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Volumn 317, Issue 1-2, 2010, Pages 1-7

T3 acutely increases GH mRNA translation rate and GH secretion in hypothyroid rats

Author keywords

Cytoskeleton; eEF1A; GH; Nongenomic action; Polysomes; T3

Indexed keywords

ACTIN; CYCLOPHILIN; F ACTIN; G ACTIN; GROWTH HORMONE; INITIATION FACTOR 1A; LIOTHYRONINE; MESSENGER RNA; SOMATOMEDIN; THYROID HORMONE;

EID: 74749083746     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2009.12.005     Document Type: Article
Times cited : (22)

References (49)
  • 1
    • 0029936236 scopus 로고    scopus 로고
    • Thyroid hormone regulation of germ cell-specific alpha expression during metamorphosis of Xenopus laevis
    • Abdallah B., Sachs L., Hourdry J., Wegnez M., Denis H., Demeneix B., and Mazabraud A. Thyroid hormone regulation of germ cell-specific alpha expression during metamorphosis of Xenopus laevis. Int. J. Dev. Biol. 40 (1996) 507-514
    • (1996) Int. J. Dev. Biol. , vol.40 , pp. 507-514
    • Abdallah, B.1    Sachs, L.2    Hourdry, J.3    Wegnez, M.4    Denis, H.5    Demeneix, B.6    Mazabraud, A.7
  • 2
    • 0032851816 scopus 로고    scopus 로고
    • Identification of 3′UTR region implicated in tau mRNA stabilization in neuronal cells
    • Aronov S., Marx R., and Ginzburg I. Identification of 3′UTR region implicated in tau mRNA stabilization in neuronal cells. J. Mol. Neurosci. 12 (1999) 131-145
    • (1999) J. Mol. Neurosci. , vol.12 , pp. 131-145
    • Aronov, S.1    Marx, R.2    Ginzburg, I.3
  • 3
    • 0034468051 scopus 로고    scopus 로고
    • Triiodothyronine stimulates the release of membrane-bound alkaline phosphatase in osteoblastic cells
    • Banovac K., and Koren E. Triiodothyronine stimulates the release of membrane-bound alkaline phosphatase in osteoblastic cells. Calcif. Tissue Int. 7 (2000) 460-465
    • (2000) Calcif. Tissue Int. , vol.7 , pp. 460-465
    • Banovac, K.1    Koren, E.2
  • 4
    • 66449091608 scopus 로고    scopus 로고
    • Potential role of growth hormone in impairment of insulin signaling in skeletal muscle, adipose tissue, and liver of rats chronically treated with arginine
    • Barbosa T.C., de Carvalho J.E., Poyares L.L., Bordin S., Machado U.F., and Nunes M.T. Potential role of growth hormone in impairment of insulin signaling in skeletal muscle, adipose tissue, and liver of rats chronically treated with arginine. Endocrinology 150 (2009) 2080-2086
    • (2009) Endocrinology , vol.150 , pp. 2080-2086
    • Barbosa, T.C.1    de Carvalho, J.E.2    Poyares, L.L.3    Bordin, S.4    Machado, U.F.5    Nunes, M.T.6
  • 5
    • 22144494707 scopus 로고    scopus 로고
    • Integrin alphaVbeta3 contains a cell surface receptor site for thyroid hormone that is linked to activation of mitogen-activated protein kinase and induction of angiogenesis
    • Bergh J.J., Lin H.Y., Lansing L., Mohamed S.N., Davis F.B., Mousa S., and Davis P.J. Integrin alphaVbeta3 contains a cell surface receptor site for thyroid hormone that is linked to activation of mitogen-activated protein kinase and induction of angiogenesis. Endocrinology 146 (2005) 2864-2871
    • (2005) Endocrinology , vol.146 , pp. 2864-2871
    • Bergh, J.J.1    Lin, H.Y.2    Lansing, L.3    Mohamed, S.N.4    Davis, F.B.5    Mousa, S.6    Davis, P.J.7
  • 6
    • 34548439796 scopus 로고    scopus 로고
    • Thyroid Hormone rapidly stimulates alveolar Na, K-ATPase by activation of phosphatidylinositol 3-kinase
    • Bhargava M., Lei J., Mariash C.N., and Ingbar D.H. Thyroid Hormone rapidly stimulates alveolar Na, K-ATPase by activation of phosphatidylinositol 3-kinase. Curr. Opin. Endocrinol. Diabetes Obes. 14 (2007) 416-420
    • (2007) Curr. Opin. Endocrinol. Diabetes Obes. , vol.14 , pp. 416-420
    • Bhargava, M.1    Lei, J.2    Mariash, C.N.3    Ingbar, D.H.4
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162 (1987) 156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 9
    • 0023182842 scopus 로고
    • The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum
    • Cheng S.Y., Gong Q.H., Parkison C., Robinson E.A., Appella E., Merlino G.T., and Pastan I. The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum. J. Biol. Chem. 262 (1987) 11221-11227
    • (1987) J. Biol. Chem. , vol.262 , pp. 11221-11227
    • Cheng, S.Y.1    Gong, Q.H.2    Parkison, C.3    Robinson, E.A.4    Appella, E.5    Merlino, G.T.6    Pastan, I.7
  • 10
    • 0019136848 scopus 로고
    • Effects of neonatal hypo- and hyperthyroidism on pituitary growth hormone content in the rat
    • Coulombe P., Ruel J., and Dussault J.H. Effects of neonatal hypo- and hyperthyroidism on pituitary growth hormone content in the rat. Endocrinology 7 (1980) 2027-2033
    • (1980) Endocrinology , vol.7 , pp. 2027-2033
    • Coulombe, P.1    Ruel, J.2    Dussault, J.H.3
  • 11
    • 0029907826 scopus 로고    scopus 로고
    • Nongenomic actions of thyroid hormone
    • Davis P.J., and Davis F.B. Nongenomic actions of thyroid hormone. Thyroid 6 (1996) 497-504
    • (1996) Thyroid , vol.6 , pp. 497-504
    • Davis, P.J.1    Davis, F.B.2
  • 12
    • 0036018267 scopus 로고    scopus 로고
    • Nongenomic actions of thyroid hormone on the heart
    • Davis P.J., and Davis F.B. Nongenomic actions of thyroid hormone on the heart. Thyroid 12 (2002) 459-466
    • (2002) Thyroid , vol.12 , pp. 459-466
    • Davis, P.J.1    Davis, F.B.2
  • 13
  • 14
    • 0033569627 scopus 로고    scopus 로고
    • Vesicle transport: the role of actin filaments and myosin motors
    • DePina A.S., and Langford G.M. Vesicle transport: the role of actin filaments and myosin motors. Microsc. Res. Tech. 47 (1999) 93-106
    • (1999) Microsc. Res. Tech. , vol.47 , pp. 93-106
    • DePina, A.S.1    Langford, G.M.2
  • 15
    • 0041659182 scopus 로고    scopus 로고
    • Actin remodeling to facilitate membrane fusion
    • Eitzen G. Actin remodeling to facilitate membrane fusion. Biochim. Biophys. Acta 1641 (2003) 175-181
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 175-181
    • Eitzen, G.1
  • 16
    • 33644963942 scopus 로고    scopus 로고
    • Multiplex bead array assay: performance evaluation and comparison of sensitivity to ELISA
    • Elshal M.F., and McCoy J.P. Multiplex bead array assay: performance evaluation and comparison of sensitivity to ELISA. Methods 38 (2006) 317-323
    • (2006) Methods , vol.38 , pp. 317-323
    • Elshal, M.F.1    McCoy, J.P.2
  • 17
    • 0026660558 scopus 로고
    • Dissociation of actin polymerization and enzyme inactivation in the hormonal regulation of type II iodothyronine 5′-deiodinase activity in astrocytes
    • Farwell A.P., and Leonard J.L. Dissociation of actin polymerization and enzyme inactivation in the hormonal regulation of type II iodothyronine 5′-deiodinase activity in astrocytes. Endocrinology 131 (1992) 721-728
    • (1992) Endocrinology , vol.131 , pp. 721-728
    • Farwell, A.P.1    Leonard, J.L.2
  • 19
    • 39149111232 scopus 로고    scopus 로고
    • Message on the web: mRNA and ER co-trafficking
    • Gerst J.E. Message on the web: mRNA and ER co-trafficking. Trends Cell. Biol. 18 (2008) 68-76
    • (2008) Trends Cell. Biol. , vol.18 , pp. 68-76
    • Gerst, J.E.1
  • 20
    • 33751503710 scopus 로고    scopus 로고
    • Thyroid hormone induction of actin polymerization in somatotrophs of hypothyroid rats: potential repercussions in growth hormone synthesis and secretion
    • Goulart da Silva F., Giannocco G., Santos M.F., and Nunes M.T. Thyroid hormone induction of actin polymerization in somatotrophs of hypothyroid rats: potential repercussions in growth hormone synthesis and secretion. Endocrinology 147 (2006) 5777-5785
    • (2006) Endocrinology , vol.147 , pp. 5777-5785
    • Goulart da Silva, F.1    Giannocco, G.2    Santos, M.F.3    Nunes, M.T.4
  • 21
    • 10344225666 scopus 로고    scopus 로고
    • Subcellular localization of multiple PREP2 isoforms is regulated by actin, tubulin, and nuclear export
    • Haller K., Rambaldi I., Daniels E., and Featherstone M. Subcellular localization of multiple PREP2 isoforms is regulated by actin, tubulin, and nuclear export. J. Biol. Chem. 279 (2004) 49384-49394
    • (2004) J. Biol. Chem. , vol.279 , pp. 49384-49394
    • Haller, K.1    Rambaldi, I.2    Daniels, E.3    Featherstone, M.4
  • 22
    • 0025021268 scopus 로고
    • Differential and tissue-specific regulation of the multiple rat c-erbA messenger
    • Hodin R.A., Lazar M.A., and Chin W.W. Differential and tissue-specific regulation of the multiple rat c-erbA messenger. J. Clin. Invest. 85 (1990) 101-105
    • (1990) J. Clin. Invest. , vol.85 , pp. 101-105
    • Hodin, R.A.1    Lazar, M.A.2    Chin, W.W.3
  • 23
    • 0030272844 scopus 로고    scopus 로고
    • The compartmentalization of protein synthesis: importance of cytoskeleton and role in mRNA targeting
    • Hovland R., Hesketh J.E., and Pryme I.F. The compartmentalization of protein synthesis: importance of cytoskeleton and role in mRNA targeting. Int. J. Biochem. Cell. Biol. 28 (1996) 1089-1105
    • (1996) Int. J. Biochem. Cell. Biol. , vol.28 , pp. 1089-1105
    • Hovland, R.1    Hesketh, J.E.2    Pryme, I.F.3
  • 24
    • 41149126160 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of five different elongation factor 1 alpha genes in the flatfish Senegalese sole (Solea senegalensis Kaup): differential gene expression and thyroid hormones dependence during metamorphosis
    • Infante C., Asensio E., Cañavate J.P., and Manchado M. Molecular characterization and expression analysis of five different elongation factor 1 alpha genes in the flatfish Senegalese sole (Solea senegalensis Kaup): differential gene expression and thyroid hormones dependence during metamorphosis. BMC Mol. Biol. 9 (2008) 19-35
    • (2008) BMC Mol. Biol. , vol.9 , pp. 19-35
    • Infante, C.1    Asensio, E.2    Cañavate, J.P.3    Manchado, M.4
  • 25
    • 0024267957 scopus 로고
    • Pulsatile intravenous growth hormone (GH) infusion to hypophysectomized rats increases insulin-like growth factor I messenger ribonucleic acid in skeletal tissues more efficiently than continuous GH infusion
    • Isgaard J., Carlsson L., Isaksson O.G., and Jansson J.O. Pulsatile intravenous growth hormone (GH) infusion to hypophysectomized rats increases insulin-like growth factor I messenger ribonucleic acid in skeletal tissues more efficiently than continuous GH infusion. Endocrinology 123 (1988) 2605-2610
    • (1988) Endocrinology , vol.123 , pp. 2605-2610
    • Isgaard, J.1    Carlsson, L.2    Isaksson, O.G.3    Jansson, J.O.4
  • 26
    • 0035320036 scopus 로고    scopus 로고
    • mRNA localization: message on the move
    • Jansen R.P. mRNA localization: message on the move. Nat. Rev. Mol. Cell. Biol. 2 (2001) 247-256
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 247-256
    • Jansen, R.P.1
  • 27
    • 3943080710 scopus 로고    scopus 로고
    • The molecular mechanics of eukaryotic translation
    • Kapp L.D., and Lorsch J.R. The molecular mechanics of eukaryotic translation. Annu. Rev. Biochem. 73 (2004) 657-704
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 657-704
    • Kapp, L.D.1    Lorsch, J.R.2
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 34547959158 scopus 로고    scopus 로고
    • Actin in membrane trafficking
    • Lanzetti L. Actin in membrane trafficking. Curr. Opin. Cell. Biol. 19 (2007) 453-458
    • (2007) Curr. Opin. Cell. Biol. , vol.19 , pp. 453-458
    • Lanzetti, L.1
  • 30
    • 0036175770 scopus 로고    scopus 로고
    • Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: implications for anchoring mRNA in cell protrusions
    • Liu G., Grant W.M., Persky D., Latham Jr. V.M., Singer R.H., and Condeelis J. Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: implications for anchoring mRNA in cell protrusions. Mol. Biol. Cell. 13 (2002) 579-592
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 579-592
    • Liu, G.1    Grant, W.M.2    Persky, D.3    Latham Jr., V.M.4    Singer, R.H.5    Condeelis, J.6
  • 31
    • 0030799897 scopus 로고    scopus 로고
    • The 3′ untranslated region plays a role in the targeting of metallothionein-I mRNA to the perinuclear cytoplasm and cytoskeletal-bound polysomes
    • Mahon P., Partridge K., Beattie J.H., Glover L.A., and Hesketh J.E. The 3′ untranslated region plays a role in the targeting of metallothionein-I mRNA to the perinuclear cytoplasm and cytoskeletal-bound polysomes. Biochim. Biophys. Acta 1358 (1997) 153-162
    • (1997) Biochim. Biophys. Acta , vol.1358 , pp. 153-162
    • Mahon, P.1    Partridge, K.2    Beattie, J.H.3    Glover, L.A.4    Hesketh, J.E.5
  • 33
    • 0033799989 scopus 로고    scopus 로고
    • Differential role of tyrosine phosphorylation in adhesion-induced transcription, mRNA stability, and cytoskeletal organization in human monocytes
    • Mondal K., Sirenko O.I., Lofquist A.K., Morris J.S., Haskill J.S., and Watson J.M. Differential role of tyrosine phosphorylation in adhesion-induced transcription, mRNA stability, and cytoskeletal organization in human monocytes. J. Leukoc. Biol. 67 (2000) 216-225
    • (2000) J. Leukoc. Biol. , vol.67 , pp. 216-225
    • Mondal, K.1    Sirenko, O.I.2    Lofquist, A.K.3    Morris, J.S.4    Haskill, J.S.5    Watson, J.M.6
  • 35
    • 0020688901 scopus 로고
    • Modulation of poly(A)(+)mRNA-metabolizing and transporting systems under special consideration of microtubule protein and actin
    • Müller W.E., Bernd A., and Schröder H.C. Modulation of poly(A)(+)mRNA-metabolizing and transporting systems under special consideration of microtubule protein and actin. Mol. Cell. Biochem. 54 (1983) 197-220
    • (1983) Mol. Cell. Biochem. , vol.54 , pp. 197-220
    • Müller, W.E.1    Bernd, A.2    Schröder, H.C.3
  • 36
    • 0025112854 scopus 로고
    • Tales of poly(A): a review
    • Munroe D., and Jacobson A. Tales of poly(A): a review. Gene 91 (1990) 151-158
    • (1990) Gene , vol.91 , pp. 151-158
    • Munroe, D.1    Jacobson, A.2
  • 37
    • 0033578662 scopus 로고    scopus 로고
    • Thyroid hormone regulates hyperpolarization-activated cyclic nucleotide-gated channel (HCN2) mRNA in the rat heart
    • Pachucki J., Burmeister L.A., and Larsen P.R. Thyroid hormone regulates hyperpolarization-activated cyclic nucleotide-gated channel (HCN2) mRNA in the rat heart. Circ. Res. 85 (1999) 498-503
    • (1999) Circ. Res. , vol.85 , pp. 498-503
    • Pachucki, J.1    Burmeister, L.A.2    Larsen, P.R.3
  • 38
    • 32544445370 scopus 로고    scopus 로고
    • The mitochondrion as a primary site of action of steroid and thyroid hormones: presence and action of steroid and thyroid hormone receptors in mitochondria of animal cells
    • Psarra A.-M.G., Solakidi S., and Sekeris C.E. The mitochondrion as a primary site of action of steroid and thyroid hormones: presence and action of steroid and thyroid hormone receptors in mitochondria of animal cells. Mol. Cell. Endocrinol. 246 (2006) 21-33
    • (2006) Mol. Cell. Endocrinol. , vol.246 , pp. 21-33
    • Psarra, A.-M.G.1    Solakidi, S.2    Sekeris, C.E.3
  • 39
    • 0036906627 scopus 로고    scopus 로고
    • Mutant actins demonstrate a role for unpolymerized actin in control of transcription by serum response factor
    • Posern G., Sotiropoulos A., and Treisman R. Mutant actins demonstrate a role for unpolymerized actin in control of transcription by serum response factor. Mol. Biol. Cell. 13 (2002) 4167-4178
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 4167-4178
    • Posern, G.1    Sotiropoulos, A.2    Treisman, R.3
  • 40
    • 0020478744 scopus 로고
    • Role of actin and tubulin in the regulation of poly (A) polymerase-endoribonuclease IV complex from calf thymus
    • Schröder H.C., Zahn R.K., and Müller W.E. Role of actin and tubulin in the regulation of poly (A) polymerase-endoribonuclease IV complex from calf thymus. J. Biol. Chem. 257 (1982) 2305-2309
    • (1982) J. Biol. Chem. , vol.257 , pp. 2305-2309
    • Schröder, H.C.1    Zahn, R.K.2    Müller, W.E.3
  • 41
    • 0031909634 scopus 로고    scopus 로고
    • Influence of the cytoskeleton on surfactant protein gene expression in cultured rat alveolar type II cells
    • Shannon J.M., Pan T., Edeen K.E., and Nielsen L.D. Influence of the cytoskeleton on surfactant protein gene expression in cultured rat alveolar type II cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 274 (1998) L87-L96
    • (1998) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.274
    • Shannon, J.M.1    Pan, T.2    Edeen, K.E.3    Nielsen, L.D.4
  • 42
    • 0026816348 scopus 로고
    • The cytoskeleton and mRNA localization
    • Singer R.H. The cytoskeleton and mRNA localization. Curr. Opin. Cell Biol. 4 (1992) 15-19
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 15-19
    • Singer, R.H.1
  • 43
    • 18344371641 scopus 로고    scopus 로고
    • Moving messages: the intracellular localization of mRNAs
    • St Johnston D. Moving messages: the intracellular localization of mRNAs. Nat. Rev. Mol. Cell Biol. 6 (2005) 363-375
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 363-375
    • St Johnston, D.1
  • 44
    • 38549147387 scopus 로고    scopus 로고
    • Cytoskeletal control of vesicle transport and exocytosis in chromaffin cells
    • Trifaró J.M., Gasman S., and Gutiérrez L.M. Cytoskeletal control of vesicle transport and exocytosis in chromaffin cells. Acta Physiol (Oxf). 192 (2008) 165-172
    • (2008) Acta Physiol (Oxf). , vol.192 , pp. 165-172
    • Trifaró, J.M.1    Gasman, S.2    Gutiérrez, L.M.3
  • 45
    • 0035743456 scopus 로고    scopus 로고
    • Functional evidence for the presence of type II 5′-deiodinase in somatotropes and its adaptive role in hyperthyroidism
    • Volpato C.B., and Nunes M.T. Functional evidence for the presence of type II 5′-deiodinase in somatotropes and its adaptive role in hyperthyroidism. Neuroendocrinology 74 (2001) 220-226
    • (2001) Neuroendocrinology , vol.74 , pp. 220-226
    • Volpato, C.B.1    Nunes, M.T.2
  • 47
    • 0022458423 scopus 로고
    • Thyroxine increases neonatal mouse submandibular gland mRNA-directed synthesis of epidermal growth factor
    • Walker P. Thyroxine increases neonatal mouse submandibular gland mRNA-directed synthesis of epidermal growth factor. Biochem. Cell Biol. 64 (1986) 290-296
    • (1986) Biochem. Cell Biol. , vol.64 , pp. 290-296
    • Walker, P.1
  • 49
    • 0034964207 scopus 로고    scopus 로고
    • Physiological and molecular basis of thyroid hormone action
    • Yen P.M. Physiological and molecular basis of thyroid hormone action. Physiol. Rev. 81 (2001) 1097-1142
    • (2001) Physiol. Rev. , vol.81 , pp. 1097-1142
    • Yen, P.M.1


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