메뉴 건너뛰기




Volumn 300, Issue 2, 2003, Pages 261-267

Reduction of protein-tyrosine phosphatase-1B increases insulin signaling in FAO hepatoma cells

Author keywords

GSK3; Insulin resistance; Insulin signaling; PKB; Protein tyrosine phosphatase 1B

Indexed keywords

ANTISENSE OLIGONUCLEOTIDE; INSULIN; INSULIN RECEPTOR; OLIGONUCLEOTIDE; PROTEIN TYROSINE PHOSPHATASE 1B; GLYCOGEN SYNTHASE KINASE 3; INSULIN RECEPTOR SUBSTRATE 1 PROTEIN; INSULIN RECEPTOR SUBSTRATE 2 PROTEIN; INSULIN RECEPTOR SUBSTRATE-1 PROTEIN; INSULIN RECEPTOR SUBSTRATE-2 PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; ONCOPROTEIN; PHOSPHOPROTEIN; PROTEIN KINASE B; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE PHOSPHATASE; SIGNAL PEPTIDE;

EID: 0037427519     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02839-5     Document Type: Article
Times cited : (43)

References (35)
  • 1
    • 0027953703 scopus 로고
    • Banting Lecture. Insulin action, diabetogenes, and the cause of type II diabetes
    • Kahn C.R. Banting Lecture. Insulin action, diabetogenes, and the cause of type II diabetes. Diabetes. 43:1994;1066-1084.
    • (1994) Diabetes , vol.43 , pp. 1066-1084
    • Kahn, C.R.1
  • 2
    • 0033593461 scopus 로고    scopus 로고
    • Signaling mechanisms that regulate glucose transport
    • Czech M.P., Corvera S. Signaling mechanisms that regulate glucose transport. J. Biol. Chem. 274:1999;1865-1868.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1865-1868
    • Czech, M.P.1    Corvera, S.2
  • 3
    • 0030998473 scopus 로고    scopus 로고
    • Insulin stimulates the phosphorylation of the 66- and 52-kDa Shc isoforms by distinct pathways
    • A.W. Kao, S.B. Waters, S. Okada, J.E. Pessin, Insulin stimulates the phosphorylation of the 66- and 52-kDa Shc isoforms by distinct pathways, Endocrinology 138, 2474-2480.
    • Endocrinology , vol.138 , pp. 2474-2480
    • Kao, A.W.1    Waters, S.B.2    Okada, S.3    Pessin, J.E.4
  • 4
    • 0033593329 scopus 로고    scopus 로고
    • Insulin-stimulated glucose transport minireview series
    • Olefsky J.M. Insulin-stimulated glucose transport minireview series. J. Biol. Chem. 274:1997;1863.
    • (1997) J. Biol. Chem. , vol.274 , pp. 1863
    • Olefsky, J.M.1
  • 5
    • 0031918624 scopus 로고    scopus 로고
    • The IRS-signaling system: A network of docking proteins that mediate insulin action
    • White M.F. The IRS-signaling system: a network of docking proteins that mediate insulin action. Mol. Cell. Biochem. 182:1998;3-11.
    • (1998) Mol. Cell. Biochem. , vol.182 , pp. 3-11
    • White, M.F.1
  • 6
    • 0031616132 scopus 로고    scopus 로고
    • The IRS-signaling system: A network of docking proteins that mediate insulin and cytokine action
    • White M.F. The IRS-signaling system: a network of docking proteins that mediate insulin and cytokine action. Recent Prog. Horm. Res. 53:1998;119-138.
    • (1998) Recent Prog. Horm. Res. , vol.53 , pp. 119-138
    • White, M.F.1
  • 7
    • 0030841793 scopus 로고    scopus 로고
    • PDK1, one of the missing links in insulin signal transduction
    • Cohen P., Alessi D.R., E Cross D.A. PDK1, one of the missing links in insulin signal transduction. FEBS Lett. 410:1997;3-10.
    • (1997) FEBS Lett. , vol.410 , pp. 3-10
    • Cohen, P.1    Alessi, D.R.2    Cross, D.A.E.3
  • 8
    • 0029908016 scopus 로고    scopus 로고
    • Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation
    • Kohn A.D., Summers S.A., Birnbaum M.J., Roth R.A. Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation. J. Biol. Chem. 271:1996;31372-31378.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31372-31378
    • Kohn, A.D.1    Summers, S.A.2    Birnbaum, M.J.3    Roth, R.A.4
  • 10
    • 0003175629 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases and the regulation of insulin action
    • D. LeRoith, J.M. Olefsky, & S.I. Taylor. Philadelphia, New York: Lippincott Publishing
    • Goldstein B.J. Protein-tyrosine phosphatases and the regulation of insulin action. LeRoith D., Olefsky J.M., Taylor S.I. Diabetes Mellitus: A Fundamental and Clinical Text. 2000;206-217 Lippincott Publishing, Philadelphia, New York.
    • (2000) Diabetes Mellitus: A Fundamental and Clinical Text , pp. 206-217
    • Goldstein, B.J.1
  • 11
    • 0034308201 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase-1B in diabetes
    • Kennedy B.P., Ramachandran C. Protein tyrosine phosphatase-1B in diabetes. Biochem. Pharmacol. 60:2000;877-883.
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 877-883
    • Kennedy, B.P.1    Ramachandran, C.2
  • 13
    • 0029810614 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-1 stimulated signaling
    • Kenner K.A., Anyanwu E., Olefsky J.M., Kusari J. Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-1 stimulated signaling. J. Biol. Chem. 271:1996;19810-19816.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19810-19816
    • Kenner, K.A.1    Anyanwu, E.2    Olefsky, J.M.3    Kusari, J.4
  • 14
    • 0029130199 scopus 로고
    • Osmotic loading of neutralizing antibodies defines a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway
    • Ahmad F., Li P.M., Meyerovitch J., Goldstein B.J. Osmotic loading of neutralizing antibodies defines a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway. J. Biol. Chem. 270:1995;20503-20508.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20503-20508
    • Ahmad, F.1    Li, P.M.2    Meyerovitch, J.3    Goldstein, B.J.4
  • 15
    • 0034674651 scopus 로고    scopus 로고
    • Overexpression of protein-tyrosine phosphatase-1B in adipocytes inhibits insulin-stimulated phosphoinositide 3-kinase activity without altering glucose transport or Akt/protein kinase B activation
    • Venable C.L., Frevert E.U., Kim Y.B., Fischer B.M., Kamatkar S., Neel B.G., Kahn B.B. Overexpression of protein-tyrosine phosphatase-1B in adipocytes inhibits insulin-stimulated phosphoinositide 3-kinase activity without altering glucose transport or Akt/protein kinase B activation. J. Biol. Chem. 275:2000;18318-18326.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18318-18326
    • Venable, C.L.1    Frevert, E.U.2    Kim, Y.B.3    Fischer, B.M.4    Kamatkar, S.5    Neel, B.G.6    Kahn, B.B.7
  • 16
    • 0034054497 scopus 로고    scopus 로고
    • Dynamics of protein-tyrosine phosphatases in rat adipocytes
    • Calera M.R., Vallega G., Pilch P.F. Dynamics of protein-tyrosine phosphatases in rat adipocytes. J. Biol. Chem. 275:2000;6308-6312.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6308-6312
    • Calera, M.R.1    Vallega, G.2    Pilch, P.F.3
  • 18
    • 0034635374 scopus 로고    scopus 로고
    • Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B
    • Goldstein B.J., Bittner-Kowalczyk A., White M.F., Harbeck M. Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B. J. Biol. Chem. 275:2000;4283-4289.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4283-4289
    • Goldstein, B.J.1    Bittner-Kowalczyk, A.2    White, M.F.3    Harbeck, M.4
  • 19
    • 0034507958 scopus 로고    scopus 로고
    • Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B
    • Salmeen A., Andersen J.N., Myers M.P., Tonks N.K., Barford D. Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B. Mol. Cell. 6:2000;1401-1412.
    • (2000) Mol. Cell , vol.6 , pp. 1401-1412
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Tonks, N.K.4    Barford, D.5
  • 20
    • 0030821972 scopus 로고    scopus 로고
    • Improved sensitivity to insulin in obese subjects following weight loss is accompanied by reduced protein-tyrosine phosphatases in adipose tissue
    • Ahmad F., Considine R.V., Bauer T.L., Ohannesian J.P., Marco C.C., Goldstein B.J. Improved sensitivity to insulin in obese subjects following weight loss is accompanied by reduced protein-tyrosine phosphatases in adipose tissue. Metabolism. 46:1997;1140-1145.
    • (1997) Metabolism , vol.46 , pp. 1140-1145
    • Ahmad, F.1    Considine, R.V.2    Bauer, T.L.3    Ohannesian, J.P.4    Marco, C.C.5    Goldstein, B.J.6
  • 21
    • 0028914922 scopus 로고
    • Thiazolidine derivatives ameliorate high glucose-induced insulin resistance via the normalization of protein-tyrosine phosphatase activities
    • Maegawa H., Ide R., Hasegawa M., Ugi S., Egawa K., Iwanishi M., Kikkawa R., Shigeta Y., Kashiwagi A. Thiazolidine derivatives ameliorate high glucose-induced insulin resistance via the normalization of protein-tyrosine phosphatase activities. J. Biol. Chem. 270:1995;7724-7730.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7724-7730
    • Maegawa, H.1    Ide, R.2    Hasegawa, M.3    Ugi, S.4    Egawa, K.5    Iwanishi, M.6    Kikkawa, R.7    Shigeta, Y.8    Kashiwagi, A.9
  • 27
    • 0031913246 scopus 로고    scopus 로고
    • Mechanism of activation and function of protein kinase B
    • Alessi D.R., Cohen P. Mechanism of activation and function of protein kinase B. Curr. Opin. Genet. Dev. 8:1998;55-62.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 55-62
    • Alessi, D.R.1    Cohen, P.2
  • 28
    • 0035856949 scopus 로고    scopus 로고
    • Mechanism of activation and function of protein kinase B
    • Saltiel A.R., Kahn C.R. Mechanism of activation and function of protein kinase B. Nature. 414:2001;799-806.
    • (2001) Nature , vol.414 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 29
    • 0030668521 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor
    • Liu F., Chernoff J. Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor. Biochem. J. 327:1997;139-145.
    • (1997) Biochem. J. , vol.327 , pp. 139-145
    • Liu, F.1    Chernoff, J.2
  • 30
    • 0029073832 scopus 로고
    • Alterations in specific protein-tyrosine phosphatases accompany insulin resistance of streptozotocin diabetes
    • Ahmad F., Goldstein B.J. Alterations in specific protein-tyrosine phosphatases accompany insulin resistance of streptozotocin diabetes. Am. J. Physiol. 268:1995;E932-E940.
    • (1995) Am. J. Physiol. , vol.268 , pp. 932-E940
    • Ahmad, F.1    Goldstein, B.J.2
  • 31
    • 0029548985 scopus 로고
    • Increased abundance of specific skeletal muscle protein-tyrosine phosphatases in a genetic model of insulin-resistant obesity and diabetes mellitus
    • Ahmad F., Goldstein B.J. Increased abundance of specific skeletal muscle protein-tyrosine phosphatases in a genetic model of insulin-resistant obesity and diabetes mellitus. Metabolism. 44:1995;1175-1184.
    • (1995) Metabolism , vol.44 , pp. 1175-1184
    • Ahmad, F.1    Goldstein, B.J.2
  • 34
    • 0030961536 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases PTP1B and syp are modulators of insulin-stimulated translocation of GLUT4 in transfected rat adipose cells
    • Chen H., Wertheimer S.J., Lin C.H., Katz S.L., Amrein K.E., Burn P., Quon M.J. Protein-tyrosine phosphatases PTP1B and syp are modulators of insulin-stimulated translocation of GLUT4 in transfected rat adipose cells. J. Biol. Chem. 272:1997;8026.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8026
    • Chen, H.1    Wertheimer, S.J.2    Lin, C.H.3    Katz, S.L.4    Amrein, K.E.5    Burn, P.6    Quon, M.J.7
  • 35
    • 0035152398 scopus 로고    scopus 로고
    • Decreased in situ insulin receptor dephosphorylation in hyperglycemia-induced insulin resistance in rat adipocytes
    • Tang S., Le-Tien H., Goldstein B.J., Shin P., Lai R., Fantus I.G. Decreased in situ insulin receptor dephosphorylation in hyperglycemia-induced insulin resistance in rat adipocytes. Diabetes. 50:2001;83-90.
    • (2001) Diabetes , vol.50 , pp. 83-90
    • Tang, S.1    Le-Tien, H.2    Goldstein, B.J.3    Shin, P.4    Lai, R.5    Fantus, I.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.