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Volumn 22, Issue 6, 2008, Pages 1427-1437

Endotoxin-induced proteolytic reduction in hepatic growth hormone (GH) receptor: A novel mechanism for GH insensitivity

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTOXIN; GROWTH HORMONE; GROWTH HORMONE BINDING PROTEIN; GROWTH HORMONE RECEPTOR; LIPOPOLYSACCHARIDE; MESSENGER RNA; METALLOPROTEINASE; MUTANT PROTEIN; STAT5 PROTEIN;

EID: 44649168952     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2007-0561     Document Type: Article
Times cited : (39)

References (60)
  • 1
    • 0021894457 scopus 로고
    • Mode of action of pituitary growth hormone on target cells
    • Isaksson OG, Eden S, Jansson JO 1985 Mode of action of pituitary growth hormone on target cells. Annu Rev Physiol 47:483-499
    • (1985) Annu Rev Physiol , vol.47 , pp. 483-499
    • Isaksson, O.G.1    Eden, S.2    Jansson, J.O.3
  • 2
    • 0011718801 scopus 로고    scopus 로고
    • Growth hormone receptor
    • Oppenheim JJ, Feldman M, eds, London, UK: Academic Press, Harcourt;
    • Frank SJ, Messina JL 2002 Growth hormone receptor. In: Oppenheim JJ, Feldman M, eds. Cytokine reference online. London, UK: Academic Press, Harcourt; 1-21
    • (2002) Cytokine reference online , pp. 1-21
    • Frank, S.J.1    Messina, J.L.2
  • 3
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos AM, Ultsch M, Kossiakoff AA 1992 Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255:306-312
    • (1992) Science , vol.255 , pp. 306-312
    • de Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 6
    • 0002440739 scopus 로고    scopus 로고
    • Growth hormone action: Signaling via a JAK/STAT-coupled receptor
    • Conn PM, Means A, eds, Totowa, NJ: Humana Press;
    • Waxman DJ, Frank SJ 2000 Growth hormone action: signaling via a JAK/STAT-coupled receptor. In: Conn PM, Means A, eds. Principles of molecular regulation: Totowa, NJ: Humana Press; 55-83
    • (2000) Principles of molecular regulation , pp. 55-83
    • Waxman, D.J.1    Frank, S.J.2
  • 7
    • 0025222521 scopus 로고
    • An inducible nuclear factor binds to a growth hormone-regulated gene
    • Yoon JB, Berry SA, Seelig S, Towle HC 1990 An inducible nuclear factor binds to a growth hormone-regulated gene. J Biol Chem 265:19947-19954
    • (1990) J Biol Chem , vol.265 , pp. 19947-19954
    • Yoon, J.B.1    Berry, S.A.2    Seelig, S.3    Towle, H.C.4
  • 9
    • 25644438861 scopus 로고    scopus 로고
    • TACE is a growth hormone binding protein sheddase: The metalloprotease TACE/ADAM-17 is critical for (PMA-induced) growth hormone receptor proteolysis and GHBP generation
    • Zhang Y, Jiang J, Black RA, Baumann G, Frank SJ 2000 TACE is a growth hormone binding protein sheddase: the metalloprotease TACE/ADAM-17 is critical for (PMA-induced) growth hormone receptor proteolysis and GHBP generation. Endocrinology 141:4324-4348
    • (2000) Endocrinology , vol.141 , pp. 4324-4348
    • Zhang, Y.1    Jiang, J.2    Black, R.A.3    Baumann, G.4    Frank, S.J.5
  • 10
    • 0035090635 scopus 로고    scopus 로고
    • Phorbol ester- and growth factor-induced growth hormone (GH) receptor proteolysis and GH-binding protein shedding: Relationship to GH receptor down-regulation
    • Guan R, Zhang Y, Jiang J, Baumann CA, Black RA, Baumann G, Frank SJ 2001 Phorbol ester- and growth factor-induced growth hormone (GH) receptor proteolysis and GH-binding protein shedding: relationship to GH receptor down-regulation. Endocrinology 142:1137-1147
    • (2001) Endocrinology , vol.142 , pp. 1137-1147
    • Guan, R.1    Zhang, Y.2    Jiang, J.3    Baumann, C.A.4    Black, R.A.5    Baumann, G.6    Frank, S.J.7
  • 11
    • 0035816531 scopus 로고    scopus 로고
    • Growth hormone (GH)-induced dimerization inhibits phorbol ester-stimulated GH receptor proteolysis
    • Zhang Y, Guan R, Jiang J, Kopchick JJ, Black RA, Baumann G, Frank SJ 2001 Growth hormone (GH)-induced dimerization inhibits phorbol ester-stimulated GH receptor proteolysis. J Biol Chem 276:24565-24573
    • (2001) J Biol Chem , vol.276 , pp. 24565-24573
    • Zhang, Y.1    Guan, R.2    Jiang, J.3    Kopchick, J.J.4    Black, R.A.5    Baumann, G.6    Frank, S.J.7
  • 14
    • 9644260490 scopus 로고    scopus 로고
    • A conformationally sensitive GHR [growth hormone (GH) receptor] antibody: Impact on GH Signaling and GHR Proteolysis
    • Jiang J, Wang X, He K, Li X, Chen C, Sayeski PP, Waters MJ, Frank SJ 2004 A conformationally sensitive GHR [growth hormone (GH) receptor] antibody: impact on GH Signaling and GHR Proteolysis. Mol Endocrinol 18:2981-2996
    • (2004) Mol Endocrinol , vol.18 , pp. 2981-2996
    • Jiang, J.1    Wang, X.2    He, K.3    Li, X.4    Chen, C.5    Sayeski, P.P.6    Waters, M.J.7    Frank, S.J.8
  • 16
    • 34347216041 scopus 로고    scopus 로고
    • Role of the growth hormone (GH) receptor transmembrane domain in receptor predimerization and GH-induced activation
    • Yang N, Wang X, Jiang J, Frank SJ 2007 Role of the growth hormone (GH) receptor transmembrane domain in receptor predimerization and GH-induced activation. Mol Endocrinol 21:1642-1655
    • (2007) Mol Endocrinol , vol.21 , pp. 1642-1655
    • Yang, N.1    Wang, X.2    Jiang, J.3    Frank, S.J.4
  • 17
    • 0036739177 scopus 로고    scopus 로고
    • Metalloproteinases and the modulation of GH signaling
    • Baumann G, Frank SJ 2002 Metalloproteinases and the modulation of GH signaling. J Endocrinol 174:361-368
    • (2002) J Endocrinol , vol.174 , pp. 361-368
    • Baumann, G.1    Frank, S.J.2
  • 20
    • 0032945579 scopus 로고    scopus 로고
    • GH insensitivity induced by endotoxin injection is associated with decreased liver GH receptors
    • Defalque D, Brandt N, Ketelslegers JM, Thissen JP 1999 GH insensitivity induced by endotoxin injection is associated with decreased liver GH receptors. Am J Physiol 276:E565-E572
    • (1999) Am J Physiol , vol.276
    • Defalque, D.1    Brandt, N.2    Ketelslegers, J.M.3    Thissen, J.P.4
  • 22
    • 0036280436 scopus 로고    scopus 로고
    • The role of endotoxin, TNF-α, and IL-6 in inducing the state of growth hormone insensitivity
    • Wang P, Li N, Li JS, Li WQ 2002 The role of endotoxin, TNF-α, and IL-6 in inducing the state of growth hormone insensitivity. World J Gastroenterol 8:531-536
    • (2002) World J Gastroenterol , vol.8 , pp. 531-536
    • Wang, P.1    Li, N.2    Li, J.S.3    Li, W.Q.4
  • 24
    • 34447572787 scopus 로고    scopus 로고
    • Endotoxin attenuates growth hormone-induced hepatic insulin-like growth factor I expression by inhibiting JAK2/STAT5 signal transduction and STAT5b DNA binding
    • Chen Y, Sun D, Krishnamurthy VM, Rabkin R 2007 Endotoxin attenuates growth hormone-induced hepatic insulin-like growth factor I expression by inhibiting JAK2/STAT5 signal transduction and STAT5b DNA binding. Am J Physiol Endocrinol Metab 292:E1856-E1862
    • (2007) Am J Physiol Endocrinol Metab , vol.292
    • Chen, Y.1    Sun, D.2    Krishnamurthy, V.M.3    Rabkin, R.4
  • 25
    • 0031946053 scopus 로고    scopus 로고
    • Systemic and splanchnic metabolic response to exogenous human growth hormone
    • Dahn MS, Lange MP 1998 Systemic and splanchnic metabolic response to exogenous human growth hormone. Surgery 123:528-538
    • (1998) Surgery , vol.123 , pp. 528-538
    • Dahn, M.S.1    Lange, M.P.2
  • 30
    • 0024712404 scopus 로고
    • The growth hormone-binding protein in rat serum is an alternatively spliced form of the rat growth hormone receptor
    • Baumbach WR, Horner DL, Logan JS 1989 The growth hormone-binding protein in rat serum is an alternatively spliced form of the rat growth hormone receptor. Genes Dev 3:1199-1205
    • (1989) Genes Dev , vol.3 , pp. 1199-1205
    • Baumbach, W.R.1    Horner, D.L.2    Logan, J.S.3
  • 31
    • 0024370011 scopus 로고
    • Mouse serum growth hormone (GH) binding protein has GH receptor extracellular and substituted transmembrane domains
    • Smith WC, Kuniyoshi J, Talamantes F 1989 Mouse serum growth hormone (GH) binding protein has GH receptor extracellular and substituted transmembrane domains. Mol Endocrinol 3:984-990
    • (1989) Mol Endocrinol , vol.3 , pp. 984-990
    • Smith, W.C.1    Kuniyoshi, J.2    Talamantes, F.3
  • 33
    • 0031698581 scopus 로고    scopus 로고
    • ADAMs: Focus on the protease domain
    • Black RA, White JM 1998 ADAMs: focus on the protease domain. Curr Opin Cell Biol 10:654-659
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 34
    • 0043272529 scopus 로고    scopus 로고
    • Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs)
    • Becherer JD, Blobel CP 2003 Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs). Curr Top Dev Biol 54:101-123
    • (2003) Curr Top Dev Biol , vol.54 , pp. 101-123
    • Becherer, J.D.1    Blobel, C.P.2
  • 36
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • Seals DF, Courtneidge SA 2003 The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 17:7-30
    • (2003) Genes Dev , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 39
    • 0034994026 scopus 로고    scopus 로고
    • TNF-α downregulates murine hepatic growth hormone receptor expression by inhibiting Sp1 and Sp3 binding
    • Denson LA, Menon RK, Shaufl A, Bajwa HS, Williams CR, Karpen SJ 2001 TNF-α downregulates murine hepatic growth hormone receptor expression by inhibiting Sp1 and Sp3 binding. J Clin Invest 107:1451-1458
    • (2001) J Clin Invest , vol.107 , pp. 1451-1458
    • Denson, L.A.1    Menon, R.K.2    Shaufl, A.3    Bajwa, H.S.4    Williams, C.R.5    Karpen, S.J.6
  • 40
    • 0033752093 scopus 로고    scopus 로고
    • Potentiation of growth hormone-induced liver suppressors of cytokine signaling messenger ribonucleic acid by cytokines
    • Colson A, Le Cam A, Maiter D, Edery M, Thissen JP 2000 Potentiation of growth hormone-induced liver suppressors of cytokine signaling messenger ribonucleic acid by cytokines. Endocrinology 141:3687-3695
    • (2000) Endocrinology , vol.141 , pp. 3687-3695
    • Colson, A.1    Le Cam, A.2    Maiter, D.3    Edery, M.4    Thissen, J.P.5
  • 41
    • 0034635550 scopus 로고    scopus 로고
    • Role of the suppressor of cytokine signaling-3 in mediating the inhibitory effects of interleukin-1β on the growth hormone-dependent transcription of the acid-labile subunit gene in liver cells
    • Boisclair YR, Wang J, Shi J, Hurst KR, Ooi GT 2000 Role of the suppressor of cytokine signaling-3 in mediating the inhibitory effects of interleukin-1β on the growth hormone-dependent transcription of the acid-labile subunit gene in liver cells. J Biol Chem 275:3841-3847
    • (2000) J Biol Chem , vol.275 , pp. 3841-3847
    • Boisclair, Y.R.1    Wang, J.2    Shi, J.3    Hurst, K.R.4    Ooi, G.T.5
  • 42
    • 34547180376 scopus 로고    scopus 로고
    • Lipopolysaccharide (LPS) directly suppresses growth hormone receptor (GHR) expression through MyD88-dependent and -independent Toll-like receptor-4/MD2 complex signaling pathways
    • Dejkhamron P, Thimmarayappa J, Kotlyarevska K, Sun J, Lu C, Bonkowski EL, Denson LA, Menon RK 2007 Lipopolysaccharide (LPS) directly suppresses growth hormone receptor (GHR) expression through MyD88-dependent and -independent Toll-like receptor-4/MD2 complex signaling pathways. Mol Cell Endocrinol 274:35-42
    • (2007) Mol Cell Endocrinol , vol.274 , pp. 35-42
    • Dejkhamron, P.1    Thimmarayappa, J.2    Kotlyarevska, K.3    Sun, J.4    Lu, C.5    Bonkowski, E.L.6    Denson, L.A.7    Menon, R.K.8
  • 43
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira S, Takeda K 2004 Toll-like receptor signalling. Nat Rev Immunol 4:499-511
    • (2004) Nat Rev Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 44
  • 45
    • 0033376608 scopus 로고    scopus 로고
    • The Lps locus: Genetic regulation of host responses to bacterial lipopolysaccharide
    • Qureshi ST, Gros P, Malo D 1999 The Lps locus: genetic regulation of host responses to bacterial lipopolysaccharide. Inflamm Res 48:613-620
    • (1999) Inflamm Res , vol.48 , pp. 613-620
    • Qureshi, S.T.1    Gros, P.2    Malo, D.3
  • 46
    • 0014546925 scopus 로고
    • Genetic factors in leucocyte responses to endotoxin: Further studies in mice
    • Sultzer BM 1969 Genetic factors in leucocyte responses to endotoxin: further studies in mice. J Immunol 103:32-38
    • (1969) J Immunol , vol.103 , pp. 32-38
    • Sultzer, B.M.1
  • 47
    • 0032200809 scopus 로고    scopus 로고
    • Genetic component in the inflammatory response induced by bacterial lipopolysaccharide
    • De Maio A, Mooney ML, Matesic LE, Paidas CN, Reeves RH 1998 Genetic component in the inflammatory response induced by bacterial lipopolysaccharide. Shock 10:319-323
    • (1998) Shock , vol.10 , pp. 319-323
    • De Maio, A.1    Mooney, M.L.2    Matesic, L.E.3    Paidas, C.N.4    Reeves, R.H.5
  • 48
    • 0033798478 scopus 로고    scopus 로고
    • Effects of interaction between Escherichia coli verotoxin and lipopolysaccharide on cytokine induction and lethality in mice
    • Suzuki K, Tateda K, Matsumoto T, Gondaira F, Tsujimoto S, Yamaguchi K 2000 Effects of interaction between Escherichia coli verotoxin and lipopolysaccharide on cytokine induction and lethality in mice. J Med Microbiol 49:905-910
    • (2000) J Med Microbiol , vol.49 , pp. 905-910
    • Suzuki, K.1    Tateda, K.2    Matsumoto, T.3    Gondaira, F.4    Tsujimoto, S.5    Yamaguchi, K.6
  • 49
    • 0029123831 scopus 로고
    • Differences in the shedding of soluble TNF receptors between endotoxin-sensitive and endotoxin-resistant mice in response to lipopolysaccharide or live bacterial challenge
    • Carpenter A, Evans TJ, Buurman WA, Bemelmans MH, Moyes D, Cohen J 1995 Differences in the shedding of soluble TNF receptors between endotoxin-sensitive and endotoxin-resistant mice in response to lipopolysaccharide or live bacterial challenge. J Immunol 155:2005-2012
    • (1995) J Immunol , vol.155 , pp. 2005-2012
    • Carpenter, A.1    Evans, T.J.2    Buurman, W.A.3    Bemelmans, M.H.4    Moyes, D.5    Cohen, J.6
  • 50
    • 34247118826 scopus 로고    scopus 로고
    • Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signaling
    • Kanneganti TD, Lamkanfi M, Kim YG, Chen G, Park JH, Franchi L, Vandenabeele P, Nunez G 2007 Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signaling. Immunity 26:433-443
    • (2007) Immunity , vol.26 , pp. 433-443
    • Kanneganti, T.D.1    Lamkanfi, M.2    Kim, Y.G.3    Chen, G.4    Park, J.H.5    Franchi, L.6    Vandenabeele, P.7    Nunez, G.8
  • 51
    • 38449086094 scopus 로고    scopus 로고
    • Cutting edge: TNF-α-converting enzyme (TACE/ADAM17) inactivation in mouse myeloid cells prevents lethality from endotoxin shock
    • Horiuchi K, Kimura T, Miyamoto T, Takaishi H, Okada Y, Toyama Y, Blobel CP 2007 Cutting edge: TNF-α-converting enzyme (TACE/ADAM17) inactivation in mouse myeloid cells prevents lethality from endotoxin shock. J Immunol 179:2686-2689
    • (2007) J Immunol , vol.179 , pp. 2686-2689
    • Horiuchi, K.1    Kimura, T.2    Miyamoto, T.3    Takaishi, H.4    Okada, Y.5    Toyama, Y.6    Blobel, C.P.7
  • 53
    • 29844431791 scopus 로고    scopus 로고
    • Treatment with GH and IGF-1 in critical illness
    • vi
    • Teng Chung T, Hinds CJ 2006 Treatment with GH and IGF-1 in critical illness. Crit Care Clin 22:29-40, vi
    • (2006) Crit Care Clin , vol.22 , pp. 29-40
    • Teng Chung, T.1    Hinds, C.J.2
  • 54
    • 2342583543 scopus 로고    scopus 로고
    • Growth hormone and insulin-like growth factor 1 levels and their relation to survival in children with bacterial sepsis and septic shock
    • Onenli-Mungan N, Yildizdas D, Yapicioglu H, Topaloglu AK, Yuksel B, Ozer G 2004 Growth hormone and insulin-like growth factor 1 levels and their relation to survival in children with bacterial sepsis and septic shock. J Paediatr Child Health 40:221-226
    • (2004) J Paediatr Child Health , vol.40 , pp. 221-226
    • Onenli-Mungan, N.1    Yildizdas, D.2    Yapicioglu, H.3    Topaloglu, A.K.4    Yuksel, B.5    Ozer, G.6
  • 57
    • 0032755252 scopus 로고    scopus 로고
    • Disulfide linkage of growth hormone (GH) receptors (GHR) reflects GH-induced GHR dimerization. Association of JAK2 with the GHR is enhanced by receptor dimerization
    • Zhang Y, Jiang J, Kopchick JJ, Frank SJ 1999 Disulfide linkage of growth hormone (GH) receptors (GHR) reflects GH-induced GHR dimerization. Association of JAK2 with the GHR is enhanced by receptor dimerization. J Biol Chem 274:33072-33084
    • (1999) J Biol Chem , vol.274 , pp. 33072-33084
    • Zhang, Y.1    Jiang, J.2    Kopchick, J.J.3    Frank, S.J.4
  • 58
    • 0031890381 scopus 로고    scopus 로고
    • Involvement of the Src homology 2-containing tyrosine phosphatase SHP-2 in growth hormone signaling
    • Kim SO, Jiang J, Yi W, Feng GS, Frank SJ 1998 Involvement of the Src homology 2-containing tyrosine phosphatase SHP-2 in growth hormone signaling. J Biol Chem 273:2344-2354
    • (1998) J Biol Chem , vol.273 , pp. 2344-2354
    • Kim, S.O.1    Jiang, J.2    Yi, W.3    Feng, G.S.4    Frank, S.J.5
  • 59
    • 36348972963 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation of growth hormone receptor in Janus kinase 2-deficient cells
    • Loesch K, Deng L, Wang X, He K, Jiang J, Frank SJ 2007 Endoplasmic reticulum-associated degradation of growth hormone receptor in Janus kinase 2-deficient cells. Endocrinology 148:5955-5965
    • (2007) Endocrinology , vol.148 , pp. 5955-5965
    • Loesch, K.1    Deng, L.2    Wang, X.3    He, K.4    Jiang, J.5    Frank, S.J.6


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