메뉴 건너뛰기




Volumn 44, Issue 10, 2011, Pages 1060-1067

Hypothyroidism decreases proinsulin gene expression and the attachment of its mRNA and eEF1A protein to the actin cytoskeleton of INS-1E cells

Author keywords

Cytoskeleton; EEF1A protein; Hypothyroidism; INS 1E cells; Proinsulin mRNA

Indexed keywords

ACTIN; BOVINE SERUM ALBUMIN; EEF1A PROTEIN; MESSENGER RNA; PROINSULIN; PROTEIN; THYROID HORMONE; UNCLASSIFIED DRUG;

EID: 80053959315     PISSN: 0100879X     EISSN: 1414431X     Source Type: Journal    
DOI: 10.1590/S0100-879X2011007500121     Document Type: Article
Times cited : (5)

References (36)
  • 1
    • 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 JJ, Lin HY, Lansing L, Mohamed SN, Davis FB, Mousa S, et al. 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 2005; 146: 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
  • 2
    • 0023182842 scopus 로고
    • The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum
    • Cheng SY, Gong QH, Parkison C, Robinson EA, Appella E, Merlino GT, et al. The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum. J Biol Chem 1987; 262: 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
  • 3
    • 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 AM, Solakidi S, Sekeris CE. 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 2006; 246: 21-33.
    • (2006) Mol Cell Endocrinol , vol.246 , pp. 21-33
    • Psarra, A.M.1    Solakidi, S.2    Sekeris, C.E.3
  • 4
    • 0034964207 scopus 로고    scopus 로고
    • Physiological and molecular basis of thyroid hormone action
    • Yen PM. Physiological and molecular basis of thyroid hormone action. Physiol Rev 2001; 81: 1097-1142.
    • (2001) Physiol Rev , vol.81 , pp. 1097-1142
    • Yen, P.M.1
  • 5
    • 34548439796 scopus 로고    scopus 로고
    • Thyroid hormone rapidly stimulates alveolar Na,K-ATPase by activation of phosphatidylinositol 3-kinase
    • Bhargava M, Lei J, Mariash CN, Ingbar DH. Thyroid hormone rapidly stimulates alveolar Na,K-ATPase by activation of phosphatidylinositol 3-kinase. Curr Opin Endocrinol Diabetes Obes 2007; 14: 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
  • 6
    • 39449085830 scopus 로고    scopus 로고
    • Thyroid hormone as a determinant of energy expenditure and the basal metabolic rate
    • Kim B. Thyroid hormone as a determinant of energy expenditure and the basal metabolic rate. Thyroid 2008; 18: 141-144.
    • (2008) Thyroid , vol.18 , pp. 141-144
    • Kim, B.1
  • 7
    • 0027210520 scopus 로고
    • Control of muscular bioenergetics by the thyroid hormones
    • Kaminsky P, Klein M, Duc M. [Control of muscular bioenergetics by the thyroid hormones]. Presse Med 1993; 22: 774-778.
    • (1993) Presse Med , vol.22 , pp. 774-778
    • Kaminsky, P.1    Klein, M.2    Duc, M.3
  • 8
    • 78651144897 scopus 로고
    • Insulin and protein metabolism
    • Lukens FD. Insulin and protein metabolism. Diabetes 1964; 13: 451-461.
    • (1964) Diabetes , vol.13 , pp. 451-461
    • Lukens, F.D.1
  • 9
    • 65249171425 scopus 로고    scopus 로고
    • Effects of growth hormone on glucose, lipid, and protein metabolism in human subjects
    • Moller N, Jorgensen JO. Effects of growth hormone on glucose, lipid, and protein metabolism in human subjects. Endocr Rev 2009; 30: 152-177.
    • (2009) Endocr Rev , vol.30 , pp. 152-177
    • Moller, N.1    Jorgensen, J.O.2
  • 12
    • 20144380224 scopus 로고    scopus 로고
    • 3,5,3'-Triiodo-L-thyronine enhances the differentiation of a human pancreatic duct cell line (hPANC-1) towards a beta-cell-like phenotype
    • Misiti S, Anastasi E, Sciacchitano S, Verga FC, Panacchia L, Bucci B, et al. 3,5,3'-Triiodo-L-thyronine enhances the differentiation of a human pancreatic duct cell line (hPANC-1) towards a beta-cell-like phenotype. J Cell Physiol 2005; 204: 286-296.
    • (2005) J Cell Physiol , vol.204 , pp. 286-296
    • Misiti, S.1    Anastasi, E.2    Sciacchitano, S.3    Verga, F.C.4    Panacchia, L.5    Bucci, B.6
  • 13
    • 0026504134 scopus 로고
    • Regulation of glucokinase and proinsulin gene expression and insulin secretion in RIN-m5F cells by dexamethasone, retinoic acid, and thyroid hormone
    • Fernandez-Mejia C, Davidson MB. Regulation of glucokinase and proinsulin gene expression and insulin secretion in RIN-m5F cells by dexamethasone, retinoic acid, and thyroid hormone. Endocrinology 1992; 130: 1660-1668.
    • (1992) Endocrinology , vol.130 , pp. 1660-1668
    • Fernandez-Mejia, C.1    Davidson, M.B.2
  • 14
    • 0037135275 scopus 로고    scopus 로고
    • Evidence for a deficient pancreatic betacell response in a rat model of hyperthyroidism
    • Fukuchi M, Shimabukuro M, Shimajiri Y, Oshiro Y, Higa M, Akamine H, et al. Evidence for a deficient pancreatic betacell response in a rat model of hyperthyroidism. Life Sci 2002; 71: 1059-1070.
    • (2002) Life Sci , vol.71 , pp. 1059-1070
    • Fukuchi, M.1    Shimabukuro, M.2    Shimajiri, Y.3    Oshiro, Y.4    Higa, M.5    Akamine, H.6
  • 15
    • 33644840217 scopus 로고    scopus 로고
    • Rethinking leptin and insulin action: Therapeutic opportunities for diabetes
    • Yildiz BO, Haznedaroglu IC. Rethinking leptin and insulin action: therapeutic opportunities for diabetes. Int J Biochem Cell Biol 2006; 38: 820-830.
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 820-830
    • Yildiz, B.O.1    Haznedaroglu, I.C.2
  • 16
    • 35748957503 scopus 로고    scopus 로고
    • The physiology of glucagon-like peptide 1
    • Holst JJ. The physiology of glucagon-like peptide 1. Physiol Rev 2007; 87: 1409-1439.
    • (2007) Physiol Rev , vol.87 , pp. 1409-1439
    • Holst, J.J.1
  • 17
    • 0034465470 scopus 로고    scopus 로고
    • Somatostatin inhibits insulin and glucagon secretion via two receptor subtypes: An in vitro study of pancreatic islets from somatostatin receptor 2 knockout mice
    • Strowski MZ, Parmar RM, Blake AD, Schaeffer JM. Somatostatin inhibits insulin and glucagon secretion via two receptor subtypes: an in vitro study of pancreatic islets from somatostatin receptor 2 knockout mice. Endocrinology 2000; 141: 111-117.
    • (2000) Endocrinology , vol.141 , pp. 111-117
    • Strowski, M.Z.1    Parmar, R.M.2    Blake, A.D.3    Schaeffer, J.M.4
  • 19
    • 78650520199 scopus 로고    scopus 로고
    • T3 rapidly modulates TSHbeta mRNA stability and translational rate in the pituitary of hypothyroid rats
    • Goulart-Silva F, de Souza PB, Nunes MT. T3 rapidly modulates TSHbeta mRNA stability and translational rate in the pituitary of hypothyroid rats. Mol Cell Endocrinol 2011; 332: 277-282.
    • (2011) Mol Cell Endocrinol , vol.332 , pp. 277-282
    • Goulart-Silva, F.1    de Souza, P.B.2    Nunes, M.T.3
  • 20
    • 0021963357 scopus 로고
    • Effect of viral infection on host protein synthesis and mRNA association with the cytoplasmic cytoskeletal structure
    • Bonneau AM, Darveau A, Sonenberg N. Effect of viral infection on host protein synthesis and mRNA association with the cytoplasmic cytoskeletal structure. J Cell Biol 1985; 100: 1209-1218.
    • (1985) J Cell Biol , vol.100 , pp. 1209-1218
    • Bonneau, A.M.1    Darveau, A.2    Sonenberg, N.3
  • 21
    • 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 WM, Persky D, Latham VM Jr, Singer RH, Condeelis J. Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: implications for anchoring mRNA in cell protrusions. Mol Biol Cell 2002; 13: 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
  • 22
    • 0029855771 scopus 로고    scopus 로고
    • Function of nuclear co-repressor protein on thyroid hormone response elements is regulated by the receptor A/B domain
    • Hollenberg AN, Monden T, Madura JP, Lee K, Wondisford FE. Function of nuclear co-repressor protein on thyroid hormone response elements is regulated by the receptor A/B domain. J Biol Chem 1996; 271: 28516-28520.
    • (1996) J Biol Chem , vol.271 , pp. 28516-28520
    • Hollenberg, A.N.1    Monden, T.2    Madura, J.P.3    Lee, K.4    Wondisford, F.E.5
  • 24
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987; 162: 156-159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 25
    • 0032864002 scopus 로고    scopus 로고
    • Assaying the polyadenylation state of mRNAs
    • Salles FJ, Richards WG, Strickland S. Assaying the polyadenylation state of mRNAs. Methods 1999; 17: 38-45.
    • (1999) Methods , vol.17 , pp. 38-45
    • Salles, F.J.1    Richards, W.G.2    Strickland, S.3
  • 26
    • 77950267899 scopus 로고    scopus 로고
    • Posttranscriptional regulation of sodium-iodide symporter mRNA expression in the rat thyroid gland by acute iodide administration
    • Serrano-Nascimento C, Calil-Silveira J, Nunes MT. Posttranscriptional regulation of sodium-iodide symporter mRNA expression in the rat thyroid gland by acute iodide administration. Am J Physiol Cell Physiol 2010; 298: C893-C899.
    • (2010) Am J Physiol Cell Physiol , vol.298
    • Serrano-Nascimento, C.1    Calil-Silveira, J.2    Nunes, M.T.3
  • 27
    • 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, Treisman R. Mutant actins demonstrate a role for unpolymerized actin in control of transcription by serum response factor. Mol Biol Cell 2002; 13: 4167-4178.
    • (2002) Mol Biol Cell , vol.13 , pp. 4167-4178
    • Posern, G.1    Sotiropoulos, A.2    Treisman, R.3
  • 28
    • 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, Featherstone M. Subcellular localization of multiple PREP2 isoforms is regulated by actin, tubulin, and nuclear export. J Biol Chem 2004; 279: 49384-49394.
    • (2004) J Biol Chem , vol.279 , pp. 49384-49394
    • Haller, K.1    Rambaldi, I.2    Daniels, E.3    Featherstone, M.4
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0030272844 scopus 로고    scopus 로고
    • The compartmentalization of protein synthesis: Importance of cytoskeleton and role in mRNA targeting
    • Hovland R, Hesketh JE, Pryme IF. The compartmentalization of protein synthesis: importance of cytoskeleton and role in mRNA targeting. Int J Biochem Cell Biol 1996; 28: 1089-1105.
    • (1996) Int J Biochem Cell Biol , vol.28 , pp. 1089-1105
    • Hovland, R.1    Hesketh, J.E.2    Pryme, I.F.3
  • 33
    • 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 JH, Glover LA, Hesketh JE. 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 1997; 1358: 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
  • 34
    • 0031909634 scopus 로고    scopus 로고
    • Influence of the cytoskeleton on surfactant protein gene expression in cultured rat alveolar type II cells
    • Shannon JM, Pan T, Edeen KE, Nielsen LD. Influence of the cytoskeleton on surfactant protein gene expression in cultured rat alveolar type II cells. Am J Physiol 1998; 274: L87-L96.
    • (1998) Am J Physiol , vol.274
    • Shannon, J.M.1    Pan, T.2    Edeen, K.E.3    Nielsen, L.D.4
  • 35
    • 33646137375 scopus 로고    scopus 로고
    • Cytoskeletal architecture differentially controls post-transcriptional processing of IL-6 and IL-8 mRNA in airway epithelial-like cells
    • van den Berg A, Freitas J, Keles F, Snoek M, van Marle J, Jansen HM, et al. Cytoskeletal architecture differentially controls post-transcriptional processing of IL-6 and IL-8 mRNA in airway epithelial-like cells. Exp Cell Res 2006; 312: 1496-1506.
    • (2006) Exp Cell Res , vol.312 , pp. 1496-1506
    • van den Berg, A.1    Freitas, J.2    Keles, F.3    Snoek, M.4    van Marle, J.5    Jansen, H.M.6
  • 36
    • 0032514754 scopus 로고    scopus 로고
    • Polyadenylation of stable RNA precursors in vivo
    • Li Z, Pandit S, Deutscher MP. Polyadenylation of stable RNA precursors in vivo. Proc Natl Acad Sci U S A 1998; 95: 12158-12162.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12158-12162
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.