메뉴 건너뛰기




Volumn 38, Issue 4, 2006, Pages 269-278

The retinol-binding protein system: A potential paradigm for steroid-binding globulins?

Author keywords

Conformations; Lipocalin; Receptor; Transport; Vitamin A

Indexed keywords

GLOBULIN; LIPOCALIN; MEMBRANE RECEPTOR; RETINOL; RETINOL BINDING PROTEIN; STEROID BINDING PROTEIN;

EID: 33744932944     PISSN: 00185043     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2006-925349     Document Type: Review
Times cited : (12)

References (92)
  • 1
    • 0346218154 scopus 로고    scopus 로고
    • Proteins of multiple classes may participate in nongenomic steroid actions
    • Watson CS, Gametchu B. Proteins of multiple classes may participate in nongenomic steroid actions. Exp Biol Med (Maywood) 2003; 228(11): 1272-1281
    • (2003) Exp Biol Med (Maywood) , vol.228 , Issue.11 , pp. 1272-1281
    • Watson, C.S.1    Gametchu, B.2
  • 2
    • 0034039993 scopus 로고    scopus 로고
    • Ligand-binding proteins: Their potential for application in systems for controlled delivery and uptake of ligands
    • de Wolf FA, Brett GM. Ligand-binding proteins: their potential for application in systems for controlled delivery and uptake of ligands. Pharmacol Rev 2000; 52(2): 207-236
    • (2000) Pharmacol Rev , vol.52 , Issue.2 , pp. 207-236
    • De Wolf, F.A.1    Brett, G.M.2
  • 3
    • 0035001384 scopus 로고    scopus 로고
    • Studies of vitamin A metabolism in mouse model systems
    • Gottesman ME, Quadro L, Blaner WS. Studies of vitamin A metabolism in mouse model systems. Bioessays 2001; 23(5): 409-419
    • (2001) Bioessays , vol.23 , Issue.5 , pp. 409-419
    • Gottesman, M.E.1    Quadro, L.2    Blaner, W.S.3
  • 4
    • 0025332589 scopus 로고
    • Interactions of retinol with binding proteins: Implications for the mechanism of uptake by cells
    • Noy N, Xu ZJ. Interactions of retinol with binding proteins: implications for the mechanism of uptake by cells. Biochemistry 1990; 29(16): 3878-3883
    • (1990) Biochemistry , vol.29 , Issue.16 , pp. 3878-3883
    • Noy, N.1    Xu, Z.J.2
  • 5
    • 0023742644 scopus 로고
    • The interaction of retinol-binding protein with its plasma-membrane receptor
    • Sivaprasadarao A, Findlay JB. The interaction of retinol-binding protein with its plasma-membrane receptor. Biochem J 1988; 255(2): 561-569
    • (1988) Biochem J , vol.255 , Issue.2 , pp. 561-569
    • Sivaprasadarao, A.1    Findlay, J.B.2
  • 6
    • 0023791217 scopus 로고
    • The mechanism of uptake of retinol by plasma-membrane vesicles
    • Sivaprasadarao A, Findlay JB. The mechanism of uptake of retinol by plasma-membrane vesicles. Biochem J 1988; 255(2): 571-579
    • (1988) Biochem J , vol.255 , Issue.2 , pp. 571-579
    • Sivaprasadarao, A.1    Findlay, J.B.2
  • 7
    • 0024843640 scopus 로고
    • Characteristics of retinol accumulation from serum retinol-binding protein by cultured Sertoli cells
    • Shingleton JL, Skinner MK, Ong DE. Characteristics of retinol accumulation from serum retinol-binding protein by cultured Sertoli cells. Biochemistry 1989; 28: 9641-9647
    • (1989) Biochemistry , vol.28 , pp. 9641-9647
    • Shingleton, J.L.1    Skinner, M.K.2    Ong, D.E.3
  • 9
    • 0028814427 scopus 로고
    • Retinol processing by the peritubular cell from rat testis
    • Davis JT, Ong DE. Retinol processing by the peritubular cell from rat testis. Biol Reprod 1995; 52: 356-364
    • (1995) Biol Reprod , vol.52 , pp. 356-364
    • Davis, J.T.1    Ong, D.E.2
  • 10
    • 0022445338 scopus 로고
    • Membrane receptors for retinol-binding protein in cultured human retinal pigment epithelium
    • Pfeffer BA, Clark VM, Flannery JG, Bok D. Membrane receptors for retinol-binding protein in cultured human retinal pigment epithelium. Invest. Ophthalmol Vis Sci 1986; 27: 1031-1040
    • (1986) Invest Ophthalmol Vis Sci , vol.27 , pp. 1031-1040
    • Pfeffer, B.A.1    Clark, V.M.2    Flannery, J.G.3    Bok, D.4
  • 11
    • 0025808061 scopus 로고
    • Identification and partial characterization of a retinal pigment epithelial membrane receptor for plasma retinol-binding protein
    • Bavik CO, Eriksson U, Allen RA, Peterson PA. Identification and partial characterization of a retinal pigment epithelial membrane receptor for plasma retinol-binding protein. J Biol Chem 1991; 266: 14978-14985
    • (1991) J Biol Chem , vol.266 , pp. 14978-14985
    • Bavik, C.O.1    Eriksson, U.2    Allen, R.A.3    Peterson, P.A.4
  • 12
    • 0022649579 scopus 로고
    • Increased levels of several retinoid binding proteins resulting from retinoic acid-induced differentiation of F9 cells
    • Eriksson U, Hansson E, Nilsson M, Jonsson KH, Sundelin J, Peterson PA. Increased levels of several retinoid binding proteins resulting from retinoic acid-induced differentiation of F9 cells. Cancer Res 1986; 46: 717-722
    • (1986) Cancer Res , vol.46 , pp. 717-722
    • Eriksson, U.1    Hansson, E.2    Nilsson, M.3    Jonsson, K.H.4    Sundelin, J.5    Peterson, P.A.6
  • 13
    • 0025283517 scopus 로고
    • Localization of cellular retinol-binding protein and retinol-binding protein in cells comprising the blood-brain barrier of rat and human
    • MacDonald PN, Bok D, Ong DE. 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 USA, 1990; 87: 4265-4269
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4265-4269
    • MacDonald, P.N.1    Bok, D.2    Ong, D.E.3
  • 14
    • 0033020144 scopus 로고    scopus 로고
    • Sex hormone-binding globulin receptor signal transduction proceeds via a G protein
    • Nakhla AM, Leonard J, Hryb DJ, Rosner W. Sex hormone-binding globulin receptor signal transduction proceeds via a G protein. Steroids 1999; 64: 213-216
    • (1999) Steroids , vol.64 , pp. 213-216
    • Nakhla, A.M.1    Leonard, J.2    Hryb, D.J.3    Rosner, W.4
  • 15
    • 0027420812 scopus 로고
    • Corticosteroid-binding globulin receptor of the rat hepatic membrane: Solubilization, partial characterization, and the effect of steroids on binding
    • Maitra US, Khan MS, Rosner W. Corticosteroid-binding globulin receptor of the rat hepatic membrane: solubilization, partial characterization, and the effect of steroids on binding. Endocrinol 1993; 133: 1817-1822
    • (1993) Endocrinol , vol.133 , pp. 1817-1822
    • Maitra, U.S.1    Khan, M.S.2    Rosner, W.3
  • 17
    • 0018113393 scopus 로고
    • Transport of retinol to ocular tissues. An overview
    • Heller J. Transport of retinol to ocular tissues. An overview. World Rev Nutr Diet 1978; 31: 42-44
    • (1978) World Rev Nutr Diet , vol.31 , pp. 42-44
    • Heller, J.1
  • 18
    • 0015523573 scopus 로고
    • The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, β-lactoglobulin, and the retinol-binding protein of human plasma
    • Futterman S, Heller J. The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, β-lactoglobulin, and the retinol-binding protein of human plasma. J Biol Chem 1972; 247(16): 5168-5172
    • (1972) J Biol Chem , vol.247 , Issue.16 , pp. 5168-5172
    • Futterman, S.1    Heller, J.2
  • 19
    • 0015898684 scopus 로고
    • Interactions of all-trans, 9-, 11-, and 13-cis-retinal, all-trans-retinyl acetate, and retinoic acid with human retinol-binding protein and prealbumin
    • Horwitz J, Heller J. Interactions of all-trans, 9-, 11-, and 13-cis-retinal, all-trans-retinyl acetate, and retinoic acid with human retinol-binding protein and prealbumin. J Biol Chem 1973; 248(18): 6317-6324
    • (1973) J Biol Chem , vol.248 , Issue.18 , pp. 6317-6324
    • Horwitz, J.1    Heller, J.2
  • 20
    • 0015910083 scopus 로고
    • Conformational changes following interaction between retinol isomers and human retinol-binding protein and between the retinol-binding protein and prealbumin
    • Heller J, Horwitz J. Conformational changes following interaction between retinol isomers and human retinol-binding protein and between the retinol-binding protein and prealbumin. J Biol Chem 1973; 248(18): 6308-6316
    • (1973) J Biol Chem , vol.248 , Issue.18 , pp. 6308-6316
    • Heller, J.1    Horwitz, J.2
  • 21
    • 0016215175 scopus 로고
    • The binding stoichiometry of human plasma retinol-binding protein to prealbumin
    • Heller J, Horwitz J. The binding stoichiometry of human plasma retinol-binding protein to prealbumin. J Biol Chem 1974; 249(18): 5933-5938
    • (1974) J Biol Chem , vol.249 , Issue.18 , pp. 5933-5938
    • Heller, J.1    Horwitz, J.2
  • 22
    • 0015968674 scopus 로고
    • Interactions of retinol-binding protein with various chromophores and with thyroxine-binding protein. A model for visual pigments
    • Heller J, Horwitz J. Interactions of retinol-binding protein with various chromophores and with thyroxine-binding protein. A model for visual pigments. Exp Eye Res 1974; 18(1): 41-49
    • (1974) Exp Eye Res , vol.18 , Issue.1 , pp. 41-49
    • Heller, J.1    Horwitz, J.2
  • 23
    • 0017112585 scopus 로고
    • Transport of retinol from the blood to the retina: An autoradiographic study of the pigment epithelial cell surface receptor for plasma retinol-binding protein
    • Bok D, Heller J. Transport of retinol from the blood to the retina: an autoradiographic study of the pigment epithelial cell surface receptor for plasma retinol-binding protein. Exp Eye Res 1976; 22(5): 395-402
    • (1976) Exp Eye Res , vol.22 , Issue.5 , pp. 395-402
    • Bok, D.1    Heller, J.2
  • 24
    • 0017755714 scopus 로고
    • Uptake of retinol and retinoic acid from serum retinol-binding protein by retinal pigment epithelial cells
    • Chen CC, Heller J. Uptake of retinol and retinoic acid from serum retinol-binding protein by retinal pigment epithelial cells. J Biol Chem 1977; 252(15): 5216-5221
    • (1977) J Biol Chem , vol.252 , Issue.15 , pp. 5216-5221
    • Chen, C.C.1    Heller, J.2
  • 25
    • 0028265730 scopus 로고
    • Cellular transport, and metabolism of vitamin A: Role of the cellular retinoid-binding proteins
    • Ong DE. Cellular transport, and metabolism of vitamin A: role of the cellular retinoid-binding proteins. Nutr Rev 1994; 52: 24-31
    • (1994) Nutr Rev , vol.52 , pp. 24-31
    • Ong, D.E.1
  • 26
    • 0018230424 scopus 로고
    • Short-term effect of zinc sulfate on plasma and hepatic concentrations of vitamins A and E in normal weanling rats
    • Ette SI, Basu TK, Dickerson JWT. Short-term effect of zinc sulfate on plasma and hepatic concentrations of vitamins A and E in normal weanling rats. Nutr Metab 1979; 23: 11-16
    • (1979) Nutr Metab , vol.23 , pp. 11-16
    • Ette, S.I.1    Basu, T.K.2    Dickerson, J.W.T.3
  • 27
    • 0029867614 scopus 로고    scopus 로고
    • Benefits and liabilities of vitamin A and carotenoids
    • Olson JA. Benefits and liabilities of vitamin A and carotenoids. J Nutr 1996; 126(4 Suppl): 1208-1212
    • (1996) J Nutr , vol.126 , Issue.4 SUPPL. , pp. 1208-1212
    • Olson, J.A.1
  • 28
    • 0042368953 scopus 로고    scopus 로고
    • Vitamin A and the regulation of fat reserves
    • Bonet ML, Ribot J, Felipe F, Palou A. Vitamin A and the regulation of fat reserves. Cell Mol Life Sci 2003; 60(7): 1311-1321
    • (2003) Cell Mol Life Sci , vol.60 , Issue.7 , pp. 1311-1321
    • Bonet, M.L.1    Ribot, J.2    Felipe, F.3    Palou, A.4
  • 30
    • 23944481843 scopus 로고    scopus 로고
    • Mechanisms of digestion and absorption of dietary vitamin A
    • Harrison EH. Mechanisms of digestion and absorption of dietary vitamin A. Annu Rev Nutr 2005; 25: 7-103
    • (2005) Annu Rev Nutr , vol.25 , pp. 7-103
    • Harrison, E.H.1
  • 31
  • 32
    • 0002801434 scopus 로고
    • Overview of vitamin A: Metabolism and function
    • Blomhoff, R. (ed.). New York: Marcel Dekker
    • Blomhoff R. Overview of vitamin A: metabolism and function. In: Blomhoff, R. (ed.). Vitamin A in health and disease. New York: Marcel Dekker, 1994: 1-35
    • (1994) Vitamin A in Health and Disease , pp. 1-35
    • Blomhoff, R.1
  • 33
    • 0002422384 scopus 로고
    • Plasma retinol-binding protein
    • Sporn, MB, Roberts, AB Goodman, DS (eds.). New York: Academic Press
    • Goodman DS. Plasma retinol-binding protein. In: Sporn, MB, Roberts, AB Goodman, DS (eds.). The Retinoids, vol. 2. 1984 New York: Academic Press: 41-88
    • (1984) The Retinoids , vol.2 , pp. 41-88
    • Goodman, D.S.1
  • 34
    • 0027998527 scopus 로고
    • Transthyretin (prealbumin) in health and disease: Nutritional implications
    • Ingenbleek Y, Young V. Transthyretin (prealbumin) in health and disease: Nutritional implications. Annual Review of Nutrition 1994; 14: 495-533
    • (1994) Annual Review of Nutrition , vol.14 , pp. 495-533
    • Ingenbleek, Y.1    Young, V.2
  • 35
    • 0030022473 scopus 로고    scopus 로고
    • Retinol-binding protein and transthyretin are secreted as a complex formed in the endoplasmic reticulum in HepG2 human hepatocarcinoma cells
    • Bellovino D, Morimoto T, Tosetti F, Gaetani S. Retinol-binding protein and transthyretin are secreted as a complex formed in the endoplasmic reticulum in HepG2 human hepatocarcinoma cells. Exp Cell Res 1996; 222: 77-83
    • (1996) Exp Cell Res , vol.222 , pp. 77-83
    • Bellovino, D.1    Morimoto, T.2    Tosetti, F.3    Gaetani, S.4
  • 36
    • 0025937134 scopus 로고
    • Retinol-binding protein and transthyretin expressed in Hela cells form a complex in the endoplasmic reticulum both in the absence and in the presence of retinol
    • Mehlus H, Nilsson T, Peterson PA, Rask L. Retinol-binding protein and transthyretin expressed in Hela cells form a complex in the endoplasmic reticulum both in the absence and in the presence of retinol. Exp Cell Res 1991; 197: 119-124
    • (1991) Exp Cell Res , vol.197 , pp. 119-124
    • Mehlus, H.1    Nilsson, T.2    Peterson, P.A.3    Rask, L.4
  • 37
    • 0034684228 scopus 로고    scopus 로고
    • Plasma retinol binding protein: Structure and function of the prototypic lipocalin
    • Newcomer ME, Ong DE. Plasma retinol binding protein: structure and function of the prototypic lipocalin. Biochim Biophys Acta 2000; 1482(1-2): 57-64
    • (2000) Biochim Biophys Acta , vol.1482 , Issue.1-2 , pp. 57-64
    • Newcomer, M.E.1    Ong, D.E.2
  • 38
    • 0032488909 scopus 로고    scopus 로고
    • The transfer of retinol from serum retinol-binding protein to cellular retinol-binding protein is mediated by a membrane receptor
    • Sundaram M, Sivaprasadarao A, DeSousa MM, Findlay JB. The transfer of retinol from serum retinol-binding protein to cellular retinol-binding protein is mediated by a membrane receptor. J Biol Chem 1998; 273: 3336-3342
    • (1998) J Biol Chem , vol.273 , pp. 3336-3342
    • Sundaram, M.1    Sivaprasadarao, A.2    Desousa, M.M.3    Findlay, J.B.4
  • 39
    • 0027960222 scopus 로고
    • Crystallographic studies on complexes between retinoids and plasma retinol-binding protein
    • Zanotti G, Marcello M, Malpeli G, Folli C, Sartori G, Berni R. Crystallographic studies on complexes between retinoids and plasma retinol-binding protein. J Biol Chem 1994; 269(47): 29613-29620
    • (1994) J Biol Chem , vol.269 , Issue.47 , pp. 29613-29620
    • Zanotti, G.1    Marcello, M.2    Malpeli, G.3    Folli, C.4    Sartori, G.5    Berni, R.6
  • 41
    • 33744933058 scopus 로고    scopus 로고
    • Functions and actions of retinoids and carotenoids: Building the vision of James Allen Olson
    • Tanumihardjo SA. Functions and actions of retinoids and carotenoids: building the vision of James Allen Olson. Am Soc Nutr Sci 2004; 290S-293S
    • (2004) Am Soc Nutr Sci
    • Tanumihardjo, S.A.1
  • 42
    • 0023138328 scopus 로고
    • Studies on the metabolism of retinol-binding protein by primary hepatocytes from retinol-deficient rats
    • Dixon JL, DS Goodman. Studies on the metabolism of retinol-binding protein by primary hepatocytes from retinol-deficient rats. J Cell Physiol 1987; 130: 14-20
    • (1987) J Cell Physiol , vol.130 , pp. 14-20
    • Dixon, J.L.1    Goodman, D.S.2
  • 43
    • 0025973306 scopus 로고
    • Vitamin A intake and in vivo expression of the genes involved in retinol transport
    • Perozzi G, Mengheri E, Colantuoni V, Gaetani S. Vitamin A intake and in vivo expression of the genes involved in retinol transport. Eur J Biochem 1991; 196: 211-217
    • (1991) Eur J Biochem , vol.196 , pp. 211-217
    • Perozzi, G.1    Mengheri, E.2    Colantuoni, V.3    Gaetani, S.4
  • 44
    • 0031928779 scopus 로고    scopus 로고
    • Interactions between zinc and vitamin A: An update
    • Christian P, West KP Jr. Interactions between zinc and vitamin A: an update. Am J Clin Nutr 1998; 68: 435S-441S
    • (1998) Am J Clin Nutr , vol.68
    • Christian, P.1    West Jr., K.P.2
  • 45
    • 0014336534 scopus 로고
    • Retinol binding protein: The transport protein for vitamin A in human plasma
    • Kanai M, Raz A, Goodman D. Retinol binding protein: the transport protein for vitamin A in human plasma. J Clin Invest 1968; 47: 2025-2044
    • (1968) J Clin Invest , vol.47 , pp. 2025-2044
    • Kanai, M.1    Raz, A.2    Goodman, D.3
  • 46
    • 0034684228 scopus 로고    scopus 로고
    • Plasma retinol binding protein: Structure and function of the prototypic lipocalin
    • Newcomer ME, Ong DE. Plasma retinol binding protein: structure and function of the prototypic lipocalin. Biochim Biophys Acta 2000; 1482(1-2): 57-64
    • (2000) Biochim Biophys Acta , vol.1482 , Issue.1-2 , pp. 57-64
    • Newcomer, M.E.1    Ong, D.E.2
  • 49
    • 0025286532 scopus 로고
    • Crystallographic refinement of human serum retinol binding protein at 2A resolution
    • Cowan SW, Newcomer ME, Jones TA. Crystallographic refinement of human serum retinol binding protein at 2A resolution. Proteins 1990; 8(1): 44-61
    • (1990) Proteins , vol.8 , Issue.1 , pp. 44-61
    • Cowan, S.W.1    Newcomer, M.E.2    Jones, T.A.3
  • 50
    • 0027176956 scopus 로고
    • Crystal structure of the trigonal form of human plasma retinol-binding protein at 2.5 A resolution
    • Zanotti G, Ottonello S, Berni R, Monaco HL. Crystal structure of the trigonal form of human plasma retinol-binding protein at 2.5 A resolution. J Mol Biol 1993; 230(2): 613-624
    • (1993) J Mol Biol , vol.230 , Issue.2 , pp. 613-624
    • Zanotti, G.1    Ottonello, S.2    Berni, R.3    Monaco, H.L.4
  • 51
    • 0027302351 scopus 로고
    • Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding protein
    • Zanotti G, Berni R, Monaco HL. Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding protein. J Biol Chem 1993; 268(15): 10728-10738
    • (1993) J Biol Chem , vol.268 , Issue.15 , pp. 10728-10738
    • Zanotti, G.1    Berni, R.2    Monaco, H.L.3
  • 54
    • 0026468669 scopus 로고
    • Interactions of retinol with binding proteins: Studies with retinol-binding protein and with transthyretin
    • Noy N, Slosberg E, Scarlata S. Interactions of retinol with binding proteins: studies with retinol-binding protein and with transthyretin. Biochemistry 1992; 31(45): 11118-1124
    • (1992) Biochemistry , vol.31 , Issue.45 , pp. 11118-11124
    • Noy, N.1    Slosberg, E.2    Scarlata, S.3
  • 55
    • 0028340147 scopus 로고
    • Structure-function studies on human retinol-binding protein using site-directed mutagenesis
    • Sivaprasadarao A, Findlay JB. Structure-function studies on human retinol-binding protein using site-directed mutagenesis. Biochem J 1994; 300: 437-442
    • (1994) Biochem J , vol.300 , pp. 437-442
    • Sivaprasadarao, A.1    Findlay, J.B.2
  • 56
    • 0028937744 scopus 로고
    • Retinoid-binding proteins: Structural determinants important for function
    • Newcomer ME. Retinoid-binding proteins: structural determinants important for function. FASEB J 1995; 9(2): 229-239
    • (1995) FASEB J , vol.9 , Issue.2 , pp. 229-239
    • Newcomer, M.E.1
  • 57
    • 0034684193 scopus 로고    scopus 로고
    • The transthyretin-retinol-binding protein complex
    • Monaco HL. The transthyretin-retinol-binding protein complex. Biochim Biophys Acta 2000; 1482(1-2): 65-72
    • (2000) Biochim Biophys Acta , vol.1482 , Issue.1-2 , pp. 65-72
    • Monaco, H.L.1
  • 58
    • 0017671806 scopus 로고
    • Vitamin A transport in plasma of the non-mammalian vertebrates: Isolation and partial characterisation of piscine retinol-binding-protein
    • Shidoji Y, Muto Y. Vitamin A transport in plasma of the non-mammalian vertebrates: isolation and partial characterisation of piscine retinol-binding-protein. Journal of Lipid Research 1977; 18: 679-691
    • (1977) Journal of Lipid Research , vol.18 , pp. 679-691
    • Shidoji, Y.1    Muto, Y.2
  • 60
    • 0027291523 scopus 로고
    • Specific uptake of retinol-binding protein by variant F9 cell lines
    • Matarese V, Lodish HF. Specific uptake of retinol-binding protein by variant F9 cell lines. J Biol Chem 1993; 268(25): 18859-18865
    • (1993) J Biol Chem , vol.268 , Issue.25 , pp. 18859-18865
    • Matarese, V.1    Lodish, H.F.2
  • 61
    • 0026446319 scopus 로고
    • Characterization of a plasma retinol-binding protein membrane receptor expressed in the retinal pigment epithelium
    • Bavik CO, Busch C, Eriksson U. Characterization of a plasma retinol-binding protein membrane receptor expressed in the retinal pigment epithelium. J Biol Chem 1992; 267(32): 23035-23042
    • (1992) J Biol Chem , vol.267 , Issue.32 , pp. 23035-23042
    • Bavik, C.O.1    Busch, C.2    Eriksson, U.3
  • 62
    • 0028169327 scopus 로고
    • Solubilization and purification of the retinol-binding protein receptor from human placental membranes
    • Sivaprasadarao A, Boudjelal M, Findlay JB. Solubilization and purification of the retinol-binding protein receptor from human placental membranes. Biochem J 1994; 302(Pt 1): 245-251
    • (1994) Biochem J , vol.302 , Issue.PART 1 , pp. 245-251
    • Sivaprasadarao, A.1    Boudjelal, M.2    Findlay, J.B.3
  • 63
    • 0036499714 scopus 로고    scopus 로고
    • The transfer of transthyretin and receptor-binding properties from the plasma retinol-binding protein to the epididymal retinoic acid-binding protein
    • Sundaram M, van Aalten DM, Findlay JB, Sivaprasadarao A. The transfer of transthyretin and receptor-binding properties from the plasma retinol-binding protein to the epididymal retinoic acid-binding protein. Biochem J 2002; 362(Pt 2): 265-271
    • (2002) Biochem J , vol.362 , Issue.PART 2 , pp. 265-271
    • Sundaram, M.1    Van Aalten, D.M.2    Findlay, J.B.3    Sivaprasadarao, A.4
  • 64
    • 21244434810 scopus 로고    scopus 로고
    • Cellular retinol-binding protein type III is needed for retinoid incorporation into milk
    • Piantedosi R, Ghyselinck N, Blaner WS, Vogel S. Cellular retinol-binding protein type III is needed for retinoid incorporation into milk. J Biol Chem 2005; 280(25): 24286-24292
    • (2005) J Biol Chem , vol.280 , Issue.25 , pp. 24286-24292
    • Piantedosi, R.1    Ghyselinck, N.2    Blaner, W.S.3    Vogel, S.4
  • 65
    • 0036829910 scopus 로고    scopus 로고
    • Ligand binding and structural analysis of a human putative cellular retinol-binding protein
    • Folli C, Calderone V, Ramazzina I, Zanotti G, Berni R. Ligand binding and structural analysis of a human putative cellular retinol-binding protein. J Biol Chem 2002; 277(44): 41970-41977
    • (2002) J Biol Chem , vol.277 , Issue.44 , pp. 41970-41977
    • Folli, C.1    Calderone, V.2    Ramazzina, I.3    Zanotti, G.4    Berni, R.5
  • 66
    • 17544369553 scopus 로고    scopus 로고
    • Contribution of cellular retinol-binding protein type 1 to retinol metabolism during mouse development
    • Matt N, Schmidt CK, Dupe V, Dennefeld C, Nau H, Chambon P, Mark M, Ghyselinck NB. Contribution of cellular retinol-binding protein type 1 to retinol metabolism during mouse development. Dev Dyn 2005; 233(1): 167-176
    • (2005) Dev Dyn , vol.233 , Issue.1 , pp. 167-176
    • Matt, N.1    Schmidt, C.K.2    Dupe, V.3    Dennefeld, C.4    Nau, H.5    Chambon, P.6    Mark, M.7    Ghyselinck, N.B.8
  • 67
    • 0034660094 scopus 로고    scopus 로고
    • Retinoid-binding proteins: Mediators of retinoid action
    • Noy N. Retinoid-binding proteins: mediators of retinoid action. Biochem J 2000; 348 (Pt 3): 481-495
    • (2000) Biochem J , vol.348 , Issue.PART 3 , pp. 481-495
    • Noy, N.1
  • 69
    • 0027310780 scopus 로고
    • Crystallographic studies on a family of cellular lipophilic transport proteins. Refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans-retinol
    • Cowan SW, Newcomer ME, Jones TA. Crystallographic studies on a family of cellular lipophilic transport proteins. Refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans-retinol. J Mol Biol 1993; 230(4): 1225-1246
    • (1993) J Mol Biol , vol.230 , Issue.4 , pp. 1225-1246
    • Cowan, S.W.1    Newcomer, M.E.2    Jones, T.A.3
  • 70
    • 0026720053 scopus 로고
    • Regulation of plasma retinol binding protein secretion in human HepG2 cells
    • Tosetti F, Ferrari N, Pfeffer U, Brigati C, Vidali G. Regulation of plasma retinol binding protein secretion in human HepG2 cells. Exp Cell Res 1992; 200: 467-472
    • (1992) Exp Cell Res , vol.200 , pp. 467-472
    • Tosetti, F.1    Ferrari, N.2    Pfeffer, U.3    Brigati, C.4    Vidali, G.5
  • 74
    • 0142216385 scopus 로고    scopus 로고
    • Understanding the physiological role of retinol-binding protein in vitamin A metabolism using transgenic and knockout mouse models
    • Quadro L, Hamberger L, Colantuoni V, Gottesman ME, Blaner WS. Understanding the physiological role of retinol-binding protein in vitamin A metabolism using transgenic and knockout mouse models. Mol Aspects Med 2003; 24(6): 421-430
    • (2003) Mol Aspects Med , vol.24 , Issue.6 , pp. 421-430
    • Quadro, L.1    Hamberger, L.2    Colantuoni, V.3    Gottesman, M.E.4    Blaner, W.S.5
  • 76
    • 24944582909 scopus 로고    scopus 로고
    • Pathways of vitamin A delivery to the embryo: Insights from a new tunable model of embryonic vitamin A deficiency
    • Quadro L, Hamberger L, Gottesman ME, Wang F, Colantuoni V, Blaner WS, Mendelsohn CL. Pathways of vitamin A delivery to the embryo: insights from a new tunable model of embryonic vitamin A deficiency. Endocrinology 2005; 146(10): 4479-4490
    • (2005) Endocrinology , vol.146 , Issue.10 , pp. 4479-4490
    • Quadro, L.1    Hamberger, L.2    Gottesman, M.E.3    Wang, F.4    Colantuoni, V.5    Blaner, W.S.6    Mendelsohn, C.L.7
  • 77
    • 0035827544 scopus 로고    scopus 로고
    • Molecular cloning of a novel lipocalin-1 interacting human cell membrane receptor using phage display
    • Wojnar P, Lechner M, Merschak P, Redl B. Molecular cloning of a novel lipocalin-1 interacting human cell membrane receptor using phage display. J Biol Chem 2001; 276(23): 20206-20212
    • (2001) J Biol Chem , vol.276 , Issue.23 , pp. 20206-20212
    • Wojnar, P.1    Lechner, M.2    Merschak, P.3    Redl, B.4
  • 78
    • 0038521291 scopus 로고    scopus 로고
    • Antisense down-regulation of lipocalin-interacting membrane receptor expression inhibits cellular internalization of lipocalin-1 in human NT2 cells
    • Wojnar P, Lechner M, Redl B. Antisense down-regulation of lipocalin-interacting membrane receptor expression inhibits cellular internalization of lipocalin-1 in human NT2 cells. J Biol Chem 2003; 278(18): 16209-16215
    • (2003) J Biol Chem , vol.278 , Issue.18 , pp. 16209-16215
    • Wojnar, P.1    Lechner, M.2    Redl, B.3
  • 79
    • 0026726499 scopus 로고
    • cDNA cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein superfamily
    • Redl B, Holzfeind P, Lottspeich F. cDNA cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein superfamily. J Biol Chem 1992; 267(28): 20282-20287
    • (1992) J Biol Chem , vol.267 , Issue.28 , pp. 20282-20287
    • Redl, B.1    Holzfeind, P.2    Lottspeich, F.3
  • 81
    • 0037062575 scopus 로고    scopus 로고
    • Evidence of an odorant-binding protein in the human olfactory mucus: Location, structural characterization, and odorant-binding properties
    • Briand L, Eloit C, Nespoulous C, Bezirard V, Huet JC, Henry C, Blon F, Trotier D, Pernollet JC. Evidence of an odorant-binding protein in the human olfactory mucus: location, structural characterization, and odorant-binding properties. Biochemistry 2002; 41(23): 7241-7252
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7241-7252
    • Briand, L.1    Eloit, C.2    Nespoulous, C.3    Bezirard, V.4    Huet, J.C.5    Henry, C.6    Blon, F.7    Trotier, D.8    Pernollet, J.C.9
  • 83
    • 4344596798 scopus 로고    scopus 로고
    • Human tear lipocalin exhibits antimicrobial activity by scavenging microbial siderophores
    • Fluckinger M, Haas H, Merschak P, Glasgow BJ, Redl B. Human tear lipocalin exhibits antimicrobial activity by scavenging microbial siderophores. Antimicrob Agents Chemother 2004; 48(9): 3367-3372
    • (2004) Antimicrob Agents Chemother , vol.48 , Issue.9 , pp. 3367-3372
    • Fluckinger, M.1    Haas, H.2    Merschak, P.3    Glasgow, B.J.4    Redl, B.5
  • 84
    • 0028286959 scopus 로고
    • Structural organization of the gene encoding the human lipocalin tear prealbumin and synthesis of the recombinant protein in Escherichia coli
    • Holzfeind P, Redl B. Structural organization of the gene encoding the human lipocalin tear prealbumin and synthesis of the recombinant protein in Escherichia coli. Gene 1994; 139(2): 177-183
    • (1994) Gene , vol.139 , Issue.2 , pp. 177-183
    • Holzfeind, P.1    Redl, B.2
  • 85
    • 0035874489 scopus 로고    scopus 로고
    • Human tear lipocalin acts as an oxidative-stress-induced scavenger of potentially harmful lipid peroxidation products in a cell culture system
    • Lechner M, Wojnar P, Redl B. Human tear lipocalin acts as an oxidative-stress-induced scavenger of potentially harmful lipid peroxidation products in a cell culture system. Biochem J 2001; 356 (Pt 1): 129-135
    • (2001) Biochem J , vol.356 , Issue.PART 1 , pp. 129-135
    • Lechner, M.1    Wojnar, P.2    Redl, B.3
  • 87
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz DH, Holmes MA, Borregaard N, Bluhm ME, Raymond KN, Strong RK. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol Cell 2000; 10(5): 1033-1043
    • (2000) Mol Cell , vol.10 , Issue.5 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 88
    • 33751500166 scopus 로고
    • Solution equilibria of enterobactin and metal-enterobactin complexes
    • Loomis LD, Raymond KN. Solution equilibria of enterobactin and metal-enterobactin complexes. Inorg Chem 1991; 30: 906-911
    • (1991) Inorg Chem , vol.30 , pp. 906-911
    • Loomis, L.D.1    Raymond, K.N.2
  • 90
    • 17644373455 scopus 로고    scopus 로고
    • Identification of differentially expressed genes in response to dietary iron deprivation in rat duodenum
    • Collins JF, Franck CA, Kowdley KV, Ghishan FK. Identification of differentially expressed genes in response to dietary iron deprivation in rat duodenum. Am J Physiol Gastrointest Liver Physiol 2005; 288(5): 964-971
    • (2005) Am J Physiol Gastrointest Liver Physiol , vol.288 , Issue.5 , pp. 964-971
    • Collins, J.F.1    Franck, C.A.2    Kowdley, K.V.3    Ghishan, F.K.4
  • 91
    • 0025013048 scopus 로고
    • Construction of cell lines that express high levels of the human estrogen receptor and are killed by estrogens
    • Kushner PJ, Hort E, Shine J, Baxter JD, Greene GL. Construction of cell lines that express high levels of the human estrogen receptor and are killed by estrogens. Mol Endocrinol 1990; 4(10): 1465-1473
    • (1990) Mol Endocrinol , vol.4 , Issue.10 , pp. 1465-1473
    • Kushner, P.J.1    Hort, E.2    Shine, J.3    Baxter, J.D.4    Greene, G.L.5
  • 92
    • 0028783678 scopus 로고
    • The other estrogen receptor in the plasma membrane: Implications for the actions of environmental estrogens
    • Watson CS, Pappas TC, Gametchu B. The other estrogen receptor in the plasma membrane: implications for the actions of environmental estrogens. Environ Health Perspect 1995; 103 (Suppl 7): 41-50
    • (1995) Environ Health Perspect , vol.103 , Issue.SUPPL. 7 , pp. 41-50
    • Watson, C.S.1    Pappas, T.C.2    Gametchu, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.