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Volumn 144, Issue 9, 2003, Pages 3821-3827

Evidence that the C terminus of the A subunit suppresses thyrotropin receptor constitutive activity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CHIMERIC PROTEIN; CYCLIC AMP; LUTEINIZING HORMONE RECEPTOR; THYROTROPIN RECEPTOR; TRYPSIN; HYBRID PROTEIN;

EID: 0042421851     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/en.2003-0430     Document Type: Article
Times cited : (28)

References (29)
  • 1
    • 0028916473 scopus 로고
    • In Chinese hamster ovary K1 cells dog and human thyrotropin receptors activate both the cyclic AMP and the phosphatidylinositol 4, 5-bisphosphate cascades in the presence of thyrotropin and the cyclic AMP cascade in its absence
    • Van Sande J, Swillens S, Gerard C, Allgeier A, Massart C, Vassart G, Dumont J 1995 In Chinese hamster ovary K1 cells dog and human thyrotropin receptors activate both the cyclic AMP and the phosphatidylinositol 4, 5-bisphosphate cascades in the presence of thyrotropin and the cyclic AMP cascade in its absence. Eur J Biochem 229:338-343
    • (1995) Eur J Biochem , vol.229 , pp. 338-343
    • Van Sande, J.1    Swillens, S.2    Gerard, C.3    Allgeier, A.4    Massart, C.5    Vassart, G.6    Dumont, J.7
  • 2
    • 0029360448 scopus 로고
    • Genetic basis of endocrine disease: Somatic and germline mutations of the TSH receptor gene in thyroid diseases
    • Van Sande J, Parma J, Tonacchera M, Swillens S, Dumont J, Vassart G 1995 Genetic basis of endocrine disease: somatic and germline mutations of the TSH receptor gene in thyroid diseases. J Clin Endocrinol Metab 80:2577-2585
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 2577-2585
    • Van Sande, J.1    Parma, J.2    Tonacchera, M.3    Swillens, S.4    Dumont, J.5    Vassart, G.6
  • 4
    • 0034457935 scopus 로고    scopus 로고
    • The extracellular domain suppresses constitutive activity of the transmembrane domain of the human TSH receptor: Implications for hormone-receptor interaction and antagonist design
    • Zhang M, Phuong K, Tong T, Fremont V, Chen J, Narayan P, Puett D, Weintraub BD, Szkudlinski MW 2000 The extracellular domain suppresses constitutive activity of the transmembrane domain of the human TSH receptor: implications for hormone-receptor interaction and antagonist design. Endocrinology 141:3514-3517
    • (2000) Endocrinology , vol.141 , pp. 3514-3517
    • Zhang, M.1    Phuong, K.2    Tong, T.3    Fremont, V.4    Chen, J.5    Narayan, P.6    Puett, D.7    Weintraub, B.D.8    Szkudlinski, M.W.9
  • 5
    • 0036214718 scopus 로고    scopus 로고
    • Activation of the cAMP pathway by the TSH receptor involves switching of the ectodomain from a tethered inverse agonist to an agonist
    • Vlaeminck-Guillem V, Ho SC, Rodien P, Vassart G, Costagliola S 2002 Activation of the cAMP pathway by the TSH receptor involves switching of the ectodomain from a tethered inverse agonist to an agonist. Mol Endocrinol 16:736-746
    • (2002) Mol Endocrinol , vol.16 , pp. 736-746
    • Vlaeminck-Guillem, V.1    Ho, S.C.2    Rodien, P.3    Vassart, G.4    Costagliola, S.5
  • 7
    • 0031916727 scopus 로고    scopus 로고
    • Thyrotropin receptor cleavage at site 1 does not involve a specific amino acid motif but instead depends on the presence of the unique, 50 amino acid insertion
    • Tanaka K, Chazenbalk GD, McLachlan SM, Rapoport B 1998 Thyrotropin receptor cleavage at site 1 does not involve a specific amino acid motif but instead depends on the presence of the unique, 50 amino acid insertion. J Biol Chem 273:1959-1963
    • (1998) J Biol Chem , vol.273 , pp. 1959-1963
    • Tanaka, K.1    Chazenbalk, G.D.2    McLachlan, S.M.3    Rapoport, B.4
  • 10
    • 0037387335 scopus 로고    scopus 로고
    • Targeted restoration of cleavage in a noncleaving thyrotropin receptor demonstrates that cleavage is insufficient to enhance ligand-ind ependent activity
    • Chen C-R, Chazenbalk GD, McLachlan SM, Rapoport B 2003 Targeted restoration of cleavage in a noncleaving thyrotropin receptor demonstrates that cleavage is insufficient to enhance ligand-ind ependent activity. Endocrinology 144:1324-1330
    • (2003) Endocrinology , vol.144 , pp. 1324-1330
    • Chen, C.-R.1    Chazenbalk, G.D.2    McLachlan, S.M.3    Rapoport, B.4
  • 11
    • 0024852495 scopus 로고
    • Molecular cloning, sequence and functional expression of the cDNA for the human thyrotropin receptor
    • Nagayama Y, Kaufman KD, Seto P, Rapoport B 1989 Molecular cloning, sequence and functional expression of the cDNA for the human thyrotropin receptor. Biochem Biophys Res Commun 165:1184-1190
    • (1989) Biochem Biophys Res Commun , vol.165 , pp. 1184-1190
    • Nagayama, Y.1    Kaufman, K.D.2    Seto, P.3    Rapoport, B.4
  • 12
    • 0031790855 scopus 로고    scopus 로고
    • A conserved tyrosine residue (Y601) in transmembrane domain 5 of the human thyrotropin receptor serves as a molecular switch to determine G-protein coupling
    • Biebermann H, Schoneberg T, Schulz A, Krause G, Gruters A, Schultz G, Gudermann T 1998 A conserved tyrosine residue (Y601) in transmembrane domain 5 of the human thyrotropin receptor serves as a molecular switch to determine G-protein coupling. FASEB J 12:1461-1471
    • (1998) FASEB J , vol.12 , pp. 1461-1471
    • Biebermann, H.1    Schoneberg, T.2    Schulz, A.3    Krause, G.4    Gruters, A.5    Schultz, G.6    Gudermann, T.7
  • 13
    • 1642618157 scopus 로고    scopus 로고
    • Substitutions of tyrosine 601 in the human thyrotropin receptor result in increase or loss of basal activation of the cyclic adenosine monophosphate pathway and disrupt coupling to Gq/11
    • Arseven OK, Wilkes WP, Jameson JL, Kopp P 2000 Substitutions of tyrosine 601 in the human thyrotropin receptor result in increase or loss of basal activation of the cyclic adenosine monophosphate pathway and disrupt coupling to Gq/11. Thyroid 10:3-10
    • (2000) Thyroid , vol.10 , pp. 3-10
    • Arseven, O.K.1    Wilkes, W.P.2    Jameson, J.L.3    Kopp, P.4
  • 14
    • 0025969701 scopus 로고
    • Thyrotropin-luteinizing hormone/chorionic gonadotropin receptor extracellular domain chimeras as probes for TSH receptor function
    • Nagayama Y, Wadsworth HL, Chazenbalk GD, Russo D, Seto P, Rapoport B 1991 Thyrotropin-luteinizing hormone/chorionic gonadotropin receptor extracellular domain chimeras as probes for TSH receptor function. Proc Natl Acad Sci USA 88:902-905
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 902-905
    • Nagayama, Y.1    Wadsworth, H.L.2    Chazenbalk, G.D.3    Russo, D.4    Seto, P.5    Rapoport, B.6
  • 15
    • 0030013462 scopus 로고    scopus 로고
    • Both the 5′ and 3′ non-coding regions of the thyrotropin receptor messenger RNA influence the level of receptor protein expression in transfected mammalian cells
    • Kakinuma A, Chazenbalk G, Filetti S, McLachlan SM, Rapoport B 1996 Both the 5′ and 3′ non-coding regions of the thyrotropin receptor messenger RNA influence the level of receptor protein expression in transfected mammalian cells. Endocrinology 137:2664-2669
    • (1996) Endocrinology , vol.137 , pp. 2664-2669
    • Kakinuma, A.1    Chazenbalk, G.2    Filetti, S.3    McLachlan, S.M.4    Rapoport, B.5
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0026518857 scopus 로고
    • Role of amino acids 261-418 in proteolytic cleavage of the extracellular region of the human thyrotropin receptor
    • Russo D, Nagayama Y, Chazenbalk GD, Wadsworth HL, Rapoport B 1992 Role of amino acids 261-418 in proteolytic cleavage of the extracellular region of the human thyrotropin receptor. Endocrinology 130:2135-2138
    • (1992) Endocrinology , vol.130 , pp. 2135-2138
    • Russo, D.1    Nagayama, Y.2    Chazenbalk, G.D.3    Wadsworth, H.L.4    Rapoport, B.5
  • 18
    • 0032247323 scopus 로고    scopus 로고
    • The thyrotropin receptor: Interaction with thyrotropin and autoantibodies
    • Rapoport B, Chazenbalk GD, Jaume JC, McLachlan SM 1998 The thyrotropin receptor: Interaction with thyrotropin and autoantibodies. Endocr Rev 19:673-716
    • (1998) Endocr Rev , vol.19 , pp. 673-716
    • Rapoport, B.1    Chazenbalk, G.D.2    Jaume, J.C.3    McLachlan, S.M.4
  • 19
    • 0035013606 scopus 로고    scopus 로고
    • Insight into thyrotropin receptor cleavage by engineering the single polypeptide chain luteinizing hormone receptor into a cleaving, two subunit receptor
    • Chazenbalk GD, McLachlan SM, Chen C-R, Rapoport B 2001 Insight into thyrotropin receptor cleavage by engineering the single polypeptide chain luteinizing hormone receptor into a cleaving, two subunit receptor. Eur J Biochem 268:2261-2269
    • (2001) Eur J Biochem , vol.268 , pp. 2261-2269
    • Chazenbalk, G.D.1    McLachlan, S.M.2    Chen, C.-R.3    Rapoport, B.4
  • 21
    • 0028568641 scopus 로고
    • Cleavage of the thyrotropin receptor does not occur at a classical subtilisin-related proprotein covertase endoproteolytic site
    • Chazenbalk GD, Rapoport B 1994 Cleavage of the thyrotropin receptor does not occur at a classical subtilisin-related proprotein covertase endoproteolytic site. J Biol Chem 269:32209-32213
    • (1994) J Biol Chem , vol.269 , pp. 32209-32213
    • Chazenbalk, G.D.1    Rapoport, B.2
  • 22
    • 0030805829 scopus 로고    scopus 로고
    • Constitutive activation of the TSH receptor by spontaneous mutations affecting the N-terminal extracellular domain
    • Duprez L, Parma J, Costagliola S, Hermans J, Van Sande J, Dumont J, Vassart G 1997 Constitutive activation of the TSH receptor by spontaneous mutations affecting the N-terminal extracellular domain. FEBS Lett 409:469-474
    • (1997) FEBS Lett , vol.409 , pp. 469-474
    • Duprez, L.1    Parma, J.2    Costagliola, S.3    Hermans, J.4    Van Sande, J.5    Dumont, J.6    Vassart, G.7
  • 23
    • 0030830146 scopus 로고    scopus 로고
    • Congenital hyperthyroidism caused by a solitary toxic adenoma harboring a novel somatic mutation (Serine281-Isoleucine) in the extracellular domain of the thyrotropin receptor
    • Kopp P, Muirhead S, Jourdain N, Gu W-X, Jameson JL, Rodd C 1997 Congenital hyperthyroidism caused by a solitary toxic adenoma harboring a novel somatic mutation (Serine281-Isoleucine) in the extracellular domain of the thyrotropin receptor. J Clin Invest 100:1634-1639
    • (1997) J Clin Invest , vol.100 , pp. 1634-1639
    • Kopp, P.1    Muirhead, S.2    Jourdain, N.3    Gu, W.-X.4    Jameson, J.L.5    Rodd, C.6
  • 24
    • 0034987731 scopus 로고    scopus 로고
    • Effects of mutations involving the highly conserved S281HCC motif in the extracellular domain of the thyrotropin (TSH) receptor on TSH binding and constitutive activity
    • Ho SC, Van Sande J, Lefort A, Vassart G, Costagliola S 2001 Effects of mutations involving the highly conserved S281HCC motif in the extracellular domain of the thyrotropin (TSH) receptor on TSH binding and constitutive activity. Endocrinology 142:2760-2767
    • (2001) Endocrinology , vol.142 , pp. 2760-2767
    • Ho, S.C.1    Van Sande, J.2    Lefort, A.3    Vassart, G.4    Costagliola, S.5
  • 25
    • 0037040202 scopus 로고    scopus 로고
    • The ectodomain of the luteinizing hormone receptor interacts with exoloop 2 to constrain the transmembrane region: Studies using chimeric human and fly receptors
    • Nishi S, Nakabayashi K, Kobilka B, Hsueh AJ 2002 The ectodomain of the luteinizing hormone receptor interacts with exoloop 2 to constrain the transmembrane region: studies using chimeric human and fly receptors. J Biol Chem 277:3958-3964
    • (2002) J Biol Chem , vol.277 , pp. 3958-3964
    • Nishi, S.1    Nakabayashi, K.2    Kobilka, B.3    Hsueh, A.J.4
  • 26
    • 0020539875 scopus 로고
    • Trypsin increases the production of cAMP in isolated bovine thyroid cells
    • Knopp J, Stolc V, Tong W 1983 Trypsin increases the production of cAMP in isolated bovine thyroid cells. FEBS Lett 155:47-49
    • (1983) FEBS Lett , vol.155 , pp. 47-49
    • Knopp, J.1    Stolc, V.2    Tong, W.3
  • 27
    • 0020589488 scopus 로고
    • Effects of proteolytic enzymes and protease inhibitors on bovine thyroid adenylate cyclase activity
    • Friedman Y, Wilger J, Crowell D, Burke G 1983 Effects of proteolytic enzymes and protease inhibitors on bovine thyroid adenylate cyclase activity. Endocrinology 112:1674-1679
    • (1983) Endocrinology , vol.112 , pp. 1674-1679
    • Friedman, Y.1    Wilger, J.2    Crowell, D.3    Burke, G.4
  • 28
    • 0025719831 scopus 로고
    • A new structural model for the thyrotropin (TSH) receptor as determined by covalent crosslinking of TSH to the recombinant receptor in intact cells: Evidence for a single polypeptide chain
    • Russo D, Chazenbalk GD, Nagayama Y, Wadsworth HL, Seto P, Rapoport B 1991 A new structural model for the thyrotropin (TSH) receptor as determined by covalent crosslinking of TSH to the recombinant receptor in intact cells: evidence for a single polypeptide chain. Mol Endocrinol 5:1607-1612
    • (1991) Mol Endocrinol , vol.5 , pp. 1607-1612
    • Russo, D.1    Chazenbalk, G.D.2    Nagayama, Y.3    Wadsworth, H.L.4    Seto, P.5    Rapoport, B.6


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