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Volumn 21, Issue 12, 2007, Pages 3240-3249

Sequential actions of ERK1/2 on the AP-1 transcription factor allow temporal integration of metabolic signals in pancreatic β cells

Author keywords

c fos; Langerhans islets; Protein stability; Proteolysis

Indexed keywords

GENE PRODUCT; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN C FOS; PROTEIN C JUN; PROTEIN FOS; PROTEIN SUBUNIT; TRANSCRIPTION FACTOR AP 1; GLUCAGON LIKE PEPTIDE 1; GLUCOSE; MESSENGER RNA;

EID: 35148901638     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.06-7798com     Document Type: Article
Times cited : (36)

References (44)
  • 1
    • 0035130272 scopus 로고    scopus 로고
    • Beta-cell adaptation and decompensation during the progression of diabetes
    • Weir, G. C., Laybutt, D. R., Kaneto, H., Bonner-Weir, S., and Sharma, A. (2001) Beta-cell adaptation and decompensation during the progression of diabetes. Diabetes 50, S154-S159
    • (2001) Diabetes , vol.50
    • Weir, G.C.1    Laybutt, D.R.2    Kaneto, H.3    Bonner-Weir, S.4    Sharma, A.5
  • 2
    • 0033553462 scopus 로고    scopus 로고
    • Chronic hyperglycemia triggers loss of pancreatic beta cell differentiation in an animal model of diabetes
    • Jonas, J. C., Sharma, A., Hasenkamp, W., Ilkova, H., Patane, G., Laybutt, R., Bonner-Weir, S., and Weir, G. C. (1999) Chronic hyperglycemia triggers loss of pancreatic beta cell differentiation in an animal model of diabetes. J. Biol. Chem. 274, 14112-14121
    • (1999) J. Biol. Chem , vol.274 , pp. 14112-14121
    • Jonas, J.C.1    Sharma, A.2    Hasenkamp, W.3    Ilkova, H.4    Patane, G.5    Laybutt, R.6    Bonner-Weir, S.7    Weir, G.C.8
  • 3
    • 0036895729 scopus 로고    scopus 로고
    • Glucose-regulated gene expression maintaining the glucose-responsive state of beta-cells
    • Schuit, F., Flamez, D., De Vos, A., and Pipeleers, D. (2002) Glucose-regulated gene expression maintaining the glucose-responsive state of beta-cells. Diabetes 51, S326-S332
    • (2002) Diabetes , vol.51
    • Schuit, F.1    Flamez, D.2    De Vos, A.3    Pipeleers, D.4
  • 4
    • 4344664674 scopus 로고    scopus 로고
    • Plasticity of the beta cell insulin secretory competence: Preparing the pancreatic beta cell for the next meal
    • Hinke, S. A., Hellemans, K., and Schuit, F. C. (2004) Plasticity of the beta cell insulin secretory competence: preparing the pancreatic beta cell for the next meal. J. Physiol. 558, 369-380
    • (2004) J. Physiol , vol.558 , pp. 369-380
    • Hinke, S.A.1    Hellemans, K.2    Schuit, F.C.3
  • 5
    • 0034705104 scopus 로고    scopus 로고
    • Expression profiling of pancreatic beta cells: Glucose regulation of secretory and metabolic pathway genes
    • Webb, G. C., Akbar, M. S., Zhao, C., and Steiner, D. F. (2000) Expression profiling of pancreatic beta cells: glucose regulation of secretory and metabolic pathway genes. Proc. Natl. Acad. Sci. U. S. A. 97, 5773-5778
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 5773-5778
    • Webb, G.C.1    Akbar, M.S.2    Zhao, C.3    Steiner, D.F.4
  • 7
    • 0031656888 scopus 로고    scopus 로고
    • Glucose and glucoincretin peptides synergize to induce c-fos, c-jun, junB, zif-268, and nur-77 gene expression in pancreatic beta(INS-1) cells
    • Susini, S., Roche, E., Prentki, M., and Schlegel, W. (1998) Glucose and glucoincretin peptides synergize to induce c-fos, c-jun, junB, zif-268, and nur-77 gene expression in pancreatic beta(INS-1) cells. FASEB J. 12, 1173-1182
    • (1998) FASEB J , vol.12 , pp. 1173-1182
    • Susini, S.1    Roche, E.2    Prentki, M.3    Schlegel, W.4
  • 8
    • 0032459512 scopus 로고    scopus 로고
    • Protein kinases, protein phosphorylation, and the regulation of insulin secretion from pancreatic beta-cells
    • Jones, P. M., and Persaud, S. J. (1998) Protein kinases, protein phosphorylation, and the regulation of insulin secretion from pancreatic beta-cells. Endocr. Rev. 19, 429-461
    • (1998) Endocr. Rev , vol.19 , pp. 429-461
    • Jones, P.M.1    Persaud, S.J.2
  • 9
    • 33644618433 scopus 로고    scopus 로고
    • The biology of incretin hormones
    • Drucker, D. J. (2006) The biology of incretin hormones. Cell Metab. 3, 153-165
    • (2006) Cell Metab , vol.3 , pp. 153-165
    • Drucker, D.J.1
  • 10
    • 0029594509 scopus 로고
    • Glucagon-like peptide-1 and control of insulin secretion
    • Thorens, B. (1995) Glucagon-like peptide-1 and control of insulin secretion. Diabete. Metab. 21, 311-318
    • (1995) Diabete. Metab , vol.21 , pp. 311-318
    • Thorens, B.1
  • 12
    • 0033978194 scopus 로고    scopus 로고
    • Essentiality of intron control in the induction of c-fos by glucose and glucoincretin peptides in INS-1 beta-cells
    • Susini, S., Van Haasteren, G., Li, S., Prentki, M., and Schlegel, W. (2000) Essentiality of intron control in the induction of c-fos by glucose and glucoincretin peptides in INS-1 beta-cells. FASEB J. 14, 128-136
    • (2000) FASEB J , vol.14 , pp. 128-136
    • Susini, S.1    Van Haasteren, G.2    Li, S.3    Prentki, M.4    Schlegel, W.5
  • 13
    • 33750966483 scopus 로고    scopus 로고
    • Mechanisms of transcriptional regulation underlying temporal integration of signals
    • Glauser, D. A., and Schlegel, W. (2006) Mechanisms of transcriptional regulation underlying temporal integration of signals. Nucleic Acids Res. 34, 5175-5183
    • (2006) Nucleic Acids Res , vol.34 , pp. 5175-5183
    • Glauser, D.A.1    Schlegel, W.2
  • 14
    • 0029937701 scopus 로고    scopus 로고
    • Phosphorylation of c-Fos at the C-terminus enhances its transforming activity
    • Chen, R. H., Juo, P. C., Curran, T., and Blenis, J. (1996) Phosphorylation of c-Fos at the C-terminus enhances its transforming activity. Oncogene 12, 1493-1502
    • (1996) Oncogene , vol.12 , pp. 1493-1502
    • Chen, R.H.1    Juo, P.C.2    Curran, T.3    Blenis, J.4
  • 15
    • 0025077481 scopus 로고
    • Redox regulation of fos and jun DNA-binding activity in vitro
    • Abate, C., Patel, L., Rauscher, F. J., 3rd, and Curran, T. (1990) Redox regulation of fos and jun DNA-binding activity in vitro. Science 249, 1157-1161
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher 3rd, F.J.3    Curran, T.4
  • 16
    • 0037390423 scopus 로고    scopus 로고
    • Differential gene expression in well-regulated and dysregulated pancreatic beta-cell (MIN6) sublines
    • Lilla, V., Webb, G., Rickenbach, K., Maturana, A., Steiner, D. F., Halban, P. A., and Irminger, J. C. (2003) Differential gene expression in well-regulated and dysregulated pancreatic beta-cell (MIN6) sublines. Endocrinology 144, 1368-1379
    • (2003) Endocrinology , vol.144 , pp. 1368-1379
    • Lilla, V.1    Webb, G.2    Rickenbach, K.3    Maturana, A.4    Steiner, D.F.5    Halban, P.A.6    Irminger, J.C.7
  • 17
    • 27844497945 scopus 로고    scopus 로고
    • FOXO transcription factors at the interface between longevity and tumor suppression
    • Greer, E. L., and Brunet, A. (2005) FOXO transcription factors at the interface between longevity and tumor suppression. Oncogene 24, 7410-7425
    • (2005) Oncogene , vol.24 , pp. 7410-7425
    • Greer, E.L.1    Brunet, A.2
  • 18
    • 0024293495 scopus 로고
    • Identification of a novel lymphoid specific octamer binding protein (OTF-2B) by proteolytic clipping bandshift assay (PCBA)
    • Schreiber, E., Matthias, P., Muller, M. M., and Schaffner, W. (1988) Identification of a novel lymphoid specific octamer binding protein (OTF-2B) by proteolytic clipping bandshift assay (PCBA). EMBO J. 7, 4221-4229
    • (1988) EMBO J , vol.7 , pp. 4221-4229
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 19
    • 0034672131 scopus 로고    scopus 로고
    • Compartment-specific regulation of extracellular signal-regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) mitogen-activated protein kinases (MAPKs) by ERK-dependent and non-ERK-dependent inductions of MAPK phosphatase (MKP)-3 and MKP-1 in differentiating P19 cells
    • Reffas, S., and Schlegel, W. (2000) Compartment-specific regulation of extracellular signal-regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) mitogen-activated protein kinases (MAPKs) by ERK-dependent and non-ERK-dependent inductions of MAPK phosphatase (MKP)-3 and MKP-1 in differentiating P19 cells. Biochem. J. 352, 701-708
    • (2000) Biochem. J , vol.352 , pp. 701-708
    • Reffas, S.1    Schlegel, W.2
  • 20
    • 2442672952 scopus 로고    scopus 로고
    • An extracellular signal-regulated kinase 1- and 2-dependent program of chromatin trafficking of c-Fos and Fra-1 is required for cyclin D1 expression during cell cycle reentry
    • Burch, P. M., Yuan, Z., Loonen, A., and Heintz, N. H. (2004) An extracellular signal-regulated kinase 1- and 2-dependent program of chromatin trafficking of c-Fos and Fra-1 is required for cyclin D1 expression during cell cycle reentry. Mol. Cell. Biol. 24, 4696-4709
    • (2004) Mol. Cell. Biol , vol.24 , pp. 4696-4709
    • Burch, P.M.1    Yuan, Z.2    Loonen, A.3    Heintz, N.H.4
  • 21
    • 0025281303 scopus 로고
    • Establishment of a pancreatic beta cell line that retains glucose-inducible insulin secretion: Special reference to expression of glucose transporter isoforms
    • Miyazaki, J., Araki, K., Yamato, E., Ikegami, H., Asano, T., Shibasaki, Y., Oka, Y., and Yamamura, K. (1990) Establishment of a pancreatic beta cell line that retains glucose-inducible insulin secretion: special reference to expression of glucose transporter isoforms. Endocrinology 127, 126-132
    • (1990) Endocrinology , vol.127 , pp. 126-132
    • Miyazaki, J.1    Araki, K.2    Yamato, E.3    Ikegami, H.4    Asano, T.5    Shibasaki, Y.6    Oka, Y.7    Yamamura, K.8
  • 23
    • 4043054381 scopus 로고    scopus 로고
    • c-Fos phosphorylation induced by H2O2 prevents proteasomal degradation of c-Fos in cardiomyocytes
    • Coronella-Wood, J., Terrand, J., Sun, H., and Chen, Q. M. (2004) c-Fos phosphorylation induced by H2O2 prevents proteasomal degradation of c-Fos in cardiomyocytes. J. Biol. Chem. 279, 33567-33574
    • (2004) J. Biol. Chem , vol.279 , pp. 33567-33574
    • Coronella-Wood, J.1    Terrand, J.2    Sun, H.3    Chen, Q.M.4
  • 24
    • 0028787249 scopus 로고
    • The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells
    • Okazaki, K., and Sagata, N. (1995) The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells. EMBO J. 14, 5048-5059
    • (1995) EMBO J , vol.14 , pp. 5048-5059
    • Okazaki, K.1    Sagata, N.2
  • 25
    • 0027361017 scopus 로고
    • Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase
    • Chen, R. H., Abate, C., and Blenis, J. (1993) Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase. Proc. Natl. Acad. Sci. U. S. A. 90, 10952-10956
    • (1993) Proc. Natl. Acad. Sci. U. S. A , vol.90 , pp. 10952-10956
    • Chen, R.H.1    Abate, C.2    Blenis, J.3
  • 26
    • 0036051342 scopus 로고    scopus 로고
    • Molecular interpretation of ERK signal duration by immediate early gene products
    • Murphy, L. O., Smith, S., Chen, R. H., Fingar, D. C., and Blenis, J. (2002) Molecular interpretation of ERK signal duration by immediate early gene products. Nat. Cell Biol. 4, 556-564
    • (2002) Nat. Cell Biol , vol.4 , pp. 556-564
    • Murphy, L.O.1    Smith, S.2    Chen, R.H.3    Fingar, D.C.4    Blenis, J.5
  • 27
    • 0037382719 scopus 로고    scopus 로고
    • Differential activation mechanisms of Erk-1/2 and p70(S6K) by glucose in pancreatic beta-cells
    • Briaud, I., Lingohr, M. K., Dickson, L. M., Wrede, C. E., and Rhodes, C. J. (2003) Differential activation mechanisms of Erk-1/2 and p70(S6K) by glucose in pancreatic beta-cells. Diabetes 52, 974-983
    • (2003) Diabetes , vol.52 , pp. 974-983
    • Briaud, I.1    Lingohr, M.K.2    Dickson, L.M.3    Wrede, C.E.4    Rhodes, C.J.5
  • 28
    • 0037073717 scopus 로고    scopus 로고
    • cAMP-dependent protein kinase and Ca2+ influx through L-type voltage-gated calcium channels mediate Raf-independent activation of extracellular regulated kinase in response to glucagonlike peptide-1 in pancreatic beta-cells
    • Gomez, E., Pritchard, C., and Herbert, T. P. (2002) cAMP-dependent protein kinase and Ca2+ influx through L-type voltage-gated calcium channels mediate Raf-independent activation of extracellular regulated kinase in response to glucagonlike peptide-1 in pancreatic beta-cells. J. Biol. Chem. 277, 48146-48151
    • (2002) J. Biol. Chem , vol.277 , pp. 48146-48151
    • Gomez, E.1    Pritchard, C.2    Herbert, T.P.3
  • 29
    • 0032553412 scopus 로고    scopus 로고
    • Growth hormone stimulates phosphorylation and activation of elk-1 and expression of c-fos, egr-1, and junB through activation of extracellular signal-regulated kinases 1 and 2
    • Hodge, C., Liao, J., Stofega, M., Guan, K., Carter-Su, C., and Schwartz, J. (1998) Growth hormone stimulates phosphorylation and activation of elk-1 and expression of c-fos, egr-1, and junB through activation of extracellular signal-regulated kinases 1 and 2. J. Biol. Chem. 273, 31327-31336
    • (1998) J. Biol. Chem , vol.273 , pp. 31327-31336
    • Hodge, C.1    Liao, J.2    Stofega, M.3    Guan, K.4    Carter-Su, C.5    Schwartz, J.6
  • 30
    • 33847381502 scopus 로고    scopus 로고
    • Gene-specific recruitment of positive and negative elongation factors during stimulated transcription of the MKP-1 gene in neuroendocrine cells
    • Fujita, T., Ryser, S., Tortola, S., Piuz, I., and Schlegel, W. (2007) Gene-specific recruitment of positive and negative elongation factors during stimulated transcription of the MKP-1 gene in neuroendocrine cells. Nucleic Acids Res. 35, 1007-1017
    • (2007) Nucleic Acids Res , vol.35 , pp. 1007-1017
    • Fujita, T.1    Ryser, S.2    Tortola, S.3    Piuz, I.4    Schlegel, W.5
  • 31
    • 33947516620 scopus 로고    scopus 로고
    • The rate of c-fos transcription in vivo is continously regulated at the level of elongation by dynamic stimulus-coupled recruitment of P-TEFb
    • Ryser, S., Fujita, T., Tortola, S., Piuz, I., and Schlegel, W. (2006) The rate of c-fos transcription in vivo is continously regulated at the level of elongation by dynamic stimulus-coupled recruitment of P-TEFb. J. Biol. Chem. 282, 5075-5084
    • (2006) J. Biol. Chem , vol.282 , pp. 5075-5084
    • Ryser, S.1    Fujita, T.2    Tortola, S.3    Piuz, I.4    Schlegel, W.5
  • 32
    • 0032526417 scopus 로고    scopus 로고
    • RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein
    • Peng, S. S., Chen, C. Y., Xu, N., and Shyu, A. B. (1998) RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein. EMBO J. 17, 3461-3470
    • (1998) EMBO J , vol.17 , pp. 3461-3470
    • Peng, S.S.1    Chen, C.Y.2    Xu, N.3    Shyu, A.B.4
  • 33
    • 0141781040 scopus 로고    scopus 로고
    • Phosphorylation of the carboxyl-terminal transactivation domain of c-Fos by extracellular signal-regulated kinase mediates the transcriptional activation of AP-1 and cellular transformation induced by platelet-derived growth factor
    • Monje, P., Marinissen, M. J., and Gutkind, J. S. (2003) Phosphorylation of the carboxyl-terminal transactivation domain of c-Fos by extracellular signal-regulated kinase mediates the transcriptional activation of AP-1 and cellular transformation induced by platelet-derived growth factor. Mol. Cell Biol. 23, 7030-7043
    • (2003) Mol. Cell Biol , vol.23 , pp. 7030-7043
    • Monje, P.1    Marinissen, M.J.2    Gutkind, J.S.3
  • 34
    • 0033563110 scopus 로고    scopus 로고
    • Mode of regulation of the extracellular signal-regulated kinases in the pancreatic beta-cell line MIN6 and their implication in the regulation of insulin gene transcription
    • Benes, C., Poitout, V., Marie, J. C., Martin-Perez, J., Roisin, M. P., and Fagard, R. (1999) Mode of regulation of the extracellular signal-regulated kinases in the pancreatic beta-cell line MIN6 and their implication in the regulation of insulin gene transcription. Biochem. J. 340, 219-225
    • (1999) Biochem. J , vol.340 , pp. 219-225
    • Benes, C.1    Poitout, V.2    Marie, J.C.3    Martin-Perez, J.4    Roisin, M.P.5    Fagard, R.6
  • 35
    • 0032941026 scopus 로고    scopus 로고
    • Pancreatic glucagon-like peptide-1 receptor couples to multiple G proteins and activates mitogen-activated protein kinase pathways in Chinese hamster ovary cells
    • Montrose-Rafizadeh, C., Avdonin, P., Garant, M. J., Rodgers, B. D., Kole, S., Yang, H., Levine, M. A., Schwindinger, W., and Bernier, M. (1999) Pancreatic glucagon-like peptide-1 receptor couples to multiple G proteins and activates mitogen-activated protein kinase pathways in Chinese hamster ovary cells. Endocrinology 140, 1132-1140
    • (1999) Endocrinology , vol.140 , pp. 1132-1140
    • Montrose-Rafizadeh, C.1    Avdonin, P.2    Garant, M.J.3    Rodgers, B.D.4    Kole, S.5    Yang, H.6    Levine, M.A.7    Schwindinger, W.8    Bernier, M.9
  • 37
    • 0036893798 scopus 로고    scopus 로고
    • Insulin receptor signaling and sarco/endoplasmic reticulum calcium ATPase in beta-cells
    • Borge, P. D., Moibi, J., Greene, S. R., Trucco, M., Young, R. A., Gao, Z., and Wolf, B. A. (2002) Insulin receptor signaling and sarco/endoplasmic reticulum calcium ATPase in beta-cells. Diabetes. 51, S427-433
    • (2002) Diabetes , vol.51
    • Borge, P.D.1    Moibi, J.2    Greene, S.R.3    Trucco, M.4    Young, R.A.5    Gao, Z.6    Wolf, B.A.7
  • 38
    • 0038498118 scopus 로고    scopus 로고
    • ERK1/2 achieves sustained activation by stimulating MAPK phosphatase-1 degradation via the ubiquitin-proteasome pathway
    • Lin, Y. W., Chuang, S. M., and Yang, J. L. (2003) ERK1/2 achieves sustained activation by stimulating MAPK phosphatase-1 degradation via the ubiquitin-proteasome pathway. J. Biol. Chem. 278, 21534-21541
    • (2003) J. Biol. Chem , vol.278 , pp. 21534-21541
    • Lin, Y.W.1    Chuang, S.M.2    Yang, J.L.3
  • 39
    • 5044228741 scopus 로고    scopus 로고
    • Mechanisms regulating the constitutive activation of the extracellular signal-regulated kinase (ERK) signaling pathway in ovarian cancer and the effect of ribonucleic acid interference for ERK1/2 on cancer cell proliferation
    • Steinmetz, R., Wagoner, H. A., Zeng, P., Hammond, J. R., Hannon, T. S., Meyers, J. L., and Pescovitz, O. H. (2004) Mechanisms regulating the constitutive activation of the extracellular signal-regulated kinase (ERK) signaling pathway in ovarian cancer and the effect of ribonucleic acid interference for ERK1/2 on cancer cell proliferation. Mol. Endocrinol. 18, 2570-2582
    • (2004) Mol. Endocrinol , vol.18 , pp. 2570-2582
    • Steinmetz, R.1    Wagoner, H.A.2    Zeng, P.3    Hammond, J.R.4    Hannon, T.S.5    Meyers, J.L.6    Pescovitz, O.H.7
  • 40
    • 0033758616 scopus 로고    scopus 로고
    • Modulation of the ERK pathway of signal transduction by cysteine proteinase inhibitors
    • Torres, C., Li, M., Walter, R., and Sierra, F. (2000) Modulation of the ERK pathway of signal transduction by cysteine proteinase inhibitors. J. Cell Biochem. 80, 11-23
    • (2000) J. Cell Biochem , vol.80 , pp. 11-23
    • Torres, C.1    Li, M.2    Walter, R.3    Sierra, F.4
  • 41
    • 0345732643 scopus 로고    scopus 로고
    • A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration
    • Murphy, L. O., MacKeigan, J. P., and Blenis, J. (2004) A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration. Mol. Cell Biol. 24, 144-153
    • (2004) Mol. Cell Biol , vol.24 , pp. 144-153
    • Murphy, L.O.1    MacKeigan, J.P.2    Blenis, J.3
  • 42
    • 33744974769 scopus 로고    scopus 로고
    • Continuous ERK activation down-regulates antiproliferative genes throughout G1 phase to allow cell-cycle progression
    • Yamamoto, T., Ebisuya, M., Ashida, F., Okamoto, K., Yonehara, S., and Nishida, E. (2006) Continuous ERK activation down-regulates antiproliferative genes throughout G1 phase to allow cell-cycle progression. Curr. Biol. 16, 1171-1182
    • (2006) Curr. Biol , vol.16 , pp. 1171-1182
    • Yamamoto, T.1    Ebisuya, M.2    Ashida, F.3    Okamoto, K.4    Yonehara, S.5    Nishida, E.6
  • 43
    • 0036224165 scopus 로고    scopus 로고
    • Activation of IRS-2-mediated signal transduction by IGF-1, but not TGF-alpha or EGF, augments pancreatic beta-cell proliferation
    • Lingohr, M. K., Dickson, L. M., McCuaig, J. F., Hugl, S. R., Twardzik, D. R., and Rhodes, C. J. (2002) Activation of IRS-2-mediated signal transduction by IGF-1, but not TGF-alpha or EGF, augments pancreatic beta-cell proliferation. Diabetes 51, 966-976
    • (2002) Diabetes , vol.51 , pp. 966-976
    • Lingohr, M.K.1    Dickson, L.M.2    McCuaig, J.F.3    Hugl, S.R.4    Twardzik, D.R.5    Rhodes, C.J.6
  • 44
    • 22844446279 scopus 로고    scopus 로고
    • ERK1/2-dependent activation of transcription factors required for acute and chronic effects of glucose on the insulin gene promoter
    • Lawrence, M. C., McGlynn, K., Park, B. H., and Cobb, M. H. (2005) ERK1/2-dependent activation of transcription factors required for acute and chronic effects of glucose on the insulin gene promoter. J. Biol. Chem. 280, 26751-26759
    • (2005) J. Biol. Chem , vol.280 , pp. 26751-26759
    • Lawrence, M.C.1    McGlynn, K.2    Park, B.H.3    Cobb, M.H.4


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