메뉴 건너뛰기




Volumn 377, Issue 1, 2004, Pages 121-130

A role for palmitoylation in the quality control, assembly and secretion of apolipoprotein B

Author keywords

Apolipoprotein B; Endoplasmic reticulum; Golgi apparatus; Palmitoylation; Secretion

Indexed keywords

BIOCHEMISTRY; BLOOD; CHOLESTEROL; ESTERS; MUTAGENESIS;

EID: 1642575961     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030951     Document Type: Article
Times cited : (10)

References (53)
  • 1
    • 0000795715 scopus 로고
    • Introduction: Structure and metabolism of plasma lipoproteins and disorders of the biogenesis and secretion of lipoproteins containing the B apolipoproteins
    • Scriver, C. E., Beaudet, A. L., Sly, W. E. and Valle, D., eds., McGraw-Hill, New York
    • Havel, R. J. and Kane, J. P. (1995) Introduction: structure and metabolism of plasma lipoproteins and disorders of the biogenesis and secretion of lipoproteins containing the B apolipoproteins. In The Metabolic and Molecular Bases of Inherited Disease (Scriver, C. E., Beaudet, A. L., Sly, W. E. and Valle, D., eds.), pp. 1841-1885, McGraw-Hill, New York
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 1841-1885
    • Havel, R.J.1    Kane, J.P.2
  • 3
    • 0017070905 scopus 로고
    • Subcellular localization of B apoprotein of plasma lipoproteins in rat liver
    • Alexander, C. A., Hamilton, R. L. and Havel, R. J. (1976) Subcellular localization of B apoprotein of plasma lipoproteins in rat liver. J. Cell Biol. 69, 241-263
    • (1976) J. Cell Biol. , vol.69 , pp. 241-263
    • Alexander, C.A.1    Hamilton, R.L.2    Havel, R.J.3
  • 4
    • 0028036640 scopus 로고
    • Studies on the assembly of apolipoprotein B-100- and B-48-containing very low density lipoproteins in McA-RH7777 cells
    • Boren, J., Rustaeus, S. and Olofsson, S. O. (1994) Studies on the assembly of apolipoprotein B-100- and B-48-containing very low density lipoproteins in McA-RH7777 cells. J. Biol. Chem. 269, 25879-25888
    • (1994) J. Biol. Chem. , vol.269 , pp. 25879-25888
    • Boren, J.1    Rustaeus, S.2    Olofsson, S.O.3
  • 5
    • 0001558236 scopus 로고
    • Nascent VLDL assembly occurs in two steps in the endoplasmic reticulum (ER) of hepatocytes
    • Woodford, X. F. P., Davignon, J. and Sniderman, A., eds., Elsevier Science, Amsterdam
    • Hamilton, R. L., Erikson, S. K. and Havel, R. J. (1995) Nascent VLDL assembly occurs in two steps in the endoplasmic reticulum (ER) of hepatocytes. In Atherosclerosis (Woodford, X. F. P., Davignon, J. and Sniderman, A., eds.), pp. 414-418, Elsevier Science, Amsterdam
    • (1995) Atherosclerosis , pp. 414-418
    • Hamilton, R.L.1    Erikson, S.K.2    Havel, R.J.3
  • 7
    • 0032410930 scopus 로고    scopus 로고
    • Apoprotein B100 has a prolonged interaction with the translocon during which its lipidation and translocation change from dependence on the microsomal triglyceride transfer protein to independence
    • Mitcnell, D. M., Zhou, M., Pariyarath, R., Wang, H., Aitchison, J. D., Ginsberg, H. N. and Fisher, E. A. (1998) Apoprotein B100 has a prolonged interaction with the translocon during which its lipidation and translocation change from dependence on the microsomal triglyceride transfer protein to independence. Proc. Natl. Acad. Sci. U.S.A. 95, 14733-14738
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14733-14738
    • Mitcnell, D.M.1    Zhou, M.2    Pariyarath, R.3    Wang, H.4    Aitchison, J.D.5    Ginsberg, H.N.6    Fisher, E.A.7
  • 8
    • 0035958917 scopus 로고    scopus 로고
    • The triple threat to nascent apolipoprotein B. Evidence for multiple, distinct degradative pathways
    • Fisher, E. A., Pan, M., Chen, X., Wu, X., Wang, H., Jamil, H., Sparks, J. D. and Williams, K. J. (2001) The triple threat to nascent apolipoprotein B. Evidence for multiple, distinct degradative pathways. J. Biol. Chem. 276, 27855-27863
    • (2001) J. Biol. Chem. , vol.276 , pp. 27855-27863
    • Fisher, E.A.1    Pan, M.2    Chen, X.3    Wu, X.4    Wang, H.5    Jamil, H.6    Sparks, J.D.7    Williams, K.J.8
  • 9
    • 0032516849 scopus 로고    scopus 로고
    • Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state
    • Linnik, K. M. and Herscovitz, H. (1998) Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state. J. Biol. Chem. 273, 21368-21373
    • (1998) J. Biol. Chem. , vol.273 , pp. 21368-21373
    • Linnik, K.M.1    Herscovitz, H.2
  • 10
    • 0032868686 scopus 로고    scopus 로고
    • Interaction of newly synthesized apolipoprotein B with calnexin and calreticulin requires glucose trimming in the endoplasmic reticulum
    • Tatu, U. and Helenius, A. (1999) Interaction of newly synthesized apolipoprotein B with calnexin and calreticulin requires glucose trimming in the endoplasmic reticulum. Biosci. Rep. 19, 189-196
    • (1999) Biosci. Rep. , vol.19 , pp. 189-196
    • Tatu, U.1    Helenius, A.2
  • 11
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner, S., Maurizi, M. R. and Gottesman, S. (1999) Posttranslational quality control: folding, refolding, and degrading proteins. Science 286, 1888-1893
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 12
    • 0031846319 scopus 로고    scopus 로고
    • Chylomicron-sized lipid particles are formed in the setting of apolipoprotein B deficiency
    • Hamilton, R. L., Wong, J. S., Cham, C. M., Nielsen, L. B. and Young, S. G. (1998) Chylomicron-sized lipid particles are formed in the setting of apolipoprotein B deficiency. J. Lipid Res. 39, 1543-1557
    • (1998) J. Lipid Res. , vol.39 , pp. 1543-1557
    • Hamilton, R.L.1    Wong, J.S.2    Cham, C.M.3    Nielsen, L.B.4    Young, S.G.5
  • 13
    • 0023646009 scopus 로고
    • Intrahepatic assembly of very low density lipoproteins. Rate of transport out of the endoplasmic reticulum determines rate of secretion
    • Borchardt, R. A. and Davis, R. A. (1987) Intrahepatic assembly of very low density lipoproteins. Rate of transport out of the endoplasmic reticulum determines rate of secretion. J. Biol. Chem. 262, 16394-16402
    • (1987) J. Biol. Chem. , vol.262 , pp. 16394-16402
    • Borchardt, R.A.1    Davis, R.A.2
  • 14
    • 0027535128 scopus 로고
    • Assembly of rat hepatic very low density lipoproteins in the endoplasmic reticulum
    • Rusinol, A., Verkade, H. and Vance, J. E. (1993) Assembly of rat hepatic very low density lipoproteins in the endoplasmic reticulum. J. Biol. Chem. 268, 3555-3562
    • (1993) J. Biol. Chem. , vol.268 , pp. 3555-3562
    • Rusinol, A.1    Verkade, H.2    Vance, J.E.3
  • 16
    • 0024295210 scopus 로고
    • Evidence that during very low density lipoprotein assembly in rat hepatocytes most of the triacylglycerol and phospholipid are packaged with apolipoprotein B in the Golgi complex
    • Higgins, J. A. (1988) Evidence that during very low density lipoprotein assembly in rat hepatocytes most of the triacylglycerol and phospholipid are packaged with apolipoprotein B in the Golgi complex. FEBS Lett. 232, 405-408
    • (1988) FEBS Lett. , vol.232 , pp. 405-408
    • Higgins, J.A.1
  • 17
    • 0025319210 scopus 로고
    • Possible role of the Golgi apparatus in the assembly of very low density lipoprotein
    • Bamberger, M. J. and Lane, M. D. (1990) Possible role of the Golgi apparatus in the assembly of very low density lipoprotein. Proc. Natl. Acad. Sci. U.S.A. 87, 2390-2394
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 2390-2394
    • Bamberger, M.J.1    Lane, M.D.2
  • 18
    • 0029128035 scopus 로고
    • Intracellular events in the assembly of very-low-density-lipoprotein lipids with apolipoprotein B in isolated rabbit hepatocytes
    • Cartwright, I. J. and Higgins, J. A. (1995) Intracellular events in the assembly of very-low-density-lipoprotein lipids with apolipoprotein B in isolated rabbit hepatocytes. Biochem. J. 310, 897-907
    • (1995) Biochem. J. , vol.310 , pp. 897-907
    • Cartwright, I.J.1    Higgins, J.A.2
  • 19
    • 0035091424 scopus 로고    scopus 로고
    • Assembly of very low density lipoproteins in mouse liver: Evidence of heterogeneity of particle density in the Golgi apparatus
    • Swift, L. L., Valyi-Nagy, K., Rowland, C. and Harris, C. (2001) Assembly of very low density lipoproteins in mouse liver: evidence of heterogeneity of particle density in the Golgi apparatus. J. Lipid Res. 42, 218-224
    • (2001) J. Lipid Res. , vol.42 , pp. 218-224
    • Swift, L.L.1    Valyi-Nagy, K.2    Rowland, C.3    Harris, C.4
  • 21
    • 0024281288 scopus 로고
    • Identification of the thiol ester linked lipids in apolipoprotein B
    • Huang, G., Lee, D. M. and Singh, S. (1988) Identification of the thiol ester linked lipids in apolipoprotein B. Biochemistry 27, 1395-1400
    • (1988) Biochemistry , vol.27 , pp. 1395-1400
    • Huang, G.1    Lee, D.M.2    Singh, S.3
  • 22
    • 0024374050 scopus 로고
    • Presence of covalently attached fatty acids in rat apolipoprotein B via thiolester linkages
    • Kamanna, V. S. and Lee, D. M. (1989) Presence of covalently attached fatty acids in rat apolipoprotein B via thiolester linkages. Biochem. Biophys. Res. Commun. 162, 1508-1514
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 1508-1514
    • Kamanna, V.S.1    Lee, D.M.2
  • 23
    • 0025033253 scopus 로고
    • Intramolecular thiolester linkages in apolipoprotein B
    • Lee, D. M. and Singh, S. (1990) Intramolecular thiolester linkages in apolipoprotein B. SAAS Bull. Biochem. Biotechnol. 3, 74-79
    • (1990) SAAS Bull. Biochem. Biotechnol. , vol.3 , pp. 74-79
    • Lee, D.M.1    Singh, S.2
  • 24
    • 0026321823 scopus 로고
    • Inter- and intramolecular thiolester linkages in apolipoprotein B
    • Lee, D. M. (1991) Inter- and intramolecular thiolester linkages in apolipoprotein B. Prog. Lipid Res. 30, 245-252
    • (1991) Prog. Lipid Res. , vol.30 , pp. 245-252
    • Lee, D.M.1
  • 25
    • 0034002307 scopus 로고    scopus 로고
    • Palmitoylation of apolipoprotein B is required for proper intracellular sorting and transport of cholesteroyl esters and triglycerides
    • Zhao, Y., McCabe, J. B., Vance, J. and Berthiaume, L. G. (2000) Palmitoylation of apolipoprotein B is required for proper intracellular sorting and transport of cholesteroyl esters and triglycerides. Mol. Biol. Cell 11, 721-734
    • (2000) Mol. Biol. Cell , vol.11 , pp. 721-734
    • Zhao, Y.1    McCabe, J.B.2    Vance, J.3    Berthiaume, L.G.4
  • 26
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: Towards an understanding at the molecular level
    • Ellgaard, L. and Helenius, A. (2001) ER quality control: towards an understanding at the molecular level. Curr. Opin. Cell Biol. 13, 431-437
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 431-437
    • Ellgaard, L.1    Helenius, A.2
  • 27
    • 0029028596 scopus 로고
    • Synthesis and use of iodo-fatty acid analogs
    • Berthiaume, L., Peseckis, S. M. and Resh, M. D. (1995) Synthesis and use of iodo-fatty acid analogs. Methods Enzymol. 250, 454-466
    • (1995) Methods Enzymol. , vol.250 , pp. 454-466
    • Berthiaume, L.1    Peseckis, S.M.2    Resh, M.D.3
  • 28
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 29
    • 0028224736 scopus 로고
    • Regulation of enzymatic activity by active site fatty acylation. A new role for long chain fatty acid acylation of proteins
    • Berthiaume, L., Deichaite, I., Peseckis, S. and Resh, M. D. (1994) Regulation of enzymatic activity by active site fatty acylation. A new role for long chain fatty acid acylation of proteins. J. Biol. Chem. 269, 6498-6505
    • (1994) J. Biol. Chem. , vol.269 , pp. 6498-6505
    • Berthiaume, L.1    Deichaite, I.2    Peseckis, S.3    Resh, M.D.4
  • 30
    • 0026041477 scopus 로고
    • Identification and immunolocalization of calreticulin in pancreatic cells: No evidence for "calciosomes"
    • Michalak, M., Baksh, S. and Opas, M. (1991) Identification and immunolocalization of calreticulin in pancreatic cells: no evidence for "calciosomes". Exp. Cell Res. 197, 91-99
    • (1991) Exp. Cell Res. , vol.197 , pp. 91-99
    • Michalak, M.1    Baksh, S.2    Opas, M.3
  • 31
    • 0026781532 scopus 로고
    • The assembly and secretion of ApoB 100-containing lipoproteins in Hep G2 cells. ApoB 100 is cotranslationally integrated into lipoproteins
    • Boren, J., Graham, L., Wettesten, M., Scott, J., White, A. and Olofsson, S. O. (1992) The assembly and secretion of ApoB 100-containing lipoproteins in Hep G2 cells. ApoB 100 is cotranslationally integrated into lipoproteins. J. Biol. Chem. 267, 9858-9867
    • (1992) J. Biol. Chem. , vol.267 , pp. 9858-9867
    • Boren, J.1    Graham, L.2    Wettesten, M.3    Scott, J.4    White, A.5    Olofsson, S.O.6
  • 32
    • 0027375043 scopus 로고
    • Influence of triacylglycerol biosynthesis rate on the assembly of apoB-100-containing lipoproteins in Hep G2 cells
    • Boren, J., Rustaeus, S., Wettesten, M., Andersson, M., Wiklund, A. and Olofsson, S. O. (1993) Influence of triacylglycerol biosynthesis rate on the assembly of apoB-100-containing lipoproteins in Hep G2 cells. Arterioscler. Thromb. 13, 1743-1754
    • (1993) Arterioscler. Thromb. , vol.13 , pp. 1743-1754
    • Boren, J.1    Rustaeus, S.2    Wettesten, M.3    Andersson, M.4    Wiklund, A.5    Olofsson, S.O.6
  • 33
    • 0034616389 scopus 로고    scopus 로고
    • The assembly and secretion of apolipoprotein B-48-containing very low density lipoproteins in McA-RH7777 cells
    • Stillemark, P., Boren, J., Andersson, M., Larsson, T., Rustaeus, S., Karlsson, K. A. and Olofsson, S. O. (2000) The assembly and secretion of apolipoprotein B-48-containing very low density lipoproteins in McA-RH7777 cells. J. Biol. Chem. 275, 10506-10513
    • (2000) J. Biol. Chem. , vol.275 , pp. 10506-10513
    • Stillemark, P.1    Boren, J.2    Andersson, M.3    Larsson, T.4    Rustaeus, S.5    Karlsson, K.A.6    Olofsson, S.O.7
  • 34
    • 0012003976 scopus 로고
    • Isolation and characterization of membranes and cell organelles
    • Rickwood, D. and Hames, B. D., eds., Oxford University Press, New York
    • Evans, W. H. (1992) Isolation and characterization of membranes and cell organelles. In Preparative Centrifugation: a Practical Approach (Rickwood, D. and Hames, B. D., eds.), pp. 233-270, Oxford University Press, New York
    • (1992) Preparative Centrifugation: A Practical Approach , pp. 233-270
    • Evans, W.H.1
  • 35
    • 0041534302 scopus 로고    scopus 로고
    • Synthesis and sorting of plasma membrane, secretory, and lysosomal proteins
    • Scientific American Books, New York
    • Lodish, H., Baltimore, D., Berk, A., Zipursky, S. L., Matsudaira, P. and Darnell, J. (1996) Synthesis and sorting of plasma membrane, secretory, and lysosomal proteins. In Molecular Cell Biology, pp. 700-711, Scientific American Books, New York
    • (1996) Molecular Cell Biology , pp. 700-711
    • Lodish, H.1    Baltimore, D.2    Berk, A.3    Zipursky, S.L.4    Matsudaira, P.5    Darnell, J.6
  • 37
    • 0033597829 scopus 로고    scopus 로고
    • Bulk flow redux?
    • Warren, G. and Mellman, I. (1999) Bulk flow redux? Cell 98, 125-127
    • (1999) Cell , vol.98 , pp. 125-127
    • Warren, G.1    Mellman, I.2
  • 38
    • 0038190928 scopus 로고    scopus 로고
    • Assembly and secretion of very low density lipoproteins containing apolipoprotein B48 in transfected McA-RH7777 cells. Lack of evidence that palmitoylation of apolipoprotein B48 is required for lipoprotein secretion
    • Vukmirica, J., Tran, K., Liang, X., Shan, J., Yuan, J., Miskie, B. A., Hegele, R. A., Resh, M. D. and Yao, Z. (2003) Assembly and secretion of very low density lipoproteins containing apolipoprotein B48 in transfected McA-RH7777 cells. Lack of evidence that palmitoylation of apolipoprotein B48 is required for lipoprotein secretion. J. Biol. Chem. 278, 14153-14161
    • (2003) J. Biol. Chem. , vol.278 , pp. 14153-14161
    • Vukmirica, J.1    Tran, K.2    Liang, X.3    Shan, J.4    Yuan, J.5    Miskie, B.A.6    Hegele, R.A.7    Resh, M.D.8    Yao, Z.9
  • 39
    • 0027076741 scopus 로고
    • Role of acylation of viral haemagglutinin during the influenza virus infectious cycle
    • Portincasa, P., Conti, G. and Chezzi, C. (1992) Role of acylation of viral haemagglutinin during the influenza virus infectious cycle. Res. Virol. 143, 401-406
    • (1992) Res. Virol. , vol.143 , pp. 401-406
    • Portincasa, P.1    Conti, G.2    Chezzi, C.3
  • 40
    • 0034610368 scopus 로고    scopus 로고
    • Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity
    • Rousso, I., Mixon, M. B., Chen, B. K. and Kim, P. S. (2000) Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity. Proc. Natl. Acad. Sci. U.S.A. 97, 13523-13525
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13523-13525
    • Rousso, I.1    Mixon, M.B.2    Chen, B.K.3    Kim, P.S.4
  • 41
    • 0029670903 scopus 로고    scopus 로고
    • Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting
    • Schweizer, A., Kornfeld, S. and Rohrer, J. (1996) Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting. J. Cell Biol. 132, 577-584
    • (1996) J. Cell Biol. , vol.132 , pp. 577-584
    • Schweizer, A.1    Kornfeld, S.2    Rohrer, J.3
  • 42
    • 0025149021 scopus 로고
    • Inhibition of the receptor-mediated endocytosis of diferric transferrin is associated with the covalent modification of the transferrin receptor with palmitic acid
    • Alvarez, E., Girones, N. and Davis, R. J. (1990) Inhibition of the receptor-mediated endocytosis of diferric transferrin is associated with the covalent modification of the transferrin receptor with palmitic acid. J. Biol. Chem. 265, 16644-16655
    • (1990) J. Biol. Chem. , vol.265 , pp. 16644-16655
    • Alvarez, E.1    Girones, N.2    Davis, R.J.3
  • 43
    • 0029833903 scopus 로고    scopus 로고
    • Palmitoylation of endothelin receptor A. Differential modulation of signal transduction activity by post-translational modification
    • Horstmeyer, A., Cramer, H., Sauer, T., Muller-Esterl, W. and Schroeder, C. (1996) Palmitoylation of endothelin receptor A. Differential modulation of signal transduction activity by post-translational modification. J. Biol. Chem. 271, 20811-20819
    • (1996) J. Biol. Chem. , vol.271 , pp. 20811-20819
    • Horstmeyer, A.1    Cramer, H.2    Sauer, T.3    Muller-Esterl, W.4    Schroeder, C.5
  • 44
    • 0031569809 scopus 로고    scopus 로고
    • Palmitoylation of muscarinic acetylcholine receptor m2 subtypes: Reduction in their ability to activate G proteins by mutation of a putative palmitoylation site, cysteine 457, in the carboxyl-terminal tail
    • Hayashi, M. K. and Haga, T. (1997) Palmitoylation of muscarinic acetylcholine receptor m2 subtypes: reduction in their ability to activate G proteins by mutation of a putative palmitoylation site, cysteine 457, in the carboxyl-terminal tail. Arch. Biochem. Biophys. 340, 376-382
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 376-382
    • Hayashi, M.K.1    Haga, T.2
  • 45
    • 0035851198 scopus 로고    scopus 로고
    • Palmitoylation of the vasopressin V1a receptor reveals different conformational requirements for signaling, agonist-induced receptor phosphorylation, and sequestration
    • Hawtin, S. R., Tobin, A. B., Patel, S. and Wheatley, M. (2001) Palmitoylation of the vasopressin V1a receptor reveals different conformational requirements for signaling, agonist-induced receptor phosphorylation, and sequestration. J. Biol. Chem. 276 38139-38146
    • (2001) J. Biol. Chem. , vol.276 , pp. 38139-38146
    • Hawtin, S.R.1    Tobin, A.B.2    Patel, S.3    Wheatley, M.4
  • 46
    • 17144467725 scopus 로고    scopus 로고
    • Insider information: How palmitoylation of Ras makes it a signaling double agent
    • Berthiaume, L. G. (2002) Insider information: how palmitoylation of Ras makes it a signaling double agent. Science STKE 2002, PE41
    • (2002) Science STKE , vol.2002
    • Berthiaume, L.G.1
  • 47
    • 0029908325 scopus 로고    scopus 로고
    • Exposed thiols confer localization in the endoplasmic reticulum by retention rather than retrieval
    • Isidore, C., Maggioni, C., Demoz, M., Pizzagalli, A., Fra, A. M. and Sitia, R. (1996) Exposed thiols confer localization in the endoplasmic reticulum by retention rather than retrieval. J. Biol. Chem. 271, 26138-26142
    • (1996) J. Biol. Chem. , vol.271 , pp. 26138-26142
    • Isidore, C.1    Maggioni, C.2    Demoz, M.3    Pizzagalli, A.4    Fra, A.M.5    Sitia, R.6
  • 48
    • 0034717028 scopus 로고    scopus 로고
    • Disulfide bonds are required for folding and secretion of apolipoproiein B regardless of its lipidation slate
    • Burch, W. L. and Herscovitz, H. (2000) Disulfide bonds are required for folding and secretion of apolipoproiein B regardless of its lipidation slate. J. Biol. Chem. 275, 16267-16274
    • (2000) J. Biol. Chem. , vol.275 , pp. 16267-16274
    • Burch, W.L.1    Herscovitz, H.2
  • 49
    • 0027966127 scopus 로고
    • Secretion of apolipoprotein B-containing lipoproteins from HeLa cells is dependent on expression of the microsomal triglyceride transfer protein and is regulated by lipid availability
    • Gordon, D. A., Jamil, H., Sharp, D., Mullaney, D., Yao, Z., Gregg, R. E. and Wetterau, J. (1994) Secretion of apolipoprotein B-containing lipoproteins from HeLa cells is dependent on expression of the microsomal triglyceride transfer protein and is regulated by lipid availability. Proc. Natl. Acad. Sci. U.S.A. 91, 7628-7632
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7628-7632
    • Gordon, D.A.1    Jamil, H.2    Sharp, D.3    Mullaney, D.4    Yao, Z.5    Gregg, R.E.6    Wetterau, J.7
  • 50
    • 0030860899 scopus 로고    scopus 로고
    • The degradation of apolipoprotein B100 is mediated by the ubiqultin-proteasome pathway and involves heat shock protein 70
    • Fisher, E. A., Zhou, M., Mitchell, D. M., Wu, X., Omura, S., Wang, H., Goldberg, A. L. and Ginsberg, H. N. (1997) The degradation of apolipoprotein B100 is mediated by the ubiqultin-proteasome pathway and involves heat shock protein 70. J. Biol. Chem. 272, 20427-20434
    • (1997) J. Biol. Chem. , vol.272 , pp. 20427-20434
    • Fisher, E.A.1    Zhou, M.2    Mitchell, D.M.3    Wu, X.4    Omura, S.5    Wang, H.6    Goldberg, A.L.7    Ginsberg, H.N.8
  • 51
    • 0030906716 scopus 로고    scopus 로고
    • Role of lipid synthesis, chaperone proteins and proteasomes in the assembly and secretion of apoprotein B-containing lipoproteins from cultured liver cells
    • Ginsberg, H. N. (1997) Role of lipid synthesis, chaperone proteins and proteasomes in the assembly and secretion of apoprotein B-containing lipoproteins from cultured liver cells. Clin. Exp. Pharmacol. Physiol. 24, A29-A32
    • (1997) Clin. Exp. Pharmacol. Physiol. , vol.24
    • Ginsberg, H.N.1
  • 52
    • 0032865070 scopus 로고    scopus 로고
    • Cell and molecular biology of the assembly and secretion of apolipoprotein B-containing lipoproteins by the liver
    • Davis, R. A. (1999) Cell and molecular biology of the assembly and secretion of apolipoprotein B-containing lipoproteins by the liver. Biochim. Biophys. Acta 1440, 1-31
    • (1999) Biochim. Biophys. Acta , vol.1440 , pp. 1-31
    • Davis, R.A.1
  • 53
    • 0033827087 scopus 로고    scopus 로고
    • Apolipoprotein B: mRNA editing, lipoprotein assembly, and presecretory degradation
    • Davidson, N. O. and Shelness, G. S. (2000) Apolipoprotein B: mRNA editing, lipoprotein assembly, and presecretory degradation. Annu. Rev. Nutr. 20, 169-193
    • (2000) Annu. Rev. Nutr. , vol.20 , pp. 169-193
    • Davidson, N.O.1    Shelness, G.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.