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Volumn 428, Issue 2, 2012, Pages 315-320

Pyrroloquinoline quinone, a novel protein tyrosine phosphatase 1B inhibitor, activates insulin signaling in C2C12 myotubes and improves impaired glucose tolerance in diabetic KK-Ay mice

Author keywords

Diabetes; Insulin resistance; Insulin signal; Protein tyrosine phosphatase 1B; Pyrroloquinoline quinone

Indexed keywords

GLUCOSE; GLUCOSE TRANSPORTER 4; INSULIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN KINASE B; PROTEIN TYROSINE PHOSPHATASE 1B; PYRROLOQUINOLINEQUINONE;

EID: 84869222944     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.10.055     Document Type: Article
Times cited : (37)

References (28)
  • 1
    • 84859441376 scopus 로고    scopus 로고
    • Obesity and type 2 diabetes: which patients are at risk?
    • Garber A.J. Obesity and type 2 diabetes: which patients are at risk?. Diabetes Obes. Metab. 2012, 14:399-408.
    • (2012) Diabetes Obes. Metab. , vol.14 , pp. 399-408
    • Garber, A.J.1
  • 2
    • 0035936763 scopus 로고    scopus 로고
    • New perspectives into the molecular pathogenesis and treatment of type 2 diabetes
    • Saltiel A.R. New perspectives into the molecular pathogenesis and treatment of type 2 diabetes. Cell 2001, 104:517-529.
    • (2001) Cell , vol.104 , pp. 517-529
    • Saltiel, A.R.1
  • 3
    • 0142090756 scopus 로고    scopus 로고
    • Clinical significance of targeting postprandial and fasting hyperglycemia in managing type 2 diabetes mellitus
    • Fonseca V. Clinical significance of targeting postprandial and fasting hyperglycemia in managing type 2 diabetes mellitus. Curr. Med. Res. Opin. 2003, 19:635-641.
    • (2003) Curr. Med. Res. Opin. , vol.19 , pp. 635-641
    • Fonseca, V.1
  • 4
    • 79960262492 scopus 로고    scopus 로고
    • Management of type 2 diabetes: new and future developments in treatment
    • Tahrani A.A., Bailey C.J., Del Prato S., et al. Management of type 2 diabetes: new and future developments in treatment. Lancet 2011, 378:182-197.
    • (2011) Lancet , vol.378 , pp. 182-197
    • Tahrani, A.A.1    Bailey, C.J.2    Del Prato, S.3
  • 5
    • 33845881411 scopus 로고    scopus 로고
    • Mechanisms linking obesity to insulin resistance and type 2 diabetes
    • Kahn S.E., Hull R.L., Utzschneider K.M. Mechanisms linking obesity to insulin resistance and type 2 diabetes. Nature 2006, 444:840-846.
    • (2006) Nature , vol.444 , pp. 840-846
    • Kahn, S.E.1    Hull, R.L.2    Utzschneider, K.M.3
  • 6
    • 0031941815 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase-1B acts as a negative regulator of insulin signal transduction
    • Byon J.C., Kusari A.B., Kusari J. Protein-tyrosine phosphatase-1B acts as a negative regulator of insulin signal transduction. Mol. Cell. Biochem. 1998, 182:101-108.
    • (1998) Mol. Cell. Biochem. , vol.182 , pp. 101-108
    • Byon, J.C.1    Kusari, A.B.2    Kusari, J.3
  • 7
    • 0029810614 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling
    • Kenner K.A., Anyanwu E., Olefsky J.M., et al. Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling. J. Biol. Chem. 1996, 271:19810-19816.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19810-19816
    • Kenner, K.A.1    Anyanwu, E.2    Olefsky, J.M.3
  • 8
    • 2642541849 scopus 로고    scopus 로고
    • Transgenic overexpression of protein-tyrosine phosphatase 1B in muscle causes insulin resistance, but overexpression with leukocyte antigen-related phosphatase does not additively impair insulin action
    • Zabolotny J.M., Haj F.G., Kim Y.B., et al. Transgenic overexpression of protein-tyrosine phosphatase 1B in muscle causes insulin resistance, but overexpression with leukocyte antigen-related phosphatase does not additively impair insulin action. J. Biol. Chem. 2004, 279:24844-24851.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24844-24851
    • Zabolotny, J.M.1    Haj, F.G.2    Kim, Y.B.3
  • 9
    • 0030840724 scopus 로고    scopus 로고
    • Alterations in skeletal muscle protein-tyrosine phosphatase activity and expression in insulin-resistant human obesity and diabetes
    • Ahmad F., Azevedo J.L., Cortright R., et al. Alterations in skeletal muscle protein-tyrosine phosphatase activity and expression in insulin-resistant human obesity and diabetes. J. Clin. Invest. 1997, 100:449-458.
    • (1997) J. Clin. Invest. , vol.100 , pp. 449-458
    • Ahmad, F.1    Azevedo, J.L.2    Cortright, R.3
  • 10
    • 0033180083 scopus 로고    scopus 로고
    • Marked impairment of protein tyrosine phosphatase 1B activity in adipose tissue of obese subjects with and without type 2 diabetes mellitus
    • Cheung A., Kusari J., Jansen D., et al. Marked impairment of protein tyrosine phosphatase 1B activity in adipose tissue of obese subjects with and without type 2 diabetes mellitus. J. Lab. Clin. Med. 1999, 134:115-123.
    • (1999) J. Lab. Clin. Med. , vol.134 , pp. 115-123
    • Cheung, A.1    Kusari, J.2    Jansen, D.3
  • 11
    • 84861846625 scopus 로고    scopus 로고
    • Skeletal muscle protein tyrosine phosphatase 1B regulates insulin sensitivity in African Americans
    • Stull A.J., Wang Z.Q., Zhang X.H., et al. Skeletal muscle protein tyrosine phosphatase 1B regulates insulin sensitivity in African Americans. Diabetes 2012, 61:1415-1422.
    • (2012) Diabetes , vol.61 , pp. 1415-1422
    • Stull, A.J.1    Wang, Z.Q.2    Zhang, X.H.3
  • 12
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene
    • Elchebly M., Payette P., Michaliszyn E., et al. Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science 1999, 283:1544-1548.
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1    Payette, P.2    Michaliszyn, E.3
  • 13
    • 0033942614 scopus 로고    scopus 로고
    • Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice
    • Klaman L.D., Boss O., Peroni O.D., et al. Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol. Cell Biol. 2000, 20:5479-5489.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 5479-5489
    • Klaman, L.D.1    Boss, O.2    Peroni, O.D.3
  • 14
    • 0037143754 scopus 로고    scopus 로고
    • PTP1B antisense oligonucleotide lowers PTP1B protein, normalizes blood glucose, and improves insulin sensitivity in diabetic mice
    • Zinker B.A., Rondinone C.M., Trevillyan J.M., et al. PTP1B antisense oligonucleotide lowers PTP1B protein, normalizes blood glucose, and improves insulin sensitivity in diabetic mice. Proc. Natl. Acad. Sci. USA 2002, 99:11357-11362.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11357-11362
    • Zinker, B.A.1    Rondinone, C.M.2    Trevillyan, J.M.3
  • 15
    • 4544356972 scopus 로고    scopus 로고
    • Reduction of PTP1B induces differential expression of PI3-kinase (p85alpha) isoforms
    • Rondinone C.M., Clampit J., Gum R.J., et al. Reduction of PTP1B induces differential expression of PI3-kinase (p85alpha) isoforms. Biochem. Biophys. Res. Commun. 2004, 323:652-659.
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 652-659
    • Rondinone, C.M.1    Clampit, J.2    Gum, R.J.3
  • 16
    • 79960073235 scopus 로고    scopus 로고
    • Novel protein tyrosine phosphatase 1B inhibitors: interaction requirements for improved intracellular efficacy in type 2 diabetes mellitus and obesity control
    • Popov D. Novel protein tyrosine phosphatase 1B inhibitors: interaction requirements for improved intracellular efficacy in type 2 diabetes mellitus and obesity control. Biochem. Biophys. Res. Commun. 2011, 410:377-381.
    • (2011) Biochem. Biophys. Res. Commun. , vol.410 , pp. 377-381
    • Popov, D.1
  • 17
    • 0034103006 scopus 로고    scopus 로고
    • Physiological importance of quinoenzymes and the o-quinone family of cofactors
    • Stites T.E., Mitchell A.E., Rucker R.B. Physiological importance of quinoenzymes and the o-quinone family of cofactors. J. Nutr. 2000, 130:719-727.
    • (2000) J. Nutr. , vol.130 , pp. 719-727
    • Stites, T.E.1    Mitchell, A.E.2    Rucker, R.B.3
  • 18
    • 0026679258 scopus 로고
    • Trace levels of pyrroloquinoline quinone in human and rat samples detected by gas chromatography/mass spectrometry
    • Kumazawa T., Seno H., Urakami T., et al. Trace levels of pyrroloquinoline quinone in human and rat samples detected by gas chromatography/mass spectrometry. Biochim. Biophys. Acta 1992, 1156:62-66.
    • (1992) Biochim. Biophys. Acta , vol.1156 , pp. 62-66
    • Kumazawa, T.1    Seno, H.2    Urakami, T.3
  • 19
    • 0028915272 scopus 로고
    • Levels of pyrroloquinoline quinone in various foods
    • Kumazawa T., Sato K., Seno H., et al. Levels of pyrroloquinoline quinone in various foods. Biochem. J. 1995, 307:331-333.
    • (1995) Biochem. J. , vol.307 , pp. 331-333
    • Kumazawa, T.1    Sato, K.2    Seno, H.3
  • 20
    • 84865288567 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone stimulates epithelial cell proliferation by activating epidermal growth factor receptor through redox cycling
    • Kimura K., Takada M., Ishii T., et al. Pyrroloquinoline quinone stimulates epithelial cell proliferation by activating epidermal growth factor receptor through redox cycling. Free Radic. Biol. Med. 2012, 53:1239-1251.
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 1239-1251
    • Kimura, K.1    Takada, M.2    Ishii, T.3
  • 21
    • 36148945620 scopus 로고    scopus 로고
    • Rapid preparation of a plasma membrane fraction from adipocytes and muscle cells: application to detection of translocated glucose transporter 4 on the plasma membrane
    • Nishiumi S., Ashida H Rapid preparation of a plasma membrane fraction from adipocytes and muscle cells: application to detection of translocated glucose transporter 4 on the plasma membrane. Biosci. Biotechnol. Biochem. 2007, 71:2343-2346.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 2343-2346
    • Nishiumi, S.1    Ashida, H.2
  • 22
    • 78751664582 scopus 로고    scopus 로고
    • Novel use of fluorescent glucose analogues to identify a new class of triazine-based insulin mimetics possessing useful secondary effects
    • Jung D.W., Ha H.H., Zheng X., et al. Novel use of fluorescent glucose analogues to identify a new class of triazine-based insulin mimetics possessing useful secondary effects. Mol. Biosyst. 2011, 7:346-358.
    • (2011) Mol. Biosyst. , vol.7 , pp. 346-358
    • Jung, D.W.1    Ha, H.H.2    Zheng, X.3
  • 23
    • 34547403216 scopus 로고    scopus 로고
    • Redox-dependent and ligand-independent trans-activation of insulin receptor by globular adiponectin
    • Fiaschi T., Buricchi F., Cozzi G., et al. Redox-dependent and ligand-independent trans-activation of insulin receptor by globular adiponectin. Hepatology 2007, 46:130-139.
    • (2007) Hepatology , vol.46 , pp. 130-139
    • Fiaschi, T.1    Buricchi, F.2    Cozzi, G.3
  • 24
    • 0037367940 scopus 로고    scopus 로고
    • Dynamics of the interaction between the insulin receptor and protein tyrosine-phosphatase 1B in living cells
    • Boute N., Boubekeur S., Lacasa D., et al. Dynamics of the interaction between the insulin receptor and protein tyrosine-phosphatase 1B in living cells. EMBO Rep. 2003, 4:313-319.
    • (2003) EMBO Rep. , vol.4 , pp. 313-319
    • Boute, N.1    Boubekeur, S.2    Lacasa, D.3
  • 25
    • 84864375702 scopus 로고    scopus 로고
    • Pyrroloquinoline-quinone and its versatile roles in biological processes
    • Misra H.S., Rajpurohit Y.S., Khairnar N.P. Pyrroloquinoline-quinone and its versatile roles in biological processes. J. Biosci. 2012, 37:313-325.
    • (2012) J. Biosci. , vol.37 , pp. 313-325
    • Misra, H.S.1    Rajpurohit, Y.S.2    Khairnar, N.P.3
  • 26
    • 0642276003 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction
    • Chiarugi P., Cirri P. Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction. Trends Biochem. Sci. 2003, 28:509-514.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 509-514
    • Chiarugi, P.1    Cirri, P.2
  • 27
    • 84867205473 scopus 로고    scopus 로고
    • Natural products possessing protein tyrosine phosphatase 1B (PTP1B) inhibitory activity found in the last decades
    • Jiang C.S., Liang L.F., Guo Y.W. Natural products possessing protein tyrosine phosphatase 1B (PTP1B) inhibitory activity found in the last decades. Acta Pharmacol. Sin. 2012, 10.1038/aps.2012.90.
    • (2012) Acta Pharmacol. Sin.
    • Jiang, C.S.1    Liang, L.F.2    Guo, Y.W.3
  • 28
    • 70350052853 scopus 로고    scopus 로고
    • Potential physiological importance of pyrroloquinoline quinone
    • Rucker R., Chowanadisai W., Nakano M. Potential physiological importance of pyrroloquinoline quinone. Altern. Med. Rev. 2009, 14:268-277.
    • (2009) Altern. Med. Rev. , vol.14 , pp. 268-277
    • Rucker, R.1    Chowanadisai, W.2    Nakano, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.