메뉴 건너뛰기




Volumn 48, Issue 2, 1999, Pages 279-286

Functional properties of leptin receptor isoforms: Internalization and degradation of leptin and ligand-induced receptor downregulation

Author keywords

[No Author keywords available]

Indexed keywords

LEPTIN RECEPTOR;

EID: 0033008075     PISSN: 00121797     EISSN: None     Source Type: Journal    
DOI: 10.2337/diabetes.48.2.279     Document Type: Article
Times cited : (214)

References (62)
  • 5
    • 0029048408 scopus 로고
    • Recombinant mouse OB protein: Evidence for a peripheral signal linking adiposity and central neural networks
    • Campfield L, Smith F, Guisez Y, Devos R, Burn P: Recombinant mouse OB protein: evidence for a peripheral signal linking adiposity and central neural networks. Science 269:546-548, 1995
    • (1995) Science , vol.269 , pp. 546-548
    • Campfield, L.1    Smith, F.2    Guisez, Y.3    Devos, R.4    Burn, P.5
  • 13
    • 0031010408 scopus 로고    scopus 로고
    • Anatomic localization of alternatively spliced leptin receptors (OBR) in mouse brain and other tissues
    • Fei H, Okano HJ, Li C, Lee G-H, Zhao C, Darnell R, Friedman JM: Anatomic localization of alternatively spliced leptin receptors (OBR) in mouse brain and other tissues. Proc Natl Acad Sci U S A 94:7001-7005, 1997
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 7001-7005
    • Fei, H.1    Okano, H.J.2    Li, C.3    Lee, G.-H.4    Zhao, C.5    Darnell, R.6    Friedman, J.M.7
  • 14
    • 0031017561 scopus 로고    scopus 로고
    • Human blood-brain barrier leptin receptor binding and endocytosis in isolated human brain microvessels
    • Golden PL, Maccagnan TJ, Pardridge WM: Human blood-brain barrier leptin receptor binding and endocytosis in isolated human brain microvessels. J Clin Invest 99:14-18, 1997
    • (1997) J Clin Invest , vol.99 , pp. 14-18
    • Golden, P.L.1    Maccagnan, T.J.2    Pardridge, W.M.3
  • 21
    • 0031436148 scopus 로고    scopus 로고
    • Divergent signaling capacities of the long and short isoforms of the leptin receptor
    • Bjørbæk C, Uotani S, da Silva B, Flier JS: Divergent signaling capacities of the long and short isoforms of the leptin receptor. J Biol Chem 272:32686-32695, 1997
    • (1997) J Biol Chem , vol.272 , pp. 32686-32695
    • Bjørbæk, C.1    Uotani, S.2    Da Silva, B.3    Flier, J.S.4
  • 24
    • 0019945866 scopus 로고
    • The endocytotic rate constant: A cellular parameter for quantitating receptor-mediated endocytosis
    • Wiley HS, Cunningham DD: The endocytotic rate constant: a cellular parameter for quantitating receptor-mediated endocytosis. J Biol Chem 257:4222-4229, 1982
    • (1982) J Biol Chem , vol.257 , pp. 4222-4229
    • Wiley, H.S.1    Cunningham, D.D.2
  • 25
    • 0026765431 scopus 로고
    • Internalization of the human insulin receptor: The insulin-independent pathway
    • Paccaud JP, Saddle K, Carpentier JL: Internalization of the human insulin receptor: the insulin-independent pathway. J Biol Chem 267:13101-13106, 1992
    • (1992) J Biol Chem , vol.267 , pp. 13101-13106
    • Paccaud, J.P.1    Saddle, K.2    Carpentier, J.L.3
  • 26
    • 0024544710 scopus 로고
    • Potassium depletion and hypertonic medium reduce "non-coated" and clathrin-coated pit formation, as well as endocytosis through these two gates
    • Carpentier JL, Sawano F, Geiger D, Gorden P, Perrelet A, Orci L: Potassium depletion and hypertonic medium reduce "non-coated" and clathrin-coated pit formation, as well as endocytosis through these two gates. J Cell Physiol 138:519-526, 1989
    • (1989) J Cell Physiol , vol.138 , pp. 519-526
    • Carpentier, J.L.1    Sawano, F.2    Geiger, D.3    Gorden, P.4    Perrelet, A.5    Orci, L.6
  • 27
    • 0019983285 scopus 로고
    • Interaction of platelet-derived growth factor with its fibroblast receptor demonstration of ligand degradation and receptor modulation
    • Heldin CH, Wasteson A, Westermark B: Interaction of platelet-derived growth factor with its fibroblast receptor demonstration of ligand degradation and receptor modulation. J Biol Chem 257:4216-4221, 1982
    • (1982) J Biol Chem , vol.257 , pp. 4216-4221
    • Heldin, C.H.1    Wasteson, A.2    Westermark, B.3
  • 28
    • 0025885433 scopus 로고
    • Identification of a hydrophobic region in the carboxyl terminus of the platelet-derived growth factor β-receptor that is important for ligand-mediated endocytosis
    • Mori S, Claesson-Welsh L, Heldin CH: Identification of a hydrophobic region in the carboxyl terminus of the platelet-derived growth factor β-receptor that is important for ligand-mediated endocytosis. J Biol Chem 266:21158-21164, 1991
    • (1991) J Biol Chem , vol.266 , pp. 21158-21164
    • Mori, S.1    Claesson-Welsh, L.2    Heldin, C.H.3
  • 30
    • 0030981063 scopus 로고    scopus 로고
    • Leptin receptor of Zucker fatty rat performs reduced signal transduction
    • Yamashita T, Murakami T, Iida M, Kuwajima M, Shima K: Leptin receptor of Zucker fatty rat performs reduced signal transduction. Diabetes 46:1077-1080, 1997
    • (1997) Diabetes , vol.46 , pp. 1077-1080
    • Yamashita, T.1    Murakami, T.2    Iida, M.3    Kuwajima, M.4    Shima, K.5
  • 33
    • 0030003317 scopus 로고    scopus 로고
    • Protein targeting by tyrosine-and di-leucine-based signals: Evidence for distinct saturable components
    • Marks MS, Woodruff L, Ohono H, Bonifacino JS: Protein targeting by tyrosine-and di-leucine-based signals: evidence for distinct saturable components. J Cell Biol 135:341-354, 1996
    • (1996) J Cell Biol , vol.135 , pp. 341-354
    • Marks, M.S.1    Woodruff, L.2    Ohono, H.3    Bonifacino, J.S.4
  • 34
    • 0030989801 scopus 로고    scopus 로고
    • Identification of cytoplasmic motifs required for short prolactin receptor internalization
    • Vincent V, Goffin V, Rozakis-Adcock M, Momon JP, Kelly PA: Identification of cytoplasmic motifs required for short prolactin receptor internalization. J Biol Chem 272:7062-7068, 1997
    • (1997) J Biol Chem , vol.272 , pp. 7062-7068
    • Vincent, V.1    Goffin, V.2    Rozakis-Adcock, M.3    Momon, J.P.4    Kelly, P.A.5
  • 35
    • 0030013247 scopus 로고    scopus 로고
    • Distinct cytoplasmic domains of the growth hormone receptor are required for glucocorticoid- and phorbol ester-induced decreases in growth hormone (GH) binding: These domains are different from that reported for GH-induced receptor internalization
    • King APJ, Tseng MJ, Logsdon CD, Billestrup N, Carter-Su C: Distinct cytoplasmic domains of the growth hormone receptor are required for glucocorticoid- and phorbol ester-induced decreases in growth hormone (GH) binding: these domains are different from that reported for GH-induced receptor internalization. J Biol Chem 271:18088-18094, 1996
    • (1996) J Biol Chem , vol.271 , pp. 18088-18094
    • King, A.P.J.1    Tseng, M.J.2    Logsdon, C.D.3    Billestrup, N.4    Carter-Su, C.5
  • 36
    • 0025369327 scopus 로고
    • Human growth hormone-stimulated growth of human cultured lymphocytes (IM-9) and its inhibition by phorbol diesters through downregulation of the hormone receptors: Possible involvement of phosphorylation of a 55,000 molecular weight protein associated with the receptor in the downregulation
    • Suzuki K, Suzuki S, Saito Y, Ikebuchi H, Terao T: Human growth hormone-stimulated growth of human cultured lymphocytes (IM-9) and its inhibition by phorbol diesters through downregulation of the hormone receptors: possible involvement of phosphorylation of a 55,000 molecular weight protein associated with the receptor in the downregulation. J Biol Chem 265:11320-11327, 1990
    • (1990) J Biol Chem , vol.265 , pp. 11320-11327
    • Suzuki, K.1    Suzuki, S.2    Saito, Y.3    Ikebuchi, H.4    Terao, T.5
  • 37
    • 0028829614 scopus 로고
    • Dexamethasone-induced antagonism of growth hormone (GH) action by downregulation of GH binding in 3T3-F442A fibroblasts
    • King AP, Carter-Su C: Dexamethasone-induced antagonism of growth hormone (GH) action by downregulation of GH binding in 3T3-F442A fibroblasts. Endocrinology 136:4796-4803, 1995
    • (1995) Endocrinology , vol.136 , pp. 4796-4803
    • King, A.P.1    Carter-Su, C.2
  • 38
    • 0020150186 scopus 로고
    • Endocytosis of peptide hormones and other ligands
    • Posner BI, Khan MN, Bergeron JJM: Endocytosis of peptide hormones and other ligands. Endocr Rev 3:280-298, 1982
    • (1982) Endocr Rev , vol.3 , pp. 280-298
    • Posner, B.I.1    Khan, M.N.2    Bergeron, J.J.M.3
  • 39
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin C-H: Dimerization of cell surface receptors in signal transduction. Cell 80:21.3-223, 1995
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.-H.1
  • 40
    • 0028221574 scopus 로고
    • Endocytosis and degradation of prolactin and its receptor in Chinese hamster ovary cells stably transfected with prolactin receptor cDNA
    • Genty N, Paly J, Edery M, Kelly PA, Djiane J, Salesse R: Endocytosis and degradation of prolactin and its receptor in Chinese hamster ovary cells stably transfected with prolactin receptor cDNA. Mol Cell Endocrinol 99:221-228, 1994
    • (1994) Mol Cell Endocrinol , vol.99 , pp. 221-228
    • Genty, N.1    Paly, J.2    Edery, M.3    Kelly, P.A.4    Djiane, J.5    Salesse, R.6
  • 41
    • 0025277673 scopus 로고
    • Endocytosis and degradation of ovine prolactin by Nb2 lymphoma cells: Characterization and effects of agents known to alter prolactin-induced mitogenesis
    • Augustine EC, Kensinger RS: Endocytosis and degradation of ovine prolactin by Nb2 lymphoma cells: characterization and effects of agents known to alter prolactin-induced mitogenesis. Endocrinology 127:200-210, 1990
    • (1990) Endocrinology , vol.127 , pp. 200-210
    • Augustine, E.C.1    Kensinger, R.S.2
  • 42
    • 0023714041 scopus 로고
    • Receptor-mediated endocytosis and degradation of bovine growth hormone in rat liver
    • Husman B, Gustafsson JA, Andersson G: Receptor-mediated endocytosis and degradation of bovine growth hormone in rat liver. Mol Cell Endocrinol 59:13-25, 1988
    • (1988) Mol Cell Endocrinol , vol.59 , pp. 13-25
    • Husman, B.1    Gustafsson, J.A.2    Andersson, G.3
  • 44
    • 0017334127 scopus 로고
    • Role of the coated endocytic vesicle in the uptake of receptor-bound low-density lipoprotein in human fibroblasts
    • Anderson RG, Brown MS, Goldstein JL: Role of the coated endocytic vesicle in the uptake of receptor-bound low-density lipoprotein in human fibroblasts. Cell 10:351-364, 1977
    • (1977) Cell , vol.10 , pp. 351-364
    • Anderson, R.G.1    Brown, M.S.2    Goldstein, J.L.3
  • 45
    • 0026343342 scopus 로고
    • Insulin receptors internalize by a rapid, saturable pathway requiring receptor autophosphorylation and an intact juxtamembrane region
    • Backer JM, Shoelson SE, Haring E, White MF: Insulin receptors internalize by a rapid, saturable pathway requiring receptor autophosphorylation and an intact juxtamembrane region. J Cell Biol 115:1535-1545, 1991
    • (1991) J Cell Biol , vol.115 , pp. 1535-1545
    • Backer, J.M.1    Shoelson, S.E.2    Haring, E.3    White, M.F.4
  • 46
    • 0030816392 scopus 로고    scopus 로고
    • Phosphorylation of four amino acid residues in the carboxyl terminus of the rat somatostatin receptor subtype 3 is crucial for its desensitization and intemalization
    • Roth A, Kreienkamp HJ, Meyerhof W, Richter D: Phosphorylation of four amino acid residues in the carboxyl terminus of the rat somatostatin receptor subtype 3 is crucial for its desensitization and intemalization. J Biol Chem 272:23764-23774, 1997
    • (1997) J Biol Chem , vol.272 , pp. 23764-23774
    • Roth, A.1    Kreienkamp, H.J.2    Meyerhof, W.3    Richter, D.4
  • 47
    • 0030797977 scopus 로고    scopus 로고
    • Protein phosphorylation events in exocytosis and endocytosis
    • Liu JP: Protein phosphorylation events in exocytosis and endocytosis. Clin Exp Pharmacol Physiol 24:611-618, 1997
    • (1997) Clin Exp Pharmacol Physiol , vol.24 , pp. 611-618
    • Liu, J.P.1
  • 48
    • 0030917081 scopus 로고    scopus 로고
    • Tyrosine phosphorylation controls internalization of CTLA-4 by regulating its interaction with clathrin-associated adaptor complex AP-2
    • Shiratori T, Miyatake S, Ohono H, Nakaseko C, Isono K, Bonifacino JS, Saito T: Tyrosine phosphorylation controls internalization of CTLA-4 by regulating its interaction with clathrin-associated adaptor complex AP-2. Immunity 6:583-589, 1997
    • (1997) Immunity , vol.6 , pp. 583-589
    • Shiratori, T.1    Miyatake, S.2    Ohono, H.3    Nakaseko, C.4    Isono, K.5    Bonifacino, J.S.6    Saito, T.7
  • 49
    • 0023091262 scopus 로고
    • Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region
    • Davis CG, Goldstein JL, Sudhof TC, Anderson RG, Russsel DW, Brown MS: Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region. Nature 326:760-765, 1987
    • (1987) Nature , vol.326 , pp. 760-765
    • Davis, C.G.1    Goldstein, J.L.2    Sudhof, T.C.3    Anderson, R.G.4    Russsel, D.W.5    Brown, M.S.6
  • 51
    • 0028793697 scopus 로고
    • Leptin levels reflect body lipid content in mice: Evidence for diet-induced resistance to leptin action
    • Frederich R, Hamann A, Anderson S, Lollmann B, Lowell BB, Flier JS: Leptin levels reflect body lipid content in mice: evidence for diet-induced resistance to leptin action. Nat Med 1:1311-1314, 1995
    • (1995) Nat Med , vol.1 , pp. 1311-1314
    • Frederich, R.1    Hamann, A.2    Anderson, S.3    Lollmann, B.4    Lowell, B.B.5    Flier, J.S.6
  • 52
    • 0029864416 scopus 로고    scopus 로고
    • Leptin enters the brain by a saturable system independent of insulin
    • Banks WA, Kastin AJ, Huang W, Jaspan JB, Maness LM: Leptin enters the brain by a saturable system independent of insulin. Peptides 17:305-311, 1996
    • (1996) Peptides , vol.17 , pp. 305-311
    • Banks, W.A.1    Kastin, A.J.2    Huang, W.3    Jaspan, J.B.4    Maness, L.M.5
  • 53
    • 0031154102 scopus 로고    scopus 로고
    • Cerebrospinal fluid leptin in anorexia nervosa: Correlation with nutritional status and potential role in resistance to weight gain
    • Mantzoros C, Flier JS, Lesen MD, Brewerton TD, Jimerson DC: Cerebrospinal fluid leptin in anorexia nervosa: correlation with nutritional status and potential role in resistance to weight gain. J Clin Endocrinol Metab 82:1845-1851, 1997
    • (1997) J Clin Endocrinol Metab , vol.82 , pp. 1845-1851
    • Mantzoros, C.1    Flier, J.S.2    Lesen, M.D.3    Brewerton, T.D.4    Jimerson, D.C.5
  • 54
    • 0029881125 scopus 로고    scopus 로고
    • Cerebrospinal fluid leptin levels: Relationship to plasma levels and to adiposity in humans
    • Schwartz MW, Peskind E, Raskind M, Boyko EJ, Porte D Jr: Cerebrospinal fluid leptin levels: relationship to plasma levels and to adiposity in humans. Nat Med 2:589-593, 1996
    • (1996) Nat Med , vol.2 , pp. 589-593
    • Schwartz, M.W.1    Peskind, E.2    Raskind, M.3    Boyko, E.J.4    Porte D., Jr.5
  • 57
    • 0027322295 scopus 로고
    • Serum proteins bypass the blood-brain fluid barriers for extracellular entry to the central nervous system
    • Broadwell RD, Sofroniew MV: Serum proteins bypass the blood-brain fluid barriers for extracellular entry to the central nervous system. Exp Neurol 120:24:5-263, 1993
    • (1993) Exp Neurol , vol.120 , Issue.24 , pp. 5-263
    • Broadwell, R.D.1    Sofroniew, M.V.2
  • 61
    • 0038189958 scopus 로고
    • Antagonism by cortisone of the linear growth induced in hypopituitary patients and hypophysectiomized rats by human growth hormone
    • Soyka LF, Crawford JD: Antagonism by cortisone of the linear growth induced in hypopituitary patients and hypophysectiomized rats by human growth hormone. J Clin Endocrinol Metab 25:469-475, 1965
    • (1965) J Clin Endocrinol Metab , vol.25 , pp. 469-475
    • Soyka, L.F.1    Crawford, J.D.2
  • 62
    • 0030903264 scopus 로고    scopus 로고
    • Glucocorticoids as counterregulatory hormones of leptin: Toward an understanding of leptin resistance
    • Zakrzewska KE, Cusin I, Sainsbury A, Rohner-Jeanrenaud F, Jeanrenaud B: Glucocorticoids as counterregulatory hormones of leptin: toward an understanding of leptin resistance. Diabetes 46:717-719, 1997
    • (1997) Diabetes , vol.46 , pp. 717-719
    • Zakrzewska, K.E.1    Cusin, I.2    Sainsbury, A.3    Rohner-Jeanrenaud, F.4    Jeanrenaud, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.