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Volumn 25, Issue 10, 2008, Pages 1037-1044

Glycoprotein hormone receptors in the sea lamprey petromyzon marinus

Author keywords

Cyclostomes; Functional divergence; Glycoprotein hormone receptor; Molecular evolution; Sea lamprey

Indexed keywords

CELL SURFACE RECEPTOR; GLYCOPROTEIN;

EID: 56849105071     PISSN: 02890003     EISSN: 02890003     Source Type: Journal    
DOI: 10.2108/zsj.25.1037     Document Type: Article
Times cited : (12)

References (51)
  • 1
    • 23044505437 scopus 로고    scopus 로고
    • Learning new tricks from an old dog: The processing of the intracellular precursor of the luteinizing hormone receptor (LHR) into the mature cell-surface LHR is a regulated process
    • Ascoli M (2005) Learning new tricks from an old dog: the processing of the intracellular precursor of the luteinizing hormone receptor (LHR) into the mature cell-surface LHR is a regulated process. Endocrinology 146: 3221-3223
    • (2005) Endocrinology , vol.146 , pp. 3221-3223
    • Ascoli, M.1
  • 2
    • 33947508030 scopus 로고    scopus 로고
    • Comparison of sequence-based and structure-based phylogenetic trees of homologous proteins: Inferences on protein evolution
    • Balaji S, Srinivasan N (2007) Comparison of sequence-based and structure-based phylogenetic trees of homologous proteins: inferences on protein evolution. J Biosci 32: 83-96
    • (2007) J Biosci , vol.32 , pp. 83-96
    • Balaji, S.1    Srinivasan, N.2
  • 3
    • 33748925566 scopus 로고    scopus 로고
    • A protein evolution model with independent sites that reproduces sitespecific amino acid distributions from the protein data bank
    • Bastolla U, Porto M, Roman HE, Vendruscolo M (2006) A protein evolution model with independent sites that reproduces sitespecific amino acid distributions from the protein data bank. BMC Evol Biol 6: 43
    • (2006) BMC Evol Biol , vol.6 , pp. 43
    • Bastolla, U.1    Porto, M.2    Roman, H.E.3    Vendruscolo, M.4
  • 4
    • 0035812291 scopus 로고    scopus 로고
    • Molecular cloning, sequence and expression of follicle-stimulating hormone receptor in the lizard Podarcis sicula
    • Borrelli L, Stasio RD, Parisi E, Filosa S (2001) Molecular cloning, sequence and expression of follicle-stimulating hormone receptor in the lizard Podarcis sicula. Gene 275: 149-156
    • (2001) Gene , vol.275 , pp. 149-156
    • Borrelli, L.1    Stasio, R.D.2    Parisi, E.3    Filosa, S.4
  • 5
    • 0030437795 scopus 로고    scopus 로고
    • Structural and functional diversity in the leucine-rich repeat family of proteins
    • Buchanan SG, Gay NJ (1996) Structural and functional diversity in the leucine-rich repeat family of proteins. Prog Biophys Mol Biol 65: 1-44
    • (1996) Prog Biophys Mol Biol , vol.65 , pp. 1-44
    • Buchanan, S.G.1    Gay, N.J.2
  • 7
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • Castresana J (2000) Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis. Mol Biol Evol 17:540-552
    • (2000) Mol Biol Evol , vol.17 , pp. 540-552
    • Castresana, J.1
  • 8
    • 0037084011 scopus 로고    scopus 로고
    • Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors
    • Costagliola S, Panneels V, Bonomi M, Koch J, Many MC, Smits G, Vassart G (2002) Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors. EMBO J 21: 504-513
    • (2002) EMBO J , vol.21 , pp. 504-513
    • Costagliola, S.1    Panneels, V.2    Bonomi, M.3    Koch, J.4    Many, M.C.5    Smits, G.6    Vassart, G.7
  • 9
    • 14644430471 scopus 로고    scopus 로고
    • Probcons: Probabilistic consistency-based multiple sequence alignment
    • Do CB, Mahabhashyam MSP, Brudno M, Batzoglou S (2005) Probcons: probabilistic consistency-based multiple sequence alignment. Genome Res 15: 330-340
    • (2005) Genome Res , vol.15 , pp. 330-340
    • Do, C.B.1    Mahabhashyam, M.S.P.2    Brudno, M.3    Batzoglou, S.4
  • 10
    • 0031916977 scopus 로고    scopus 로고
    • The luteinizing hormone receptor
    • Dufau ML (1998) The luteinizing hormone receptor. Annu Rev Physiol 60: 461-496
    • (1998) Annu Rev Physiol , vol.60 , pp. 461-496
    • Dufau, M.L.1
  • 11
    • 3042666256 scopus 로고    scopus 로고
    • Muscle: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) Muscle: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792-1797
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 12
    • 0033855185 scopus 로고    scopus 로고
    • Molecular cloning, genomic organization, developmental regulation, and a knock-out mutant of a novel leu-rich repeats-containing g protein-coupled receptor (dLGR-2) from Drosophila melanogaster
    • Eriksen KK, Hauser F, Schiott M, Pedersen KM, Sondergaard L, Grimmelikhuijzen CJ (2000) Molecular cloning, genomic organization, developmental regulation, and a knock-out mutant of a novel leu-rich repeats-containing g protein-coupled receptor (dLGR-2) from Drosophila melanogaster. Genome Res 10: 924-938
    • (2000) Genome Res , vol.10 , pp. 924-938
    • Eriksen, K.K.1    Hauser, F.2    Schiott, M.3    Pedersen, K.M.4    Sondergaard, L.5    Grimmelikhuijzen, C.J.6
  • 13
    • 12744280744 scopus 로고    scopus 로고
    • Structure of human follicle-stimulating hormone in complex with its receptor
    • Fan QR, Hendrickson WA (2005) Structure of human follicle-stimulating hormone in complex with its receptor. Nature 433: 269-277
    • (2005) Nature , vol.433 , pp. 269-277
    • Fan, Q.R.1    Hendrickson, W.A.2
  • 14
    • 0024152983 scopus 로고
    • Phylogenies from molecular sequences: Inference and reliability
    • Felsenstein J (1988) Phylogenies from molecular sequences: inference and reliability. Annu Rev Genet 22: 521-565
    • (1988) Annu Rev Genet , vol.22 , pp. 521-565
    • Felsenstein, J.1
  • 15
    • 0035105355 scopus 로고    scopus 로고
    • Three-dimensional structure of human follicle-stimulating hormone
    • Fox KM, Dias JA, Roey PV (2001) Three-dimensional structure of human follicle-stimulating hormone. Mol Endocrinol 15: 378-389
    • (2001) Mol Endocrinol , vol.15 , pp. 378-389
    • Fox, K.M.1    Dias, J.A.2    Roey, P.V.3
  • 16
    • 55749086789 scopus 로고    scopus 로고
    • A sea lamprey glycoprotein hormone receptor similar with gnathostome thyrotropin hormone receptor
    • Freamat M, Sower SA (2008) A sea lamprey glycoprotein hormone receptor similar with gnathostome thyrotropin hormone receptor. J Mol Endocrinol 41: 219-228
    • (2008) J Mol Endocrinol , vol.41 , pp. 219-228
    • Freamat, M.1    Sower, S.A.2
  • 17
    • 33747890722 scopus 로고    scopus 로고
    • Identification and cloning of a glycoprotein hormone receptor from sea lamprey, Petromyzon marinus
    • Freamat M, Kawauchi H, Nozaki M, Sower SA (2006) Identification and cloning of a glycoprotein hormone receptor from sea lamprey, Petromyzon marinus. J Mol Endocrinol 37: 135-146
    • (2006) J Mol Endocrinol , vol.37 , pp. 135-146
    • Freamat, M.1    Kawauchi, H.2    Nozaki, M.3    Sower, S.A.4
  • 18
    • 33750456225 scopus 로고    scopus 로고
    • A lamprey from the devonian period of South Africa
    • Gess RW, Coates Ml, Rubidge BS (2006) A lamprey from the devonian period of South Africa. Nature 443: 981-984
    • (2006) Nature , vol.443 , pp. 981-984
    • Gess, R.W.1    Coates, M.2    Rubidge, B.S.3
  • 19
    • 0030852648 scopus 로고    scopus 로고
    • Novel insights into the molecular mechanisms of human thyrotropin action: Structural, physiological, and therapeutic implications for the glycoprotein hormone family
    • Grossmann M, Weintraub BD, Szkudlinski MW (1997) Novel insights into the molecular mechanisms of human thyrotropin action: structural, physiological, and therapeutic implications for the glycoprotein hormone family. Endocr Rev 18: 476-501
    • (1997) Endocr Rev , vol.18 , pp. 476-501
    • Grossmann, M.1    Weintraub, B.D.2    Szkudlinski, M.W.3
  • 20
    • 0026666278 scopus 로고
    • 2+ mobilization. Studies with the cloned murine luteinizing hormone receptor expressed in L cells
    • 2+ mobilization. Studies with the cloned murine luteinizing hormone receptor expressed in L cells. J Biol Chem 267: 4479-4488
    • (1992) J Biol Chem , vol.267 , pp. 4479-4488
    • Gudermann, T.1    Birnbaumer, M.2    Birnbaumer, L.3
  • 21
    • 0031033312 scopus 로고    scopus 로고
    • Molecular cloning, genomic organization, and developmental regulation of a novel receptor from Drosophila melanogaster structurally related to members of the thyroid-stimulating hormone, folliclestimulating hormone, luteinizing hormone/choriogonadotropin receptor family from mammals
    • Hauser F, Nothacker HP, Grimmelikhuijzen CJ (1997) Molecular cloning, genomic organization, and developmental regulation of a novel receptor from Drosophila melanogaster structurally related to members of the thyroid-stimulating hormone, folliclestimulating hormone, luteinizing hormone/choriogonadotropin receptor family from mammals. J Biol Chem 272: 1002-1010
    • (1997) J Biol Chem , vol.272 , pp. 1002-1010
    • Hauser, F.1    Nothacker, H.P.2    Grimmelikhuijzen, C.J.3
  • 22
    • 0028598861 scopus 로고
    • Gene duplications and the origins of vertebrate development
    • Holland PW, Garcia-Fernandez J, Williams NA, Sidow A (1994) Gene duplications and the origins of vertebrate development. Development 120 (Suppl): 125-133
    • (1994) Development , vol.120 , Issue.SUPPL. , pp. 125-133
    • Holland, P.W.1    Garcia-Fernandez, J.2    Williams, N.A.3    Sidow, A.4
  • 23
    • 33846861518 scopus 로고    scopus 로고
    • Lgr4 regulates the postnatal development and integrity of male reproductive tracts in mice
    • Hoshii T, Takeo T, Nakagata N, Takeya M, Araki K, Yamamura K-l (2007) Lgr4 regulates the postnatal development and integrity of male reproductive tracts in mice. Biol Reprod 76: 303-313
    • (2007) Biol Reprod , vol.76 , pp. 303-313
    • Hoshii, T.1    Takeo, T.2    Nakagata, N.3    Takeya, M.4    Araki, K.5    Yamamura, K.-L.6
  • 24
    • 0000437998 scopus 로고    scopus 로고
    • Characterization of two LGR genes homologous to gonadotropin and thyrotropin receptors with extracellular leucine-rich repeats and a G protein-coupled, seven-transmembrane region
    • Hsu SY, Liang SG, Hsueh AJ (1998) Characterization of two LGR genes homologous to gonadotropin and thyrotropin receptors with extracellular leucine-rich repeats and a G protein-coupled, seven-transmembrane region. Mol Endocrinol 12: 1830-1845
    • (1998) Mol Endocrinol , vol.12 , pp. 1830-1845
    • Hsu, S.Y.1    Liang, S.G.2    Hsueh, A.J.3
  • 25
    • 33750447326 scopus 로고    scopus 로고
    • Palaeontology: Modern look for ancient lamprey
    • Janvier P (2006) Palaeontology: modern look for ancient lamprey. Nature 443: 921-924
    • (2006) Nature , vol.443 , pp. 921-924
    • Janvier, P.1
  • 26
    • 0035807886 scopus 로고    scopus 로고
    • A likelihood ratio test for evolutionary rate shifts and functional divergence among proteins
    • Knudsen B, Miyamoto MM (2001) A likelihood ratio test for evolutionary rate shifts and functional divergence among proteins. Proc Natl Acad Sci USA 98: 14512-14517
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14512-14517
    • Knudsen, B.1    Miyamoto, M.M.2
  • 27
    • 0034457910 scopus 로고    scopus 로고
    • The nematode leucine-rich repeat-containing, G protein-coupled receptor (LGR) protein homologous to vertebrate gonadotropin and thyrotropin receptors is constitutively active in mammalian cells
    • Kudo M, Chen T, Nakabayashi K, Hsu SY, Hsueh AJ (2000) The nematode leucine-rich repeat-containing, G protein-coupled receptor (LGR) protein homologous to vertebrate gonadotropin and thyrotropin receptors is constitutively active in mammalian cells. Mol Endocrinol 14: 272-284
    • (2000) Mol Endocrinol , vol.14 , pp. 272-284
    • Kudo, M.1    Chen, T.2    Nakabayashi, K.3    Hsu, S.Y.4    Hsueh, A.J.5
  • 28
    • 0034982737 scopus 로고    scopus 로고
    • Piscine glycoprotein hormone (gonadotropin and thyrotropin) receptors: A review of recent developments
    • Kumar RS, Trant JM (2001) Piscine glycoprotein hormone (gonadotropin and thyrotropin) receptors: a review of recent developments. Comp Biochem Physiol B 129: 347-355
    • (2001) Comp Biochem Physiol B , vol.129 , pp. 347-355
    • Kumar, R.S.1    Trant, J.M.2
  • 29
    • 31144442881 scopus 로고    scopus 로고
    • Automatic assessment of alignment quality
    • Lassmann T, Sonnhammer ELL (2005) Automatic assessment of alignment quality. Nucleic Acids Res 33: 7120-7128
    • (2005) Nucleic Acids Res , vol.33 , pp. 7120-7128
    • Lassmann, T.1    Sonnhammer, E.L.L.2
  • 30
    • 26444504861 scopus 로고    scopus 로고
    • Chimeric GNRH-LH receptors and LH receptors lacking C-terminus palmitoylation sites do not localize to plasma membrane rafts
    • Lei Y, Hagen GM, Smith SML, Barisas BG, Roess DA (2005) Chimeric GNRH-LH receptors and LH receptors lacking C-terminus palmitoylation sites do not localize to plasma membrane rafts. Biochem Bioph Res Co 337: 430-434
    • (2005) Biochem Bioph Res Co , vol.337 , pp. 430-434
    • Lei, Y.1    Hagen, G.M.2    Smith, S.M.L.3    Barisas, B.G.4    Roess, D.A.5
  • 32
    • 0015231127 scopus 로고
    • Structure of the porcine LH- and FSH-releasing hormone, i. The proposed amino acid sequence
    • Matsuo H, Baba Y, Nair RM, Arimura A, Schally AV (1971) Structure of the porcine LH- and FSH-releasing hormone, i. The proposed amino acid sequence. Biochem Bioph Res Co 43: 1334-1339
    • (1971) Biochem Bioph Res Co , vol.43 , pp. 1334-1339
    • Matsuo, H.1    Baba, Y.2    Nair, R.M.3    Arimura, A.4    Schally, A.V.5
  • 33
    • 43049109876 scopus 로고    scopus 로고
    • The thyrotropin receptor hinge region is not simply a scaffold for the leucine-rich domain but contributes to ligand binding and signal transduction
    • Mizutori Y, Chen C-R, McLachlan SM, Rapoport B (2008) The thyrotropin receptor hinge region is not simply a scaffold for the leucine-rich domain but contributes to ligand binding and signal transduction. Mol Endocrinol 22: 1171-1182
    • (2008) Mol Endocrinol , vol.22 , pp. 1171-1182
    • Mizutori, Y.1    Chen, C.-R.2    McLachlan, S.M.3    Rapoport, B.4
  • 34
    • 0016819546 scopus 로고
    • Role of carbohydrate of human chorionic gonadotropin in the mechanism of hormone action
    • Moyle WR, Bahl OP, Marz L (1975) Role of carbohydrate of human chorionic gonadotropin in the mechanism of hormone action. J Biol Chem 250: 9163-9169
    • (1975) J Biol Chem , vol.250 , pp. 9163-9169
    • Moyle, W.R.1    Bahl, O.P.2    Marz, L.3
  • 37
    • 0036259465 scopus 로고    scopus 로고
    • Thyrostimulin, a heterodimer of two new human glycoprotein hormone subunits, activates the thyroidstimulating hormone receptor
    • Nakabayashi K, Matsumi H, Bhalla A, Bae J, Mosselman S, Hsu SY, Hsueh AJW (2002) Thyrostimulin, a heterodimer of two new human glycoprotein hormone subunits, activates the thyroidstimulating hormone receptor. J Clin Invest 109: 1445-1452
    • (2002) J Clin Invest , vol.109 , pp. 1445-1452
    • Nakabayashi, K.1    Matsumi, H.2    Bhalla, A.3    Bae, J.4    Mosselman, S.5    Hsu, S.Y.6    Hsueh, A.J.W.7
  • 38
    • 0027751626 scopus 로고
    • Molecular cloning of a novel, putative G protein-coupled receptor from sea anemones structurally related to members of the FSH, TSH, LH/CG receptor family from mammals
    • Nothacker HP, Grimmelikhuijzen CJ (1993) Molecular cloning of a novel, putative G protein-coupled receptor from sea anemones structurally related to members of the FSH, TSH, LH/CG receptor family from mammals. Biochem Biophys Res Commun 197: 1062-1069
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 1062-1069
    • Nothacker, H.P.1    Grimmelikhuijzen, C.J.2
  • 40
    • 56849105663 scopus 로고    scopus 로고
    • Characterization of novel splice variants of LGR7 and LGR8 reveals that receptor signaling is mediated by their unique low density lipoprotein class a modules
    • Scott DJ, Layfield S, Yan Y, Sudo S, Hsueh AJW, Tregear GW, Bathgate RAD (2006) Characterization of novel splice variants of LGR7 and LGR8 reveals that receptor signaling is mediated by their unique low density lipoprotein class a modules. Mol Endocrinol 20: 1880-1893
    • (2006) Mol Endocrinol , vol.20 , pp. 1880-1893
    • Scott, D.J.1    Layfield, S.2    Yan, Y.3    Sudo, S.4    Hsueh, A.J.W.5    Tregear, G.W.6    Bathgate, R.A.D.7
  • 41
    • 0037387451 scopus 로고    scopus 로고
    • Significantly different patterns of amino acid replacement after gene duplication as compared to after speciation
    • Seoighe C, Johnston CR, Shields DC (2003) Significantly different patterns of amino acid replacement after gene duplication as compared to after speciation. Mol Biol Evol 20: 484-490
    • (2003) Mol Biol Evol , vol.20 , pp. 484-490
    • Seoighe, C.1    Johnston, C.R.2    Shields, D.C.3
  • 42
    • 0030473920 scopus 로고    scopus 로고
    • Gen(om)e duplications in the evolution of early vertebrates
    • Sidow A (1996) Gen(om)e duplications in the evolution of early vertebrates. Curr Opin Genet Dev 6: 715-722
    • (1996) Curr Opin Genet Dev , vol.6 , pp. 715-722
    • Sidow, A.1
  • 43
    • 0031457992 scopus 로고    scopus 로고
    • The follicle-stimulating hormone receptor: Biochemistry, molecular biology, physiology, and pathophysiology
    • Simoni M, Gromoll J, Nieschlag E (1997) The follicle-stimulating hormone receptor: biochemistry, molecular biology, physiology, and pathophysiology. Endocr Rev 18: 739-773
    • (1997) Endocr Rev , vol.18 , pp. 739-773
    • Simoni, M.1    Gromoll, J.2    Nieschlag, E.3
  • 45
    • 0036083401 scopus 로고    scopus 로고
    • Thyroidstimulating hormone and thyroid-stimulating hormone receptor structure-function relationships
    • Szkudlinski MW, Fremont V, Ronin C, Weintraub BD (2002) Thyroidstimulating hormone and thyroid-stimulating hormone receptor structure-function relationships. Physiol Rev 82: 473-502
    • (2002) Physiol Rev , vol.82 , pp. 473-502
    • Szkudlinski, M.W.1    Fremont, V.2    Ronin, C.3    Weintraub, B.D.4
  • 46
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 47
    • 0037230248 scopus 로고    scopus 로고
    • Cloning and functional characterization of a gonadal luteinizing hormone receptor complementary DNA from the African catfish (Clarias gariepinus)
    • Vischer HF, Bogerd J (2003a) Cloning and functional characterization of a gonadal luteinizing hormone receptor complementary DNA from the African catfish (Clarias gariepinus). Biol Reprod 68: 262-271
    • (2003) Biol Reprod , vol.68 , pp. 262-271
    • Vischer, H.F.1    Bogerd, J.2
  • 48
    • 0038363823 scopus 로고    scopus 로고
    • Cloning and functional characterization of a testicular TSH receptor cDNA from the African catfish (Clarias gariepinus)
    • Vischer HF, Bogerd J (2003b) Cloning and functional characterization of a testicular TSH receptor cDNA from the African catfish (Clarias gariepinus). J Mol Endocrinol 30: 227-238
    • (2003) J Mol Endocrinol , vol.30 , pp. 227-238
    • Vischer, H.F.1    Bogerd, J.2
  • 50
    • 0033973296 scopus 로고    scopus 로고
    • Three different turkey luteinizing hormone receptor (tLH-R) isoforms I: Characterization of alternatively spliced tLH-R isoforms and their regulated expression in diverse tissues
    • You S, Kim H, Hsu CC, Halawani MEE, Foster DN (2000b) Three different turkey luteinizing hormone receptor (tLH-R) isoforms I: Characterization of alternatively spliced tLH-R isoforms and their regulated expression in diverse tissues. Biol Reprod 62: 108-116
    • (2000) Biol Reprod , vol.62 , pp. 108-116
    • You, S.1    Kim, H.2    Hsu, C.C.3    Halawani, M.E.E.4    Foster, D.N.5
  • 51
    • 0033971096 scopus 로고    scopus 로고
    • Three different turkey luteinizing hormone receptor (tLH-R) isoforms II: Characterization of differentially regulated tLH-R messenger ribonucleic acid isoforms in the ovary
    • You S, Kim H, Halawani MEE, Foster DN (2000a) Three different turkey luteinizing hormone receptor (tLH-R) isoforms II: Characterization of differentially regulated tLH-R messenger ribonucleic acid isoforms in the ovary. Biol Reprod 62: 117-124
    • (2000) Biol Reprod , vol.62 , pp. 117-124
    • You, S.1    Kim, H.2    Halawani, M.E.E.3    Foster, D.N.4


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