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Volumn 33, Issue , 2003, Pages 9-28

Intestinal uptake and transport of fatty acids

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EID: 33847770531     PISSN: 15692558     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2558(03)33002-4     Document Type: Review
Times cited : (5)

References (120)
  • 1
    • 0027537924 scopus 로고
    • Overview of retinoid metabolism
    • A.C Ross Overview of retinoid metabolism J. Nutr. 123 1993 346 350
    • (1993) J. Nutr. , vol.123 , pp. 346-350
    • Ross, A.C1
  • 2
    • 0035292695 scopus 로고    scopus 로고
    • Structural, biochemical and signaling properties of the low-density lipoprotein receptor gene family
    • M.M Hussain Structural, biochemical and signaling properties of the low-density lipoprotein receptor gene family Front. Biosci. 6 2001 D417 D428
    • (2001) Front. Biosci. , vol.6 , pp. D417-D428
    • Hussain, M.M1
  • 3
    • 0030139934 scopus 로고    scopus 로고
    • How do long-chain free fatty acids cross cell membranes?
    • P.D Berk How do long-chain free fatty acids cross cell membranes? Proc. Soc. Exp. Biol. Med. 212 1996 1 4
    • (1996) Proc. Soc. Exp. Biol. Med. , vol.212 , pp. 1-4
    • Berk, P.D1
  • 4
    • 0029877955 scopus 로고    scopus 로고
    • Fatty acids enter cells by simple diffusion
    • D Zakim Fatty acids enter cells by simple diffusion Proc. Soc. Exp. Biol. Med. 212 1996 5 14
    • (1996) Proc. Soc. Exp. Biol. Med. , vol.212 , pp. 5-14
    • Zakim, D1
  • 6
    • 0032444832 scopus 로고    scopus 로고
    • Membrane transport of long-chain fatty acids: evidence for a facilitated process
    • N Abumrad C Harmon A Ibrahimi Membrane transport of long-chain fatty acids: evidence for a facilitated process J. Lipid Res. 39 1998 2309 2318
    • (1998) J. Lipid Res. , vol.39 , pp. 2309-2318
    • Abumrad, N1    Harmon, C2    Ibrahimi, A3
  • 7
    • 0031921236 scopus 로고    scopus 로고
    • Fatty acid transport: difficult or easy?
    • J.A Hamilton Fatty acid transport: difficult or easy? J. Lipid Res. 39 1998 467 481
    • (1998) J. Lipid Res. , vol.39 , pp. 467-481
    • Hamilton, J.A1
  • 9
    • 0036812909 scopus 로고    scopus 로고
    • Mechanism of cellular uptake of long-chain fatty acids: do we need cellular proteins?
    • J.A Hamilton W Guo F Kamp Mechanism of cellular uptake of long-chain fatty acids: do we need cellular proteins? Mol. Cell. Biochem. 239 2002 17 23
    • (2002) Mol. Cell. Biochem. , vol.239 , pp. 17-23
    • Hamilton, J.A1    Guo, W2    Kamp, F3
  • 10
    • 0030720253 scopus 로고    scopus 로고
    • Transport of long-chain native fatty acids across lipid bilayer membranes indicates that transbilayer flip–flop is rate limiting
    • A.M Kleinfeld P Chu C Romero Transport of long-chain native fatty acids across lipid bilayer membranes indicates that transbilayer flip–flop is rate limiting Biochemistry 36 1997 14146 14158
    • (1997) Biochemistry , vol.36 , pp. 14146-14158
    • Kleinfeld, A.M1    Chu, P2    Romero, C3
  • 11
    • 0027439285 scopus 로고
    • Movement of fatty acids, fatty acid analogues and bile acids across phospholipid bilayers
    • F Kamp H.V Westterhoff J.A Hamilton Movement of fatty acids, fatty acid analogues and bile acids across phospholipid bilayers Biochemistry 32 1993 11074 11086
    • (1993) Biochemistry , vol.32 , pp. 11074-11086
    • Kamp, F1    Westterhoff, H.V2    Hamilton, J.A3
  • 12
    • 0029090984 scopus 로고
    • Fatty acid flip–flop in phospholipid bilayers is extremely fast
    • F Kamp D Zakim F Zhang N Noy J.A Hamilton Fatty acid flip–flop in phospholipid bilayers is extremely fast Biochemistry 34 1995 11928 11937
    • (1995) Biochemistry , vol.34 , pp. 11928-11937
    • Kamp, F1    Zakim, D2    Zhang, F3    Noy, N4    Hamilton, J.A5
  • 13
    • 0023664119 scopus 로고
    • Lipid asymmetry induced by transmembrane pH gradients in large unilamellar vesicles
    • M.J Hope P.R Cullis Lipid asymmetry induced by transmembrane pH gradients in large unilamellar vesicles J. Biol. Chem. 262 1987 4360 4366
    • (1987) J. Biol. Chem. , vol.262 , pp. 4360-4366
    • Hope, M.J1    Cullis, P.R2
  • 14
    • 0030048273 scopus 로고    scopus 로고
    • The effect of intracellular pH on long-chain fatty acid uptake in 3T3-L1 adipocytes: evidence that uptake involves the passive diffusion of protonated long-chain fatty acids across the plasma membrane
    • B.L Trigatti G.E Gerber The effect of intracellular pH on long-chain fatty acid uptake in 3T3-L1 adipocytes: evidence that uptake involves the passive diffusion of protonated long-chain fatty acids across the plasma membrane Biochem. J. 313 1996 487 494
    • (1996) Biochem. J. , vol.313 , pp. 487-494
    • Trigatti, B.L1    Gerber, G.E2
  • 15
    • 0018581740 scopus 로고
    • Linoleic acid absorption in the unanesthetized rat: mechanism of transport and influence of luminal factors on absorption
    • S.L Chow D Hollander Linoleic acid absorption in the unanesthetized rat: mechanism of transport and influence of luminal factors on absorption Lipids 14 1979 378 385
    • (1979) Lipids , vol.14 , pp. 378-385
    • Chow, S.L1    Hollander, D2
  • 16
    • 0015209610 scopus 로고
    • Unstirred water layers in intestine: rate determinant of fatty acid absorption from micellar solutions
    • F.A Wilson V.L Sallee J.M Dietschy Unstirred water layers in intestine: rate determinant of fatty acid absorption from micellar solutions Science 174 1971 1031 1033
    • (1971) Science , vol.174 , pp. 1031-1033
    • Wilson, F.A1    Sallee, V.L2    Dietschy, J.M3
  • 17
    • 0022081201 scopus 로고
    • Mechanisms maintaining a low-pH microclimate in the intestine
    • Y.F Shiau P Fernandez M.J Jackson S McMonagle Mechanisms maintaining a low-pH microclimate in the intestine Am. J. Physiol. 248 1985 G608 G617
    • (1985) Am. J. Physiol. , vol.248 , pp. G608-G617
    • Shiau, Y.F1    Fernandez, P2    Jackson, M.J3    McMonagle, S4
  • 18
    • 0025300525 scopus 로고
    • Characterization of basolateral membrane Na/H antiport in rat jejunum
    • M.N Orsenigo M Tosco S Zoppi A Faelli Characterization of basolateral membrane Na/H antiport in rat jejunum Biochim. Biophys. Acta 1026 1990 64 68
    • (1990) Biochim. Biophys. Acta , vol.1026 , pp. 64-68
    • Orsenigo, M.N1    Tosco, M2    Zoppi, S3    Faelli, A4
  • 19
    • 85112954302 scopus 로고
    • P Tso Intestinal Lipid Absorption 3rd ed. Physiology of the Gastrointestinal Tract 1994
    • (1994)
    • Tso, P1
  • 20
    • 0019398065 scopus 로고
    • Mechanism of fat absorption
    • Y.F Shiau Mechanism of fat absorption Am. J. Physiol. 240 1981 G1 G9
    • (1981) Am. J. Physiol. , vol.240 , pp. G1-G9
    • Shiau, Y.F1
  • 22
    • 0024244050 scopus 로고
    • Uptake of fatty acids by jejunal mucosal cells is mediated by a fatty acid binding membrane protein
    • W Stremmel Uptake of fatty acids by jejunal mucosal cells is mediated by a fatty acid binding membrane protein J. Clin. Invest. 82 1988 2001 2010
    • (1988) J. Clin. Invest. , vol.82 , pp. 2001-2010
    • Stremmel, W1
  • 23
    • 13344276570 scopus 로고    scopus 로고
    • Fatty acid uptake by Caco-2 human intestinal cells
    • P.J Trotter S.Y Ho J Storch Fatty acid uptake by Caco-2 human intestinal cells J. Lipid Res. 37 1996 336 346
    • (1996) J. Lipid Res. , vol.37 , pp. 336-346
    • Trotter, P.J1    Ho, S.Y2    Storch, J3
  • 25
    • 0028152492 scopus 로고
    • Expression, cloning and characterization of a novel adipocyte long-chain fatty acid transport protein
    • J.E Schaffer H.F Lodish Expression, cloning and characterization of a novel adipocyte long-chain fatty acid transport protein Cell 79 1994 427 436
    • (1994) Cell , vol.79 , pp. 427-436
    • Schaffer, J.E1    Lodish, H.F2
  • 26
    • 0025721161 scopus 로고
    • Photoaffinity labeling and fatty acid permeation in 3T3-L1 adipocytes
    • B.L Trigatti D Mangroo G.E Gerber Photoaffinity labeling and fatty acid permeation in 3T3-L1 adipocytes J. Biol. Chem. 266 1991 22621 22625
    • (1991) J. Biol. Chem. , vol.266 , pp. 22621-22625
    • Trigatti, B.L1    Mangroo, D2    Gerber, G.E3
  • 27
    • 0027240176 scopus 로고
    • Cloning of a rat adipocyte membrane protein implicated in binding or transport of long-chain fatty acids that is induced during preadipocyte differentiation. Homology with human CD36
    • N.A Abumrad M.R el-Maghrabi E.Z Amri E Lopez P.A Grimaldi Cloning of a rat adipocyte membrane protein implicated in binding or transport of long-chain fatty acids that is induced during preadipocyte differentiation. Homology with human CD36 J. Biol. Chem. 268 1993 17665 17668
    • (1993) J. Biol. Chem. , vol.268 , pp. 17665-17668
    • Abumrad, N.A1    el-Maghrabi, M.R2    Amri, E.Z3    Lopez, E4    Grimaldi, P.A5
  • 28
    • 0021981778 scopus 로고
    • Identification, isolation, and partial characterization of a fatty acid binding protein from rat jejunal microvillous membranes
    • W Stremmel G Lotz G Strohmeyer P.D Berk Identification, isolation, and partial characterization of a fatty acid binding protein from rat jejunal microvillous membranes J. Clin. Invest. 75 1985 1068 1076
    • (1985) J. Clin. Invest. , vol.75 , pp. 1068-1076
    • Stremmel, W1    Lotz, G2    Strohmeyer, G3    Berk, P.D4
  • 29
    • 0032555136 scopus 로고    scopus 로고
    • A family of fatty acid transporters conserved from mycobacterium to man
    • D Hirsch A Stahl H.F Lodish A family of fatty acid transporters conserved from mycobacterium to man Proc. Natl Acad. Sci. USA 95 1998 8625 8629
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8625-8629
    • Hirsch, D1    Stahl, A2    Lodish, H.F3
  • 32
    • 0035972814 scopus 로고    scopus 로고
    • Mouse fatty acid transport protein 4 (FATP4): characterization of the gene and functional assessment as a very long chain acyl-CoA synthetase
    • T Herrmann F Buchkremer I Gosch A.M Hall D.A Bernlohr W Stremmel Mouse fatty acid transport protein 4 (FATP4): characterization of the gene and functional assessment as a very long chain acyl-CoA synthetase Gene 270 2001 31 40
    • (2001) Gene , vol.270 , pp. 31-40
    • Herrmann, T1    Buchkremer, F2    Gosch, I3    Hall, A.M4    Bernlohr, D.A5    Stremmel, W6
  • 33
    • 0033579432 scopus 로고    scopus 로고
    • The fatty acid transport protein (FATP1) is a very long chain acyl-CoA synthetase
    • N.R Coe A.J Smith B.I Frohnert P.A Watkins D.A Bernlohr The fatty acid transport protein (FATP1) is a very long chain acyl-CoA synthetase J. Biol. Chem. 274 1999 36300 36304
    • (1999) J. Biol. Chem. , vol.274 , pp. 36300-36304
    • Coe, N.R1    Smith, A.J2    Frohnert, B.I3    Watkins, P.A4    Bernlohr, D.A5
  • 34
    • 0032771089 scopus 로고    scopus 로고
    • Molecular aspects of fatty acid transport: mutations in the IYTSGTTGXPK motif impair fatty acid transport protein function
    • S.M Stuhlsatz-Krouper N.E Bennett J.E Schaffer Molecular aspects of fatty acid transport: mutations in the IYTSGTTGXPK motif impair fatty acid transport protein function Prostaglandins Leukot. Essent. Fatty Acids 60 1999 285 289
    • (1999) Prostaglandins Leukot. Essent. Fatty Acids , vol.60 , pp. 285-289
    • Stuhlsatz-Krouper, S.M1    Bennett, N.E2    Schaffer, J.E3
  • 35
    • 0036239115 scopus 로고    scopus 로고
    • Endocytosis via caveolae
    • L Pelkmans A Helenius Endocytosis via caveolae Traffic 3 2002 311 320
    • (2002) Traffic , vol.3 , pp. 311-320
    • Pelkmans, L1    Helenius, A2
  • 36
    • 0027323805 scopus 로고
    • Identification of high affinity membrane-bound fatty acid-binding proteins using a photoreactive fatty acid
    • G.E Gerber D Mangroo B.L Trigatti Identification of high affinity membrane-bound fatty acid-binding proteins using a photoreactive fatty acid Mol. Cell. Biochem. 123 1993 39 44
    • (1993) Mol. Cell. Biochem. , vol.123 , pp. 39-44
    • Gerber, G.E1    Mangroo, D2    Trigatti, B.L3
  • 40
    • 0033203564 scopus 로고    scopus 로고
    • Identification of caveolin-1 in lipoprotein particles secreted by exocrine cells
    • P Liu W.P Li T Machleidt R.G Anderson Identification of caveolin-1 in lipoprotein particles secreted by exocrine cells Nat. Cell. Biol. 1 1999 369 375
    • (1999) Nat. Cell. Biol. , vol.1 , pp. 369-375
    • Liu, P1    Li, W.P2    Machleidt, T3    Anderson, R.G4
  • 41
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • P Liu M Rudick R.G Anderson Multiple functions of caveolin-1 J. Biol. Chem. 277 2002 41295 41298
    • (2002) J. Biol. Chem. , vol.277 , pp. 41295-41298
    • Liu, P1    Rudick, M2    Anderson, R.G3
  • 42
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins
    • J Couet S Li T Okamoto T Ikezu M.P Lisanti Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins J. Biol. Chem. 272 1997 6525 6533
    • (1997) J. Biol. Chem. , vol.272 , pp. 6525-6533
    • Couet, J1    Li, S2    Okamoto, T3    Ikezu, T4    Lisanti, M.P5
  • 43
    • 0029560256 scopus 로고
    • Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps
    • P.A Conrad E.J Smart Y.S Ying R.G Anderson G.S Bloom Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps J. Cell. Biol. 131 1995 1421 1433
    • (1995) J. Cell. Biol. , vol.131 , pp. 1421-1433
    • Conrad, P.A1    Smart, E.J2    Ying, Y.S3    Anderson, R.G4    Bloom, G.S5
  • 44
    • 0031706594 scopus 로고    scopus 로고
    • Caveolin is present in intestinal cells: role in cholesterol trafficking?
    • F.J Field E Born S Murthy S.N Mathur Caveolin is present in intestinal cells: role in cholesterol trafficking? J. Lipid Res. 39 1998 1938 1950
    • (1998) J. Lipid Res. , vol.39 , pp. 1938-1950
    • Field, F.J1    Born, E2    Murthy, S3    Mathur, S.N4
  • 47
    • 0026738318 scopus 로고
    • Membrane glycoprotein CD36: a review of its roles in adherence, signal transduction, and transfusion medicine
    • D.E Greenwalt R.H Lipsky C.F Ockenhouse H Ikeda N.N Tandon G.A Jamieson Membrane glycoprotein CD36: a review of its roles in adherence, signal transduction, and transfusion medicine Blood 80 1992 1105 1115
    • (1992) Blood , vol.80 , pp. 1105-1115
    • Greenwalt, D.E1    Lipsky, R.H2    Ockenhouse, C.F3    Ikeda, H4    Tandon, N.N5    Jamieson, G.A6
  • 48
    • 0029787399 scopus 로고    scopus 로고
    • Reversible binding of long-chain fatty acids to purified FAT, the adipose CD36 homolog
    • A.G Baillie C.T Coburn N.A Abumrad Reversible binding of long-chain fatty acids to purified FAT, the adipose CD36 homolog J. Membr. Biol. 153 1996 75 81
    • (1996) J. Membr. Biol. , vol.153 , pp. 75-81
    • Baillie, A.G1    Coburn, C.T2    Abumrad, N.A3
  • 51
    • 0029809772 scopus 로고    scopus 로고
    • CD36 is palmitoylated on both N- and C-terminal cytoplasmic tails
    • N Tao S.J Wagner D.M Lublin CD36 is palmitoylated on both N- and C-terminal cytoplasmic tails J. Biol. Chem. 271 1996 22315 22320
    • (1996) J. Biol. Chem. , vol.271 , pp. 22315-22320
    • Tao, N1    Wagner, S.J2    Lublin, D.M3
  • 52
    • 0033520482 scopus 로고    scopus 로고
    • Phenotypic behavior of caveolin-3 mutations that cause autosomal dominant limb girdle muscular dystrophy (LGMD-1C)
    • F Galbiati D Volonté C Minetti J.B Chu M.P Lisanti Phenotypic behavior of caveolin-3 mutations that cause autosomal dominant limb girdle muscular dystrophy (LGMD-1C) J. Biol. Chem. 274 1999 25632 25641
    • (1999) J. Biol. Chem. , vol.274 , pp. 25632-25641
    • Galbiati, F1    Volonté, D2    Minetti, C3    Chu, J.B4    Lisanti, M.P5
  • 53
    • 0036514622 scopus 로고    scopus 로고
    • Role of CD36 in membrane transport of long-chain fatty acids
    • A Ibrahimi N.A Abumrad Role of CD36 in membrane transport of long-chain fatty acids Curr. Opin. Clin. Nutr. Metab. Care 5 2002 139 145
    • (2002) Curr. Opin. Clin. Nutr. Metab. Care , vol.5 , pp. 139-145
    • Ibrahimi, A1    Abumrad, N.A2
  • 54
    • 0029948676 scopus 로고    scopus 로고
    • Localization and regulation of the putative membrane fatty-acid transporter (FAT) in the small intestine. Comparison with fatty acid-binding proteins (FABP)
    • H Poirier P Degrace I Niot A Bernard P Besnard Localization and regulation of the putative membrane fatty-acid transporter (FAT) in the small intestine. Comparison with fatty acid-binding proteins (FABP) Eur. J. Biochem. 238 1996 368 373
    • (1996) Eur. J. Biochem. , vol.238 , pp. 368-373
    • Poirier, H1    Degrace, P2    Niot, I3    Bernard, A4    Besnard, P5
  • 55
    • 0034819066 scopus 로고    scopus 로고
    • Localization of the lipid receptors CD36 and CLA-1/SR-BI in the human gastrointestinal tract: towards the identification of receptors mediating the intestinal absorption of dietary lipids
    • M.V Lobo L Huerta N Ruiz-Velasco E Teixeiro P de la Cueva A Celdran A Martin-Hidalgo M.A Vega R Bragado Localization of the lipid receptors CD36 and CLA-1/SR-BI in the human gastrointestinal tract: towards the identification of receptors mediating the intestinal absorption of dietary lipids J. Histochem. Cytochem. 49 2001 1253 1260
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 1253-1260
    • Lobo, M.V1    Huerta, L2    Ruiz-Velasco, N3    Teixeiro, E4    de la Cueva, P5    Celdran, A6    Martin-Hidalgo, A7    Vega, M.A8    Bragado, R9
  • 56
    • 0343337216 scopus 로고    scopus 로고
    • Effect of low fat diet on lipid absorption and fatty-acid transport following bowel resection
    • I Sukhotnik A.S Gork M Chen R.A Drongowski A.G Coran C.M Harmon Effect of low fat diet on lipid absorption and fatty-acid transport following bowel resection Pediatr. Surg. Int. 17 2001 259 264
    • (2001) Pediatr. Surg. Int. , vol.17 , pp. 259-264
    • Sukhotnik, I1    Gork, A.S2    Chen, M3    Drongowski, R.A4    Coran, A.G5    Harmon, C.M6
  • 57
    • 0035203991 scopus 로고    scopus 로고
    • Gut expression and regulation of FAT/CD36: possible role in fatty acid transport in rat enterocytes
    • M Chen Y Yang E Braunstein K.E Georgeson C.M Harmon Gut expression and regulation of FAT/CD36: possible role in fatty acid transport in rat enterocytes Am. J. Physiol. Endocrinol. Metab. 281 2001 E916 E923
    • (2001) Am. J. Physiol. Endocrinol. Metab. , vol.281 , pp. E916-E923
    • Chen, M1    Yang, Y2    Braunstein, E3    Georgeson, K.E4    Harmon, C.M5
  • 58
    • 0034640498 scopus 로고    scopus 로고
    • Acute regulation of fatty acid uptake involves the cellular redistribution of fatty acid translocase
    • A Bonen J.J Luiken Y Arumugam J.F Glatz N.N Tandon Acute regulation of fatty acid uptake involves the cellular redistribution of fatty acid translocase J. Biol. Chem. 275 2000 14501 14508
    • (2000) J. Biol. Chem. , vol.275 , pp. 14501-14508
    • Bonen, A1    Luiken, J.J2    Arumugam, Y3    Glatz, J.F4    Tandon, N.N5
  • 60
    • 0037088653 scopus 로고    scopus 로고
    • Chronic leptin administration decreases fatty acid uptake and fatty acid transporters in rat skeletal muscle
    • G.R Steinberg D.J Dyck J Calles-Escandon N.N Tandon J.J Luiken J.F Glatz A Bonen Chronic leptin administration decreases fatty acid uptake and fatty acid transporters in rat skeletal muscle J. Biol. Chem. 277 2002 8854 8860
    • (2002) J. Biol. Chem. , vol.277 , pp. 8854-8860
    • Steinberg, G.R1    Dyck, D.J2    Calles-Escandon, J3    Tandon, N.N4    Luiken, J.J5    Glatz, J.F6    Bonen, A7
  • 61
    • 0037150119 scopus 로고    scopus 로고
    • Cellular cholesterol stimulates acute uptake of palmitate by redistribution of fatty acid translocase in type II pneumocytes
    • I Kolleck F Guthmann A.M Ladhoff N.N Tandon M Schlame B Rustow Cellular cholesterol stimulates acute uptake of palmitate by redistribution of fatty acid translocase in type II pneumocytes Biochemistry 41 2002 6369 6375
    • (2002) Biochemistry , vol.41 , pp. 6369-6375
    • Kolleck, I1    Guthmann, F2    Ladhoff, A.M3    Tandon, N.N4    Schlame, M5    Rustow, B6
  • 65
    • 0023652878 scopus 로고
    • Isolation and partial characterization of plasma membrane fatty acid binding proteins from myocardium and adipose tissue and their relationship to analogous proteins in liver and gut
    • B.J Potter D Stump W Schwieterman D Sorrentino L.N Jacobs C.L Kiang J.H Rand P.D Berk Isolation and partial characterization of plasma membrane fatty acid binding proteins from myocardium and adipose tissue and their relationship to analogous proteins in liver and gut Biochem. Biophys. Res. Commun. 148 1987 1370 1376
    • (1987) Biochem. Biophys. Res. Commun. , vol.148 , pp. 1370-1376
    • Potter, B.J1    Stump, D2    Schwieterman, W3    Sorrentino, D4    Jacobs, L.N5    Kiang, C.L6    Rand, J.H7    Berk, P.D8
  • 67
    • 0027143338 scopus 로고
    • Comparison of plasma membrane FABP and mitochondrial isoform of aspartate aminotransferase from rat liver
    • D.D Stump S.L Zhou P.D Berk Comparison of plasma membrane FABP and mitochondrial isoform of aspartate aminotransferase from rat liver Am. J. Physiol. 265 1993 G894 G902
    • (1993) Am. J. Physiol. , vol.265 , pp. G894-G902
    • Stump, D.D1    Zhou, S.L2    Berk, P.D3
  • 68
    • 0028786938 scopus 로고
    • 3T3 fibroblasts transfected with a cDNA for mitochondrial aspartate aminotransferase express plasma membrane fatty acid-binding protein and saturable fatty acid uptake
    • L.M Isola S.L Zhou C.L Kiang D.D Stump M.W Bradbury P.D Berk 3T3 fibroblasts transfected with a cDNA for mitochondrial aspartate aminotransferase express plasma membrane fatty acid-binding protein and saturable fatty acid uptake Proc. Natl Acad. Sci. USA 92 1995 9866 9870
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9866-9870
    • Isola, L.M1    Zhou, S.L2    Kiang, C.L3    Stump, D.D4    Bradbury, M.W5    Berk, P.D6
  • 69
    • 0028069754 scopus 로고
    • Constitutive expression of a saturable transport system for non-esterified fatty acids in Xenopus laevis oocytes
    • S.L Zhou D Stump L Isola P.D Berk Constitutive expression of a saturable transport system for non-esterified fatty acids in Xenopus laevis oocytes Biochem. J. 297 1994 315 319
    • (1994) Biochem. J. , vol.297 , pp. 315-319
    • Zhou, S.L1    Stump, D2    Isola, L3    Berk, P.D4
  • 70
    • 0031059829 scopus 로고    scopus 로고
    • Fasting increases plasma membrane fatty acid-binding protein (FABP(PM)) in red skeletal muscle
    • L.P Turcotte A.K Srivastava J.L Chiasson Fasting increases plasma membrane fatty acid-binding protein (FABP(PM)) in red skeletal muscle Mol. Cell. Biochem. 166 1997 153 158
    • (1997) Mol. Cell. Biochem. , vol.166 , pp. 153-158
    • Turcotte, L.P1    Srivastava, A.K2    Chiasson, J.L3
  • 71
    • 0030991677 scopus 로고    scopus 로고
    • Uptake of long chain free fatty acids is selectively up-regulated in adipocytes of Zucker rats with genetic obesity and non-insulin-dependent diabetes mellitus
    • P.D Berk S.L Zhou C.L Kiang D Stump M Bradbury L.M Isola Uptake of long chain free fatty acids is selectively up-regulated in adipocytes of Zucker rats with genetic obesity and non-insulin-dependent diabetes mellitus J. Biol. Chem. 272 1997 8830 8835
    • (1997) J. Biol. Chem. , vol.272 , pp. 8830-8835
    • Berk, P.D1    Zhou, S.L2    Kiang, C.L3    Stump, D4    Bradbury, M5    Isola, L.M6
  • 72
    • 0031900079 scopus 로고    scopus 로고
    • Ethanol up-regulates fatty acid uptake and plasma membrane expression and export of mitochondrial aspartate aminotransferase in HepG2 cells
    • S.L Zhou R.E Gordon M Bradbury D Stump C.L Kiang P.D Berk Ethanol up-regulates fatty acid uptake and plasma membrane expression and export of mitochondrial aspartate aminotransferase in HepG2 cells Hepatology 19998 1998 1064 1074
    • (1998) Hepatology , vol.19998 , pp. 1064-1074
    • Zhou, S.L1    Gordon, R.E2    Bradbury, M3    Stump, D4    Kiang, C.L5    Berk, P.D6
  • 74
    • 0030986132 scopus 로고    scopus 로고
    • The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates
    • J Thompson N Winter D Terwey J Bratt L Banaszak The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates J. Biol. Chem. 272 1997 7140 7150
    • (1997) J. Biol. Chem. , vol.272 , pp. 7140-7150
    • Thompson, J1    Winter, N2    Terwey, D3    Bratt, J4    Banaszak, L5
  • 75
    • 0027244075 scopus 로고
    • Rat intestinal fatty acid binding protein. A model system for analyzing the forces that can bind fatty acids to proteins
    • J.C Sacchettini J.I Gordon Rat intestinal fatty acid binding protein. A model system for analyzing the forces that can bind fatty acids to proteins J. Biol. Chem. 268 1993 18399 18402
    • (1993) J. Biol. Chem. , vol.268 , pp. 18399-18402
    • Sacchettini, J.C1    Gordon, J.I2
  • 76
    • 0030719448 scopus 로고    scopus 로고
    • Morphological and biochemical status of the mammary gland as influenced by conjugated linoleic acid: implication for a reduction in mammary cancer risk
    • H Thompson Z Zhu S Banni K Darcy T Loftus C Ip Morphological and biochemical status of the mammary gland as influenced by conjugated linoleic acid: implication for a reduction in mammary cancer risk Cancer Res. 57 1997 5067 5072
    • (1997) Cancer Res. , vol.57 , pp. 5067-5072
    • Thompson, H1    Zhu, Z2    Banni, S3    Darcy, K4    Loftus, T5    Ip, C6
  • 77
    • 0031106978 scopus 로고    scopus 로고
    • Metallothionein-IIA promoter induction alters rat intestinal fatty acid binding protein expression, fatty acid uptake, and lipid metabolism in transfected L-cells
    • D.R Prows F Schroeder Metallothionein-IIA promoter induction alters rat intestinal fatty acid binding protein expression, fatty acid uptake, and lipid metabolism in transfected L-cells Arch. Biochem. Biophys. 340 1997 135 143
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 135-143
    • Prows, D.R1    Schroeder, F2
  • 79
    • 0032484882 scopus 로고    scopus 로고
    • Oleic acid distribution in small intestinal epithelial cells expressing intestinal-fatty acid binding protein
    • E.L Holehouse M.L Liu G.W Aponte Oleic acid distribution in small intestinal epithelial cells expressing intestinal-fatty acid binding protein Biochim. Biophys. Acta 1390 1998 52 64
    • (1998) Biochim. Biophys. Acta , vol.1390 , pp. 52-64
    • Holehouse, E.L1    Liu, M.L2    Aponte, G.W3
  • 80
    • 0032957086 scopus 로고    scopus 로고
    • Phytanic acid is ligand and transcriptional activator of murine liver fatty acid binding protein
    • C Wolfrum P Ellinghaus M Fobker U Seedorf G Assmann T Börchers F Spener Phytanic acid is ligand and transcriptional activator of murine liver fatty acid binding protein J. Lipid Res. 40 1999 708 714
    • (1999) J. Lipid Res. , vol.40 , pp. 708-714
    • Wolfrum, C1    Ellinghaus, P2    Fobker, M3    Seedorf, U4    Assmann, G5    Börchers, T6    Spener, F7
  • 81
    • 0030443383 scopus 로고    scopus 로고
    • The binding of cholesterol and bile salts to recombinant rat liver fatty acid-binding protein
    • A.E Thumser D.C Wilton The binding of cholesterol and bile salts to recombinant rat liver fatty acid-binding protein Biochem. J. 320 1996 729 733
    • (1996) Biochem. J. , vol.320 , pp. 729-733
    • Thumser, A.E1    Wilton, D.C2
  • 82
    • 0032906887 scopus 로고    scopus 로고
    • The liver fatty acid binding protein – comparison of cavity properties of intracellular lipid-binding proteins
    • J Thompson J Ory A Reese-Wagoner L Banaszak The liver fatty acid binding protein – comparison of cavity properties of intracellular lipid-binding proteins Mol. Cell. Biochem. 192 1999 9 16
    • (1999) Mol. Cell. Biochem. , vol.192 , pp. 9-16
    • Thompson, J1    Ory, J2    Reese-Wagoner, A3    Banaszak, L4
  • 83
    • 0028076831 scopus 로고
    • Equilibrium constants for the binding of fatty acids with fatty acid-binding proteins from adipocyte, intestine, heart, and liver measured with the fluorescent probe ADIFAB
    • G.V Richieri R.T Ogata A.M Kleinfeld Equilibrium constants for the binding of fatty acids with fatty acid-binding proteins from adipocyte, intestine, heart, and liver measured with the fluorescent probe ADIFAB J. Biol. Chem. 269 1994 23918 23930
    • (1994) J. Biol. Chem. , vol.269 , pp. 23918-23930
    • Richieri, G.V1    Ogata, R.T2    Kleinfeld, A.M3
  • 84
    • 0030774420 scopus 로고    scopus 로고
    • Fatty acid regulation of fatty acid-binding protein expression in the small intestine
    • H Poirier I Niot P Degrace M.C Monnot A Bernard P Besnard Fatty acid regulation of fatty acid-binding protein expression in the small intestine Am. J. Physiol. 273 1997 G289 G295
    • (1997) Am. J. Physiol. , vol.273 , pp. G289-G295
    • Poirier, H1    Niot, I2    Degrace, P3    Monnot, M.C4    Bernard, A5    Besnard, P6
  • 85
    • 0027970680 scopus 로고
    • Expression of intestinal fatty acid binding protein in intestinal epithelial cell lines, hBRIE, 380 cells
    • G Hallden E.L Holehouse X Dong G.W Aponte Expression of intestinal fatty acid binding protein in intestinal epithelial cell lines, hBRIE, 380 cells Am. J. Physiol. 267 1994 G730 G743
    • (1994) Am. J. Physiol. , vol.267 , pp. G730-G743
    • Hallden, G1    Holehouse, E.L2    Dong, X3    Aponte, G.W4
  • 86
    • 0031563828 scopus 로고    scopus 로고
    • A complete epithelial organization of Caco-2 cells induces I-FABP and potentializes apolipoprotein gene expression
    • J Le Beyec F Delers F Jourdant C Schreider J Chambaz P Cardot M Pincon-Raymond A complete epithelial organization of Caco-2 cells induces I-FABP and potentializes apolipoprotein gene expression Exp. Cell Res. 236 1997 311 320
    • (1997) Exp. Cell Res. , vol.236 , pp. 311-320
    • Le Beyec, J1    Delers, F2    Jourdant, F3    Schreider, C4    Chambaz, J5    Cardot, P6    Pincon-Raymond, M7
  • 87
    • 0030918711 scopus 로고    scopus 로고
    • Evidence for a role of the gut hormone PYY in the regulation of intestinal fatty acid-binding protein transcripts in differentiated subpopulations of intestinal epithelial cell hybrids
    • G Hallden G.W Aponte Evidence for a role of the gut hormone PYY in the regulation of intestinal fatty acid-binding protein transcripts in differentiated subpopulations of intestinal epithelial cell hybrids J. Biol. Chem. 272 1997 12591 12600
    • (1997) J. Biol. Chem. , vol.272 , pp. 12591-12600
    • Hallden, G1    Aponte, G.W2
  • 88
    • 0022652642 scopus 로고
    • Interaction of peptide YY with rat intestinal epithelial plasma membranes: binding of the radioiodinated peptide
    • M Laburthe B Chenut C Rouyer-Fessard K Tatemoto A Couvineau A Servin B Amiranoff Interaction of peptide YY with rat intestinal epithelial plasma membranes: binding of the radioiodinated peptide Endocrinology 118 1986 1910 1917
    • (1986) Endocrinology , vol.118 , pp. 1910-1917
    • Laburthe, M1    Chenut, B2    Rouyer-Fessard, C3    Tatemoto, K4    Couvineau, A5    Servin, A6    Amiranoff, B7
  • 89
    • 0024261601 scopus 로고
    • The cellular fatty acid binding proteins: aspects of structure, regulation, and function
    • N.M Bass The cellular fatty acid binding proteins: aspects of structure, regulation, and function Int. Rev. Cytol. 111 1988 143 184
    • (1988) Int. Rev. Cytol. , vol.111 , pp. 143-184
    • Bass, N.M1
  • 90
    • 0032918443 scopus 로고    scopus 로고
    • Epidermal growth factor regulates fatty acid uptake and metabolism in Caco-2 cells
    • C Darimont N Gradoux A de Pover Epidermal growth factor regulates fatty acid uptake and metabolism in Caco-2 cells Am. J. Physiol. 276 1999 G606 G612
    • (1999) Am. J. Physiol. , vol.276 , pp. G606-G612
    • Darimont, C1    Gradoux, N2    de Pover, A3
  • 91
    • 0028940934 scopus 로고
    • An amino acid substitution in the human intestinal fatty acid binding protein is associated with increased fatty acid binding, increased fat oxidation, and insulin resistance
    • L.J Baier J.C Sacchettini W.C Knowler J Eads G Paolisso P.A Tataranni H Mochizuki P.H Bennett C Bogardus M Prochazka An amino acid substitution in the human intestinal fatty acid binding protein is associated with increased fatty acid binding, increased fat oxidation, and insulin resistance J. Clin. Invest. 95 1995 1281 1287
    • (1995) J. Clin. Invest. , vol.95 , pp. 1281-1287
    • Baier, L.J1    Sacchettini, J.C2    Knowler, W.C3    Eads, J4    Paolisso, G5    Tataranni, P.A6    Mochizuki, H7    Bennett, P.H8    Bogardus, C9    Prochazka, M10
  • 92
    • 0029823857 scopus 로고    scopus 로고
    • Genetic variation of intestinal fatty acid-binding protein associated with variation in body mass in aboriginal Canadians
    • R.A Hegele S.B Harris A.J Hanley S Sadikian P.W Connelly B Zinman Genetic variation of intestinal fatty acid-binding protein associated with variation in body mass in aboriginal Canadians J. Clin. Endocrinol. Metab. 81 1996 4334 4337
    • (1996) J. Clin. Endocrinol. Metab. , vol.81 , pp. 4334-4337
    • Hegele, R.A1    Harris, S.B2    Hanley, A.J3    Sadikian, S4    Connelly, P.W5    Zinman, B6
  • 93
    • 15844387761 scopus 로고    scopus 로고
    • A polymorphism in the human intestinal fatty acid binding protein alters fatty acid transport across Caco-2 cells
    • L.J Baier C Bogardus J.C Sacchettini A polymorphism in the human intestinal fatty acid binding protein alters fatty acid transport across Caco-2 cells J. Biol. Chem. 271 1996 10892 10896
    • (1996) J. Biol. Chem. , vol.271 , pp. 10892-10896
    • Baier, L.J1    Bogardus, C2    Sacchettini, J.C3
  • 95
    • 0029993073 scopus 로고    scopus 로고
    • Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms
    • K.T Hsu J Storch Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms J. Biol. Chem. 271 1996 13317 13323
    • (1996) J. Biol. Chem. , vol.271 , pp. 13317-13323
    • Hsu, K.T1    Storch, J2
  • 96
    • 0032514695 scopus 로고    scopus 로고
    • The helical domain of intestinal fatty acid binding protein is critical for collisional transfer of fatty acids to phospholipid membranes
    • B Corsico D.P Cistola C Frieden J Storch The helical domain of intestinal fatty acid binding protein is critical for collisional transfer of fatty acids to phospholipid membranes Proc. Natl Acad. Sci. USA 95 1998 12174 12178
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12174-12178
    • Corsico, B1    Cistola, D.P2    Frieden, C3    Storch, J4
  • 97
    • 0031036243 scopus 로고    scopus 로고
    • Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: implications for the mechanism of ligand entry
    • M.E Hodsdon D.P Cistola Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: implications for the mechanism of ligand entry Biochemistry 36 1997 1450 1460
    • (1997) Biochemistry , vol.36 , pp. 1450-1460
    • Hodsdon, M.E1    Cistola, D.P2
  • 98
    • 0034717896 scopus 로고    scopus 로고
    • The fatty acid transport function of fatty acid-binding proteins
    • J Storch A.E Thumser The fatty acid transport function of fatty acid-binding proteins Biochim. Biophys. Acta 1486 2000 28 44
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 28-44
    • Storch, J1    Thumser, A.E2
  • 99
    • 0033959591 scopus 로고    scopus 로고
    • Intestinal fatty acid binding protein may favor differential apical fatty acid binding in the intestine
    • D.H Alpers N.M Bass M.J Engle K DeSchryver-Kecskemeti Intestinal fatty acid binding protein may favor differential apical fatty acid binding in the intestine Biochim. Biophys. Acta 1483 2000 352 362
    • (2000) Biochim. Biophys. Acta , vol.1483 , pp. 352-362
    • Alpers, D.H1    Bass, N.M2    Engle, M.J3    DeSchryver-Kecskemeti, K4
  • 100
    • 0003020238 scopus 로고    scopus 로고
    • Fatty acids and drugs interacting with FABP and PPAR in hepatocytes: a signaling path to the nucleus
    • C Wolfrum C.M Borrmann W.W Franke J Gorski F Spener Fatty acids and drugs interacting with FABP and PPAR in hepatocytes: a signaling path to the nucleus Chem. Phys. Lipids 101 1999 149
    • (1999) Chem. Phys. Lipids , vol.101 , pp. 149
    • Wolfrum, C1    Borrmann, C.M2    Franke, W.W3    Gorski, J4    Spener, F5
  • 101
    • 0033815312 scopus 로고    scopus 로고
    • The intestinal fatty acid binding protein is not essential for dietary fat absorption in mice
    • G Vassileva L Huwyler K Poirier L.B Agellon M.J Toth The intestinal fatty acid binding protein is not essential for dietary fat absorption in mice Faseb J. 14 2000 2040 2046
    • (2000) Faseb J. , vol.14 , pp. 2040-2046
    • Vassileva, G1    Huwyler, L2    Poirier, K3    Agellon, L.B4    Toth, M.J5
  • 102
    • 85112950668 scopus 로고    scopus 로고
    • Decreased liver fatty acid binding capacity and altered liver lipid distribution in mice lacking the liver fatty acid binding protein (L-FABP) gene
    • G.G Martin H Danneberg L.S Kumar B.P Atshaves E Erol M Bader F Schroeder B Binas Decreased liver fatty acid binding capacity and altered liver lipid distribution in mice lacking the liver fatty acid binding protein (L-FABP) gene J. Biol. Chem. 1 2003 1
    • (2003) J. Biol. Chem. , vol.1 , pp. 1
    • Martin, G.G1    Danneberg, H2    Kumar, L.S3    Atshaves, B.P4    Erol, E5    Bader, M6    Schroeder, F7    Binas, B8
  • 103
    • 0033960380 scopus 로고    scopus 로고
    • Role of acyl-CoA binding protein in acyl-CoA metabolism and acyl-CoA-mediated cell signaling
    • J Knudsen T.B Neergaard B Gaigg M.V Jensen J.K Hansen Role of acyl-CoA binding protein in acyl-CoA metabolism and acyl-CoA-mediated cell signaling J. Nutr. 130 2000 294S 298S
    • (2000) J. Nutr. , vol.130 , pp. 294S-298S
    • Knudsen, J1    Neergaard, T.B2    Gaigg, B3    Jensen, M.V4    Hansen, J.K5
  • 105
    • 0027289149 scopus 로고
    • Three-dimensional structure of the complex between acyl-coenzyme A binding protein and palmitoyl-coenzyme A
    • B.B Kragelund K.V Andersen J.C Madsen J Knudsen F.M Poulsen Three-dimensional structure of the complex between acyl-coenzyme A binding protein and palmitoyl-coenzyme A J. Mol. Biol. 230 1993 1260 1277
    • (1993) J. Mol. Biol. , vol.230 , pp. 1260-1277
    • Kragelund, B.B1    Andersen, K.V2    Madsen, J.C3    Knudsen, J4    Poulsen, F.M5
  • 107
    • 0032079544 scopus 로고    scopus 로고
    • Acyl coenzyme A binding protein. Conformational sensitivity to long chain fatty acyl-CoA
    • A Frolov F Schroeder Acyl coenzyme A binding protein. Conformational sensitivity to long chain fatty acyl-CoA J. Biol. Chem. 273 1998 11049 11055
    • (1998) J. Biol. Chem. , vol.273 , pp. 11049-11055
    • Frolov, A1    Schroeder, F2
  • 108
    • 0027534461 scopus 로고
    • Characterization of ligand binding to acyl-CoA-binding protein
    • J Rosendal P Ertbjerg J Knudsen Characterization of ligand binding to acyl-CoA-binding protein Biochem. J. 290 1993 321 326
    • (1993) Biochem. J. , vol.290 , pp. 321-326
    • Rosendal, J1    Ertbjerg, P2    Knudsen, J3
  • 109
    • 0035193124 scopus 로고    scopus 로고
    • Cellular localization of the diazepam binding inhibitor (DBI) in the gastrointestinal tract of mice and its coexistence with the fatty acid binding protein (FABP)
    • H Yanase H Shimizu T Kanda H Fujii T Iwanaga Cellular localization of the diazepam binding inhibitor (DBI) in the gastrointestinal tract of mice and its coexistence with the fatty acid binding protein (FABP) Arch. Histol. Cytol. 64 2001 449 460
    • (2001) Arch. Histol. Cytol. , vol.64 , pp. 449-460
    • Yanase, H1    Shimizu, H2    Kanda, T3    Fujii, H4    Iwanaga, T5
  • 111
    • 0033729385 scopus 로고    scopus 로고
    • Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm
    • T Helledie M Antonius R.V Sorensen A.V Hertzel D.A Bernlohr S Kolvraa K Kristiansen S Mandrup Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm J. Lipid Res. 41 2000 1740 1751
    • (2000) J. Lipid Res. , vol.41 , pp. 1740-1751
    • Helledie, T1    Antonius, M2    Sorensen, R.V3    Hertzel, A.V4    Bernlohr, D.A5    Kolvraa, S6    Kristiansen, K7    Mandrup, S8
  • 112
    • 0035168901 scopus 로고    scopus 로고
    • A new concept of cellular uptake and intracellular trafficking of long-chain fatty acids
    • W Stremmel L Pohl A Ring T Herrmann A new concept of cellular uptake and intracellular trafficking of long-chain fatty acids Lipids 36 2001 981 989
    • (2001) Lipids , vol.36 , pp. 981-989
    • Stremmel, W1    Pohl, L2    Ring, A3    Herrmann, T4
  • 113
    • 0034988023 scopus 로고    scopus 로고
    • Unravelling the significance of cellular fatty acid-binding proteins
    • J.F Glatz J Storch Unravelling the significance of cellular fatty acid-binding proteins Curr. Opin. Lipidol. 12 2001 267 274
    • (2001) Curr. Opin. Lipidol. , vol.12 , pp. 267-274
    • Glatz, J.F1    Storch, J2
  • 114
    • 0036737860 scopus 로고    scopus 로고
    • Uptake of long-chain fatty acids in HepG2 cells involves caveolae: analysis of a novel pathway
    • J Pohl A Ring W Stremmel Uptake of long-chain fatty acids in HepG2 cells involves caveolae: analysis of a novel pathway J. Lipid Res. 43 2002 1390 1399
    • (2002) J. Lipid Res. , vol.43 , pp. 1390-1399
    • Pohl, J1    Ring, A2    Stremmel, W3
  • 115
    • 0036915381 scopus 로고    scopus 로고
    • Evidence for vesicles that mediate long-chain fatty acid uptake by human microvascular endothelial cells
    • A Ring J Pohl A Volkl W Stremmel Evidence for vesicles that mediate long-chain fatty acid uptake by human microvascular endothelial cells J. Lipid Res. 43 2002 2095 2104
    • (2002) J. Lipid Res. , vol.43 , pp. 2095-2104
    • Ring, A1    Pohl, J2    Volkl, A3    Stremmel, W4
  • 117
    • 0029155535 scopus 로고
    • Ventromedial hypothalamic lesions induce the proliferation of gastrointestinal mucosal cells in the rat
    • T Kiba K Tanaka M Hoshino K Numata K Okano S Inoue Ventromedial hypothalamic lesions induce the proliferation of gastrointestinal mucosal cells in the rat Life Sci. 57 1995 827 832
    • (1995) Life Sci. , vol.57 , pp. 827-832
    • Kiba, T1    Tanaka, K2    Hoshino, M3    Numata, K4    Okano, K5    Inoue, S6
  • 120
    • 0035940435 scopus 로고    scopus 로고
    • Modulation of specific intestinal epithelial progenitors by enteric neurons
    • M Bjerknes H Cheng Modulation of specific intestinal epithelial progenitors by enteric neurons Proc. Natl Acad. Sci. USA 98 2001 12497 12502
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12497-12502
    • Bjerknes, M1    Cheng, H2


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