메뉴 건너뛰기




Volumn 299, Issue 2, 2010, Pages

Regulation of glucose- and mitochondrial fuel-induced insulin secretion by a cytosolic protein histidine phosphatase in pancreatic β-cells

Author keywords

Adenosine 5 triphosphate citrate lyase; nm23 H1

Indexed keywords

ADENOSINE TRIPHOSPHATE CITRATE LYASE; GLUCOSE; GUANINE NUCLEOTIDE BINDING PROTEIN; INSULIN; MASTOPARAN; PHOSPHATASE; PHOSPHOPROTEIN; POTASSIUM CHLORIDE; PROTEIN HISTIDINE PHOSPHATASE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; DYES, REAGENTS, INDICATORS, MARKERS AND BUFFERS; PHPT1 PROTEIN, HUMAN; PHPT1 PROTEIN, RAT;

EID: 77954897362     PISSN: 01931849     EISSN: 15221555     Source Type: Journal    
DOI: 10.1152/ajpendo.00091.2010     Document Type: Article
Times cited : (16)

References (45)
  • 1
    • 0028282042 scopus 로고
    • Protein histidine kinases and signal transduction in prokaryotes and eukaryotes
    • DOI 10.1016/0168-9525(94)90215-1
    • Alex LA, Simon MI. Protein histidine kinases and signal transduction in prokaryotes and eukaryotes. Trends Genet 10: 133-138, 1994. (Pubitemid 24107646)
    • (1994) Trends in Genetics , vol.10 , Issue.4 , pp. 133-138
    • Alex, L.A.1    Simon, M.I.2
  • 3
    • 30544433533 scopus 로고    scopus 로고
    • ATP citrate lyase is an important component of cell growth and transformation
    • DOI 10.1038/sj.onc.1208773, PII 1208773
    • Bauer DE, Hatzivassiliou G, Zhao F, Andreadis C, Thompson CB. ATP citrate lyase is an important component of cell growth and transformation. Oncogene 24: 6314-6322, 2005. (Pubitemid 43080054)
    • (2005) Oncogene , vol.24 , Issue.41 , pp. 6314-6322
    • Bauer, D.E.1    Hatzivassiliou, G.2    Zhao, F.3    Andreadis, C.4    Thompson, C.B.5
  • 4
    • 34447266956 scopus 로고    scopus 로고
    • Expression of protein histidine phosphatase in escherichia coli, purification, and determination of enzyme activity
    • Bäumer N, Mäurer A, Krieglstein J, Klumpp S. Expression of protein histidine phosphatase in escherichia coli, purification, and determination of enzyme activity. Methods Mol Biol 365: 247-260, 2007.
    • (2007) Methods Mol Biol , vol.365 , pp. 247-260
    • Bäumer, N.1    Mäurer, A.2    Krieglstein, J.3    Klumpp, S.4
  • 6
    • 0032993913 scopus 로고    scopus 로고
    • CaM kinase II: A protein kinase with extraordinary talents germane to insulin exocytosis
    • Easom RA. CaM kinase II: a protein kinase with extraordinary talents germane to insulin exocytosis. Diabetes 48: 675-684, 1999.
    • (1999) Diabetes , vol.48 , pp. 675-684
    • Easom, R.A.1
  • 7
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman AG. G proteins: transducers of receptor-generated signals. Annu Rev Biochem 56: 615-649, 1987.
    • (1987) Annu Rev Biochem , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 8
    • 37249016344 scopus 로고    scopus 로고
    • A role for ATP-citrate lyase, malic enzyme, and puruvate/citrate cycling in glucose-induced insulin secretion
    • Guay C, Madiraju SR, Aumais A, Joly E, Prentki M. A role for ATP-citrate lyase, malic enzyme, and puruvate/citrate cycling in glucose-induced insulin secretion. J Biol Chem 282: 35657-35665, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 35657-35665
    • Guay, C.1    Madiraju, S.R.2    Aumais, A.3    Joly, E.4    Prentki, M.5
  • 10
    • 0032459512 scopus 로고    scopus 로고
    • Protein kinases, protein phosphorylation, and the regulation of insulin secretion from pancreatic beta-cells
    • Jones PM, Persaud SJ. Protein kinases, protein phosphorylation, and the regulation of insulin secretion from pancreatic beta-cells. Endocr Rev 19: 429-461, 1998.
    • (1998) Endocr Rev , vol.19 , pp. 429-461
    • Jones, P.M.1    Persaud, S.J.2
  • 11
    • 0027325513 scopus 로고
    • Mastoparan stimulates insulin secretion from pancreatic beta-cells by effects at a late stage in the secretory pathway
    • Jones PM, Mann FM, Persaud SJ, Wheeler-Jones CP. Mastoparan stimulates insulin secretion from pancreatic beta-cells by effects at a late stage in the secretory pathway. Mol Cell Endocrinol 94: 97-103, 1993.
    • (1993) Mol Cell Endocrinol , vol.94 , pp. 97-103
    • Jones, P.M.1    Mann, F.M.2    Persaud, S.J.3    Wheeler-Jones, C.P.4
  • 12
  • 14
    • 0027279242 scopus 로고
    • Protein phosphatases 1, 2A, and 2C are protein histidine phosphatases
    • Kim Y, Huang J, Cohen P, Matthews HR. Protein phosphatases 1, 2A, and 2C are protein histidine phosphatases. J Biol Chem 268: 18513-18518, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 18513-18518
    • Kim, Y.1    Huang, J.2    Cohen, P.3    Matthews, H.R.4
  • 15
    • 0036176615 scopus 로고    scopus 로고
    • Phosphorylation and dephosphorylation of histidine residues in proteins
    • DOI 10.1046/j.1432-1033.2002.02755.x
    • Klumpp S, Krieglstein J. Phosphorylation and dephosphorylation of histidine residues in proteins. Eur J Biochem 269: 1067-1071, 2002. (Pubitemid 34175364)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.4 , pp. 1067-1071
    • Klumpp, S.1    Krieglstein, J.2
  • 16
    • 66149112136 scopus 로고    scopus 로고
    • Reversible phosphorylation of histidine residues in proteins from vertebrates
    • Klumpp S, Krieglstein J. Reversible phosphorylation of histidine residues in proteins from vertebrates. Sci Signal 2: pe13, 2009.
    • (2009) Sci Signal , vol.2
    • Klumpp, S.1    Krieglstein, J.2
  • 17
    • 0344665688 scopus 로고    scopus 로고
    • Detection of protein histidine phosphatase in vertebrates
    • Klumpp S, Hermesmeier J, Krieglstein J. Detection of protein histidine phosphatase in vertebrates. Methods Enzymol 366: 56-64, 2003.
    • (2003) Methods Enzymol , vol.366 , pp. 56-64
    • Klumpp, S.1    Hermesmeier, J.2    Krieglstein, J.3
  • 20
    • 0027425528 scopus 로고
    • Mastoparan stimulates exocytosis at a Ca(2+)-independent late site in stimulussecretion coupling. Studies with the RINm5F beta-cell line
    • Komatsu M, McDermott AM, Gillison SL, Sharp GW. Mastoparan stimulates exocytosis at a Ca(2+)-independent late site in stimulussecretion coupling. Studies with the RINm5F beta-cell line. J Biol Chem 268: 23297-23306, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 23297-23306
    • Komatsu, M.1    McDermott, A.M.2    Gillison, S.L.3    Sharp, G.W.4
  • 21
    • 0030065070 scopus 로고    scopus 로고
    • A novel regulatory mechanism for trimeric GTP-binding proteins in the membrane and secretory granule fractions of human and rodent beta cells
    • Kowluru A, Seavey SE, Rhodes CJ, Metz SA. A novel regulatory mechanism for trimeric GTP-binding proteins in the membrane and secretory granule fractions of human and rodent beta cells. Biochem J 313: 97-107, 1996. (Pubitemid 26013431)
    • (1996) Biochemical Journal , vol.313 , Issue.1 , pp. 97-107
    • Kowluru, A.1    Seavey, S.E.2    Rhodes, C.J.3    Metz, S.A.4
  • 22
    • 33644695681 scopus 로고    scopus 로고
    • Rho guanosine diphosphate-dissociation inhibitor plays a negative modulatory role in glucose-stimulated insulin secretion
    • Kowluru A, Veluthakal R. Rho guanosine diphosphate-dissociation inhibitor plays a negative modulatory role in glucose-stimulated insulin secretion. Diabetes 54: 3523-3529, 2005.
    • (2005) Diabetes , vol.54 , pp. 3523-3529
    • Kowluru, A.1    Veluthakal, R.2
  • 23
    • 0027947423 scopus 로고
    • Characterization of nucleoside diphosphokinase activity in human and rodent pancreatic beta cells: Evidence for its role in the formation of guanosine triphosphate, a permissive factor for nutrient-induced insulin secretion
    • Kowluru A, Metz SA. Characterization of nucleoside diphosphokinase activity in human and rodent pancreatic beta cells: evidence for its role in the formation of guanosine triphosphate, a permissive factor for nutrient-induced insulin secretion. Biochemistry 33: 12495-12503, 1994.
    • (1994) Biochemistry , vol.33 , pp. 12495-12503
    • Kowluru, A.1    Metz, S.A.2
  • 24
    • 0041464710 scopus 로고    scopus 로고
    • Defective protein histidine phosphorylation in islets from the Goto-Kakizaki diabetic rat
    • Kowluru A. Defective protein histidine phosphorylation in islets from the Goto-Kakizaki diabetic rat. Am J Physiol Endocrinol Metab 285: E498-E503, 2003. (Pubitemid 37010826)
    • (2003) American Journal of Physiology - Endocrinology and Metabolism , vol.285 , Issue.3
    • Kowluru, A.1
  • 25
    • 55149087200 scopus 로고    scopus 로고
    • Emerging roles for protein histidine phosphorylation in cellular signal transduction: Lessons from the islet beta-cell
    • Kowluru A. Emerging roles for protein histidine phosphorylation in cellular signal transduction: lessons from the islet beta-cell. J Cell Mol Med 12: 1885-1908, 2008.
    • (2008) J Cell Mol Med , vol.12 , pp. 1885-1908
    • Kowluru, A.1
  • 26
    • 76149107841 scopus 로고    scopus 로고
    • Small G proteins in islet beta-cell function
    • Kowluru A. Small G proteins in islet beta-cell function. Endocr Rev 31: 52-78, 2010.
    • (2010) Endocr Rev , vol.31 , pp. 52-78
    • Kowluru, A.1
  • 27
    • 35648954584 scopus 로고    scopus 로고
    • Feasibility of pathways for transfer of acyl groups from mitochondria to the cytosol to form short chain acyl-CoAs in the pancreatic beta-cell
    • MacDonald MJ, Smith AD, Hasan NM, Sabat G, Fahien LA. Feasibility of pathways for transfer of acyl groups from mitochondria to the cytosol to form short chain acyl-CoAs in the pancreatic beta-cell. J Biol Chem 282: 30596-30606, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 30596-30606
    • MacDonald, M.J.1    Smith, A.D.2    Hasan, N.M.3    Sabat, G.4    Fahien, L.A.5
  • 28
    • 0025597875 scopus 로고
    • Elusive proximal signals of beta-cells for insulin secretion
    • MacDonald MJ. Elusive proximal signals of beta-cells for insulin secretion. Diabetes 39: 1461-1466, 1990.
    • (1990) Diabetes , vol.39 , pp. 1461-1466
    • MacDonald, M.J.1
  • 29
    • 0034708619 scopus 로고    scopus 로고
    • The SixA phospho-histidine phosphatase modulates the ArcB phosphorelay signal transduction in Escherichia coli
    • Matsubara M, Mizuno T. The SixA phospho-histidine phosphatase modulates the ArcB phosphorelay signal transduction in Escherichia coli. FEBS Lett 470: 118-124, 2000.
    • (2000) FEBS Lett , vol.470 , pp. 118-124
    • Matsubara, M.1    Mizuno, T.2
  • 30
    • 0028829688 scopus 로고
    • Protein kinases and phosphatases that act on histidine, lysine, or arginine residues in eukaryotic proteins: A possible regulator of the mitogen-activated protein kinase cascade
    • Matthews HR. Protein kinases and phosphatases that act on histidine, lysine, or arginine residues in eukaryotic proteins: a possible regulator of the mitogen-activated protein kinase cascade. Pharmacol Ther 67: 323-350, 1995.
    • (1995) Pharmacol Ther , vol.67 , pp. 323-350
    • Matthews, H.R.1
  • 32
    • 0026331927 scopus 로고
    • The pancreatic islet as Rubik's Cube. Is phospholipid hydrolysis a piece of the puzzle?
    • Metz SA. The pancreatic islet as Rubik's Cube. Is phospholipid hydrolysis a piece of the puzzle? Diabetes 40: 1565-1573, 1991.
    • (1991) Diabetes , vol.40 , pp. 1565-1573
    • Metz, S.A.1
  • 34
    • 0029071517 scopus 로고
    • Metabolic coupling factors in pancreatic beta-cell signal transduction
    • Newgard CB, McGarry JD. Metabolic coupling factors in pancreatic beta-cell signal transduction. Annu Rev Biochem 64: 689-719, 1995.
    • (1995) Annu Rev Biochem , vol.64 , pp. 689-719
    • Newgard, C.B.1    McGarry, J.D.2
  • 35
    • 0027483305 scopus 로고
    • Two phosphatases for 6-phospholysine and 3-phosphohistidine from rat brain
    • Ohmori H, Kuba M, Kumon A. Two phosphatases for 6-phospholysine and 3-phosphohistidine from rat brain. J Biol Chem 268: 7625-7627, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 7625-7627
    • Ohmori, H.1    Kuba, M.2    Kumon, A.3
  • 36
    • 0023525741 scopus 로고
    • Ca2+, cAMP, and phospholipid-derived messengers in coupling mechanisms of insulin secretion
    • Prentki M, Matschinsky FM. Ca2+, cAMP, and phospholipid-derived messengers in coupling mechanisms of insulin secretion. Physiol Rev 67: 1185-1248, 1987.
    • (1987) Physiol Rev , vol.67 , pp. 1185-1248
    • Prentki, M.1    Matschinsky, F.M.2
  • 37
    • 0000203136 scopus 로고
    • The citrate cleavage enzyme. I. Distribution and purification
    • Srere PA. The citrate cleavage enzyme. I. Distribution and purification. J Biol Chem 234: 2544-2547, 1959.
    • (1959) J Biol Chem , vol.234 , pp. 2544-2547
    • Srere, P.A.1
  • 38
    • 0037177222 scopus 로고    scopus 로고
    • Mammalian histidine kinases: Do they REALLY exist?
    • Tan E, Besant PG, Attwood PV. Mammalian histidine kinases: do they REALLY exist? Biochemistry 41: 3843-3851, 2002.
    • (2002) Biochemistry , vol.41 , pp. 3843-3851
    • Tan, E.1    Besant, P.G.2    Attwood, P.V.3
  • 39
    • 33847042302 scopus 로고    scopus 로고
    • Dominant-negative alpha-subunit of farnesyl- and geranyltransferase inhibits glucose-stimulated, but not KCl-stimulated, insulin secretion in INS 832/13 cells
    • DOI 10.2337/db06-0668
    • Veluthakal R, Kaur H, Goalstone M, Kowluru A. Dominant-negative alpha-subunit of farnesyl- and geranyltransferase inhibits glucose-stimulated, but not KCl-stimulated, insulin secretion in INS 832/13 cells. Diabetes 56: 204-210, 2007. (Pubitemid 46263120)
    • (2007) Diabetes , vol.56 , Issue.1 , pp. 204-210
    • Veluthakal, R.1    Kaur, H.2    Goalstone, M.3    Kowluru, A.4
  • 40
    • 70449730103 scopus 로고    scopus 로고
    • Down-regulation of expression and function of nucleoside diphosphate kinase in insulin-secreting beta-cells under in vitro conditions of glucolipotoxicity
    • Veluthakal R, Suresh MV, Kowluru A. Down-regulation of expression and function of nucleoside diphosphate kinase in insulin-secreting beta-cells under in vitro conditions of glucolipotoxicity. Mol Cell Biochem 329:121-129, 2009.
    • (2009) Mol Cell Biochem , vol.329 , pp. 121-129
    • Veluthakal, R.1    Suresh, M.V.2    Kowluru, A.3
  • 41
    • 0029101744 scopus 로고
    • Phosphorylation of ATP-citrate lyase by nucleoside diphosphate kinase
    • Wagner PD, Vu ND. Phosphorylation of ATP-citrate lyase by nucleoside diphosphate kinase. J Biol Chem 270: 21758-21764, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 21758-21764
    • Wagner, P.D.1    Vu, N.D.2
  • 42
    • 0025114462 scopus 로고
    • A filter-based protein kinase assay selective for alkali-stable protein phosphorylation and suitable for acid-labile protein phosphorylation
    • Wei YF, Matthews HR. A filter-based protein kinase assay selective for alkali-stable protein phosphorylation and suitable for acid-labile protein phosphorylation. Anal Biochem 190: 188-192, 1990.
    • (1990) Anal Biochem , vol.190 , pp. 188-192
    • Wei, Y.F.1    Matthews, H.R.2
  • 43
    • 0027494437 scopus 로고
    • Phosphohistidine and phospholysine phosphatase activities in the rat: Potential protein-lysine and protein-histidine phosphatases?
    • Wong C, Faiola B, Wu W, Kennelly PJ. Phosphohistidine and phospholysine phosphatase activities in the rat: potential protein-lysine and protein-histidine phosphatases? Biochem J 296: 293-296, 1993. (Pubitemid 23350825)
    • (1993) Biochemical Journal , vol.296 , Issue.2 , pp. 293-296
    • Wong, C.1    Faiola, B.2    Wu, W.3    Kennelly, P.J.4
  • 44
    • 71549168985 scopus 로고    scopus 로고
    • 14-kDa phosphohistidine phosphatase and its role in human lung cancer cell migration and invasion
    • Xu A, Hao J, Zhang Z, Tian T, Jiang S, Hao J, Liu C, Huang L, Xiao X, He D. 14-kDa phosphohistidine phosphatase and its role in human lung cancer cell migration and invasion. Lung Cancer 67: 48-56, 2010.
    • (2010) Lung Cancer , vol.67 , pp. 48-56
    • Xu, A.1    Hao, J.2    Zhang, Z.3    Tian, T.4    Jiang, S.5    Hao, J.6    Liu, C.7    Huang, L.8    Xiao, X.9    He, D.10
  • 45
    • 67650608424 scopus 로고    scopus 로고
    • Immunohistochemical localization of phosphohistidine phosphatase PHPT1 in mouse and human tissues
    • Zhang XQ, Sundh UB, Jansson L, Zetterqvist O, Ek P. Immunohistochemical localization of phosphohistidine phosphatase PHPT1 in mouse and human tissues. Ups J Med Sci 114: 65-72, 2009.
    • (2009) Ups J Med Sci , vol.114 , pp. 65-72
    • Zhang, X.Q.1    Sundh, U.B.2    Jansson, L.3    Zetterqvist, O.4    Ek, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.