (1996) Human Mutations , vol.8 , pp. 79-82
    • Owen, J.S.1    Wiebusch, H.2    Cullen, P.3    Watts, G.F.4    Lima, V.L.M.5    Funke, H.6    Assmann, G.7
  • 114
    • 0024355330 scopus 로고
    • Glycoproteins: What are the sugar chains for?
    • Paulson J.C. Glycoproteins: what are the sugar chains for? Trends in Biochemical Sciences. 14:1989;272-276.
    • (1989) Trends in Biochemical Sciences , vol.14 , pp. 272-276
    • Paulson, J.C.1
  • 115
    • 0024431691 scopus 로고
    • Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation
    • Paulson J.C., Colley K.J. Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. Journal of Biological Chemistry. 264:1989;17615-17618.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 17615-17618
    • Paulson, J.C.1    Colley, K.J.2
  • 118
    • 0022588210 scopus 로고
    • The effect of carbonyl cyanide trifluoromethoxyphenylhydrazone and methylamine on the processing and secretion of the glycoprotein hormone chorionic gonadotropin by human choriocarcinoma cells
    • Peters B.P., Krzesicki R.F., Perini F., Huddon R.W. The effect of carbonyl cyanide trifluoromethoxyphenylhydrazone and methylamine on the processing and secretion of the glycoprotein hormone chorionic gonadotropin by human choriocarcinoma cells. Endocrinology. 119:1986;416-428.
    • (1986) Endocrinology , vol.119 , pp. 416-428
    • Peters, B.P.1    Krzesicki, R.F.2    Perini, F.3    Huddon, R.W.4
  • 119
    • 0018773226 scopus 로고
    • Utilization of various sterols by lecithin-cholesterol acyltransferase as acyl acceptors
    • Piran U., Nishida T. Utilization of various sterols by lecithin-cholesterol acyltransferase as acyl acceptors. Lipids. 14:1979;478-482.
    • (1979) Lipids , vol.14 , pp. 478-482
    • Piran, U.1    Nishida, T.2
  • 120
    • 0027281785 scopus 로고
    • Effects of site-directed mutagenesis on the N-glycosylation sites of human lecithin:cholesterol acyltransferase
    • Qu S.-J., Fan H.-Z., Vaca F.B., Pownall H.J. Effects of site-directed mutagenesis on the N-glycosylation sites of human lecithin:cholesterol acyltransferase. Biochemistry. 32:1993;8732-8736.
    • (1993) Biochemistry , vol.32 , pp. 8732-8736
    • Qu, S.-J.1    Fan, H.-Z.2    Vaca, F.B.3    Pownall, H.J.4
  • 121
    • 0022384675 scopus 로고
    • Serum activity and hepatic secretion of lecithin: Cholesterol acyltransferase in experimental hypothyroidism and hypercholesterolemia
    • Ridgway N.D., Dolphin P.J. Serum activity and hepatic secretion of lecithin: cholesterol acyltransferase in experimental hypothyroidism and hypercholesterolemia. Journal of Lipid Research. 26:1985;1300-1313.
    • (1985) Journal of Lipid Research , vol.26 , pp. 1300-1313
    • Ridgway, N.D.1    Dolphin, P.J.2
  • 124
    • 0026658579 scopus 로고
    • Apolipoproteins, membrane cholesterol domains, and the regulation of cholesterol efflux
    • Rothblat G.H., Mahlberg F.H., Johnson W.J., Philips M.C. Apolipoproteins, membrane cholesterol domains, and the regulation of cholesterol efflux. Journal of Lipid Research. 33:1992;1091-1097.
    • (1992) Journal of Lipid Research , vol.33 , pp. 1091-1097
    • Rothblat, G.H.1    Mahlberg, F.H.2    Johnson, W.J.3    Philips, M.C.4
  • 125
    • 0001800992 scopus 로고
    • Lipid transfer activities and apolipoproteins
    • M. Rosseneu. Boca Raton, FL: CRC Press
    • Rye K.-A., Barter P.J. Lipid transfer activities and apolipoproteins. Rosseneu M. Structure and function of lipoproteins. 1992;401-426 CRC Press, Boca Raton, FL.
    • (1992) Structure and Function of Lipoproteins , pp. 401-426
    • Rye, K.-A.1    Barter, P.J.2
  • 126
    • 0001813430 scopus 로고
    • Molecular cloning of glycosyltransferase genes
    • M. Fukuda, & O. Hindsgaul. New York: IRL Press
    • Schachter H. Molecular cloning of glycosyltransferase genes. Fukuda M., Hindsgaul O. Molecular glycobiology. 1994;88-162 IRL Press, New York.
    • (1994) Molecular Glycobiology , pp. 88-162
    • Schachter, H.1
  • 127
    • 0028962142 scopus 로고
    • Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion
    • Schindler P.A., Settineri C.A., Collet X., Fielding C.J., Burlingame A.L. Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion. Protein Science. 4:1995;791-803.
    • (1995) Protein Science , vol.4 , pp. 791-803
    • Schindler, P.A.1    Settineri, C.A.2    Collet, X.3    Fielding, C.J.4    Burlingame, A.L.5
  • 129
    • 0019992236 scopus 로고
    • Kinetics of internalization and recycling of the asialoglycoprotein receptor in a hepatoma cell line
    • Schwartz A.L., Fridovitch S.E., Lodish H.F. Kinetics of internalization and recycling of the asialoglycoprotein receptor in a hepatoma cell line. Journal of Biological Chemistry. 257:1982;4230-4237.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 4230-4237
    • Schwartz, A.L.1    Fridovitch, S.E.2    Lodish, H.F.3
  • 131
    • 0027050126 scopus 로고
    • Characterization of lipoprotein lipase activity, secretion, and degradation at different sites of post-translational processing in primary cultures of rat adipocytes
    • Simsolo R.B., Ong J.M., Kern P.A. Characterization of lipoprotein lipase activity, secretion, and degradation at different sites of post-translational processing in primary cultures of rat adipocytes. Journal of Lipid Research. 33:1992;1777-1784.
    • (1992) Journal of Lipid Research , vol.33 , pp. 1777-1784
    • Simsolo, R.B.1    Ong, J.M.2    Kern, P.A.3
  • 132
    • 0025315872 scopus 로고
    • Cellular localization of apolipoprotein D and lecithin:cholesterol acyltransferase mRNA in rhesus monkey tissues by in situ hybridisation
    • Smith K.M., Lawn R.M., Wilcox J.N. Cellular localization of apolipoprotein D and lecithin:cholesterol acyltransferase mRNA in rhesus monkey tissues by in situ hybridisation. Journal of Lipid Research. 31:1990;995-1004.
    • (1990) Journal of Lipid Research , vol.31 , pp. 995-1004
    • Smith, K.M.1    Lawn, R.M.2    Wilcox, J.N.3
  • 133
    • 0017734882 scopus 로고
    • Hepatic secretion and turnover of serum phosphatidylcholine-cholesterol acyltransferase in male and female rats
    • Soler-Argilaga C., Russel R., Goh E.H., Heimberg M. Hepatic secretion and turnover of serum phosphatidylcholine-cholesterol acyltransferase in male and female rats. Biochimica et Biophysica Acta. 488:1977;69-75.
    • (1977) Biochimica et Biophysica Acta , vol.488 , pp. 69-75
    • Soler-Argilaga, C.1    Russel, R.2    Goh, E.H.3    Heimberg, M.4
  • 134
    • 0025347085 scopus 로고
    • Lecithin-cholesterol acyltransferase (LCAT) catalyses transacylation of intact cholesteryl esters. Evidence for the partial reversal of the forward LCAT reaction
    • Sorci-Thomas M., Babiak J., Rudel L.L. Lecithin-cholesterol acyltransferase (LCAT) catalyses transacylation of intact cholesteryl esters. Evidence for the partial reversal of the forward LCAT reaction. Journal of Biological Chemistry. 265:1990;2665-2670.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 2665-2670
    • Sorci-Thomas, M.1    Babiak, J.2    Rudel, L.L.3
  • 136
    • 0003044366 scopus 로고
    • The function of saccharide-lipids in synthesis of glycoproteins
    • LennarzW.J. New York: Plenum Press
    • Struck D.K., Lennarz W.J. The function of saccharide-lipids in synthesis of glycoproteins. Lennarz W.J. Biochemistry of glycoproteins and proteoglycans. 35-83:1980;35-83 Plenum Press, New York.
    • (1980) Biochemistry of Glycoproteins and Proteoglycans , pp. 35-83
    • Struck, D.K.1    Lennarz, W.J.2
  • 137
    • 0017815660 scopus 로고
    • Effect of tunicamycin on the secretion of serum proteins by primary cultures of rat and chick hepatocytes. Studies on transferrin, very low density lipoprotein, and serum albumin
    • Struck D.K., Suita P.B., Lane M.D., Lennarz W.J. Effect of tunicamycin on the secretion of serum proteins by primary cultures of rat and chick hepatocytes. Studies on transferrin, very low density lipoprotein, and serum albumin. Journal of Biological Chemistry. 253:1978;5332-5337.
    • (1978) Journal of Biological Chemistry , vol.253 , pp. 5332-5337
    • Struck, D.K.1    Suita, P.B.2    Lane, M.D.3    Lennarz, W.J.4
  • 138
    • 0018097847 scopus 로고
    • Demonstration of enzymatic conversion of lysolecithin to lecithin in normal plasma
    • Subbaiah P.V., Bagdade J.D. Demonstration of enzymatic conversion of lysolecithin to lecithin in normal plasma. Life Sciences. 22:1978;1971-1977.
    • (1978) Life Sciences , vol.22 , pp. 1971-1977
    • Subbaiah, P.V.1    Bagdade, J.D.2
  • 139
    • 0028261414 scopus 로고
    • Enzymatic deglycosylation of asparagine-linked glycans: Purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum
    • Tarentino A.L., Plummere T.H. Jr. Enzymatic deglycosylation of asparagine-linked glycans: purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum. Methods in Enzymology. 230:1994;44-57.
    • (1994) Methods in Enzymology , vol.230 , pp. 44-57
    • Tarentino, A.L.1    Plummere Jr., T.H.2
  • 140
    • 0020635123 scopus 로고
    • Perturbation of vesicular traffic with the carboxylic ionophore monensin
    • Tartakoff A.M. Perturbation of vesicular traffic with the carboxylic ionophore monensin. Cell. 32:1983;1026-1028.
    • (1983) Cell , vol.32 , pp. 1026-1028
    • Tartakoff, A.M.1
  • 142
    • 0016757289 scopus 로고
    • Tunicamycin inhibition of polyisoprenyl N-acetylglucosaminyl pyrophosphate formation in calf-liver microsomes
    • Tkacz J.S., Lampen J.O. Tunicamycin inhibition of polyisoprenyl N-acetylglucosaminyl pyrophosphate formation in calf-liver microsomes. Biochemical and Biophysical Research Communications. 65:1975;248-257.
    • (1975) Biochemical and Biophysical Research Communications , vol.65 , pp. 248-257
    • Tkacz, J.S.1    Lampen, J.O.2
  • 143
    • 0026020091 scopus 로고
    • Identification of distinct endoglycosidase (endo) activities in Flavobacterium meningosepticum: Endo F1, endo F2, and endo F3. Endo F1 and endo H hydrolyze only high mannose and hybrid glycans
    • Trimble R.B., Tarentino A.L. Identification of distinct endoglycosidase (endo) activities in Flavobacterium meningosepticum: endo F1, endo F2, and endo F3. Endo F1 and endo H hydrolyze only high mannose and hybrid glycans. Journal of Biological Chemistry. 266:1991;1646-1651.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 1646-1651
    • Trimble, R.B.1    Tarentino, A.L.2
  • 144
    • 0020469388 scopus 로고
    • Swainsonine inhibits the biosynthesis of complex glycoproteins by inhibition of golgi mannosidase II
    • Tulsiani D.R.P., Harris T.M., Touster O. Swainsonine inhibits the biosynthesis of complex glycoproteins by inhibition of golgi mannosidase II. Journal of Biological Chemistry. 257:1982;7936-7939.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 7936-7939
    • Tulsiani, D.R.P.1    Harris, T.M.2    Touster, O.3
  • 145
    • 0026772958 scopus 로고
    • N-glycosylation of serum proteins in disease and its investigation using lectins
    • Turner G.A. N-glycosylation of serum proteins in disease and its investigation using lectins. Clinica Chimica Acta. 208:1992;149-171.
    • (1992) Clinica Chimica Acta , vol.208 , pp. 149-171
    • Turner, G.A.1
  • 146
    • 0018393233 scopus 로고
    • Monovalent ionophores inhibit secretion of procollagen and fibronectin from cultured human fibroblasts
    • Uchida N., Smilowitz H., Tanzer M.L. Monovalent ionophores inhibit secretion of procollagen and fibronectin from cultured human fibroblasts. Proceedings of the National Academy of Sciences USA. 76:1979;1868-1872.
    • (1979) Proceedings of the National Academy of Sciences USA , vol.76 , pp. 1868-1872
    • Uchida, N.1    Smilowitz, H.2    Tanzer, M.L.3
  • 147
    • 0019311557 scopus 로고
    • Substitution in vitro of lecithin-cholesterol acyltransferase. Analysis of changes in plasma lipoproteins
    • Utermann G., Menzel H.-J., Adler G., Dieker P., Weber W. Substitution in vitro of lecithin-cholesterol acyltransferase. Analysis of changes in plasma lipoproteins. European Journal of Biochemistry. 107:1980;225-241.
    • (1980) European Journal of Biochemistry , vol.107 , pp. 225-241
    • Utermann, G.1    Menzel, H.-J.2    Adler, G.3    Dieker, P.4    Weber, W.5
  • 148
    • 0024819307 scopus 로고
    • Tissue-specific expression, developmental regulation, and chromosomal mapping of the lecithin-cholesterol acyltransferase gene: Evidence for expression in brain and testes as well as liver
    • Warden C.H., Langner C.A., Gorden J.I., Taylor B.A., McLean J.W., Lusis A.J. Tissue-specific expression, developmental regulation, and chromosomal mapping of the lecithin-cholesterol acyltransferase gene: evidence for expression in brain and testes as well as liver. Journal of Biological Chemistry. 264:1989;21573-21581.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 21573-21581
    • Warden, C.H.1    Langner, C.A.2    Gorden, J.I.3    Taylor, B.A.4    McLean, J.W.5    Lusis, A.J.6
  • 151
    • 0029153435 scopus 로고
    • Human plasma lecithin:cholesterol acyltransferase. On the substrate efficiency of cholest-5-ene-3(-thiol as a fatty acyl acceptor
    • Zhou G., Dolphin P.J. Human plasma lecithin:cholesterol acyltransferase. On the substrate efficiency of cholest-5-ene-3(-thiol as a fatty acyl acceptor. Biochimica et Biophysica Acta. 1258:1995;101-106.
    • (1995) Biochimica et Biophysica Acta , vol.1258 , pp. 101-106
    • Zhou, G.1    Dolphin, P.J.2


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