메뉴 건너뛰기




Volumn 1821, Issue 1, 2012, Pages 113-123

Retinyl ester hydrolases and their roles in vitamin A homeostasis

Author keywords

Lipid droplet; Mobilization; Neutral lipid; Retinyl ester hydrolase; Store; Vitamin A

Indexed keywords

CHOLESTEROL ESTER; MESSENGER RNA; RETINOL ESTER; TAURODEOXYCHOLIC ACID; VERY LOW DENSITY LIPOPROTEIN;

EID: 83255192145     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2011.05.001     Document Type: Review
Times cited : (47)

References (195)
  • 1
    • 33745387612 scopus 로고    scopus 로고
    • Overview of retinoid metabolism and function
    • R. Blomhoff, and H.K. Blomhoff Overview of retinoid metabolism and function J. Neurobiol. 66 2006 606 630
    • (2006) J. Neurobiol. , vol.66 , pp. 606-630
    • Blomhoff, R.1    Blomhoff, H.K.2
  • 2
    • 0029007929 scopus 로고
    • The roles of retinoids in vertebrate development
    • A.L. Means, and L.J. Gudas The roles of retinoids in vertebrate development Annu. Rev. Biochem. 64 1995 201 233
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 201-233
    • Means, A.L.1    Gudas, L.J.2
  • 3
    • 0028136788 scopus 로고
    • Retinoids. A window into vertebrate development
    • M.B. Rogers Retinoids. A window into vertebrate development J. Fla. Med. Assoc. 81 1994 553 556
    • (1994) J. Fla. Med. Assoc. , vol.81 , pp. 553-556
    • Rogers, M.B.1
  • 6
    • 79952734461 scopus 로고    scopus 로고
    • Signaling by vitamin A and retinol-binding protein regulates gene expression to inhibit insulin responses
    • D.C. Berry, H. Jin, A. Majumdar, and N. Noy Signaling by vitamin A and retinol-binding protein regulates gene expression to inhibit insulin responses Proc. Natl. Acad. Sci. U. S. A. 108 2011 4340 4345
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 4340-4345
    • Berry, D.C.1    Jin, H.2    Majumdar, A.3    Noy, N.4
  • 8
    • 0023767618 scopus 로고
    • Distribution of retinol in rat liver cells: Effect of age, sex and nutritional status
    • R. Blomhoff, T. Berg, and K.R. Norum Distribution of retinol in rat liver cells: effect of age, sex and nutritional status Br. J. Nutr. 60 1988 233 239
    • (1988) Br. J. Nutr. , vol.60 , pp. 233-239
    • Blomhoff, R.1    Berg, T.2    Norum, K.R.3
  • 10
    • 0025734994 scopus 로고
    • Perisinusoidal stellate cells of the liver: Important roles in retinol metabolism and fibrosis
    • R. Blomhoff, and K. Wake Perisinusoidal stellate cells of the liver: important roles in retinol metabolism and fibrosis FASEB J. 5 1991 271 277
    • (1991) FASEB J. , vol.5 , pp. 271-277
    • Blomhoff, R.1    Wake, K.2
  • 11
    • 33947248972 scopus 로고    scopus 로고
    • Vitamin A-storing cells (stellate cells)
    • H. Senoo, N. Kojima, and M. Sato Vitamin A-storing cells (stellate cells) Vitam. Horm. 75 2007 131 159
    • (2007) Vitam. Horm. , vol.75 , pp. 131-159
    • Senoo, H.1    Kojima, N.2    Sato, M.3
  • 13
    • 0026561017 scopus 로고
    • A retinyl ester hydrolase activity intrinsic to the brush border membrane of rat small intestine
    • K.M. Rigtrup, and D.E. Ong A retinyl ester hydrolase activity intrinsic to the brush border membrane of rat small intestine Biochemistry 31 1992 2920 2926
    • (1992) Biochemistry , vol.31 , pp. 2920-2926
    • Rigtrup, K.M.1    Ong, D.E.2
  • 14
    • 0035014463 scopus 로고    scopus 로고
    • Mechanisms involved in the intestinal digestion and absorption of dietary vitamin A
    • E.H. Harrison, and M.M. Hussain Mechanisms involved in the intestinal digestion and absorption of dietary vitamin A J. Nutr. 131 2001 1405 1408
    • (2001) J. Nutr. , vol.131 , pp. 1405-1408
    • Harrison, E.H.1    Hussain, M.M.2
  • 15
    • 23944481843 scopus 로고    scopus 로고
    • Mechanisms of digestion and absorption of dietary vitamin A
    • E.H. Harrison Mechanisms of digestion and absorption of dietary vitamin A Annu. Rev. Nutr. 25 2005 87 103
    • (2005) Annu. Rev. Nutr. , vol.25 , pp. 87-103
    • Harrison, E.H.1
  • 16
    • 0028135717 scopus 로고
    • Uptake of retinoids by adipose tissue
    • G. Wolf Uptake of retinoids by adipose tissue Nutr. Rev. 52 1994 356 358
    • (1994) Nutr. Rev. , vol.52 , pp. 356-358
    • Wolf, G.1
  • 19
    • 0024321466 scopus 로고
    • The morphology of release of vitamin A-containing lipid droplets by hepatocytes in rat liver
    • S. Kudo The morphology of release of vitamin A-containing lipid droplets by hepatocytes in rat liver Anat. Rec. 225 1989 11 20
    • (1989) Anat. Rec. , vol.225 , pp. 11-20
    • Kudo, S.1
  • 20
    • 0029047296 scopus 로고
    • Chylomicron remnants: Hepatic receptors and metabolism
    • R.J. Havel Chylomicron remnants: hepatic receptors and metabolism Curr. Opin. Lipidol. 6 1995 312 316
    • (1995) Curr. Opin. Lipidol. , vol.6 , pp. 312-316
    • Havel, R.J.1
  • 22
    • 0027467140 scopus 로고
    • Bile salt-activated lipase. A multiple function lipolytic enzyme
    • C.S. Wang, and J.A. Hartsuck Bile salt-activated lipase. A multiple function lipolytic enzyme Biochim. Biophys. Acta 1166 1993 1 19
    • (1993) Biochim. Biophys. Acta , vol.1166 , pp. 1-19
    • Wang, C.S.1    Hartsuck, J.A.2
  • 23
    • 0019876856 scopus 로고
    • Retinyl palmitate hydrolase activity in normal rat liver
    • J.H. Prystowsky, J.E. Smith, and D.S. Goodman Retinyl palmitate hydrolase activity in normal rat liver J. Biol. Chem. 256 1981 4498 4503
    • (1981) J. Biol. Chem. , vol.256 , pp. 4498-4503
    • Prystowsky, J.H.1    Smith, J.E.2    Goodman, D.S.3
  • 24
    • 0021251390 scopus 로고
    • Rat liver retinyl palmitate hydrolase activity. Relationship to cholesteryl oleate and triolein hydrolase activities
    • W.S. Blaner, J.H. Prystowsky, J.E. Smith, and D.S. Goodman Rat liver retinyl palmitate hydrolase activity. Relationship to cholesteryl oleate and triolein hydrolase activities Biochim. Biophys. Acta 794 1984 419 427
    • (1984) Biochim. Biophys. Acta , vol.794 , pp. 419-427
    • Blaner, W.S.1    Prystowsky, J.H.2    Smith, J.E.3    Goodman, D.S.4
  • 25
    • 0023816688 scopus 로고
    • Bile salt-dependent, neutral cholesteryl ester hydrolase of rat liver: Possible relationship with pancreatic cholesteryl ester hydrolase
    • E.H. Harrison Bile salt-dependent, neutral cholesteryl ester hydrolase of rat liver: possible relationship with pancreatic cholesteryl ester hydrolase Biochim. Biophys. Acta 963 1988 28 34
    • (1988) Biochim. Biophys. Acta , vol.963 , pp. 28-34
    • Harrison, E.H.1
  • 26
    • 0026691385 scopus 로고
    • Characterization of a bile salt-dependent cholesteryl ester hydrolase activity secreted from HepG2 cells
    • K.E. Winkler, E.H. Harrison, J.B. Marsh, J.M. Glick, and A.C. Ross Characterization of a bile salt-dependent cholesteryl ester hydrolase activity secreted from HepG2 cells Biochim. Biophys. Acta 1126 1992 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
  • 27
    • 0024396756 scopus 로고
    • Hydrolysis of retinyl palmitate by enzymes of rat pancreas and liver. Differentiation of bile salt-dependent and bile salt-independent, neutral retinyl ester hydrolases in rat liver
    • E.H. Harrison, and M.Z. Gad Hydrolysis of retinyl palmitate by enzymes of rat pancreas and liver. Differentiation of bile salt-dependent and bile salt-independent, neutral retinyl ester hydrolases in rat liver J. Biol. Chem. 264 1989 17142 17147
    • (1989) J. Biol. Chem. , vol.264 , pp. 17142-17147
    • Harrison, E.H.1    Gad, M.Z.2
  • 28
    • 0018842463 scopus 로고
    • Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. II. Action on cholesterol esters and lipid-soluble vitamin esters
    • D. Lombardo, and O. Guy Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. II. Action on cholesterol esters and lipid-soluble vitamin esters Biochim. Biophys. Acta 611 1980 147 155
    • (1980) Biochim. Biophys. Acta , vol.611 , pp. 147-155
    • Lombardo, D.1    Guy, O.2
  • 29
    • 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
    • W. Weng, L. Li, A.M. van Bennekum, S.H. Potter, E.H. Harrison, W.S. Blaner, J.L. Breslow, and E.A. Fisher Intestinal absorption of dietary cholesteryl ester is decreased but retinyl ester absorption is normal in carboxyl ester lipase knockout mice Biochemistry 38 1999 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
  • 30
    • 0011176871 scopus 로고
    • Studies on metabolism of Vitamin A. 4. Studies on the mode of absorption of Vitamin A by rat intestine in vitro
    • S. Mahadevan, P.S. Sastry, and J. Ganguly Studies on metabolism of Vitamin A. 4. Studies on the mode of absorption of Vitamin A by rat intestine in vitro Biochem. J. 88 1963 534 539
    • (1963) Biochem. J. , vol.88 , pp. 534-539
    • Mahadevan, S.1    Sastry, P.S.2    Ganguly, J.3
  • 31
    • 0013239529 scopus 로고
    • Studies of metabolism of Vitamin A. 3. The mode of absorption of Vitamin A esters in the living rat
    • S. Mahadevan, P.S. Sastry, and J. Ganguly Studies of metabolism of Vitamin A. 3. The mode of absorption of Vitamin A esters in the living rat Biochem. J. 88 1963 531 534
    • (1963) Biochem. J. , vol.88 , pp. 531-534
    • Mahadevan, S.1    Sastry, P.S.2    Ganguly, J.3
  • 33
    • 0033616699 scopus 로고    scopus 로고
    • Carboxyl ester lipase overexpression in rat hepatoma cells and CEL deficiency in mice have no impact on hepatic uptake or metabolism of chylomicron-retinyl ester
    • A.M. van Bennekum, L. Li, R. Piantedosi, R. Shamir, S. Vogel, E.A. Fisher, W.S. Blaner, and E.H. Harrison Carboxyl ester lipase overexpression in rat hepatoma cells and CEL deficiency in mice have no impact on hepatic uptake or metabolism of chylomicron-retinyl ester Biochemistry 38 1999 4150 4156
    • (1999) Biochemistry , vol.38 , pp. 4150-4156
    • Van Bennekum, A.M.1    Li, L.2    Piantedosi, R.3    Shamir, R.4    Vogel, S.5    Fisher, E.A.6    Blaner, W.S.7    Harrison, E.H.8
  • 34
    • 0036915668 scopus 로고    scopus 로고
    • The triglyceride lipases of the pancreas
    • M.E. Lowe The triglyceride lipases of the pancreas J. Lipid Res. 43 2002 2007 2016
    • (2002) J. Lipid Res. , vol.43 , pp. 2007-2016
    • Lowe, M.E.1
  • 35
    • 34548349298 scopus 로고    scopus 로고
    • Carboxyl ester lipase deficiency exacerbates dietary lipid absorption abnormalities and resistance to diet-induced obesity in pancreatic triglyceride lipase knockout mice
    • D. Gilham, E.D. Labonte, J.C. Rojas, R.J. Jandacek, P.N. Howles, and D.Y. Hui Carboxyl ester lipase deficiency exacerbates dietary lipid absorption abnormalities and resistance to diet-induced obesity in pancreatic triglyceride lipase knockout mice J. Biol. Chem. 282 2007 24642 24649
    • (2007) J. Biol. Chem. , vol.282 , pp. 24642-24649
    • Gilham, D.1    Labonte, E.D.2    Rojas, J.C.3    Jandacek, R.J.4    Howles, P.N.5    Hui, D.Y.6
  • 36
    • 0026671201 scopus 로고
    • Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity
    • T. Giller, P. Buchwald, D. Blum-Kaelin, and W. Hunziker Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity J. Biol. Chem. 267 1992 16509 16516
    • (1992) J. Biol. Chem. , vol.267 , pp. 16509-16516
    • Giller, T.1    Buchwald, P.2    Blum-Kaelin, D.3    Hunziker, W.4
  • 37
    • 0037060460 scopus 로고    scopus 로고
    • High expression in adult horse of PLRP2 displaying a low phospholipase activity
    • S. Jayne, B. Kerfelec, E. Foglizzo, C. Chapus, and I. Crenon High expression in adult horse of PLRP2 displaying a low phospholipase activity Biochim. Biophys. Acta 1594 2002 255 265
    • (2002) Biochim. Biophys. Acta , vol.1594 , pp. 255-265
    • Jayne, S.1    Kerfelec, B.2    Foglizzo, E.3    Chapus, C.4    Crenon, I.5
  • 39
    • 0000392201 scopus 로고    scopus 로고
    • Pancreatic lipase-related protein 2 but not classical pancreatic lipase hydrolyzes galactolipids
    • L. Andersson, F. Carriere, M.E. Lowe, A. Nilsson, and R. Verger Pancreatic lipase-related protein 2 but not classical pancreatic lipase hydrolyzes galactolipids Biochim. Biophys. Acta 1302 1996 236 240
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 236-240
    • Andersson, L.1    Carriere, F.2    Lowe, M.E.3    Nilsson, A.4    Verger, R.5
  • 40
    • 33646477172 scopus 로고    scopus 로고
    • Pancreatic lipase and pancreatic lipase-related protein 2, but not pancreatic lipase-related protein 1, hydrolyze retinyl palmitate in physiological conditions
    • E. Reboul, A. Berton, M. Moussa, C. Kreuzer, I. Crenon, and P. Borel Pancreatic lipase and pancreatic lipase-related protein 2, but not pancreatic lipase-related protein 1, hydrolyze retinyl palmitate in physiological conditions Biochim. Biophys. Acta 1761 2006 4 10
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 4-10
    • Reboul, E.1    Berton, A.2    Moussa, M.3    Kreuzer, C.4    Crenon, I.5    Borel, P.6
  • 41
    • 0032553539 scopus 로고    scopus 로고
    • Decreased neonatal dietary fat absorption and T cell cytotoxicity in pancreatic lipase-related protein 2-deficient mice
    • M.E. Lowe, M.H. Kaplan, L. Jackson-Grusby, D. D'Agostino, and M.J. Grusby Decreased neonatal dietary fat absorption and T cell cytotoxicity in pancreatic lipase-related protein 2-deficient mice J. Biol. Chem. 273 1998 31215 31221
    • (1998) J. Biol. Chem. , vol.273 , pp. 31215-31221
    • Lowe, M.E.1    Kaplan, M.H.2    Jackson-Grusby, L.3    D'Agostino, D.4    Grusby, M.J.5
  • 42
    • 0028238733 scopus 로고
    • Retinyl ester hydrolytic activity associated with human intestinal brush border membranes
    • K.M. Rigtrup, L.R. McEwen, H.M. Said, and D.E. Ong Retinyl ester hydrolytic activity associated with human intestinal brush border membranes Am. J. Clin. Nutr. 60 1994 111 116
    • (1994) Am. J. Clin. Nutr. , vol.60 , pp. 111-116
    • Rigtrup, K.M.1    McEwen, L.R.2    Said, H.M.3    Ong, D.E.4
  • 43
    • 0028351890 scopus 로고
    • Purification and partial characterization of a retinyl ester hydrolase from the brush border of rat small intestine mucosa: Probable identity with brush border phospholipase B
    • K.M. Rigtrup, B. Kakkad, and D.E. Ong Purification and partial characterization of a retinyl ester hydrolase from the brush border of rat small intestine mucosa: probable identity with brush border phospholipase B Biochemistry 33 1994 2661 2666
    • (1994) Biochemistry , vol.33 , pp. 2661-2666
    • Rigtrup, K.M.1    Kakkad, B.2    Ong, D.E.3
  • 44
    • 78651177609 scopus 로고
    • Tissue distribution and metabolism of newly absorbed Vitamin A in the rat
    • D.W. Goodman, H.S. Huang, and T. Shiratori Tissue distribution and metabolism of newly absorbed Vitamin A in the rat J. Lipid Res. 6 1965 390 396
    • (1965) J. Lipid Res. , vol.6 , pp. 390-396
    • Goodman, D.W.1    Huang, H.S.2    Shiratori, T.3
  • 45
    • 0020406127 scopus 로고
    • In vivo uptake of chylomicron [3H]retinyl ester by rat liver: Evidence for retinol transfer from parenchymal to nonparenchymal cells
    • R. Blomhoff, P. Helgerud, M. Rasmussen, T. Berg, and K.R. Norum In vivo uptake of chylomicron [3H]retinyl ester by rat liver: evidence for retinol transfer from parenchymal to nonparenchymal cells Proc. Natl. Acad. Sci. U. S. A. 79 1982 7326 7330
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 7326-7330
    • Blomhoff, R.1    Helgerud, P.2    Rasmussen, M.3    Berg, T.4    Norum, K.R.5
  • 46
    • 0142216385 scopus 로고    scopus 로고
    • Understanding the physiological role of retinol-binding protein in vitamin A metabolism using transgenic and knockout mouse models
    • L. Quadro, L. Hamberger, V. Colantuoni, M.E. Gottesman, and W.S. Blaner Understanding the physiological role of retinol-binding protein in vitamin A metabolism using transgenic and knockout mouse models Mol. Aspects Med. 24 2003 421 430
    • (2003) Mol. Aspects Med. , vol.24 , pp. 421-430
    • Quadro, L.1    Hamberger, L.2    Colantuoni, V.3    Gottesman, M.E.4    Blaner, W.S.5
  • 47
    • 0032895028 scopus 로고    scopus 로고
    • Remnant lipoprotein metabolism: Key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein e
    • R.W. Mahley, and Z.S. Ji Remnant lipoprotein metabolism: key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein E J. Lipid Res. 40 1999 1 16
    • (1999) J. Lipid Res. , vol.40 , pp. 1-16
    • Mahley, R.W.1    Ji, Z.S.2
  • 48
    • 0032895834 scopus 로고    scopus 로고
    • Plasma clearance and liver uptake of chylomicron remnants generated by hepatic lipase lipolysis: Evidence for a lactoferrin-sensitive and apolipoprotein E-independent pathway
    • S.E. Crawford, and J. Borensztajn Plasma clearance and liver uptake of chylomicron remnants generated by hepatic lipase lipolysis: evidence for a lactoferrin-sensitive and apolipoprotein E-independent pathway J. Lipid Res. 40 1999 797 805
    • (1999) J. Lipid Res. , vol.40 , pp. 797-805
    • Crawford, S.E.1    Borensztajn, J.2
  • 49
    • 0028284556 scopus 로고
    • Inhibition of hepatic chylomicron remnant uptake by gene transfer of a receptor antagonist
    • T.E. Willnow, Z. Sheng, S. Ishibashi, and J. Herz Inhibition of hepatic chylomicron remnant uptake by gene transfer of a receptor antagonist Science 264 1994 1471 1474
    • (1994) Science , vol.264 , pp. 1471-1474
    • Willnow, T.E.1    Sheng, Z.2    Ishibashi, S.3    Herz, J.4
  • 50
    • 69849100882 scopus 로고    scopus 로고
    • Inactivation of the LRP1 intracellular NPxYxxL motif in LDLR-deficient mice enhances postprandial dyslipidemia and atherosclerosis
    • P.L. Gordts, S. Reekmans, A. Lauwers, A. Van Dongen, L. Verbeek, and A.J. Roebroek Inactivation of the LRP1 intracellular NPxYxxL motif in LDLR-deficient mice enhances postprandial dyslipidemia and atherosclerosis Arterioscler. Thromb. Vasc. Biol. 29 2009 1258 1264
    • (2009) Arterioscler. Thromb. Vasc. Biol. , vol.29 , pp. 1258-1264
    • Gordts, P.L.1    Reekmans, S.2    Lauwers, A.3    Van Dongen, A.4    Verbeek, L.5    Roebroek, A.J.6
  • 51
    • 67349108867 scopus 로고    scopus 로고
    • Insulin stimulates hepatic low density lipoprotein receptor-related protein 1 (LRP1) to increase postprandial lipoprotein clearance
    • A. Laatsch, M. Merkel, P.J. Talmud, T. Grewal, U. Beisiegel, and J. Heeren Insulin stimulates hepatic low density lipoprotein receptor-related protein 1 (LRP1) to increase postprandial lipoprotein clearance Atherosclerosis 204 2009 105 111
    • (2009) Atherosclerosis , vol.204 , pp. 105-111
    • Laatsch, A.1    Merkel, M.2    Talmud, P.J.3    Grewal, T.4    Beisiegel, U.5    Heeren, J.6
  • 53
    • 70449408083 scopus 로고    scopus 로고
    • Syndecan-1 is the primary heparan sulfate proteoglycan mediating hepatic clearance of triglyceride-rich lipoproteins in mice
    • K.I. Stanford, J.R. Bishop, E.M. Foley, J.C. Gonzales, I.R. Niesman, J.L. Witztum, and J.D. Esko Syndecan-1 is the primary heparan sulfate proteoglycan mediating hepatic clearance of triglyceride-rich lipoproteins in mice J. Clin. Invest. 119 2009 3236 3245
    • (2009) J. Clin. Invest. , vol.119 , pp. 3236-3245
    • Stanford, K.I.1    Bishop, J.R.2    Foley, E.M.3    Gonzales, J.C.4    Niesman, I.R.5    Witztum, J.L.6    Esko, J.D.7
  • 54
    • 33846012847 scopus 로고    scopus 로고
    • Liver heparan sulfate proteoglycans mediate clearance of triglyceride-rich lipoproteins independently of LDL receptor family members
    • J.M. MacArthur, J.R. Bishop, K.I. Stanford, L. Wang, A. Bensadoun, J.L. Witztum, and J.D. Esko Liver heparan sulfate proteoglycans mediate clearance of triglyceride-rich lipoproteins independently of LDL receptor family members J. Clin. Invest. 117 2007 153 164
    • (2007) J. Clin. Invest. , vol.117 , pp. 153-164
    • MacArthur, J.M.1    Bishop, J.R.2    Stanford, K.I.3    Wang, L.4    Bensadoun, A.5    Witztum, J.L.6    Esko, J.D.7
  • 57
    • 0029055278 scopus 로고
    • Lipoprotein lipase enhances removal of chylomicrons and chylomicron remnants by the perfused rat liver
    • N. Skottova, R. Savonen, A. Lookene, M. Hultin, and G. Olivecrona Lipoprotein lipase enhances removal of chylomicrons and chylomicron remnants by the perfused rat liver J. Lipid Res. 36 1995 1334 1344
    • (1995) J. Lipid Res. , vol.36 , pp. 1334-1344
    • Skottova, N.1    Savonen, R.2    Lookene, A.3    Hultin, M.4    Olivecrona, G.5
  • 58
    • 0029789930 scopus 로고    scopus 로고
    • The role of lipoprotein lipase and apoprotein e in the recognition of chylomicrons and chylomicron remnants by cultured isolated mouse hepatocytes
    • S. Chang, N. Maeda, and J. Borensztajn The role of lipoprotein lipase and apoprotein E in the recognition of chylomicrons and chylomicron remnants by cultured isolated mouse hepatocytes Biochem. J. 318 Pt 1 1996 29 34
    • (1996) Biochem. J. , vol.318 , Issue.PART 1 , pp. 29-34
    • Chang, S.1    Maeda, N.2    Borensztajn, J.3
  • 59
    • 66349126859 scopus 로고    scopus 로고
    • Regulation of fatty acid uptake into tissues: Lipoprotein lipase- and CD36-mediated pathways
    • I.J. Goldberg, R.H. Eckel, and N.A. Abumrad Regulation of fatty acid uptake into tissues: lipoprotein lipase- and CD36-mediated pathways J. Lipid Res. 50 Suppl 2009 S86 S90
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Goldberg, I.J.1    Eckel, R.H.2    Abumrad, N.A.3
  • 60
    • 78649658552 scopus 로고    scopus 로고
    • Chylomicron- and VLDL-derived lipids enter the heart through different pathways: In vivo evidence for receptor- and non-receptor-mediated fatty acid uptake
    • K.G. Bharadwaj, Y. Hiyama, Y. Hu, L.A. Huggins, R. Ramakrishnan, N.A. Abumrad, G.I. Shulman, W.S. Blaner, and I.J. Goldberg Chylomicron- and VLDL-derived lipids enter the heart through different pathways: in vivo evidence for receptor- and non-receptor-mediated fatty acid uptake J. Biol. Chem. 285 2010 37976 37986
    • (2010) J. Biol. Chem. , vol.285 , pp. 37976-37986
    • Bharadwaj, K.G.1    Hiyama, Y.2    Hu, Y.3    Huggins, L.A.4    Ramakrishnan, R.5    Abumrad, N.A.6    Shulman, G.I.7    Blaner, W.S.8    Goldberg, I.J.9
  • 64
    • 28844503063 scopus 로고    scopus 로고
    • Disruption of the lecithin:retinol acyltransferase gene makes mice more susceptible to vitamin A deficiency
    • L. Liu, and L.J. Gudas Disruption of the lecithin:retinol acyltransferase gene makes mice more susceptible to vitamin A deficiency J. Biol. Chem. 280 2005 40226 40234
    • (2005) J. Biol. Chem. , vol.280 , pp. 40226-40234
    • Liu, L.1    Gudas, L.J.2
  • 65
    • 0034657162 scopus 로고    scopus 로고
    • Net release of individual fatty acids from white adipose tissue during lipolysis in vitro: Evidence for selective fatty acid re-uptake
    • T. Raclot, and H. Oudart Net release of individual fatty acids from white adipose tissue during lipolysis in vitro: evidence for selective fatty acid re-uptake Biochem. J. 348 Pt 1 2000 129 136
    • (2000) Biochem. J. , vol.348 , Issue.PART 1 , pp. 129-136
    • Raclot, T.1    Oudart, H.2
  • 66
    • 33947118627 scopus 로고    scopus 로고
    • Use of model-based compartmental analysis to study vitamin A kinetics and metabolism
    • C.J. Cifelli, J.B. Green, and M.H. Green Use of model-based compartmental analysis to study vitamin A kinetics and metabolism Vitam. Horm. 75 2007 161 195
    • (2007) Vitam. Horm. , vol.75 , pp. 161-195
    • Cifelli, C.J.1    Green, J.B.2    Green, M.H.3
  • 69
  • 70
    • 0030661590 scopus 로고    scopus 로고
    • Hepatic uptake of chylomicron remnants
    • A.D. Cooper Hepatic uptake of chylomicron remnants J. Lipid Res. 38 1997 2173 2192
    • (1997) J. Lipid Res. , vol.38 , pp. 2173-2192
    • Cooper, A.D.1
  • 71
    • 0029131275 scopus 로고
    • Hepatic uptake and metabolism of chylomicron retinyl esters: Probable role of plasma membrane/endosomal retinyl ester hydrolases
    • E.H. Harrison, M.Z. Gad, and A.C. Ross Hepatic uptake and metabolism of chylomicron retinyl esters: probable role of plasma membrane/endosomal retinyl ester hydrolases J. Lipid Res. 36 1995 1498 1506
    • (1995) J. Lipid Res. , vol.36 , pp. 1498-1506
    • Harrison, E.H.1    Gad, M.Z.2    Ross, A.C.3
  • 72
    • 0029920693 scopus 로고    scopus 로고
    • Lipoprotein lipase and lipolysis: Central roles in lipoprotein metabolism and atherogenesis
    • I.J. Goldberg Lipoprotein lipase and lipolysis: central roles in lipoprotein metabolism and atherogenesis J. Lipid Res. 37 1996 693 707
    • (1996) J. Lipid Res. , vol.37 , pp. 693-707
    • Goldberg, I.J.1
  • 73
    • 0017037406 scopus 로고
    • Hepatic vitamin A fat-storage cells and the metabolism of chylomicron cholesterol
    • T.G. Redgrave, and N. Vakakis Hepatic vitamin A fat-storage cells and the metabolism of chylomicron cholesterol Aust. J. Exp. Biol. Med. Sci. 54 1976 519 525
    • (1976) Aust. J. Exp. Biol. Med. Sci. , vol.54 , pp. 519-525
    • Redgrave, T.G.1    Vakakis, N.2
  • 74
    • 0021289022 scopus 로고
    • Newly administered [3H]retinol is transferred from hepatocytes to stellate cells in liver for storage
    • R. Blomhoff, K. Holte, L. Naess, and T. Berg Newly administered [3H]retinol is transferred from hepatocytes to stellate cells in liver for storage Exp. Cell Res. 150 1984 186 193
    • (1984) Exp. Cell Res. , vol.150 , pp. 186-193
    • Blomhoff, R.1    Holte, K.2    Naess, L.3    Berg, T.4
  • 75
    • 0022380578 scopus 로고
    • Intracellular transport of endocytosed chylomicron [3H]retinyl ester in rat liver parenchymal cells. Evidence for translocation of a [3H]retinoid from endosomes to endoplasmic reticulum
    • R. Blomhoff, W. Eskild, G.M. Kindberg, K. Prydz, and T. Berg Intracellular transport of endocytosed chylomicron [3H]retinyl ester in rat liver parenchymal cells. Evidence for translocation of a [3H]retinoid from endosomes to endoplasmic reticulum J. Biol. Chem. 260 1985 13566 13570
    • (1985) J. Biol. Chem. , vol.260 , pp. 13566-13570
    • Blomhoff, R.1    Eskild, W.2    Kindberg, G.M.3    Prydz, K.4    Berg, T.5
  • 76
    • 0016836751 scopus 로고
    • Role of lysosomal acid lipase in the metabolism of plasma low density lipoprotein. Observations in cultured fibroblasts from a patient with cholesteryl ester storage disease
    • J.L. Goldstein, S.E. Dana, J.R. Faust, A.L. Beaudet, and M.S. Brown Role of lysosomal acid lipase in the metabolism of plasma low density lipoprotein. Observations in cultured fibroblasts from a patient with cholesteryl ester storage disease J. Biol. Chem. 250 1975 8487 8495
    • (1975) J. Biol. Chem. , vol.250 , pp. 8487-8495
    • Goldstein, J.L.1    Dana, S.E.2    Faust, J.R.3    Beaudet, A.L.4    Brown, M.S.5
  • 77
    • 0032908013 scopus 로고    scopus 로고
    • Retinyl esters are hydrolyzed in early endosomes of J774 macrophages
    • E. Hagen, A.M. Myhre, T.E. Tjelle, T. Berg, and K.R. Norum Retinyl esters are hydrolyzed in early endosomes of J774 macrophages J. Lipid Res. 40 1999 309 317
    • (1999) J. Lipid Res. , vol.40 , pp. 309-317
    • Hagen, E.1    Myhre, A.M.2    Tjelle, T.E.3    Berg, T.4    Norum, K.R.5
  • 78
    • 0023395997 scopus 로고
    • Hydrolysis of retinyl esters by non-specific carboxylesterases from rat liver endoplasmic reticulum
    • R. Mentlein, and E. Heymann Hydrolysis of retinyl esters by non-specific carboxylesterases from rat liver endoplasmic reticulum Biochem. J. 245 1987 863 867
    • (1987) Biochem. J. , vol.245 , pp. 863-867
    • Mentlein, R.1    Heymann, E.2
  • 79
    • 0025759066 scopus 로고
    • Neutral and acid retinyl ester hydrolases associated with rat liver microsomes: Relationships to microsomal cholesteryl ester hydrolases
    • M.Z. Gad, and E.H. Harrison Neutral and acid retinyl ester hydrolases associated with rat liver microsomes: relationships to microsomal cholesteryl ester hydrolases J. Lipid Res. 32 1991 685 693
    • (1991) J. Lipid Res. , vol.32 , pp. 685-693
    • Gad, M.Z.1    Harrison, E.H.2
  • 80
    • 0031800635 scopus 로고    scopus 로고
    • The mammalian carboxylesterases: From molecules to functions
    • T. Satoh, and M. Hosokawa The mammalian carboxylesterases: from molecules to functions Annu. Rev. Pharmacol. Toxicol. 38 1998 257 288
    • (1998) Annu. Rev. Pharmacol. Toxicol. , vol.38 , pp. 257-288
    • Satoh, T.1    Hosokawa, M.2
  • 81
    • 0028153358 scopus 로고
    • Regulation of two rat liver microsomal carboxylesterase isozymes: Species differences, tissue distribution, and the effects of age, sex, and xenobiotic treatment of rats
    • E.W. Morgan, B. Yan, D. Greenway, and A. Parkinson Regulation of two rat liver microsomal carboxylesterase isozymes: species differences, tissue distribution, and the effects of age, sex, and xenobiotic treatment of rats Arch. Biochem. Biophys. 315 1994 513 526
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 513-526
    • Morgan, E.W.1    Yan, B.2    Greenway, D.3    Parkinson, A.4
  • 82
    • 0029146341 scopus 로고
    • Rat serum carboxylesterase. Cloning, expression, regulation, and evidence of secretion from liver
    • B. Yan, D. Yang, P. Bullock, and A. Parkinson Rat serum carboxylesterase. Cloning, expression, regulation, and evidence of secretion from liver J. Biol. Chem. 270 1995 19128 19134
    • (1995) J. Biol. Chem. , vol.270 , pp. 19128-19134
    • Yan, B.1    Yang, D.2    Bullock, P.3    Parkinson, A.4
  • 83
    • 0021262869 scopus 로고
    • Hydrolysis of ester- and amide-type drugs by the purified isoenzymes of nonspecific carboxylesterase from rat liver
    • R. Mentlein, and E. Heymann Hydrolysis of ester- and amide-type drugs by the purified isoenzymes of nonspecific carboxylesterase from rat liver Biochem. Pharmacol. 33 1984 1243 1248
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 1243-1248
    • Mentlein, R.1    Heymann, E.2
  • 84
    • 20744455504 scopus 로고    scopus 로고
    • Isolation and characterization of a microsomal acid retinyl ester hydrolase
    • T. Linke, H. Dawson, and E.H. Harrison Isolation and characterization of a microsomal acid retinyl ester hydrolase J. Biol. Chem. 280 2005 23287 23294
    • (2005) J. Biol. Chem. , vol.280 , pp. 23287-23294
    • Linke, T.1    Dawson, H.2    Harrison, E.H.3
  • 85
    • 0030804651 scopus 로고    scopus 로고
    • Purification and characterization of a neutral, bile salt-independent retinyl ester hydrolase from rat liver microsomes. Relationship to rat carboxylesterase ES-2
    • G. Sun, S.E. Alexson, and E.H. Harrison Purification and characterization of a neutral, bile salt-independent retinyl ester hydrolase from rat liver microsomes. Relationship To rat carboxylesterase ES-2 J. Biol. Chem. 272 1997 24488 24493
    • (1997) J. Biol. Chem. , vol.272 , pp. 24488-24493
    • Sun, G.1    Alexson, S.E.2    Harrison, E.H.3
  • 86
    • 0026718901 scopus 로고
    • The carboxylesterase family exhibits C-terminal sequence diversity reflecting the presence or absence of endoplasmic-reticulum-retention sequences
    • S. Medda, and R.L. Proia The carboxylesterase family exhibits C-terminal sequence diversity reflecting the presence or absence of endoplasmic-reticulum- retention sequences Eur. J. Biochem. / FEBS 206 1992 801 806
    • (1992) Eur. J. Biochem. / FEBS , vol.206 , pp. 801-806
    • Medda, S.1    Proia, R.L.2
  • 88
    • 0020574679 scopus 로고
    • Ligand-dependent regulation of intracellular protein transport: Effect of vitamin a on the secretion of the retinol-binding protein
    • H. Ronne, C. Ocklind, K. Wiman, L. Rask, B. Obrink, and P.A. Peterson Ligand-dependent regulation of intracellular protein transport: effect of vitamin a on the secretion of the retinol-binding protein J. Cell Biol. 96 1983 907 910
    • (1983) J. Cell Biol. , vol.96 , pp. 907-910
    • Ronne, H.1    Ocklind, C.2    Wiman, K.3    Rask, L.4    Obrink, B.5    Peterson, P.A.6
  • 89
    • 0023138328 scopus 로고
    • Studies on the metabolism of retinol-binding protein by primary hepatocytes from retinol-deficient rats
    • J.L. Dixon, and D.S. Goodman Studies on the metabolism of retinol-binding protein by primary hepatocytes from retinol-deficient rats J. Cell. Physiol. 130 1987 14 20
    • (1987) J. Cell. Physiol. , vol.130 , pp. 14-20
    • Dixon, J.L.1    Goodman, D.S.2
  • 90
    • 0032006083 scopus 로고    scopus 로고
    • Purification and characterization of retinyl ester hydrolase as a member of the non-specific carboxylesterase supergene family
    • R. Schindler, R. Mentlein, and W. Feldheim Purification and characterization of retinyl ester hydrolase as a member of the non-specific carboxylesterase supergene family Eur. J. Biochem. / FEBS 251 1998 863 873
    • (1998) Eur. J. Biochem. / FEBS , vol.251 , pp. 863-873
    • Schindler, R.1    Mentlein, R.2    Feldheim, W.3
  • 92
    • 0036379359 scopus 로고    scopus 로고
    • Identification of microsomal rat liver carboxylesterases and their activity with retinyl palmitate
    • S.P. Sanghani, W.I. Davis, N.G. Dumaual, A. Mahrenholz, and W.F. Bosron Identification of microsomal rat liver carboxylesterases and their activity with retinyl palmitate Eur. J. Biochem. / FEBS 269 2002 4387 4398
    • (2002) Eur. J. Biochem. / FEBS , vol.269 , pp. 4387-4398
    • Sanghani, S.P.1    Davis, W.I.2    Dumaual, N.G.3    Mahrenholz, A.4    Bosron, W.F.5
  • 93
    • 68549135297 scopus 로고    scopus 로고
    • Hormone-sensitive lipase (HSL) is also a retinyl ester hydrolase: Evidence from mice lacking HSL
    • K. Strom, T.E. Gundersen, O. Hansson, S. Lucas, C. Fernandez, R. Blomhoff, and C. Holm Hormone-sensitive lipase (HSL) is also a retinyl ester hydrolase: evidence from mice lacking HSL FASEB J. 23 2009 2307 2316
    • (2009) FASEB J. , vol.23 , pp. 2307-2316
    • Strom, K.1    Gundersen, T.E.2    Hansson, O.3    Lucas, S.4    Fernandez, C.5    Blomhoff, R.6    Holm, C.7
  • 94
    • 0023653510 scopus 로고
    • Immunological evidence for the presence of hormone-sensitive lipase in rat tissues other than adipose tissue
    • C. Holm, P. Belfrage, and G. Fredrikson Immunological evidence for the presence of hormone-sensitive lipase in rat tissues other than adipose tissue Biochem. Biophys. Res. Commun. 148 1987 99 105
    • (1987) Biochem. Biophys. Res. Commun. , vol.148 , pp. 99-105
    • Holm, C.1    Belfrage, P.2    Fredrikson, G.3
  • 97
    • 35948954244 scopus 로고    scopus 로고
    • Hepatic stellate cells: Protean, multifunctional, and enigmatic cells of the liver
    • S.L. Friedman Hepatic stellate cells: protean, multifunctional, and enigmatic cells of the liver Physiol. Rev. 88 2008 125 172
    • (2008) Physiol. Rev. , vol.88 , pp. 125-172
    • Friedman, S.L.1
  • 98
    • 0034808310 scopus 로고    scopus 로고
    • History, heterogeneity, developmental biology, and functions of quiescent hepatic stellate cells
    • A. Geerts History, heterogeneity, developmental biology, and functions of quiescent hepatic stellate cells Semin. Liver Dis. 21 2001 311 335
    • (2001) Semin. Liver Dis. , vol.21 , pp. 311-335
    • Geerts, A.1
  • 99
    • 0001572310 scopus 로고
    • Fat-storing (Ito) cell biology
    • I.M. Arias, J.L. Boyer, N. Fausto, W.B. Jakoby, D. Schachter, D.A. Shafritz, 3rd Ed. Raven Press Ltd. New York
    • A. Geerts, P. De Bleser, M.L. Hautekeete, T. Niki, and E. Wisse Fat-storing (Ito) cell biology I.M. Arias, J.L. Boyer, N. Fausto, W.B. Jakoby, D. Schachter, D.A. Shafritz, The Liver: Biology and Pathobiology 3rd Ed. 1994 Raven Press Ltd. New York 819 837
    • (1994) The Liver: Biology and Pathobiology , pp. 819-837
    • Geerts, A.1    De Bleser, P.2    Hautekeete, M.L.3    Niki, T.4    Wisse, E.5
  • 101
    • 0015177686 scopus 로고
    • "sternzellen" in the liver: Perisinusoidal cells with special reference to storage of vitamin A
    • K. Wake "Sternzellen" in the liver: perisinusoidal cells with special reference to storage of vitamin A Am. J. Anat. 132 1971 429 462
    • (1971) Am. J. Anat. , vol.132 , pp. 429-462
    • Wake, K.1
  • 104
    • 0023902733 scopus 로고
    • Morphological and biochemical analyses, of lipid granules isolated from fat-storing cells in rat liver
    • S. Yumoto, K. Ueno, S. Mori, N. Takebayashi, and S. Handa Morphological and biochemical analyses, of lipid granules isolated from fat-storing cells in rat liver Biomed. Res. 2 1988 147 160
    • (1988) Biomed. Res. , vol.2 , pp. 147-160
    • Yumoto, S.1    Ueno, K.2    Mori, S.3    Takebayashi, N.4    Handa, S.5
  • 105
    • 0024215032 scopus 로고
    • Effects of dietary retinoid and triglyceride on the lipid composition of rat liver stellate cells and stellate cell lipid droplets
    • H. Moriwaki, W.S. Blaner, R. Piantedosi, and D.S. Goodman Effects of dietary retinoid and triglyceride on the lipid composition of rat liver stellate cells and stellate cell lipid droplets J. Lipid Res. 29 1988 1523 1534
    • (1988) J. Lipid Res. , vol.29 , pp. 1523-1534
    • Moriwaki, H.1    Blaner, W.S.2    Piantedosi, R.3    Goodman, D.S.4
  • 106
    • 0031055373 scopus 로고    scopus 로고
    • Lecithin:retinol acyltransferase and retinyl ester hydrolase activities are differentially regulated by retinoids and have distinct distributions between hepatocyte and nonparenchymal cell fractions of rat liver
    • T. Matsuura, M.Z. Gad, E.H. Harrison, and A.C. Ross Lecithin:retinol acyltransferase and retinyl ester hydrolase activities are differentially regulated by retinoids and have distinct distributions between hepatocyte and nonparenchymal cell fractions of rat liver J. Nutr. 127 1997 218 224
    • (1997) J. Nutr. , vol.127 , pp. 218-224
    • Matsuura, T.1    Gad, M.Z.2    Harrison, E.H.3    Ross, A.C.4
  • 107
    • 0022198149 scopus 로고
    • Retinoids, retinoid-binding proteins, and retinyl palmitate hydrolase distributions in different types of rat liver cells
    • W.S. Blaner, H.F. Hendriks, A. Brouwer, A.M. de Leeuw, D.L. Knook, and D.S. Goodman Retinoids, retinoid-binding proteins, and retinyl palmitate hydrolase distributions in different types of rat liver cells J. Lipid Res. 26 1985 1241 1251
    • (1985) J. Lipid Res. , vol.26 , pp. 1241-1251
    • Blaner, W.S.1    Hendriks, H.F.2    Brouwer, A.3    De Leeuw, A.M.4    Knook, D.L.5    Goodman, D.S.6
  • 108
    • 0031844055 scopus 로고    scopus 로고
    • Lipases and carboxylesterases: Possible roles in the hepatic metabolism of retinol
    • E.H. Harrison Lipases and carboxylesterases: possible roles in the hepatic metabolism of retinol Annu. Rev. Nutr. 18 1998 259 276
    • (1998) Annu. Rev. Nutr. , vol.18 , pp. 259-276
    • Harrison, E.H.1
  • 109
    • 0033969142 scopus 로고    scopus 로고
    • Lipases and carboxylesterases: Possible roles in the hepatic utilization of vitamin A
    • E.H. Harrison Lipases and carboxylesterases: possible roles in the hepatic utilization of vitamin A J. Nutr. 130 2000 340S 344S
    • (2000) J. Nutr. , vol.130
    • Harrison, E.H.1
  • 114
    • 0024459947 scopus 로고
    • Expression in Xenopus oocytes of rat liver mRNA coding for a bile salt-dependent cholesteryl ester hydrolase
    • E.H. Zolfaghari Expression in Xenopus oocytes of rat liver mRNA coding for a bile salt-dependent cholesteryl ester hydrolase Proc. Natl. Acad. Sci. U. S. A. 86 1989 6913 6916
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 6913-6916
    • Zolfaghari, E.H.1
  • 115
    • 0018725451 scopus 로고
    • Unusual properties of retinyl palmitate hydrolase activity in rat liver
    • E.H. Harrison, J.E. Smith, and D.S. Goodman Unusual properties of retinyl palmitate hydrolase activity in rat liver J. Lipid Res. 6 1979 753 759
    • (1979) J. Lipid Res. , vol.6 , pp. 753-759
    • Harrison, E.H.1    Smith, J.E.2    Goodman, D.S.3
  • 117
    • 0028279396 scopus 로고
    • Hydrolysis of retinyl esters in rat liver. Description of a lysosomal activity
    • M. Mercier, A. Forget, P. Grolier, and V. Azais-Braesco Hydrolysis of retinyl esters in rat liver. Description of a lysosomal activity Biochim. Biophys. Acta 1212 1994 176 182
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 176-182
    • Mercier, M.1    Forget, A.2    Grolier, P.3    Azais-Braesco, V.4
  • 119
    • 0011834209 scopus 로고
    • Ultrastructural observations of ito cells in the aged rats
    • E. Wise, D.L. Knook, R.S. Mc Cuskey, The Kupffer Cell Foundation Leiden, The Netherlands
    • H. Enzan, T. Saibara, H. Ueda, S. Onishi, Y. Yamamoto, T. Okada, and H. Hara Ultrastructural observations of ito cells in the aged rats E. Wise, D.L. Knook, R.S. Mc Cuskey, Cells of the Hepatic Sinusoid 1991 The Kupffer Cell Foundation Leiden, The Netherlands 226 229
    • (1991) Cells of the Hepatic Sinusoid , pp. 226-229
    • Enzan, H.1    Saibara, T.2    Ueda, H.3    Onishi, S.4    Yamamoto, Y.5    Okada, T.6    Hara, H.7
  • 122
    • 0024562494 scopus 로고
    • Localization of retinol-binding protein messenger RNA in the rat kidney and in perinephric fat tissue
    • A. Makover, D.R. Soprano, M.L. Wyatt, and D.S. Goodman Localization of retinol-binding protein messenger RNA in the rat kidney and in perinephric fat tissue J. Lipid Res. 30 1989 171 180
    • (1989) J. Lipid Res. , vol.30 , pp. 171-180
    • Makover, A.1    Soprano, D.R.2    Wyatt, M.L.3    Goodman, D.S.4
  • 123
    • 0030716808 scopus 로고    scopus 로고
    • Clearance of lipoprotein remnant particles in adipose tissue and muscle in humans
    • F. Karpe, S.M. Humphreys, J.S. Samra, L.K. Summers, and K.N. Frayn Clearance of lipoprotein remnant particles in adipose tissue and muscle in humans J. Lipid Res. 38 1997 2335 2343
    • (1997) J. Lipid Res. , vol.38 , pp. 2335-2343
    • Karpe, F.1    Humphreys, S.M.2    Samra, J.S.3    Summers, L.K.4    Frayn, K.N.5
  • 125
    • 78650107057 scopus 로고    scopus 로고
    • Lipolysis-a highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores
    • A. Lass, R. Zimmermann, M. Oberer, and R. Zechner Lipolysis-a highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores Prog. Lipid Res. 50 2011 14 27
    • (2011) Prog. Lipid Res. , vol.50 , pp. 14-27
    • Lass, A.1    Zimmermann, R.2    Oberer, M.3    Zechner, R.4
  • 126
    • 0017581424 scopus 로고
    • Hormone-sensitive lipase of rat adipose tissue: Identification and some properties of the enzyme protein
    • P. Belfrage, B. Jergil, P. Stralfors, and H. Tornqvist Hormone-sensitive lipase of rat adipose tissue: identification and some properties of the enzyme protein FEBS Lett. 75 1977 259 264
    • (1977) FEBS Lett. , vol.75 , pp. 259-264
    • Belfrage, P.1    Jergil, B.2    Stralfors, P.3    Tornqvist, H.4
  • 127
    • 0025273134 scopus 로고
    • Hormone-sensitive lipase-a multipurpose enzyme in lipid metabolism
    • S.J. Yeaman Hormone-sensitive lipase-a multipurpose enzyme in lipid metabolism Biochim. Biophys. Acta 1052 1990 128 132
    • (1990) Biochim. Biophys. Acta , vol.1052 , pp. 128-132
    • Yeaman, S.J.1
  • 129
    • 77955274518 scopus 로고    scopus 로고
    • PPARgamma in adipocyte differentiation and metabolism-novel insights from genome-wide studies
    • R. Siersbaek, R. Nielsen, and S. Mandrup PPARgamma in adipocyte differentiation and metabolism-novel insights from genome-wide studies FEBS Lett. 584 2010 3242 3249
    • (2010) FEBS Lett. , vol.584 , pp. 3242-3249
    • Siersbaek, R.1    Nielsen, R.2    Mandrup, S.3
  • 130
    • 77955266460 scopus 로고    scopus 로고
    • Brown vs white adipocytes: The PPARgamma coregulator story
    • A. Koppen, and E. Kalkhoven Brown vs white adipocytes: the PPARgamma coregulator story FEBS Lett. 584 2010 3250 3259
    • (2010) FEBS Lett. , vol.584 , pp. 3250-3259
    • Koppen, A.1    Kalkhoven, E.2
  • 131
    • 76749146390 scopus 로고    scopus 로고
    • Transcriptional factors that promote formation of white adipose tissue
    • U.A. White, and J.M. Stephens Transcriptional factors that promote formation of white adipose tissue Mol. Cell. Endocrinol. 318 2010 10 14
    • (2010) Mol. Cell. Endocrinol. , vol.318 , pp. 10-14
    • White, U.A.1    Stephens, J.M.2
  • 134
    • 69549108861 scopus 로고    scopus 로고
    • Expression of retinoic acid receptor alpha in the germline is essential for proper cellular association and spermiogenesis during spermatogenesis
    • S.S. Chung, X. Wang, and D.J. Wolgemuth Expression of retinoic acid receptor alpha in the germline is essential for proper cellular association and spermiogenesis during spermatogenesis Development 136 2009 2091 2100
    • (2009) Development , vol.136 , pp. 2091-2100
    • Chung, S.S.1    Wang, X.2    Wolgemuth, D.J.3
  • 135
    • 0030945024 scopus 로고    scopus 로고
    • Downregulation of RAR alpha in mice by antisense transgene leads to a compensatory increase in RAR beta and RAR gamma and development of lymphoma
    • T. Manshouri, Y. Yang, H. Lin, S.A. Stass, A.B. Glassman, M.J. Keating, and M. Albitar Downregulation of RAR alpha in mice by antisense transgene leads to a compensatory increase in RAR beta and RAR gamma and development of lymphoma Blood 89 1997 2507 2515
    • (1997) Blood , vol.89 , pp. 2507-2515
    • Manshouri, T.1    Yang, Y.2    Lin, H.3    Stass, S.A.4    Glassman, A.B.5    Keating, M.J.6    Albitar, M.7
  • 136
    • 34547838930 scopus 로고    scopus 로고
    • Retinoid signaling during spermatogenesis as revealed by genetic and metabolic manipulations of retinoic acid receptor alpha
    • D.J. Wolgemuth, and S.S. Chung Retinoid signaling during spermatogenesis as revealed by genetic and metabolic manipulations of retinoic acid receptor alpha Soc. Reprod. Fertil. Suppl. 63 2007 11 23
    • (2007) Soc. Reprod. Fertil. Suppl. , vol.63 , pp. 11-23
    • Wolgemuth, D.J.1    Chung, S.S.2
  • 141
    • 0030011415 scopus 로고    scopus 로고
    • Auto-regulation of retinoic acid biosynthesis through regulation of retinol esterification in human keratinocytes
    • S.B. Kurlandsky, E.A. Duell, S. Kang, J.J. Voorhees, and G.J. Fisher Auto-regulation of retinoic acid biosynthesis through regulation of retinol esterification in human keratinocytes J. Biol. Chem. 271 1996 15346 15352
    • (1996) J. Biol. Chem. , vol.271 , pp. 15346-15352
    • Kurlandsky, S.B.1    Duell, E.A.2    Kang, S.3    Voorhees, J.J.4    Fisher, G.J.5
  • 142
    • 0023090773 scopus 로고
    • Retinol esterification by mouse epidermal microsomes: Evidence for acyl-CoA:retinol acyltransferase activity
    • H. Torma, and A. Vahlquist Retinol esterification by mouse epidermal microsomes: evidence for acyl-CoA:retinol acyltransferase activity J. Invest. Dermatol. 88 1987 398 402
    • (1987) J. Invest. Dermatol. , vol.88 , pp. 398-402
    • Torma, H.1    Vahlquist, A.2
  • 143
    • 20544442848 scopus 로고    scopus 로고
    • Identification of a novel keratinocyte retinyl ester hydrolase as a transacylase and lipase
    • J. Gao, and M. Simon Identification of a novel keratinocyte retinyl ester hydrolase as a transacylase and lipase J. Invest. Dermatol. 124 2005 1259 1266
    • (2005) J. Invest. Dermatol. , vol.124 , pp. 1259-1266
    • Gao, J.1    Simon, M.2
  • 144
    • 66349121084 scopus 로고    scopus 로고
    • Mammalian patatin domain containing proteins: A family with diverse lipolytic activities involved in multiple biological functions
    • P.C. Kienesberger, M. Oberer, A. Lass, and R. Zechner Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions J. Lipid Res. 50 Suppl 2009 S63 S68
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Kienesberger, P.C.1    Oberer, M.2    Lass, A.3    Zechner, R.4
  • 145
    • 0028071435 scopus 로고
    • Isolation of a new gene GS2 (DXS1283E) from a CpG island between STS and KAL1 on Xp22.3
    • W.C. Lee, E. Salido, and P.H. Yen Isolation of a new gene GS2 (DXS1283E) from a CpG island between STS and KAL1 on Xp22.3 Genomics 22 1994 372 376
    • (1994) Genomics , vol.22 , pp. 372-376
    • Lee, W.C.1    Salido, E.2    Yen, P.H.3
  • 147
    • 33747367181 scopus 로고    scopus 로고
    • Molecular screening for GS2 lipase regulators: Inhibition of keratinocyte retinylester hydrolysis by TIP47
    • J.G. Gao, and M. Simon Molecular screening for GS2 lipase regulators: inhibition of keratinocyte retinylester hydrolysis by TIP47 J. Invest. Dermatol. 126 2006 2087 2095
    • (2006) J. Invest. Dermatol. , vol.126 , pp. 2087-2095
    • Gao, J.G.1    Simon, M.2
  • 150
    • 68049092870 scopus 로고    scopus 로고
    • Neutral lipid storage disease: Genetic disorders caused by mutations in adipose triglyceride lipase/PNPLA2 or CGI-58/ABHD5
    • M. Schweiger, A. Lass, R. Zimmermann, T.O. Eichmann, and R. Zechner Neutral lipid storage disease: genetic disorders caused by mutations in adipose triglyceride lipase/PNPLA2 or CGI-58/ABHD5 Am. J. Physiol. Endocrinol. Metab. 297 2009 E289 E296
    • (2009) Am. J. Physiol. Endocrinol. Metab. , vol.297
    • Schweiger, M.1    Lass, A.2    Zimmermann, R.3    Eichmann, T.O.4    Zechner, R.5
  • 153
    • 77956402413 scopus 로고    scopus 로고
    • Culture of highly differentiated human retinal pigment epithelium for analysis of the polarized uptake, processing, and secretion of retinoids
    • J. Hu, and D. Bok Culture of highly differentiated human retinal pigment epithelium for analysis of the polarized uptake, processing, and secretion of retinoids Methods Mol. Biol. 652 2010 55 73
    • (2010) Methods Mol. Biol. , vol.652 , pp. 55-73
    • Hu, J.1    Bok, D.2
  • 154
    • 0842266594 scopus 로고    scopus 로고
    • Noninvasive two-photon imaging reveals retinyl ester storage structures in the eye
    • Y. Imanishi, M.L. Batten, D.W. Piston, W. Baehr, and K. Palczewski Noninvasive two-photon imaging reveals retinyl ester storage structures in the eye J. Cell Biol. 164 2004 373 383
    • (2004) J. Cell Biol. , vol.164 , pp. 373-383
    • Imanishi, Y.1    Batten, M.L.2    Piston, D.W.3    Baehr, W.4    Palczewski, K.5
  • 155
    • 4143126732 scopus 로고    scopus 로고
    • Retinosomes: New insights into intracellular managing of hydrophobic substances in lipid bodies
    • Y. Imanishi, V. Gerke, and K. Palczewski Retinosomes: new insights into intracellular managing of hydrophobic substances in lipid bodies J. Cell Biol. 166 2004 447 453
    • (2004) J. Cell Biol. , vol.166 , pp. 447-453
    • Imanishi, Y.1    Gerke, V.2    Palczewski, K.3
  • 156
    • 78649454765 scopus 로고    scopus 로고
    • Retinol dehydrogenases (RDHs) in the visual cycle
    • R.O. Parker, and R.K. Crouch Retinol dehydrogenases (RDHs) in the visual cycle Exp. Eye Res. 91 2010 788 792
    • (2010) Exp. Eye Res. , vol.91 , pp. 788-792
    • Parker, R.O.1    Crouch, R.K.2
  • 157
    • 77954620409 scopus 로고    scopus 로고
    • Membrane-binding and enzymatic properties of RPE65
    • P.D. Kiser, and K. Palczewski Membrane-binding and enzymatic properties of RPE65 Prog. Retin. Eye Res. 29 2010 428 442
    • (2010) Prog. Retin. Eye Res. , vol.29 , pp. 428-442
    • Kiser, P.D.1    Palczewski, K.2
  • 159
    • 65549131951 scopus 로고    scopus 로고
    • Purified RPE65 shows isomerohydrolase activity after reassociation with a phospholipid membrane
    • O. Nikolaeva, Y. Takahashi, G. Moiseyev, and J.X. Ma Purified RPE65 shows isomerohydrolase activity after reassociation with a phospholipid membrane FEBS J. 276 2009 3020 3030
    • (2009) FEBS J. , vol.276 , pp. 3020-3030
    • Nikolaeva, O.1    Takahashi, Y.2    Moiseyev, G.3    Ma, J.X.4
  • 160
    • 0038629063 scopus 로고    scopus 로고
    • All-trans-retinyl esters are the substrates for isomerization in the vertebrate visual cycle
    • D.R. Gollapalli, and R.R. Rando All-trans-retinyl esters are the substrates for isomerization in the vertebrate visual cycle Biochemistry 42 2003 5809 5818
    • (2003) Biochemistry , vol.42 , pp. 5809-5818
    • Gollapalli, D.R.1    Rando, R.R.2
  • 165
    • 77954620055 scopus 로고    scopus 로고
    • Leber congenital amaurosis due to RPE65 mutations and its treatment with gene therapy
    • A.V. Cideciyan Leber congenital amaurosis due to RPE65 mutations and its treatment with gene therapy Prog. Retin. Eye Res. 29 2010 398 427
    • (2010) Prog. Retin. Eye Res. , vol.29 , pp. 398-427
    • Cideciyan, A.V.1
  • 166
    • 50349088772 scopus 로고    scopus 로고
    • Retinal pigment epithelium-retinal G protein receptor-opsin mediates light-dependent translocation of all-trans-retinyl esters for synthesis of visual chromophore in retinal pigment epithelial cells
    • R.A. Radu, J. Hu, J. Peng, D. Bok, N.L. Mata, and G.H. Travis Retinal pigment epithelium-retinal G protein receptor-opsin mediates light-dependent translocation of all-trans-retinyl esters for synthesis of visual chromophore in retinal pigment epithelial cells J. Biol. Chem. 283 2008 19730 19738
    • (2008) J. Biol. Chem. , vol.283 , pp. 19730-19738
    • Radu, R.A.1    Hu, J.2    Peng, J.3    Bok, D.4    Mata, N.L.5    Travis, G.H.6
  • 168
    • 0026761223 scopus 로고
    • McCollum Award Lecture, 1992: Vitamin A absorption, transport, cellular uptake, and storage
    • K.R. Norum, and R. Blomhoff McCollum Award Lecture, 1992: vitamin A absorption, transport, cellular uptake, and storage Am. J. Clin. Nutr. 56 1992 735 744
    • (1992) Am. J. Clin. Nutr. , vol.56 , pp. 735-744
    • Norum, K.R.1    Blomhoff, R.2
  • 169
    • 0024742764 scopus 로고
    • Cholate effects on all-trans-retinyl palmitate hydrolysis in tissue homogenates: Solubilization of multiple kidney membrane hydrolases
    • J.L. Napoli, E.B. Pacia, and G.J. Salerno Cholate effects on all-trans-retinyl palmitate hydrolysis in tissue homogenates: solubilization of multiple kidney membrane hydrolases Arch. Biochem. Biophys. 274 1989 192 199
    • (1989) Arch. Biochem. Biophys. , vol.274 , pp. 192-199
    • Napoli, J.L.1    Pacia, E.B.2    Salerno, G.J.3
  • 170
    • 77951187480 scopus 로고    scopus 로고
    • The key role of vitamin A in spermatogenesis
    • C.A. Hogarth, and M.D. Griswold The key role of vitamin A in spermatogenesis J. Clin. Invest. 120 2010 956 962
    • (2010) J. Clin. Invest. , vol.120 , pp. 956-962
    • Hogarth, C.A.1    Griswold, M.D.2
  • 172
    • 0024843640 scopus 로고
    • Characteristics of retinol accumulation from serum retinol-binding protein by cultured Sertoli cells
    • J.L. Shingleton, M.K. Skinner, and D.E. Ong Characteristics of retinol accumulation from serum retinol-binding protein by cultured Sertoli cells Biochemistry 28 1989 9641 9647
    • (1989) Biochemistry , vol.28 , pp. 9641-9647
    • Shingleton, J.L.1    Skinner, M.K.2    Ong, D.E.3
  • 173
    • 0024853354 scopus 로고
    • Retinol esterification in Sertoli cells by lecithin-retinol acyltransferase
    • J.L. Shingleton, M.K. Skinner, and D.E. Ong Retinol esterification in Sertoli cells by lecithin-retinol acyltransferase Biochemistry 28 1989 9647 9653
    • (1989) Biochemistry , vol.28 , pp. 9647-9653
    • Shingleton, J.L.1    Skinner, M.K.2    Ong, D.E.3
  • 174
    • 77951067503 scopus 로고    scopus 로고
    • Significance of vitamin A to brain function, behavior and learning
    • C.R. Olson, and C.V. Mello Significance of vitamin A to brain function, behavior and learning Mol. Nutr. Food Res. 54 2010 489 495
    • (2010) Mol. Nutr. Food Res. , vol.54 , pp. 489-495
    • Olson, C.R.1    Mello, C.V.2
  • 175
    • 79952201893 scopus 로고    scopus 로고
    • The neurobehavioral teratology of retinoids: A 50-year history
    • J. Adams The neurobehavioral teratology of retinoids: a 50-year history Birth Defects Res. A Clin. Mol. Teratol. 88 2010 895 905
    • (2010) Birth Defects Res. A Clin. Mol. Teratol. , vol.88 , pp. 895-905
    • Adams, J.1
  • 176
    • 0026834014 scopus 로고
    • Vitamin neurotoxicity
    • S.R. Snodgrass Vitamin neurotoxicity Mol. Neurobiol. 6 1992 41 73
    • (1992) Mol. Neurobiol. , vol.6 , pp. 41-73
    • Snodgrass, S.R.1
  • 178
    • 0030967058 scopus 로고    scopus 로고
    • Developmental expression pattern of Stra6, a retinoic acid-responsive gene encoding a new type of membrane protein
    • P. Bouillet, V. Sapin, C. Chazaud, N. Messaddeq, D. Decimo, P. Dolle, and P. Chambon Developmental expression pattern of Stra6, a retinoic acid-responsive gene encoding a new type of membrane protein Mech. Dev. 63 1997 173 186
    • (1997) Mech. Dev. , vol.63 , pp. 173-186
    • Bouillet, P.1    Sapin, V.2    Chazaud, C.3    Messaddeq, N.4    Decimo, D.5    Dolle, P.6    Chambon, P.7
  • 179
    • 0025283517 scopus 로고
    • Localization of cellular retinol-binding protein and retinol-binding protein in cells comprising the blood-brain barrier of rat and human
    • P.N. MacDonald, D. Bok, and D.E. Ong Localization of cellular retinol-binding protein and retinol-binding protein in cells comprising the blood-brain barrier of rat and human Proc. Natl. Acad. Sci. U. S. A. 87 1990 4265 4269
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 4265-4269
    • MacDonald, P.N.1    Bok, D.2    Ong, D.E.3
  • 180
    • 43849100786 scopus 로고    scopus 로고
    • HPLC/UV quantitation of retinal, retinol, and retinyl esters in serum and tissues
    • M.A. Kane, A.E. Folias, and J.L. Napoli HPLC/UV quantitation of retinal, retinol, and retinyl esters in serum and tissues Anal. Biochem. 378 2008 71 79
    • (2008) Anal. Biochem. , vol.378 , pp. 71-79
    • Kane, M.A.1    Folias, A.E.2    Napoli, J.L.3
  • 181
    • 79952496231 scopus 로고    scopus 로고
    • An enzymatic mechanism for generating the precursor of endogenous 13-cis retinoic acid in the brain
    • Y. Takahashi, G. Moiseyev, Y. Chen, K. Farjo, O. Nikolaeva, and J.X. Ma An enzymatic mechanism for generating the precursor of endogenous 13-cis retinoic acid in the brain FEBS J. 278 2011 973 987
    • (2011) FEBS J. , vol.278 , pp. 973-987
    • Takahashi, Y.1    Moiseyev, G.2    Chen, Y.3    Farjo, K.4    Nikolaeva, O.5    Ma, J.X.6
  • 183
  • 184
    • 44849131178 scopus 로고    scopus 로고
    • Isotretinoin and the risk of depression in patients with acne vulgaris: A case-crossover study
    • L. Azoulay, L. Blais, G. Koren, J. LeLorier, and A. Berard Isotretinoin and the risk of depression in patients with acne vulgaris: a case-crossover study J. Clin. Psychiatry 69 2008 526 532
    • (2008) J. Clin. Psychiatry , vol.69 , pp. 526-532
    • Azoulay, L.1    Blais, L.2    Koren, G.3    Lelorier, J.4    Berard, A.5
  • 187
    • 0026702496 scopus 로고
    • Esterase-1: Developmental expression in the mouse and distribution of related proteins in other species
    • S.S. Kadner, J. Katz, and T.H. Finlay Esterase-1: developmental expression in the mouse and distribution of related proteins in other species Arch. Biochem. Biophys. 296 1992 435 441
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 435-441
    • Kadner, S.S.1    Katz, J.2    Finlay, T.H.3
  • 189
    • 0033485637 scopus 로고    scopus 로고
    • Human egasyn binds beta-glucuronidase but neither the esterase active site of egasyn nor the C terminus of beta-glucuronidase is involved in their interaction
    • M.R. Islam, A. Waheed, G.N. Shah, S. Tomatsu, and W.S. Sly Human egasyn binds beta-glucuronidase but neither the esterase active site of egasyn nor the C terminus of beta-glucuronidase is involved in their interaction Arch. Biochem. Biophys. 372 1999 53 61
    • (1999) Arch. Biochem. Biophys. , vol.372 , pp. 53-61
    • Islam, M.R.1    Waheed, A.2    Shah, G.N.3    Tomatsu, S.4    Sly, W.S.5
  • 190
    • 34548498086 scopus 로고    scopus 로고
    • Carboxylesterase in the liver and small intestine of experimental animals and human
    • M. Taketani, M. Shii, K. Ohura, S. Ninomiya, and T. Imai Carboxylesterase in the liver and small intestine of experimental animals and human Life Sci. 81 2007 924 932
    • (2007) Life Sci. , vol.81 , pp. 924-932
    • Taketani, M.1    Shii, M.2    Ohura, K.3    Ninomiya, S.4    Imai, T.5
  • 191
    • 0021996062 scopus 로고
    • Clinical significance of esterases in man
    • F.M. Williams Clinical significance of esterases in man Clin. Pharmacokinet. 10 1985 392 403
    • (1985) Clin. Pharmacokinet. , vol.10 , pp. 392-403
    • Williams, F.M.1
  • 192
    • 0031550250 scopus 로고    scopus 로고
    • Differentiation-dependent expression of a human carboxylesterase in monocytic cells and transcription factor binding to the promoter
    • T. Langmann, C. Aslanidis, M. Schuierer, and G. Schmitz Differentiation-dependent expression of a human carboxylesterase in monocytic cells and transcription factor binding to the promoter Biochem. Biophys. Res. Commun. 230 1997 215 219
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 215-219
    • Langmann, T.1    Aslanidis, C.2    Schuierer, M.3    Schmitz, G.4
  • 193
    • 0031557664 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver
    • H. Schwer, T. Langmann, R. Daig, A. Becker, C. Aslanidis, and G. Schmitz Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver Biochem. Biophys. Res. Commun. 233 1997 117 120
    • (1997) Biochem. Biophys. Res. Commun. , vol.233 , pp. 117-120
    • Schwer, H.1    Langmann, T.2    Daig, R.3    Becker, A.4    Aslanidis, C.5    Schmitz, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.