메뉴 건너뛰기




Volumn 43, Issue 12, 2002, Pages 2017-2030

Carboxyl ester lipase: Structure-function relationship and physiological role in lipoprotein metabolism and atherosclerosis

Author keywords

Atherosclerosis; Cholesterol absorption; Chylomicron assembly; Lipid absorption; Reverse cholesterol transport

Indexed keywords

ASPARTIC ACID; BILE SALT; CARBOXYL ESTER LIPASE; CHOLESTEROL ESTER; CHOLESTEROL ESTERASE; CHYLOMICRON; DIACYLGLYCEROL; HISTIDINE; LIPOPROTEIN; LYSOPHOSPHOLIPID; MONOACYLGLYCEROL; OXIDIZED LOW DENSITY LIPOPROTEIN; PHOSPHOLIPID; SERINE; TRIACYLGLYCEROL; UNCLASSIFIED DRUG; BILE ACID; CARBOXYLESTERASE; VITAMIN;

EID: 0036915534     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: 10.1194/jlr.R200013-JLR200     Document Type: Review
Times cited : (199)

References (150)
  • 1
    • 0003022666 scopus 로고
    • Pancreatic carboxyl ester lipase (cholesterol esterase)
    • B. Borgstrom and H. L. Brockman, editors. Elsevier Science, New York, NY
    • Rudd, E. A., and H. L. Brockman. 1984. Pancreatic carboxyl ester lipase (cholesterol esterase). In Lipases. B. Borgstrom and H. L. Brockman, editors. Elsevier Science, New York, NY. 185-204.
    • (1984) Lipases , pp. 185-204
    • Rudd, E.A.1    Brockman, H.L.2
  • 2
    • 0027467140 scopus 로고
    • Bile salt-activated lipase: A multiple function lipolytic enzyme
    • Wang, C. S., and J. A. Hartsuck. 1993. Bile salt-activated lipase: A multiple function lipolytic enzyme. Biochim. Biophys. Acta. 1166: 1-19.
    • (1993) Biochim. Biophys. Acta , vol.1166 , pp. 1-19
    • Wang, C.S.1    Hartsuck, J.A.2
  • 3
    • 0030572703 scopus 로고    scopus 로고
    • Molecular biology of enzymes involved with cholesterol ester hydrolysis in mammalian tissues
    • Hui, D. Y. 1996. Molecular biology of enzymes involved with cholesterol ester hydrolysis in mammalian tissues. Biochim. Biophys. Acta. 1303: 1-14.
    • (1996) Biochim. Biophys. Acta , vol.1303 , pp. 1-14
    • Hui, D.Y.1
  • 4
    • 0024459947 scopus 로고
    • Expression in Xenopus oocytes of rat liver mRNA coding for a bile salt-dependent cholesteryl ester hydrolase
    • Zolfaghari, R., E. H. Harrison, A. C. Ross, and E. A. Fisher. 1989. Expression in Xenopus oocytes of rat liver mRNA coding for a bile salt-dependent cholesteryl ester hydrolase. Proc. Natl. Acad. Sci. USA. 86: 6913-6916.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6913-6916
    • Zolfaghari, R.1    Harrison, E.H.2    Ross, A.C.3    Fisher, E.A.4
  • 5
    • 0026607299 scopus 로고
    • Tissue and species differences in bile salt-dependent neutral cholesteryl ester hydrolase activity and gene expression
    • Zolfaghari, R., E. H. Harrison, J. H. Han, W. J. Rutter, and E. A. Fisher. 1992. Tissue and species differences in bile salt-dependent neutral cholesteryl ester hydrolase activity and gene expression. Arterioscler. Thromb. 12: 295-301.
    • (1992) Arterioscler. Thromb. , vol.12 , pp. 295-301
    • Zolfaghari, R.1    Harrison, E.H.2    Han, J.H.3    Rutter, W.J.4    Fisher, E.A.5
  • 6
    • 0024384937 scopus 로고
    • Identity of a cytozolic neutral cholesterol esterase in rat liver with the pancreatic bile salt stimulated cholesterol esterase
    • Camulli, E. A., M. J. Linke, H. L. Brockman, and D. Y. Hui. 1989. Identity of a cytozolic neutral cholesterol esterase in rat liver with the pancreatic bile salt stimulated cholesterol esterase. Biochim. Biophys. Acta. 1005: 177-182.
    • (1989) Biochim. Biophys. Acta , vol.1005 , pp. 177-182
    • Camulli, E.A.1    Linke, M.J.2    Brockman, H.L.3    Hui, D.Y.4
  • 8
    • 0029034721 scopus 로고
    • Presence in human eosinophils of a lysophospholipase similar to that found in the pancreas
    • Holtsberg, F. W., L. E. Ozgur, D. E. Garsetti, J. Myers, R. W. Egan, and M. A. Clark. 1995. Presence in human eosinophils of a lysophospholipase similar to that found in the pancreas. Biochem. J. 309: 141-144.
    • (1995) Biochem. J. , vol.309 , pp. 141-144
    • Holtsberg, F.W.1    Ozgur, L.E.2    Garsetti, D.E.3    Myers, J.4    Egan, R.W.5    Clark, M.A.6
  • 9
    • 0030658032 scopus 로고    scopus 로고
    • Modified low density lipoprotein enhances the secretion of bile salt-stimulated cholesterol esterase by human monocyte-macrophages. Species-specific difference in macrophage cholesteryl ester hydrola
    • Li, F., and D. Y. Hui. 1997. Modified low density lipoprotein enhances the secretion of bile salt-stimulated cholesterol esterase by human monocyte-macrophages. Species-specific difference in macrophage cholesteryl ester hydrola. J. Biol. Chem. 272:28666-28671.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28666-28671
    • Li, F.1    Hui, D.Y.2
  • 10
    • 0032007866 scopus 로고    scopus 로고
    • Synthesis and secretion of the pancreatic-type carboxyl ester lipase by human endothelial cells
    • Li, F., and D. Y. Hui. 1998. Synthesis and secretion of the pancreatic-type carboxyl ester lipase by human endothelial cells. Biochem. J. 329: 675-679.
    • (1998) Biochem. J. , vol.329 , pp. 675-679
    • Li, F.1    Hui, D.Y.2
  • 11
    • 0035968445 scopus 로고    scopus 로고
    • Bile salt-dependent lipase: Its pathophysiological implications
    • Lombardo, D. 2001. Bile salt-dependent lipase: Its pathophysiological implications. Biochim. Biophys. Acta. 1533: 1-28.
    • (2001) Biochim. Biophys. Acta , vol.1533 , pp. 1-28
    • Lombardo, D.1
  • 12
    • 0025184929 scopus 로고
    • Identification of the active site serine in pancreatic cholesterol esterase by chemical modification and site specific mutagenesis
    • DiPersio, L. P., R. N. Fontaine, and D. Y. Hui. 1990. Identification of the active site serine in pancreatic cholesterol esterase by chemical modification and site specific mutagenesis. J. Biol. Chem. 265: 16801-16806.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16801-16806
    • DiPersio, L.P.1    Fontaine, R.N.2    Hui, D.Y.3
  • 13
    • 0025884172 scopus 로고
    • Site-specific mutagenesis of an essential histidine residue in pancreatic cholesterol esterase
    • DiPersio, L. P., R. N. Fontaine, and D. Y. Hui. 1991. Site-specific mutagenesis of an essential histidine residue in pancreatic cholesterol esterase. J. Biol. Chem. 266: 4033-4036.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4033-4036
    • DiPersio, L.P.1    Fontaine, R.N.2    Hui, D.Y.3
  • 14
    • 0021984457 scopus 로고
    • Acylenzyme mechanism and solvent isotope effects for cholesterol esterasecatalyzed hydrolysis of p-nitrophenyl butyrate
    • Stout, J. S., L. D. Sutton, and D. M. Quinn. 1985. Acylenzyme mechanism and solvent isotope effects for cholesterol esterasecatalyzed hydrolysis of p-nitrophenyl butyrate. Biochim. Biophys. Acta. 837: 6-12.
    • (1985) Biochim. Biophys. Acta , vol.837 , pp. 6-12
    • Stout, J.S.1    Sutton, L.D.2    Quinn, D.M.3
  • 15
    • 0031012947 scopus 로고    scopus 로고
    • Molecular modeling of the structures of human and rat pancreatic cholesterol esterases
    • Feaster, S. R., D. M. Quinn, and B. I., Barnett. 1997. Molecular modeling of the structures of human and rat pancreatic cholesterol esterases. Protein Sci. 6: 73-79.
    • (1997) Protein Sci. , vol.6 , pp. 73-79
    • Feaster, S.R.1    Quinn, D.M.2    Barnett, B.I.3
  • 16
    • 0027402684 scopus 로고
    • Aspartic acid 320 is required for optimal activity of rat pancreatic cholesterol esterase
    • DiPersio, L. P., and D. Y Hui. 1993. Aspartic acid 320 is required for optimal activity of rat pancreatic cholesterol esterase. J. Biol. Chem. 268: 300-304.
    • (1993) J. Biol. Chem. , vol.268 , pp. 300-304
    • DiPersio, L.P.1    Hui, D.Y.2
  • 17
    • 0027478486 scopus 로고
    • Lipoamidase activity in normal and mutagenized pancreatic cholesterol esterase (bile salt-stimulated lipase)
    • Hui, D. Y., K. Hayakawa, and J. Oizumi. 1993. Lipoamidase activity in normal and mutagenized pancreatic cholesterol esterase (bile salt-stimulated lipase). Biochem. J. 291: 65-69.
    • (1993) Biochem. J. , vol.291 , pp. 65-69
    • Hui, D.Y.1    Hayakawa, K.2    Oizumi, J.3
  • 19
    • 0037040172 scopus 로고    scopus 로고
    • Bile salt-stimulated carboxyl ester lipase influences lipoprotein assembly and secretion in intestine. A process mediated via ceramide hydrolysis
    • Kirby, R. J., S. Zheng, P. Tso, P. N. Howles, and D. Y. Hui. 2002. Bile salt-stimulated carboxyl ester lipase influences lipoprotein assembly and secretion in intestine. A process mediated via ceramide hydrolysis. J. Biol. Chem. 277: 4104-4109.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4104-4109
    • Kirby, R.J.1    Zheng, S.2    Tso, P.3    Howles, P.N.4    Hui, D.Y.5
  • 20
    • 0031572180 scopus 로고    scopus 로고
    • The crystal structure of bovine bile salt activated lipase: Insights into the bile salt activation mechanism
    • Wang, X., C. S. Wang, J. Tang, F. Dyda, and X. C. Zhang. 1997. The crystal structure of bovine bile salt activated lipase: Insights into the bile salt activation mechanism. Structure. 5: 1209-1218.
    • (1997) Structure , vol.5 , pp. 1209-1218
    • Wang, X.1    Wang, C.S.2    Tang, J.3    Dyda, F.4    Zhang, X.C.5
  • 22
    • 0035929324 scopus 로고    scopus 로고
    • The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active site loop and provides insights into heparin binding
    • Moore, S. A., R. L. Kingston, K. M. Loomes, O. Hernell, L. Blackberg, H. M. Baker, and E. N. Baker. 2001. The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active site loop and provides insights into heparin binding. J. Mo. Biol. 312: 511-523.
    • (2001) J. Mo. Biol. , vol.312 , pp. 511-523
    • Moore, S.A.1    Kingston, R.L.2    Loomes, K.M.3    Hernell, O.4    Blackberg, L.5    Baker, H.M.6    Baker, E.N.7
  • 23
    • 0030768420 scopus 로고    scopus 로고
    • Structure as a basis for understanding interfacial properties of lipases
    • Cugler, M., and J. D. Schrag. 1997. Structure as a basis for understanding interfacial properties of lipases. Methods Enzymol. 284: 3-27.
    • (1997) Methods Enzymol. , vol.284 , pp. 3-27
    • Cugler, M.1    Schrag, J.D.2
  • 24
    • 0019841747 scopus 로고
    • Bile salt-stimulated lipase in human milk and carboxyl ester hydrolase in pancreatic juice
    • Blackberg, L., D. Lombardo, O. Hernell, O. Guy, and T. Olivecrona. 1981. Bile salt-stimulated lipase in human milk and carboxyl ester hydrolase in pancreatic juice. FEBS Lett. 136: 284-288.
    • (1981) FEBS Lett. , vol.136 , pp. 284-288
    • Blackberg, L.1    Lombardo, D.2    Hernell, O.3    Guy, O.4    Olivecrona, T.5
  • 25
    • 0020966819 scopus 로고
    • Oh the probable involvement of arginine residues in the bile salt binding site of human pancreatic carboxylic ester hydrolase
    • Lombardo, D., D. Campese, L. Multigner, H. LaFont, and A. DeCaro. 1983. Oh the probable involvement of arginine residues in the bile salt binding site of human pancreatic carboxylic ester hydrolase. Eur. J. Biochem. 133: 327-333.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 327-333
    • Lombardo, D.1    Campese, D.2    Multigner, L.3    LaFont, H.4    DeCaro, A.5
  • 26
    • 0027204575 scopus 로고
    • Bile salt-stimulated lipase in human milk. Evidence that bile salt induces lipid binding and activation via hinding to different sites
    • Blackberg, L., and O. Hernell. 1993. Bile salt-stimulated lipase in human milk. Evidence that bile salt induces lipid binding and activation via hinding to different sites. FEBS Lett. 323: 207-210.
    • (1993) FEBS Lett. , vol.323 , pp. 207-210
    • Blackberg, L.1    Hernell, O.2
  • 27
    • 0028053729 scopus 로고
    • Pancreatic carboxylester lipase from Atlantic salmon (Salmo salar). cDNA sequence and computer-assisted modelling of tertiary structure
    • Gejellesvik, D. R., J. B. Lorens, and R. Male. 1994. Pancreatic carboxylester lipase from Atlantic salmon (Salmo salar). cDNA sequence and computer-assisted modelling of tertiary structure. Eur. J. Biochem. 226: 603-612.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 603-612
    • Gejellesvik, D.R.1    Lorens, J.B.2    Male, R.3
  • 28
    • 0034604561 scopus 로고    scopus 로고
    • Importance of arginines 63 and 423 in modulating the bile salt-dependent and bile salt-independent hydrolytic activities of rat carboxyl ester lipase
    • Liang, Y., R. Medhekar, H. L. Brockman, D. M. Quinn, and D. Y. Hui. 2000. Importance of arginines 63 and 423 in modulating the bile salt-dependent and bile salt-independent hydrolytic activities of rat carboxyl ester lipase. J. Biol. Chem. 275: 24040-24046.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24040-24046
    • Liang, Y.1    Medhekar, R.2    Brockman, H.L.3    Quinn, D.M.4    Hui, D.Y.5
  • 29
    • 0025186770 scopus 로고
    • Sodium cholate-induced changes in the conformation and activity of rat pancreatic cholesterol esterase
    • Jacobson, P. W., P. W. Wiesenfeld, L. L. Gallo, R. L. Tate, and J. C. Osborne. 1990. Sodium cholate-induced changes in the conformation and activity of rat pancreatic cholesterol esterase. J. Biol. Chem. 268: 515-521.
    • (1990) J. Biol. Chem. , vol.268 , pp. 515-521
    • Jacobson, P.W.1    Wiesenfeld, P.W.2    Gallo, L.L.3    Tate, R.L.4    Osborne, J.C.5
  • 30
    • 0025685397 scopus 로고
    • Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase
    • Hui, D. Y., and J. A. Kissel. 1990. Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase. FEBS Lett. 276: 131-134.
    • (1990) FEBS Lett. , vol.276 , pp. 131-134
    • Hui, D.Y.1    Kissel, J.A.2
  • 32
    • 0036181364 scopus 로고    scopus 로고
    • Human bile salt-stimulated lipase has a high frequency of size variation due to a hypervariable region in exon 11
    • Lindquist, S., L. Blackberg, and O. Hernell. 2002. Human bile salt-stimulated lipase has a high frequency of size variation due to a hypervariable region in exon 11. Eur. J. Biochem. 269: 759-767.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 759-767
    • Lindquist, S.1    Blackberg, L.2    Hernell, O.3
  • 33
    • 0030833432 scopus 로고    scopus 로고
    • O-glycosylation of C-terminal tandem repeated sequences regulates the secretion of rat pancreatic bile salt dependent lipase
    • Bruneau, N., A. Nganga, E. A. Fisher, and D. Lombardo. 1997. O-glycosylation of C-terminal tandem repeated sequences regulates the secretion of rat pancreatic bile salt dependent lipase. J. Biol. Chem. 272: 27353-27361.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27353-27361
    • Bruneau, N.1    Nganga, A.2    Fisher, E.A.3    Lombardo, D.4
  • 35
    • 0031297858 scopus 로고    scopus 로고
    • Identification of 5′-flanking sequences that affect human pancreatic cholesterol esterase gene expression
    • Kumar, V. B., T. Sasser, J. B. Mandava, H. Al Sadi, and C. Spilburg. 1997. Identification of 5′-flanking sequences that affect human pancreatic cholesterol esterase gene expression. Biochim. Cell Biol. 75: 247-254.
    • (1997) Biochim. Cell Biol. , vol.75 , pp. 247-254
    • Kumar, V.B.1    Sasser, T.2    Mandava, J.B.3    Al Sadi, H.4    Spilburg, C.5
  • 36
    • 0025355489 scopus 로고
    • Pancreatic cholesterol esterases. I. Pancreatic cholesterol esterase induction during maturation
    • Cox, D. G., C. K. T. Leung, E. M. Kyger, C. A. Spilburg, and L. G. Lange. 1990. Pancreatic cholesterol esterases. I. Pancreatic cholesterol esterase induction during maturation. Biochemistry. 29: 3842-3848.
    • (1990) Biochemistry , vol.29 , pp. 3842-3848
    • Cox, D.G.1    Leung, C.K.T.2    Kyger, E.M.3    Spilburg, C.A.4    Lange, L.G.5
  • 37
    • 0016277571 scopus 로고
    • Human milk lipases. II. Bile salt stimulated lipase
    • Hernell, O., and T. Olivecrona. 1974. Human milk lipases. II. Bile salt stimulated lipase. Biochim. Biophys. Acta. 369: 234-244.
    • (1974) Biochim. Biophys. Acta , vol.369 , pp. 234-244
    • Hernell, O.1    Olivecrona, T.2
  • 38
    • 0025183485 scopus 로고
    • cDNA cloning of human milk bile salt stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase
    • Nilsson, J., L. Blackberg, P. Carlsson, S. Enerback, O. Hemell, and G. Bjursell. 1990. cDNA cloning of human milk bile salt stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. Eur. J. Biochem. 192: 543-550.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 543-550
    • Nilsson, J.1    Blackberg, L.2    Carlsson, P.3    Enerback, S.4    Hemell, O.5    Bjursell, G.6
  • 39
  • 40
    • 0029097743 scopus 로고
    • Molecular cloning and characterization of the mouse carboxyl ester lipase gene and evidence for expression in the lactating mammary gland
    • Lidmer, A. S., M. Kannius, L. Lundberg, G. Bjursell, and J. Nilsson: 1995. Molecular cloning and characterization of the mouse carboxyl ester lipase gene and evidence for expression in the lactating mammary gland. Genomics. 29: 115-122.
    • (1995) Genomics , vol.29 , pp. 115-122
    • Lidmer, A.S.1    Kannius, M.2    Lundberg, L.3    Bjursell, G.4    Nilsson, J.5
  • 42
    • 0032553423 scopus 로고    scopus 로고
    • Transcriptional regulation of the human carboxyl ester lipase gene in exocrine pancreas. Evidence for a unique tissue-specific enhancer
    • Lidberg, U., M. Kannius-Janson, J. Nilsson, and G. Bjursell. 1998. Transcriptional regulation of the human carboxyl ester lipase gene in exocrine pancreas. Evidence for a unique tissue-specific enhancer. J. Biol. Chem. 273: 31417-31426.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31417-31426
    • Lidberg, U.1    Kannius-Janson, M.2    Nilsson, J.3    Bjursell, G.4
  • 43
    • 0026660088 scopus 로고
    • Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene
    • Lidberg, U., J. Nilsson, K. Stromberg, G. Stenman, P. Sahlin, S. Enerback, and G. Bjursell. 1992. Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene. Genomica. 13: 630-640.
    • (1992) Genomica. , vol.13 , pp. 630-640
    • Lidberg, U.1    Nilsson, J.2    Stromberg, K.3    Stenman, G.4    Sahlin, P.5    Enerback, S.6    Bjursell, G.7
  • 44
    • 0021265935 scopus 로고
    • Similarity of the nucleotide sequences of rat alpha-lactalbumin and the chicken lysozyme genes
    • Qasba, M., and S. K. Safaya. 1984. Similarity of the nucleotide sequences of rat alpha-lactalbumin and the chicken lysozyme genes. Nature. 308: 377-380.
    • (1984) Nature , vol.308 , pp. 377-380
    • Qasba, M.1    Safaya, S.K.2
  • 45
    • 0022649663 scopus 로고
    • Evolution of the casein multigene family: Conserved sequences in the 5′ flanking and exon regions
    • Yu-Lee, L., L. Richter-Mann, C. Couch, F. Stewart, G. Mackinlay, and J. Rosen. 1986. Evolution of the casein multigene family: Conserved sequences in the 5′ flanking and exon regions. Nucleic Acids Res. 14: 1883-1902.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 1883-1902
    • Yu-Lee, L.1    Richter-Mann, L.2    Couch, C.3    Stewart, F.4    Mackinlay, G.5    Rosen, J.6
  • 46
    • 0037101764 scopus 로고    scopus 로고
    • Transcriptional regulation of the human carboxyl ester lipase gene in THP-1 monocytes: An E-box required for activation binds upstream stimulatory factors 1 and 2
    • Bengtsson; S. H. M., K. Madeyski-Bengtson, J. Nilsson, and G. Bjursell. 2002. Transcriptional regulation of the human carboxyl ester lipase gene in THP-1 monocytes: An E-box required for activation binds upstream stimulatory factors 1 and 2. Biochem. J. 365: 481-488.
    • (2002) Biochem. J. , vol.365 , pp. 481-488
    • Bengtsson, S.H.M.1    Madeyski-Bengtson, K.2    Nilsson, J.3    Bjursell, G.4
  • 47
    • 0025642582 scopus 로고
    • Metabolic fate of pancreasderived cholesterol esterase in intestine. An in vitro study using Caco-2 cells
    • Huang, Y., and D. Y. Hui. 1990. Metabolic fate of pancreasderived cholesterol esterase in intestine. An in vitro study using Caco-2 cells. J. Lipid Res. 31: 2029-2037.
    • (1990) J. Lipid Res. , vol.31 , pp. 2029-2037
    • Huang, Y.1    Hui, D.Y.2
  • 48
    • 0027434874 scopus 로고
    • Cholesterol transport function of pancreatic cholesterol esterase: Directed sterol uptake and esterification in enterocytes
    • Lopez-Candales, A., M. S. Bosner, C. A. Spilburg, and L. G. Lange. 1993. Cholesterol transport function of pancreatic cholesterol esterase: Directed sterol uptake and esterification in enterocytes. Biochemistry. 32: 12085-12089.
    • (1993) Biochemistry , vol.32 , pp. 12085-12089
    • Lopez-Candales, A.1    Bosner, M.S.2    Spilburg, C.A.3    Lange, L.G.4
  • 49
    • 0029066878 scopus 로고
    • Role of bile salt-dependent cholesteryl ester hydrolase in the uptake of micellar cholesterol by intestinal cells
    • Shamir, R., W. J. Johnson, R. Zolfaghari, H. S. Lee, and E. A. Fisher. 1995. Role of bile salt-dependent cholesteryl ester hydrolase in the uptake of micellar cholesterol by intestinal cells. Biochemistry. 34: 6351-6358.
    • (1995) Biochemistry , vol.34 , pp. 6351-6358
    • Shamir, R.1    Johnson, W.J.2    Zolfaghari, R.3    Lee, H.S.4    Fisher, E.A.5
  • 50
    • 0030949925 scopus 로고    scopus 로고
    • Phosphatidylcholine hydrolysis is required for pancreatic cholesterol esterase- and phospholipase A2-facilitated cholesterol uptake into intestinal Caco-2 cells
    • Mackay, K., J. R. Starr, R. M. Lawn, and J. L. Ellsworth. 1997. Phosphatidylcholine hydrolysis is required for pancreatic cholesterol esterase- and phospholipase A2-facilitated cholesterol uptake into intestinal Caco-2 cells. J. Biol. Chem. 272:13380-13389.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13380-13389
    • Mackay, K.1    Starr, J.R.2    Lawn, R.M.3    Ellsworth, J.L.4
  • 51
    • 0015547044 scopus 로고
    • Lingual lipase and its role in the digestion of dietary, lipid
    • Hamosh, M., and R. O. Scow. 1973. Lingual lipase and its role in the digestion of dietary, lipid. J. Clin. Invest. 52: 88-95.
    • (1973) J. Clin. Invest. , vol.52 , pp. 88-95
    • Hamosh, M.1    Scow, R.O.2
  • 52
    • 0025731269 scopus 로고
    • Milk lipid digestion in the neonatal dog: The combined actions of gastric and bile salt stimulated lipase
    • Iverson, S. J., C. L. Kirk, M. Manosh, and J. Newsome. 1991. Milk lipid digestion in the neonatal dog: The combined actions of gastric and bile salt stimulated lipase. Biochim. Biophys. Acta. 1083: 109-119.
    • (1991) Biochim. Biophys. Acta , vol.1083 , pp. 109-119
    • Iverson, S.J.1    Kirk, C.L.2    Manosh, M.3    Newsome, J.4
  • 53
    • 0033746041 scopus 로고    scopus 로고
    • Intracellular events in the assembly of chylomicrons in rabbit enterocytes
    • Cartwright, I. J., D. Plonne, and J. A. Higgins. 2000. Intracellular events in the assembly of chylomicrons in rabbit enterocytes. J. Lipid Res. 41: 1728-1739.
    • (2000) J. Lipid Res. , vol.41 , pp. 1728-1739
    • Cartwright, I.J.1    Plonne, D.2    Higgins, J.A.3
  • 54
    • 0031898269 scopus 로고    scopus 로고
    • Intracellular movement of triacylglycerols in the intestine
    • Mansbach, C. M., and P. Nevin. 1998. Intracellular movement of triacylglycerols in the intestine. J. Lipid Res. 39: 963-968.
    • (1998) J. Lipid Res. , vol.39 , pp. 963-968
    • Mansbach, C.M.1    Nevin, P.2
  • 55
    • 0025743782 scopus 로고
    • Apolipoprotein synthesis in normal and abetalipoproteinemic intestinal mucosa
    • Glickman, R. M., J. N. Glickman, A. Magnn, and M. Brin. 1991. Apolipoprotein synthesis in normal and abetalipoproteinemic intestinal mucosa. Gastroenterology. 101: 749-755.
    • (1991) Gastroenterology , vol.101 , pp. 749-755
    • Glickman, R.M.1    Glickman, J.N.2    Magnn, A.3    Brin, M.4
  • 58
    • 0032895028 scopus 로고    scopus 로고
    • Remnant lipoprotein metabolism: Key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein E
    • Mahley, R. W., and Z. S. Ji. 1999. Remnant lipoprotein metabolism: Key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein E. J. Lipid Res. 40: 1-16.
    • (1999) J. Lipid Res. , vol.40 , pp. 1-16
    • Mahley, R.W.1    Ji, Z.S.2
  • 59
    • 0026561017 scopus 로고
    • A retinyl ester hydrolase activity intrinsic to the brush border membrane of rat small intestine
    • Rigtrup, K. M., and D. E. Ong. 1992. A retinyl ester hydrolase activity intrinsic to the brush border membrane of rat small intestine. Biochemistry. 31: 2920-2926.
    • (1992) Biochemistry , vol.31 , pp. 2920-2926
    • Rigtrup, K.M.1    Ong, D.E.2
  • 60
    • 0028238733 scopus 로고
    • Retinyl ester hydrolytic activity associated with human intestinal brush border membranes
    • Rigtrup, K. M., L. R. McEwen, H. M. Said, and D. E. Ong. 1994. Retinyl ester hydrolytic activity associated with human intestinal brush border membranes. Am. J. Clin. Nut. 60: 111-116.
    • (1994) Am. J. Clin. Nut. , vol.60 , pp. 111-116
    • Rigtrup, K.M.1    McEwen, L.R.2    Said, H.M.3    Ong, D.E.4
  • 62
    • 0019139563 scopus 로고
    • Localization and origin of rat intestinal cholesterol esterase determined by immunocytochemistry
    • Gallo, L. L., Y. Chiang, G. V. Vahouny, and C. R. Treadwell. 1980. Localization and origin of rat intestinal cholesterol esterase determined by immunocytochemistry. J. Lipid Res. 21: 537-545.
    • (1980) J. Lipid Res. , vol.21 , pp. 537-545
    • Gallo, L.L.1    Chiang, Y.2    Vahouny, G.V.3    Treadwell, C.R.4
  • 63
    • 0034004780 scopus 로고    scopus 로고
    • The affinity binding sites of pancreatic bile salt-dependent lipase in pancreatic and intestinal tissues
    • Bruncau, N., D. Lombardo, and M. Bendayan. 2000. The affinity binding sites of pancreatic bile salt-dependent lipase in pancreatic and intestinal tissues. J. Histochem. Cytochem. 48: 267-276.
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 267-276
    • Bruncau, N.1    Lombardo, D.2    Bendayan, M.3
  • 64
    • 0035890263 scopus 로고    scopus 로고
    • Transcytosis of pancreatic bile salt-dependent lipase through human Int407 intestinal cells
    • Bruneau, N., A. Nganga, M. Bendayan, and D. Lombardo. 2001. Transcytosis of pancreatic bile salt-dependent lipase through human Int407 intestinal cells. Exp. Cell Res. 271: 94-108.
    • (2001) Exp. Cell Res. , vol.271 , pp. 94-108
    • Bruneau, N.1    Nganga, A.2    Bendayan, M.3    Lombardo, D.4
  • 65
    • 0024306906 scopus 로고
    • Molecular cloning and expression of cDNA for rat pancreatic cholesterol esterase
    • Kissel, J. A., R. N. Fontaine, C. Turck, H. L. Brockman, and D. Y. Hui. 1989. Molecular cloning and expression of cDNA for rat pancreatic cholesterol esterase. Biochim. Biophys. Acta. 1006: 227-236.
    • (1989) Biochim. Biophys. Acta , vol.1006 , pp. 227-236
    • Kissel, J.A.1    Fontaine, R.N.2    Turck, C.3    Brockman, H.L.4    Hui, D.Y.5
  • 66
    • 0031696368 scopus 로고    scopus 로고
    • Participation of GRP94-related protein in secretion of pancreatic bile saltdependent lipase and in its internalization by the intestinal epithelium
    • Bruneau, N., D. Lombardo, and M. Bendayan. 1998. Participation of GRP94-related protein in secretion of pancreatic bile saltdependent lipase and in its internalization by the intestinal epithelium. J. Cell Sci. 111: 2665-2679.
    • (1998) J. Cell Sci. , vol.111 , pp. 2665-2679
    • Bruneau, N.1    Lombardo, D.2    Bendayan, M.3
  • 68
    • 0003144604 scopus 로고
    • Prenatal and posnatal development of the human exocrine pancreas
    • Liang and W. Go. editors. Raven Press, New York, NY
    • Lee, P. C., and E. Lebenthal. 1993. Prenatal and posnatal development of the human exocrine pancreas. In The Pancreas: Biology, Pathobiology, and Disease. V. Liang and W. Go. editors. Raven Press, New York, NY. 57-173.
    • (1993) The Pancreas: Biology, Pathobiology, and Disease , vol.5 , pp. 57-173
    • Lee, P.C.1    Lebenthal, E.2
  • 69
    • 0017846069 scopus 로고
    • Decrease of lipasc and esterase activities in intestinal contents of newborn infants during test meats
    • Fredrikzon, B., and T. Olivecrona. 1978. Decrease of lipasc and esterase activities in intestinal contents of newborn infants during test meats. Pediatr. Res. 12: 631-634.
    • (1978) Pediatr. Res. , vol.12 , pp. 631-634
    • Fredrikzon, B.1    Olivecrona, T.2
  • 70
    • 0018911087 scopus 로고
    • Development of functional responses in human exocrine pancreas
    • Lebenthal, F., and P. C. Lee. 1980. Development of functional responses in human exocrine pancreas. Pediatrics. 66: 556-560.
    • (1980) Pediatrics , vol.66 , pp. 556-560
    • Lebenthal, F.1    Lee, P.C.2
  • 71
    • 0017846667 scopus 로고
    • Effect of heat treatment of human milk on absorption of nitrogen, fat, sodium, and phosphorus by preterm infants
    • Williamson, S., E. Finucane, H. Ellis, and H. R. Gamsu. 1978. Effect of heat treatment of human milk on absorption of nitrogen, fat, sodium, and phosphorus by preterm infants. Arch. Dis. Child. 53: 555-563.
    • (1978) Arch. Dis. Child. , vol.53 , pp. 555-563
    • Williamson, S.1    Finucane, E.2    Ellis, H.3    Gamsu, H.R.4
  • 72
    • 0019492740 scopus 로고
    • Fat digestion in very low birth-weight infants: Effect of addition of human milk to low birth weight formula
    • Alemi, B., M. Hamosh, J. W. Scanlon, C. Salzman-Mann, and P. Hamosh. 1981. Fat digestion in very low birth-weight infants: Effect of addition of human milk to low birth weight formula. Pediatrics. 68: 484-489.
    • (1981) Pediatrics , vol.68 , pp. 484-489
    • Alemi, B.1    Hamosh, M.2    Scanlon, J.W.3    Salzman-Mann, C.4    Hamosh, P.5
  • 73
    • 0024506046 scopus 로고
    • Bile-salt-activated lipase: Effect on kitten growth rate
    • Wang, C. S., M. E. Martindale, M. M. King, and J. Tang. 1989. Bile-salt-activated lipase: Effect on kitten growth rate. Am. J. Clin. Nutr. 49: 457-463.
    • (1989) Am. J. Clin. Nutr. , vol.49 , pp. 457-463
    • Wang, C.S.1    Martindale, M.E.2    King, M.M.3    Tang, J.4
  • 74
    • 4243748955 scopus 로고    scopus 로고
    • Bile salt stimulated lipase is required for proper digestion and absorption of milk triglycerides in neonatal mice
    • Howles, P., B. Wagner, and L. Davis. 1998. Bile salt stimulated lipase is required for proper digestion and absorption of milk triglycerides in neonatal mice. (Abstract). FASEB J. 12: A851.
    • (1998) FASEB J , vol.12
    • Howles, P.1    Wagner, B.2    Davis, L.3
  • 75
    • 0032871233 scopus 로고    scopus 로고
    • Carboxyl ester lipase activity in milk prevents fatderived intestinal injury in neonatal mice
    • Howles, P. N., G. N. Stemmerman, C. M. Fenoglio-Preiser, and D. Y. Hui. 1999. Carboxyl ester lipase activity in milk prevents fatderived intestinal injury in neonatal mice. Am. J. Physiol. 277: G653-G661.
    • (1999) Am. J. Physiol. , vol.277
    • Howles, P.N.1    Stemmerman, G.N.2    Fenoglio-Preiser, C.M.3    Hui, D.Y.4
  • 76
    • 0028348475 scopus 로고
    • An animal model of necrotizing enterocolitis induced by infant formula and ischemia in developing piglets
    • Crissinger, K. D., D. L. Burney, O. R. Velasquez, and E. Gonzalez. 1994. An animal model of necrotizing enterocolitis induced by infant formula and ischemia in developing piglets. Gastroenterol. 106: 1215-1222.
    • (1994) Gastroenterol. , vol.106 , pp. 1215-1222
    • Crissinger, K.D.1    Burney, D.L.2    Velasquez, O.R.3    Gonzalez, E.4
  • 77
    • 0027300415 scopus 로고
    • Fatty acid-induced injury in developing piglet intestine: Effect of degree of saturation and carbon chain length
    • Velasquez, O. R., P. Tso, and K. D. Crinninger. 1993. Fatty acid-induced injury in developing piglet intestine: Effect of degree of saturation and carbon chain length. Pediatr. Res. 33: 543-547.
    • (1993) Pediatr. Res. , vol.33 , pp. 543-547
    • Velasquez, O.R.1    Tso, P.2    Crinninger, K.D.3
  • 79
    • 0028206885 scopus 로고
    • Developing intestine is injured during absorption of oleic acid but not its ethyl ester
    • Velasquez, O. R., A. R. Piace, P. Tso, and K. D. Crissinger. 1994. Developing intestine is injured during absorption of oleic acid but not its ethyl ester. J. Clin. Invest. 93: 479-485.
    • (1994) J. Clin. Invest. , vol.93 , pp. 479-485
    • Velasquez, O.R.1    Piace, A.R.2    Tso, P.3    Crissinger, K.D.4
  • 80
    • 0019497087 scopus 로고
    • Development of gastrointestinal mucosal barrier. II. The effect of natural versus artificial feeding on intestinal permeability to macromolecules
    • Udall, J. N., P. Colony, L. Fritze, K. Pang, J. S. Trier, and W. A. Walker. 1981. Development of gastrointestinal mucosal barrier. II. The effect of natural versus artificial feeding on intestinal permeability to macromolecules. Pediatr. Res. 15: 245-249.
    • (1981) Pediatr. Res. , vol.15 , pp. 245-249
    • Udall, J.N.1    Colony, P.2    Fritze, L.3    Pang, K.4    Trier, J.S.5    Walker, W.A.6
  • 81
    • 0025762725 scopus 로고
    • Neonatal gastrointestinal growth and function: Are they regulated by composition of feeds
    • Weaver, L. T., L. Landymore-Lim, and A. Lucas. 1991. Neonatal gastrointestinal growth and function: Are they regulated by composition of feeds. Biol. Neonate. 59: 330-345.
    • (1991) Biol. Neonate , vol.59 , pp. 330-345
    • Weaver, L.T.1    Landymore-Lim, L.2    Lucas, A.3
  • 82
    • 0027772447 scopus 로고
    • Intestinal ischemia in the newborn: The role of intestinal maturation
    • Musemeche, C. A., R. P. Pizzini, and R.J. Andrassy. 1993. Intestinal ischemia in the newborn: The role of intestinal maturation. J. Surg. Res. 55: 595-598.
    • (1993) J. Surg. Res. , vol.55 , pp. 595-598
    • Musemeche, C.A.1    Pizzini, R.P.2    Andrassy, R.J.3
  • 83
  • 85
    • 0024446393 scopus 로고
    • Hydrolysis of triacylglycerol arachidonic and linoleic acid ester bonds by human pancreatic lipase and carboxyl ester lipase
    • Chen, Q., B. Sternby, and A. Nilsson. 1989. Hydrolysis of triacylglycerol arachidonic and linoleic acid ester bonds by human pancreatic lipase and carboxyl ester lipase. Biochim. Biophys. Acta. 1004: 372-385.
    • (1989) Biochim. Biophys. Acta , vol.1004 , pp. 372-385
    • Chen, Q.1    Sternby, B.2    Nilsson, A.3
  • 86
    • 0025329858 scopus 로고
    • Effects of human pancreatic lipase-colipase and carboxyl ester lipase on eicosapentaenoic and arachidonic acid ester bonds of triacylglycerols rich in fish oil fatty acids
    • Chen, Q., B. Sternby, B. Akesson, and A. Nilsson. 1990. Effects of human pancreatic lipase-colipase and carboxyl ester lipase on eicosapentaenoic and arachidonic acid ester bonds of triacylglycerols rich in fish oil fatty acids. Biochim. Biophys. Acta. 1044: 111-117.
    • (1990) Biochim. Biophys. Acta , vol.1044 , pp. 111-117
    • Chen, Q.1    Sternby, B.2    Akesson, B.3    Nilsson, A.4
  • 87
    • 0028013634 scopus 로고
    • Digestion of triacylglycerols containing long-chain polyenoic fatty acids in vitro by colipase-dependent pancreatic lipase and human milk bile salt-stimulated lipase
    • Chen, Q., L. Blackberg, A. Nilsson, B. Sternby, and O. Hernell. 1994. Digestion of triacylglycerols containing long-chain polyenoic fatty acids in vitro by colipase-dependent pancreatic lipase and human milk bile salt-stimulated lipase. Biochim. Biophys. Acta. 1210: 239-243.
    • (1994) Biochim. Biophys. Acta , vol.1210 , pp. 239-243
    • Chen, Q.1    Blackberg, L.2    Nilsson, A.3    Sternby, B.4    Hernell, O.5
  • 88
    • 0027230043 scopus 로고
    • Does the bile salt-stimulated lipase of human milk have a role in the use of the milk long-chain polyunsaturated fatty acids
    • Hernell, O., L. Blackberg, Q. Chen, B. Sternby, and A. Nilsson. 1993. Does the bile salt-stimulated lipase of human milk have a role in the use of the milk long-chain polyunsaturated fatty acids. J. Pediatr. Gastroenterol. Nutr. 16: 426-431.
    • (1993) J. Pediatr. Gastroenterol. Nutr. , vol.16 , pp. 426-431
    • Hernell, O.1    Blackberg, L.2    Chen, Q.3    Sternby, B.4    Nilsson, A.5
  • 89
    • 0015400251 scopus 로고
    • Rate and extent of absorption of the fatty acids of fully esterified glycerol, erythritol, and sucrose as measured in thoracic duct cannulated rats
    • Mattson, F. H., and R. A. Volpenhein. 1972. Rate and extent of absorption of the fatty acids of fully esterified glycerol, erythritol, and sucrose as measured in thoracic duct cannulated rats. J. Nutr. 102: 1177-1180.
    • (1972) J. Nutr. , vol.102 , pp. 1177-1180
    • Mattson, F.H.1    Volpenhein, R.A.2
  • 90
    • 0029989318 scopus 로고    scopus 로고
    • Dietary free and esterified cholesterol absorption in cholesterol esterase (bile salt-stimulated lipase) gene-targeted mice
    • Howles, P. N., C. P. Carter, and D. Y. Hui. 1996. Dietary free and esterified cholesterol absorption in cholesterol esterase (bile salt-stimulated lipase) gene-targeted mice. J. Biol. Chem. 271: 7196-7202.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7196-7202
    • Howles, P.N.1    Carter, C.P.2    Hui, D.Y.3
  • 91
    • 0033616639 scopus 로고    scopus 로고
    • Intestinal absorption of dietary cholesteryl ester is decreased but retinyl ester absorption is normal in carboxyl ester lipase knockout mice
    • Weng, W., L. Li, A. M. van Bennekum, S. H. Potter, E. H. Harrison, W. S. Blaner, J. L. Breslow, and E. A. Fisher. 1999. Intestinal absorption of dietary cholesteryl ester is decreased but retinyl ester absorption is normal in carboxyl ester lipase knockout mice. Biochemistry. 38: 4143-4149.
    • (1999) Biochemistry , vol.38 , pp. 4143-4149
    • Weng, W.1    Li, L.2    Van Bennekum, A.M.3    Potter, S.H.4    Harrison, E.H.5    Blaner, W.S.6    Breslow, J.L.7    Fisher, E.A.8
  • 92
    • 0021211108 scopus 로고
    • Cholesterol absorption in rat intestine: Role of cholesterol esterase and acyl coenzyme A:cholesterol acyltransferase
    • Gallo, L. L., S. B. Clark, S. Myers, and G. V. Vahouny. 1984. Cholesterol absorption in rat intestine: Role of cholesterol esterase and acyl coenzyme A:cholesterol acyltransferase. J. Lipid Res. 25: 604-612.
    • (1984) J. Lipid Res. , vol.25 , pp. 604-612
    • Gallo, L.L.1    Clark, S.B.2    Myers, S.3    Vahouny, G.V.4
  • 93
    • 0000388220 scopus 로고
    • Effects of inhibitors of pancreatic cholesterol ester hydrolase (PCEH) on 14-C cholesterol absorption in animals models
    • Abstract
    • McKean, M. I., T. J. Commons, M. S. Berens, P. L. Hsu, D. M. Ackerman, K. E. Steiner, and S. J. Adelman. 1992. Effects of inhibitors of pancreatic cholesterol ester hydrolase (PCEH) on 14-C cholesterol absorption in animals models. FASEB J. 6: A1388 (Abstract).
    • (1992) FASEB J. , vol.6
    • McKean, M.I.1    Commons, T.J.2    Berens, M.S.3    Hsu, P.L.4    Ackerman, D.M.5    Steiner, K.E.6    Adelman, S.J.7
  • 94
    • 0031774704 scopus 로고    scopus 로고
    • Lipid-lowering effects of WAY-121,898, an inhibitor of pancreatic cholesteryl ester hydrolase
    • Krause, B. R., D. R. Sliskovic, M. Anderson, and R. Homan. 1998. Lipid-lowering effects of WAY-121,898, an inhibitor of pancreatic cholesteryl ester hydrolase. Lipids. 33: 489-498.
    • (1998) Lipids , vol.33 , pp. 489-498
    • Krause, B.R.1    Sliskovic, D.R.2    Anderson, M.3    Homan, R.4
  • 95
    • 0019412208 scopus 로고
    • The effect of pancreatic diversion on lymphatic absorption and esterification of cholesterol in the rat
    • Watt, S. M., and W. J. Simmonds. 1981. The effect of pancreatic diversion on lymphatic absorption and esterification of cholesterol in the rat. J. Lipid Res. 22:157-165.
    • (1981) J. Lipid Res. , vol.22 , pp. 157-165
    • Watt, S.M.1    Simmonds, W.J.2
  • 98
    • 0033136612 scopus 로고    scopus 로고
    • Pancreatic lipase-colipase mediated triglyceride hydrolysis is required for cholesterol transport from lipid emulsions to intestinal cells
    • Young, S. C., and D. Y. Hui. 1999. Pancreatic lipase-colipase mediated triglyceride hydrolysis is required for cholesterol transport from lipid emulsions to intestinal cells. Biochem. J. 339: 615-620.
    • (1999) Biochem. J. , vol.339 , pp. 615-620
    • Young, S.C.1    Hui, D.Y.2
  • 99
    • 0035079697 scopus 로고    scopus 로고
    • Compensatory phospholipid digestion is required for cholesterol absorption in pancreatic phospholipid A(2) deficient mice
    • Richmond, B. L., A. C. Boileau, S. Zheng, K. W. Huggins, N. A. Granholm, P. Tso, and D. Y. Hui. 2001. Compensatory phospholipid digestion is required for cholesterol absorption in pancreatic phospholipid A(2) deficient mice. Gastroenterology. 120: 1193-1202.
    • (2001) Gastroenterology , vol.120 , pp. 1193-1202
    • Richmond, B.L.1    Boileau, A.C.2    Zheng, S.3    Huggins, K.W.4    Granholm, N.A.5    Tso, P.6    Hui, D.Y.7
  • 100
    • 0026164229 scopus 로고
    • Further characterization of a novel phospholipase B (Phospholipase A2-lysophospholipase) from intestinal brush border membranes
    • Pind, S., and A. Kuksis. 1991. Further characterization of a novel phospholipase B (Phospholipase A2-lysophospholipase) from intestinal brush border membranes. Biochem. Cell Biol. 69: 346-357.
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 346-357
    • Pind, S.1    Kuksis, A.2
  • 101
    • 0031940847 scopus 로고    scopus 로고
    • Identification of functional domains of rat intestinal phospholipase B/lipase. Its cDNA cloning, expression, and tissue distribution
    • Takemori, H., F. N. Zolotaryov, L. Ting, T. Urbain, T. Komatsubara, O. Hatano, M. Okamoto, and H. Tojo. 1998. Identification of functional domains of rat intestinal phospholipase B/lipase. Its cDNA cloning, expression, and tissue distribution. J. Biol. Chem. 273: 2222-2231.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2222-2231
    • Takemori, H.1    Zolotaryov, F.N.2    Ting, L.3    Urbain, T.4    Komatsubara, T.5    Hatano, O.6    Okamoto, M.7    Tojo, H.8
  • 102
    • 0031941433 scopus 로고    scopus 로고
    • Purification and characterization of a catalytic domain of rat intestinal phospholipase B/lipase associated with brush border membranes
    • Tojo, H., T. Ichida, and M. Okamoto. 1998. Purification and characterization of a catalytic domain of rat intestinal phospholipase B/lipase associated with brush border membranes. J. Biol. Chem. 273: 2214-2221.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2214-2221
    • Tojo, H.1    Ichida, T.2    Okamoto, M.3
  • 103
    • 0035013221 scopus 로고    scopus 로고
    • The effect of phospholipids and fatty acids on tight junction permeability and bacterial translocatioin
    • Sawai, T., R. A. Drongowski, R. W. Lampman, A. G. Coran, and C. M. Harmon. 2001. The effect of phospholipids and fatty acids on tight junction permeability and bacterial translocatioin. Pediatr. Surg. Int. 17: 269-274.
    • (2001) Pediatr. Surg. Int. , vol.17 , pp. 269-274
    • Sawai, T.1    Drongowski, R.A.2    Lampman, R.W.3    Coran, A.G.4    Harmon, C.M.5
  • 105
    • 0025168636 scopus 로고
    • Intestinal absorption of retinol and retinyl palmitate in the rat
    • Fernandez, E., and B. Borgstrom. 1990. Intestinal absorption of retinol and retinyl palmitate in the rat. Lipids. 25: 549-552.
    • (1990) Lipids , vol.25 , pp. 549-552
    • Fernandez, E.1    Borgstrom, B.2
  • 106
    • 0034712645 scopus 로고    scopus 로고
    • Hydrolysis of retinyl esters by pancreatic triglyceride lipase
    • van Bennekum, A. M., E. A. Fisher, W. S. Blaner, and E. H. Harrison. 2000. Hydrolysis of retinyl esters by pancreatic triglyceride lipase. Biochemistry. 39: 4900-4906.
    • (2000) Biochemistry , vol.39 , pp. 4900-4906
    • Van Bennekum, A.M.1    Fisher, E.A.2    Blaner, W.S.3    Harrison, E.H.4
  • 107
    • 0027133217 scopus 로고
    • Release of ceramide after membrane sphingomyelin hydrolysis decreases the basolateral secretion of triacylglycerol and apolipoprotein B in cultured human intestinal cells
    • Field, F. J., H. Chen, E. Born, B. Dixon, and S. Mathur. 1993. Release of ceramide after membrane sphingomyelin hydrolysis decreases the basolateral secretion of triacylglycerol and apolipoprotein B in cultured human intestinal cells. J. Clin. Invest. 92: 2609-2619.
    • (1993) J. Clin. Invest. , vol.92 , pp. 2609-2619
    • Field, F.J.1    Chen, H.2    Born, E.3    Dixon, B.4    Mathur, S.5
  • 108
    • 0026701622 scopus 로고
    • Sphingonlyelin content of intestinal cell membranes regulates cholesterol absorption. Evidence for pancreatic and intestinal cell sphingomyelinase activity
    • Chen, H., E. Born, S. N. Mathur, F. C. Johlin, and F. J. Field. 1992. Sphingonlyelin content of intestinal cell membranes regulates cholesterol absorption. Evidence for pancreatic and intestinal cell sphingomyelinase activity. Biochem. J. 286: 771-777.
    • (1992) Biochem. J. , vol.286 , pp. 771-777
    • Chen, H.1    Born, E.2    Mathur, S.N.3    Johlin, F.C.4    Field, F.J.5
  • 109
    • 0029586083 scopus 로고
    • Triacylglycerol-rich lipoprotein cholesterol is derived from the plasma membrane in Caco-2 cells
    • Field, F. J., E. Born, and S. N. Mathur. 1995. Triacylglycerol-rich lipoprotein cholesterol is derived from the plasma membrane in Caco-2 cells. J. Lipid Res. 36: 2651-2660.
    • (1995) J. Lipid Res. , vol.36 , pp. 2651-2660
    • Field, F.J.1    Born, E.2    Mathur, S.N.3
  • 110
    • 0029154712 scopus 로고
    • Esterification of plasma memhrane cholesterol and triacylglycerol-rich lipoprotein secretion in Caco-2 cells: Possible role of p-glycoproteins
    • Field, F. J., E. Born, H. Chen, S. Murthy, and S. N. Mathur. 1995. Esterification of plasma memhrane cholesterol and triacylglycerol-rich lipoprotein secretion in Caco-2 cells: Possible role of p-glycoproteins. J. Lipid Res. 36: 1533-1543.
    • (1995) J. Lipid Res. , vol.36 , pp. 1533-1543
    • Field, F.J.1    Born, E.2    Chen, H.3    Murthy, S.4    Mathur, S.N.5
  • 111
    • 0030993910 scopus 로고    scopus 로고
    • Effect of micellar β-sitosterol on cholesterol metabolism in Caco-2 cells
    • Field, F. J., E. Born, and S. N. Mathur. 1997. Effect of micellar β-sitosterol on cholesterol metabolism in Caco-2 cells. J. Lipid Res. 38: 348-360.
    • (1997) J. Lipid Res. , vol.38 , pp. 348-360
    • Field, F.J.1    Born, E.2    Mathur, S.N.3
  • 112
    • 0023839340 scopus 로고
    • Depletion of plasma membrane sphingomyelin rapidly almers the distribution of cholesterol between plasma membranes and intracellular cholesterol pools in cultured fibroblasts
    • Slotte, J. P., and E. L. Bierman. 1988. Depletion of plasma membrane sphingomyelin rapidly almers the distribution of cholesterol between plasma membranes and intracellular cholesterol pools in cultured fibroblasts. Biochem. J. 250: 653-658.
    • (1988) Biochem. J. , vol.250 , pp. 653-658
    • Slotte, J.P.1    Bierman, E.L.2
  • 113
    • 0025976207 scopus 로고
    • Plasma membrane sphingomyelin and the regulation of HMG-CoA reductase activity and cholesterol biosynthesis in cell cultures
    • Gupta, A. K., and H. Rudney. 1991. Plasma membrane sphingomyelin and the regulation of HMG-CoA reductase activity and cholesterol biosynthesis in cell cultures. J. Lipid Res. 32: 125-136.
    • (1991) J. Lipid Res. , vol.32 , pp. 125-136
    • Gupta, A.K.1    Rudney, H.2
  • 114
    • 0033789028 scopus 로고    scopus 로고
    • Implication of sphingolipid metabolism in the stability of the Golgi apparatus
    • Fukunaga, T., M. Nagahama, K. Hatsuzawa, K. Tani, A. Yamamoto, and M. Tagaya. 2000. Implication of sphingolipid metabolism in the stability of the Golgi apparatus. J. Cell Sci. 113: 3290-3307.
    • (2000) J. Cell Sci. , vol.113 , pp. 3290-3307
    • Fukunaga, T.1    Nagahama, M.2    Hatsuzawa, K.3    Tani, K.4    Yamamoto, A.5    Tagaya, M.6
  • 115
    • 0027416461 scopus 로고
    • Inhibition of glycoprotein traffic through the secretory pathway by ceramide
    • Rosenwald, A. G., and R. E. Pagano. 1993. Inhibition of glycoprotein traffic through the secretory pathway by ceramide. J. Biol. Chem. 268: 4577-4579.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4577-4579
    • Rosenwald, A.G.1    Pagano, R.E.2
  • 116
    • 0027424327 scopus 로고
    • Hepatic expression of genes regulating lipid metabolism in rabbits
    • Rea, T. J., R. B. DeMattos, and M. E. Pape. 1993. Hepatic expression of genes regulating lipid metabolism in rabbits. J. Lipid Res. 34: 1901-1910.
    • (1993) J. Lipid Res. , vol.34 , pp. 1901-1910
    • Rea, T.J.1    DeMattos, R.B.2    Pape, M.E.3
  • 117
    • 0028876953 scopus 로고
    • Plasma cholesterol esterase level is a determinant for an atherogenic lipoprotein profile in normolipidemic human subjects
    • Brodt-Eppley, J., P. White, S. Jenkins, and D. Y. Hui. 1995. Plasma cholesterol esterase level is a determinant for an atherogenic lipoprotein profile in normolipidemic human subjects. Biochim. Biophys. Acta. 1272: 69-72.
    • (1995) Biochim. Biophys. Acta , vol.1272 , pp. 69-72
    • Brodt-Eppley, J.1    White, P.2    Jenkins, S.3    Hui, D.Y.4
  • 118
    • 0023816688 scopus 로고
    • Bile salt-dependent, neutral cholesteryl ester hydrolase of rat liver: Possible relationship with pancreatic cholesteryl ester hydrolase
    • Harrison, E. H. 1988. Bile salt-dependent, neutral cholesteryl ester hydrolase of rat liver: Possible relationship with pancreatic cholesteryl ester hydrolase. Biochim. Biophys. Acta. 963: 28-34.
    • (1988) Biochim. Biophys. Acta , vol.963 , pp. 28-34
    • Harrison, E.H.1
  • 120
    • 0016713317 scopus 로고
    • The measurement of sulphated and non-sulphated bile acids in serum using gas liquid chromatography
    • Campbell, C. B., C. McGulfie, and L. W. Powell. 1975, The measurement of sulphated and non-sulphated bile acids in serum using gas liquid chromatography. Clin. Chim. Acta. 63: 249-262.
    • (1975) Clin. Chim. Acta , vol.63 , pp. 249-262
    • Campbell, C.B.1    McGulfie, C.2    Powell, L.W.3
  • 121
    • 0034763246 scopus 로고    scopus 로고
    • Acute effects of dietary fat composition on postprandial plasma bile acid and cholecystokinin concentrations in healthy premenopausal women
    • Costarelli, V., and T. A. B. Sanders. 2001. Acute effects of dietary fat composition on postprandial plasma bile acid and cholecystokinin concentrations in healthy premenopausal women. Br. J. Nutr. 86: 471-477.
    • (2001) Br. J. Nutr. , vol.86 , pp. 471-477
    • Costarelli, V.1    Sanders, T.A.B.2
  • 123
    • 0030583307 scopus 로고    scopus 로고
    • Catalytic properties of the purified rat hepatic cytosolic cholesteryl ester hydrolase
    • Natarjan, R., S. Ghosh, S., and W. M. Grogan. 1996. Catalytic properties of the purified rat hepatic cytosolic cholesteryl ester hydrolase. Biochem. Biophys. Res. Commun. 225: 413-419.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 413-419
    • Natarjan, R.1    Ghosh, S.2    Grogan, W.M.3
  • 124
    • 0030919788 scopus 로고    scopus 로고
    • Age-related changes in catalytic activity, enzyme mass, mRNA, and subcellular distribution of hepatic neutral cholesterol ester hydrolase in female rats
    • Natarajan, R., S. Ghosh, and W. M. Grogan. 1997. Age-related changes in catalytic activity, enzyme mass, mRNA, and subcellular distribution of hepatic neutral cholesterol ester hydrolase in female rats. Lipids. 32: 463-470.
    • (1997) Lipids , vol.32 , pp. 463-470
    • Natarajan, R.1    Ghosh, S.2    Grogan, W.M.3
  • 125
    • 0032512556 scopus 로고    scopus 로고
    • Molecular cloning of the promoter for rat hepatic neutral cholesterol ester hydrolase: Evidence for transcriptional regulation by sterols
    • Natarajan, R., S. Ghosh, and W. M. Grogan. 1998. Molecular cloning of the promoter for rat hepatic neutral cholesterol ester hydrolase: Evidence for transcriptional regulation by sterols. Biochem. Biophys. Res. Commun, 243: 349-355.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 349-355
    • Natarajan, R.1    Ghosh, S.2    Grogan, W.M.3
  • 126
    • 0031968413 scopus 로고    scopus 로고
    • Regulation of hepatic neutral cholesteryl ester hydrolase by hormones and changes in cholesterol flux
    • Ghosh, S., R. Natarajan, W. M. Pandak, P. B. Hylemon, and W. M. Grogan. 1998. Regulation of hepatic neutral cholesteryl ester hydrolase by hormones and changes in cholesterol flux. Am. J. Physiol. 274: G662-G668.
    • (1998) Am. J. Physiol. , vol.274
    • Ghosh, S.1    Natarajan, R.2    Pandak, W.M.3    Hylemon, P.B.4    Grogan, W.M.5
  • 127
    • 0030879972 scopus 로고    scopus 로고
    • A role for retrosomes in intracellular cholesterol transport from endosomes to the plasma membrane
    • Hornick, C. A., D. Y. Hui, and J. G. DeLamatre. 1997. A role for retrosomes in intracellular cholesterol transport from endosomes to the plasma membrane. Am. J. Physiol. 273: C1075-C1081.
    • (1997) Am. J. Physiol. , vol.273
    • Hornick, C.A.1    Hui, D.Y.2    DeLamatre, J.G.3
  • 128
    • 0026691385 scopus 로고
    • Characterization of a bile salt-dependent cholesteryl ester hydrolase activity secreted from HepG2 cells
    • Winkler, K. E., E. H. Harrison, J. B. Marsh, J. M. Glick, and A. C. Ross. 1992. Characterization of a bile salt-dependent cholesteryl ester hydrolase activity secreted from HepG2 cells. Biochim. Biophys. Acta. 1126:151-158.
    • (1992) Biochim. Biophys. Acta , vol.1126 , pp. 151-158
    • Winkler, K.E.1    Harrison, E.H.2    Marsh, J.B.3    Glick, J.M.4    Ross, A.C.5
  • 129
    • 0029983998 scopus 로고    scopus 로고
    • Bile salt stimulated cholesterol esterase increases uptake of high density lipoprotein-associated cholesteryl esters by HepG2 cells
    • Li, F., Y. Huang, and D. Y. Hui. 1996. Bile salt stimulated cholesterol esterase increases uptake of high density lipoprotein-associated cholesteryl esters by HepG2 cells. Biochemistry. 35: 6657-6663.
    • (1996) Biochemistry , vol.35 , pp. 6657-6663
    • Li, F.1    Huang, Y.2    Hui, D.Y.3
  • 130
    • 4243386288 scopus 로고    scopus 로고
    • Carboxyl ester lipase effects selective uptake and hydrolysis of HDL-cholesterol esters
    • Camarota, L. M., J. C. Chapman, D. Y. Hui, and P. N. Howles. 2002. Carboxyl ester lipase effects selective uptake and hydrolysis of HDL-cholesterol esters (Abstract). Gastroenterology. 122 (suppl. 1): A625.
    • (2002) Gastroenterology , vol.122 , Issue.SUPPL. 1
    • Camarota, L.M.1    Chapman, J.C.2    Hui, D.Y.3    Howles, P.N.4
  • 131
    • 0015922728 scopus 로고
    • Aortic cholesterl esterase: Characteristics of normal rat and rabbit enzyme
    • Kothari, H. V., B. F. Miller, and D. Kritchevsky. 1973. Aortic cholesterl esterase: Characteristics of normal rat and rabbit enzyme. Biochim. Biophys. Acta. 296: 446-454.
    • (1973) Biochim. Biophys. Acta , vol.296 , pp. 446-454
    • Kothari, H.V.1    Miller, B.F.2    Kritchevsky, D.3
  • 132
    • 0016704103 scopus 로고
    • Purification and proper ties of aortic cholesteryl ester hydrolase
    • Kothari, H. V., and D. Kritchevsky. 1975. Purification and proper ties of aortic cholesteryl ester hydrolase. Lipids. 10: 322-330.
    • (1975) Lipids , vol.10 , pp. 322-330
    • Kothari, H.V.1    Kritchevsky, D.2
  • 133
    • 0026333959 scopus 로고
    • Role of oxidized low density lipoprotein in atherogenesis
    • Witztum, J. L., and D. Steinberg. 1991. Role of oxidized low density lipoprotein in atherogenesis. J. Clin. Invest. 88: 1785-1792.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1785-1792
    • Witztum, J.L.1    Steinberg, D.2
  • 134
    • 0028128943 scopus 로고
    • The oxidation hypothesis of atherosclerosis
    • Witztum, J. L. 1994. The oxidation hypothesis of atherosclerosis. Lancet. 344: 793-795.
    • (1994) Lancet , vol.344 , pp. 793-795
    • Witztum, J.L.1
  • 135
    • 0014480993 scopus 로고
    • Lysophosphatidylcholine concentrations and metabolism in aortic intima plus inner media: Effect of nutritionally induced atherosclerosis
    • Portman, O. W., and M. Alexander. 1969. Lysophosphatidylcholine concentrations and metabolism in aortic intima plus inner media: Effect of nutritionally induced atherosclerosis. J. Lipid Res. 10: 158-165.
    • (1969) J. Lipid Res. , vol.10 , pp. 158-165
    • Portman, O.W.1    Alexander, M.2
  • 136
    • 0025286558 scopus 로고
    • Impairment of endothelium-dependent arterial relaxation by lysolecithin in modified low density lipoproteins
    • Kugiyama, K., S. A. Kerns, J. D. Morrisett, R. Roberts, and P. D. Henry. 1990. Impairment of endothelium-dependent arterial relaxation by lysolecithin in modified low density lipoproteins. Nature. 344: 160-162.
    • (1990) Nature , vol.344 , pp. 160-162
    • Kugiyama, K.1    Kerns, S.A.2    Morrisett, J.D.3    Roberts, R.4    Henry, P.D.5
  • 137
    • 0001096583 scopus 로고
    • Lysophosphatidylcholine: A chemotactic factor for human monocytes and its potential role in atherogenesis
    • Quinn, M. T., S. Parthasarathy, and D. Steinberg. 1988. Lysophosphatidylcholine: A chemotactic factor for human monocytes and its potential role in atherogenesis. Proc. Natl. Acad. Sci. USA. 85: 2805-2809.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2805-2809
    • Quinn, M.T.1    Parthasarathy, S.2    Steinberg, D.3
  • 138
    • 0026781978 scopus 로고
    • Lysophosphatidylcholine, a component of atherogenic lipoproteins, induces mononuclear leukocyte adhesion molecules in cultured human and rabbit arterial endothelial cells
    • Kume, N., M. I. Cybulsky, and M. A. Gimbrone, 1992. Lysophosphatidylcholine, a component of atherogenic lipoproteins, induces mononuclear leukocyte adhesion molecules in cultured human and rabbit arterial endothelial cells. J. Clin. Invest. 90: 1138-1144.
    • (1992) J. Clin. Invest. , vol.90 , pp. 1138-1144
    • Kume, N.1    Cybulsky, M.I.2    Gimbrone, M.A.3
  • 139
    • 0028079980 scopus 로고
    • Lysophosphatidylcholine plays an essential role in the mitogen effect of oxidized low density lipoprotein on taurine macrophages
    • Sakai, M., A. Miyazaki, H. Hakamata, T. Sasaki, S. Yui, M. Yamazaki, M. Shichiri, and S, Horiuchi. 1994. Lysophosphatidylcholine plays an essential role in the mitogen effect of oxidized low density lipoprotein on taurine macrophages. J. Biol. Chem. 269: 31430-31435.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31430-31435
    • Sakai, M.1    Miyazaki, A.2    Hakamata, H.3    Sasaki, T.4    Yui, S.5    Yamazaki, M.6    Shichiri, M.7    Horiuchi, S.8
  • 140
    • 0025572630 scopus 로고
    • Phospholipase A-2 activity of low density lipoprotein: Evidence for an intrinsic phospholipase A-2 activity of apoprotein B-100
    • Parthasarathy, S., and J. Barnett. 1990. Phospholipase A-2 activity of low density lipoprotein: Evidence for an intrinsic phospholipase A-2 activity of apoprotein B-100. Proc. Natl. Acad. Sci. USA. 87: 9741-9745.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9741-9745
    • Parthasarathy, S.1    Barnett, J.2
  • 142
    • 0031029342 scopus 로고    scopus 로고
    • Localization of nonpancreatic secretory phospholipase A2 in normal and atherosclerotic arteries. Activity of the isolated enzyme on low density lipoproteins
    • Hurt-Camejo, E., S. Andersen, R. Standal, B. Rosengren, P. Sartipy, E. Stadberg, and B. Johansen. 1997. Localization of nonpancreatic secretory phospholipase A2 in normal and atherosclerotic arteries. Activity of the isolated enzyme on low density lipoproteins. Arterioscler. Thromb. Vasc. Biol. 17: 300-309.
    • (1997) Arterioscler. Thromb. Vasc. Biol. , vol.17 , pp. 300-309
    • Hurt-Camejo, E.1    Andersen, S.2    Standal, R.3    Rosengren, B.4    Sartipy, P.5    Stadberg, E.6    Johansen, B.7
  • 143
    • 0031956684 scopus 로고    scopus 로고
    • Ultra-structural localization of secretory type II phospholipase A2 in atherosclerotic and nonatherosclerotic regions of human arteries
    • Romano, M., E. Romano, S. Bjorkerud, and E. Hurt-Camejo. 1998. Ultra-structural localization of secretory type II phospholipase A2 in atherosclerotic and nonatherosclerotic regions of human arteries. Arterioscler. Thromb. Vasc. Biol. 18: 519-525.
    • (1998) Arterioscler. Thromb. Vasc. Biol. , vol.18 , pp. 519-525
    • Romano, M.1    Romano, E.2    Bjorkerud, S.3    Hurt-Camejo, E.4
  • 146
    • 0029762320 scopus 로고    scopus 로고
    • Rabbit aorta and human atherosclerotic lesions hydrolyze the sphingomyelin of retained low density lipoprotein
    • Schissel, S. L., J. Tweedie-Hardman, J. H. Rapp, G. Graham, K. J. Williams, and I. Tabas. 1996. Rabbit aorta and human atherosclerotic lesions hydrolyze the sphingomyelin of retained low density lipoprotein. J. Clin. Invest. 98: 1455-1464.
    • (1996) J. Clin. Invest. , vol.98 , pp. 1455-1464
    • Schissel, S.L.1    Tweedie-Hardman, J.2    Rapp, J.H.3    Graham, G.4    Williams, K.J.5    Tabas, I.6
  • 148
    • 0033618381 scopus 로고    scopus 로고
    • Role of sphingosine J-phosphate in the mitogenesis induced by oxidized low density lipoprotein in smooth muscle cells via activation of sphingomyelinase, ceramidase, and sphingosine kinase
    • Auge, N., M. Nikolova-Karakashian, S. Carpentier. S. Parthasarathy, A. Negre-Salvayre, R. Salvayre, A. H. Merrill, and T. Levade. 1999. Role of sphingosine J-phosphate in the mitogenesis induced by oxidized low density lipoprotein in smooth muscle cells via activation of sphingomyelinase, ceramidase, and sphingosine kinase. J. Biol. Chem. 274: 21533-21538.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21533-21538
    • Auge, N.1    Nikolova-Karakashian, M.2    Carpentier, S.3    Parthasarathy, S.4    Negre-Salvayre, A.5    Salvayre, R.6    Merrill, A.H.7    Levade, T.8
  • 149
    • 0030952830 scopus 로고    scopus 로고
    • Redox-regulated signaling by lactosylceramide in the proliferation of human aortic smooth muscle cells
    • Bhunia, A. K. H. Han, A. Snowden, and S. Chatterjee. 1997. Redox-regulated signaling by lactosylceramide in the proliferation of human aortic smooth muscle cells. J. Biol. Chem. 272: 15642-15649.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15642-15649
    • Bhunia, A.K.1    Han, H.2    Snowden, A.3    Chatterjee, S.4
  • 150
    • 0031694479 scopus 로고    scopus 로고
    • Sphingolipids in atherosclerosis and vascular biology
    • Chatterjee, S. 1998. Sphingolipids in atherosclerosis and vascular biology. Arterioscler. Thromb. Vasc. Biol. 18: 1523-1533.
    • (1998) Arterioscler. Thromb. Vasc. Biol. , vol.18 , pp. 1523-1533
    • Chatterjee, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.