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Volumn 6, Issue 4, 2005, Pages 303-315

Have we overlooked the importance of serine/threonine protein phosphatases in pancreatic beta-cells? Role played by protein phosphatase 2A in insulin secretion

Author keywords

Insulin; Islets of Langerhans; Phosphoprotein phosphatase; Phosphorylation

Indexed keywords

GLUCOSE; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PROTEIN KINASE; CALCINEURIN; INSULIN; PHOSPHOPROTEIN; PHOSPHOPROTEIN PHOSPHATASE;

EID: 27244432413     PISSN: 15908577     EISSN: 15908577     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (9)

References (99)
  • 1
    • 6344272636 scopus 로고    scopus 로고
    • Type 2 diabetes and disease management: Exploring the connections
    • Segal KR. Type 2 diabetes and disease management: exploring the connections. Dis Manag 2004; 7(Suppl 1):S11-22.
    • (2004) Dis. Manag. , vol.7 , Issue.SUPPL. 1
    • Segal, K.R.1
  • 2
    • 0345374579 scopus 로고    scopus 로고
    • Minireview: Weapons of lean body mass destruction: The role of ectopic lipids in the metabolic syndrome
    • Unger RH. Minireview: weapons of lean body mass destruction: the role of ectopic lipids in the metabolic syndrome. Endocrinology 2003; 144:5159-65.
    • (2003) Endocrinology , vol.144 , pp. 5159-5165
    • Unger, R.H.1
  • 3
    • 0036402110 scopus 로고    scopus 로고
    • Metabolic lessons from genetically lean mice
    • Reitman ML. Metabolic lessons from genetically lean mice Annu Rev Nutr 2002; 22:459-82.
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 459-482
    • Reitman, M.L.1
  • 4
    • 0348162332 scopus 로고    scopus 로고
    • Insulin resistance: From benign to type 2 diabetes mellitus
    • Goldstein BJ. Insulin resistance: from benign to type 2 diabetes mellitus. Rev Cardiovasc Med 2003; 4(Suppl 6):S3-10.
    • (2003) Rev. Cardiovasc. Med. , vol.4 , Issue.SUPPL. 6
    • Goldstein, B.J.1
  • 5
    • 2342509113 scopus 로고    scopus 로고
    • Pathophysiology of insulin secretion
    • Scheen AJ. Pathophysiology of insulin secretion. Ann Endocrinol (Paris) 2004; 65:29-36.
    • (2004) Ann. Endocrinol. (Paris) , vol.65 , pp. 29-36
    • Scheen, A.J.1
  • 6
    • 0141762722 scopus 로고    scopus 로고
    • Transmitted beta-cell dysfunction as a cause for type 2-diabetes
    • Portha B. Transmitted beta-cell dysfunction as a cause for type 2-diabetes. Med Sci (Paris) 2003; 19:847-53.
    • (2003) Med. Sci. (Paris) , vol.19 , pp. 847-853
    • Portha, B.1
  • 7
    • 0036910731 scopus 로고    scopus 로고
    • Apoptosis in the beta cells: Cause or consequence of insulin secretion defect in diabetes?
    • Sesti G. Apoptosis in the beta cells: cause or consequence of insulin secretion defect in diabetes? Ann Med 2002; 34:444-50.
    • (2002) Ann. Med. , vol.34 , pp. 444-450
    • Sesti, G.1
  • 8
    • 0028610124 scopus 로고
    • New perspectives on the actions of sulphonylureas and hyperglycaemic sulphonamides on the pancreatic beta-cell
    • Flatt PR, Shibier O, Szecowka J, Berggren PO. New perspectives on the actions of sulphonylureas and hyperglycaemic sulphonamides on the pancreatic beta-cell. Diabete Metab 1994; 20:157-62.
    • (1994) Diabete Metab. , vol.20 , pp. 157-162
    • Flatt, P.R.1    Shibier, O.2    Szecowka, J.3    Berggren, P.O.4
  • 10
    • 0347990624 scopus 로고    scopus 로고
    • Epac: A new cAMP-binding protein in support of glucagon-like peptide-1 receptor-mediated signal transduction in the pancreatic beta-cell
    • Holz GG. Epac: A new cAMP-binding protein in support of glucagon-like peptide-1 receptor-mediated signal transduction in the pancreatic beta-cell. Diabetes 2004; 53:5-13.
    • (2004) Diabetes , vol.53 , pp. 5-13
    • Holz, G.G.1
  • 11
    • 0036155789 scopus 로고    scopus 로고
    • Intracellular Ca(2+) modulation of ATP-sensitive K(+) channel activity in acetylcholine-induced activation of rat pancreatic beta-cells
    • Nakano K, Suga S, Takeo T, Ogawa Y, Suda T, Kanno T, Wakui M. Intracellular Ca(2+) modulation of ATP-sensitive K(+) channel activity in acetylcholine-induced activation of rat pancreatic beta-cells. Endocrinology 2002; 143:569-76.
    • (2002) Endocrinology , vol.143 , pp. 569-576
    • Nakano, K.1    Suga, S.2    Takeo, T.3    Ogawa, Y.4    Suda, T.5    Kanno, T.6    Wakui, M.7
  • 12
    • 0036311359 scopus 로고    scopus 로고
    • Role of oscillations in membrane potential, cytoplasmic Ca2+, and metabolism for plasma insulin oscillations
    • Bergsten P. Role of oscillations in membrane potential, cytoplasmic Ca2+, and metabolism for plasma insulin oscillations. Diabetes 2002; 51(Suppl 1):S171-6.
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 1
    • Bergsten, P.1
  • 13
    • 0032575599 scopus 로고    scopus 로고
    • Nutrient stimulation results in a rapid Ca2+-dependent threonine phosphorylation of myosin heavy chain in rat pancreatic islets and RINm5F cells
    • Wilson JR, Ludowyke RI, Biden TJ. Nutrient stimulation results in a rapid Ca2+-dependent threonine phosphorylation of myosin heavy chain in rat pancreatic islets and RINm5F cells. J Biol Chem 1998; 273:22729-37.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22729-22737
    • Wilson, J.R.1    Ludowyke, R.I.2    Biden, T.J.3
  • 14
    • 0030809973 scopus 로고    scopus 로고
    • Calcium-stimulated phosphorylation of MAP-2 in pancreatic betaTC3-cells is mediated by Ca2+/calmodulin-dependent kinase II
    • Krueger KA, Bhatt H, Landt M, Easom RA. Calcium-stimulated phosphorylation of MAP-2 in pancreatic betaTC3-cells is mediated by Ca2+/calmodulin-dependent kinase II. J Biol Chem 1997; 272:27464-9.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27464-27469
    • Krueger, K.A.1    Bhatt, H.2    Landt, M.3    Easom, R.A.4
  • 15
    • 0036314213 scopus 로고    scopus 로고
    • Beta-cell protein kinases and the dynamics of the insulin response to glucose
    • Nesher R, Anteby E, Yedovizky M, Warwar N, Kaiser N, Cerasi E. Beta-cell protein kinases and the dynamics of the insulin response to glucose. Diabetes 2002; 51(Suppl 1):S68-73.
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 1
    • Nesher, R.1    Anteby, E.2    Yedovizky, M.3    Warwar, N.4    Kaiser, N.5    Cerasi, E.6
  • 16
    • 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 1998; 19:429-61.
    • (1998) Endocr. Rev. , vol.19 , pp. 429-461
    • Jones, P.M.1    Persaud, S.J.2
  • 17
    • 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 1999; 48:675-84.
    • (1999) Diabetes , vol.48 , pp. 675-684
    • Easom, R.A.1
  • 19
    • 1942504876 scopus 로고    scopus 로고
    • Cell signalling in vascular cells exposed to cyclic strain: The emerging role of protein phosphatases
    • Lee T, Sumpio BE. Cell signalling in vascular cells exposed to cyclic strain: the emerging role of protein phosphatases. Biotechnol Appl Biochem 2004; 39(Pt 2):129-39.
    • (2004) Biotechnol. Appl. Biochem. , vol.39 , Issue.PART 2 , pp. 129-139
    • Lee, T.1    Sumpio, B.E.2
  • 20
    • 0036667397 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatases in apoptosis
    • Klumpp S, Krieglstein J. Serine/threonine protein phosphatases in apoptosis. Curr Opin Pharmacol 2002; 2:458-62.
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 458-462
    • Klumpp, S.1    Krieglstein, J.2
  • 21
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • Wera S, Hemmings BA. Serine/threonine protein phosphatases. Biochem J 1995; 311(Pt. 1):17-29.
    • (1995) Biochem. J. , vol.311 , Issue.PART 1 , pp. 17-29
    • Wera, S.1    Hemmings, B.A.2
  • 22
    • 0034614490 scopus 로고    scopus 로고
    • Signaling - 2000 and beyond
    • Hunter T. Signaling - 2000 and beyond. Cell 2000; 100:113-27.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 23
  • 24
    • 0028955176 scopus 로고
    • An emerging family of dual specificity MAP kinase phosphatases
    • Keyse SM. An emerging family of dual specificity MAP kinase phosphatases. Biochim Biophys Acta 1995; 1265:152-60.
    • (1995) Biochim. Biophys. Acta , vol.1265 , pp. 152-160
    • Keyse, S.M.1
  • 25
    • 27744461943 scopus 로고    scopus 로고
    • Laboratory of Marc Mumby at the University of Texas Southwestern Medical Center. Protein serine/threonine phosphatases (Viewed on May 13th,)
    • Laboratory of Marc Mumby at the University of Texas Southwestern Medical Center. Protein serine/threonine phosphatases (Viewed on May 13th, 2005). http://www4.utsouthwestern.edu/mumbylab/PPPTBL.htm
    • (2005)
  • 26
    • 0033153258 scopus 로고    scopus 로고
    • Brain protein serine/threonine phosphatases
    • Price NE, Mumby MC. Brain protein serine/threonine phosphatases. Curr Opin Neurobiol 1999; 9:336-42.
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 336-342
    • Price, N.E.1    Mumby, M.C.2
  • 27
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. The structure and regulation of protein phosphatases. Annu Rev Biochem 1989; 58:453-508.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 453-508
    • Cohen, P.1
  • 28
    • 0029885298 scopus 로고    scopus 로고
    • The phosphatase inhibitor okadaic acid blocks KCl-depolarization-induced rise of cytosolic calcium of rat insulinoma cells (RINm5F)
    • Ammon HP, Heurich RO, Kolb HA, Lang F, Schaich R, Drews G, Leiers T. The phosphatase inhibitor okadaic acid blocks KCl-depolarization-induced rise of cytosolic calcium of rat insulinoma cells (RINm5F). Naunyn Schmiedebergs Arch Pharmacol 1996; 354:95-101.
    • (1996) Naunyn Schmiedebergs Arch. Pharmacol. , vol.354 , pp. 95-101
    • Ammon, H.P.1    Heurich, R.O.2    Kolb, H.A.3    Lang, F.4    Schaich, R.5    Drews, G.6    Leiers, T.7
  • 29
    • 0035856942 scopus 로고    scopus 로고
    • Mitochondrial function in normal and diabetic beta-cells
    • Maechler P, Wollheim CB. Mitochondrial function in normal and diabetic beta-cells. Nature 2001; 414:807-12.
    • (2001) Nature , vol.414 , pp. 807-812
    • Maechler, P.1    Wollheim, C.B.2
  • 30
    • 13444291243 scopus 로고    scopus 로고
    • Glutamate inhibits protein phosphatases and promotes insulin exocytosis in pancreatic beta-c.ells
    • Lehtihet M, Honkanen RE, Sjoholm A. Glutamate inhibits protein phosphatases and promotes insulin exocytosis in pancreatic beta-c.ells Biochem Biophys Res Commun 2005; 328:601-7.
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 601-607
    • Lehtihet, M.1    Honkanen, R.E.2    Sjoholm, A.3
  • 31
    • 0030667979 scopus 로고    scopus 로고
    • Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate
    • Larsson O, Barker CJ, Sjoholm A, Carlqvist H, Michell RH, Bertorello A, et al. Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate. Science 1997; 278:471-4.
    • (1997) Science , vol.278 , pp. 471-474
    • Larsson, O.1    Barker, C.J.2    Sjoholm, A.3    Carlqvist, H.4    Michell, R.H.5    Bertorello, A.6
  • 32
    • 0343986297 scopus 로고    scopus 로고
    • Polyamines regulate serine/threonine protein phosphatases in insulin-secreting cells
    • Sjoholm A, Honkanen RE. Polyamines regulate serine/threonine protein phosphatases in insulin-secreting cells. Pancreas 2000; 20:32-7.
    • (2000) Pancreas , vol.20 , pp. 32-37
    • Sjoholm, A.1    Honkanen, R.E.2
  • 33
    • 0030898013 scopus 로고    scopus 로고
    • Inhibitory effect of sulfonylureas on protein phosphatase activity in rat pancreatic islets
    • Gagliardino, J. J., Rossi, P. F., and Garcia, M. E. Inhibitory effect of sulfonylureas on protein phosphatase activity in rat pancreatic islets. Acta Diabetol 1997; 34:6-9.
    • (1997) Acta Diabetol. , vol.34 , pp. 6-9
    • Gagliardino, J.J.1    Rossi, P.F.2    Garcia, M.E.3
  • 34
    • 1642373039 scopus 로고    scopus 로고
    • Inositol hexakisphosphate and sulfonylureas regulate beta-cell protein phosphatases
    • Lehtihet M, Honkanen RE, Sjoholm A. Inositol hexakisphosphate and sulfonylureas regulate beta-cell protein phosphatases. Biochem Biophys Res Commun 2004; 316:893-7.
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 893-897
    • Lehtihet, M.1    Honkanen, R.E.2    Sjoholm, A.3
  • 35
    • 1442285922 scopus 로고    scopus 로고
    • PP2A fulfills its promises as tumor suppressor: Which subunits are important?
    • Van Hoof C, Goris J. PP2A fulfills its promises as tumor suppressor: which subunits are important? Cancer Cell 2004; 5:105-6.
    • (2004) Cancer Cell , vol.5 , pp. 105-106
    • Van Hoof, C.1    Goris, J.2
  • 36
    • 0025275038 scopus 로고
    • Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure
    • Hemmings BA, Adams-Pearson C, Maurer F, Muller P, Goris J, Merlevede W, et al. alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure. Biochemistry 1990; 29:3166-73.
    • (1990) Biochemistry , vol.29 , pp. 3166-3173
    • Hemmings, B.A.1    Adams-Pearson, C.2    Maurer, F.3    Muller, P.4    Goris, J.5    Merlevede, W.6
  • 37
    • 0029834655 scopus 로고    scopus 로고
    • The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm
    • McCright B, Rivers AM, Audlin S, Virshup DM. The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm. J Biol Chem 1996; 271:22081-9.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22081-22089
    • McCright, B.1    Rivers, A.M.2    Audlin, S.3    Virshup, D.M.4
  • 38
    • 0032536810 scopus 로고    scopus 로고
    • Brain protein phosphatase 2A: Developmental regulation and distinct cellular and subcellular localization by B subunits
    • Strack S, Zaucha JA, Ebner FF, Colbran RJ, Wadzinski BE. Brain protein phosphatase 2A: developmental regulation and distinct cellular and subcellular localization by B subunits. J Comp Neurol 1998; 392:515-27.
    • (1998) J. Comp. Neurol. , vol.392 , pp. 515-527
    • Strack, S.1    Zaucha, J.A.2    Ebner, F.F.3    Colbran, R.J.4    Wadzinski, B.E.5
  • 39
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer EJ, Schmidt CJ, Nambudripad R, Smith TF. The ancient regulatory-protein family of WD-repeat proteins. Nature 1994; 371:297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 40
    • 0034050449 scopus 로고    scopus 로고
    • WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A
    • Moreno CS, Park S, Nelson K, Ashby D, Hubalek F, Lane WS, Pallas DC. WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A. J Biol Chem 2000; 275:5257-63.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5257-5263
    • Moreno, C.S.1    Park, S.2    Nelson, K.3    Ashby, D.4    Hubalek, F.5    Lane, W.S.6    Pallas, D.C.7
  • 42
    • 0037705347 scopus 로고    scopus 로고
    • Glucose regulates EF-2 phosphorylation and protein translation by a protein phosphatase-2A-dependent mechanism in INS-1-derived 832/13 cells
    • Yan L, Nairn AC, Palfrey HC, Brady MJ. Glucose regulates EF-2 phosphorylation and protein translation by a protein phosphatase-2A-dependent mechanism in INS-1-derived 832/13 cells. J Biol Chem 2003; 278:18177-83.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18177-18183
    • Yan, L.1    Nairn, A.C.2    Palfrey, H.C.3    Brady, M.J.4
  • 43
    • 0030296869 scopus 로고    scopus 로고
    • Molecular mechanisms of the protein serine/threonine phosphatases
    • Barford D. Molecular mechanisms of the protein serine/threonine phosphatases. Trends Biochem Sci 1996; 21:407-12.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 407-412
    • Barford, D.1
  • 44
    • 0028168815 scopus 로고
    • Okadaic acid indicates a major function for protein phosphatases in stimulus-response coupling of RINm5F rat insulinoma cells
    • Mayer P, Jochum C, Schatz H, Pfeiffer A. Okadaic acid indicates a major function for protein phosphatases in stimulus-response coupling of RINm5F rat insulinoma cells Exp Clin Endocrinol 1994; 102:313-9.
    • (1994) Exp. Clin. Endocrinol. , vol.102 , pp. 313-319
    • Mayer, P.1    Jochum, C.2    Schatz, H.3    Pfeiffer, A.4
  • 45
    • 0027441369 scopus 로고
    • Effects of okadaic acid on insulin secretion from rat islets of Langerhans
    • Ratcliff H, Jones PM. Effects of okadaic acid on insulin secretion from rat islets of Langerhans. Biochim Biophys Acta 1993; 1175:188-91.
    • (1993) Biochim. Biophys. Acta , vol.1175 , pp. 188-191
    • Ratcliff, H.1    Jones, P.M.2
  • 46
    • 0025635610 scopus 로고
    • Tautomycin from the bacterium Streptomyces verticillatus. Another potent and specific inhibitor of protein phosphatases 1 and 2A
    • MacKintosh C, Klumpp S. Tautomycin from the bacterium Streptomyces verticillatus. Another potent and specific inhibitor of protein phosphatases 1 and 2A. FEBS Lett 1990; 277:137-40.
    • (1990) FEBS Lett. , vol.277 , pp. 137-140
    • MacKintosh, C.1    Klumpp, S.2
  • 47
    • 0030720062 scopus 로고    scopus 로고
    • Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A
    • Walsh AH, Cheng A, Honkanen RE. Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A. FEBS Lett 1997; 416:230-4.
    • (1997) FEBS Lett. , vol.416 , pp. 230-234
    • Walsh, A.H.1    Cheng, A.2    Honkanen, R.E.3
  • 48
    • 0032167375 scopus 로고    scopus 로고
    • Fostriecin, an inhibitor of protein phosphatase 2A, limits myocardial infarct size even when administered after onset of ischemia
    • Weinbrenner C, Baines CP, Liu GS, Armstrong SC, Ganote CE, Walsh AH, et al. Fostriecin, an inhibitor of protein phosphatase 2A, limits myocardial infarct size even when administered after onset of ischemia. Circulation 1998; 98:899-905.
    • (1998) Circulation , vol.98 , pp. 899-905
    • Weinbrenner, C.1    Baines, C.P.2    Liu, G.S.3    Armstrong, S.C.4    Ganote, C.E.5    Walsh, A.H.6
  • 49
    • 0035941486 scopus 로고    scopus 로고
    • Characterization of a rice (Oryza sativa L.) Bowman-Birk proteinase inhibitor: Tightly light regulated induction in response to cut, jasmonic acid, ethylene and protein phosphatase 2A inhibitors
    • Rakwal R, Kumar Agrawal G, Jwa NS. Characterization of a rice (Oryza sativa L.) Bowman-Birk proteinase inhibitor: tightly light regulated induction in response to cut, jasmonic acid, ethylene and protein phosphatase 2A inhibitors. Gene 2001; 263:189-98.
    • (2001) Gene , vol.263 , pp. 189-198
    • Rakwal, R.1    Kumar Agrawal, G.2    Jwa, N.S.3
  • 50
    • 0028295386 scopus 로고
    • Inhibition of serine/threonine protein phosphatases promotes opening of voltage-activated L-type Ca2+ channels in insulin-secreting cells
    • Haby C, Larsson O, Islam MS, Aunis D, Berggren PO, Zwiller J. Inhibition of serine/threonine protein phosphatases promotes opening of voltage-activated L-type Ca2+ channels in insulin-secreting cells. Biochem J 1994; 298(Pt 2):341-6.
    • (1994) Biochem. J. , vol.298 , Issue.PART 2 , pp. 341-346
    • Haby, C.1    Larsson, O.2    Islam, M.S.3    Aunis, D.4    Berggren, P.O.5    Zwiller, J.6
  • 51
    • 0028205382 scopus 로고
    • Activation of protein kinases and inhibition of protein phosphatases play a central role in the regulation of exocytosis in mouse pancreatic beta cells
    • Ammala C, Eliasson L, Bokvist K, Berggren PO, Honkanen RE, Sjoholm A, Rorsman P. Activation of protein kinases and inhibition of protein phosphatases play a central role in the regulation of exocytosis in mouse pancreatic beta cells. Proc Natl Acad Sci U S A 1994; 91:4343-7.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 4343-4347
    • Ammala, C.1    Eliasson, L.2    Bokvist, K.3    Berggren, P.O.4    Honkanen, R.E.5    Sjoholm, A.6    Rorsman, P.7
  • 52
    • 0026732757 scopus 로고
    • Effects of the protein phosphatase inhibitors okadaic acid and calyculin A on insulin release from rat pancreatic islets
    • Tamagawa T, Iguchi A, Uemura K, Miura H, Nonogaki K, Ishiguro T, Sakamoto N. Effects of the protein phosphatase inhibitors okadaic acid and calyculin A on insulin release from rat pancreatic islets. Endocrinol Jpn 1992; 39:325-9.
    • (1992) Endocrinol. Jpn. , vol.39 , pp. 325-329
    • Tamagawa, T.1    Iguchi, A.2    Uemura, K.3    Miura, H.4    Nonogaki, K.5    Ishiguro, T.6    Sakamoto, N.7
  • 53
    • 0031963810 scopus 로고    scopus 로고
    • Okadaic acid-induced decrease in the magnitude and efficacy of the Ca2+ signal in pancreatic beta cells and inhibition of insulin secretion
    • Sato Y, Mariot P, Detimary P, Gilon P, Henquin JC. Okadaic acid-induced decrease in the magnitude and efficacy of the Ca2+ signal in pancreatic beta cells and inhibition of insulin secretion. Br J Pharmacol 1998; 123:97-105.
    • (1998) Br. J. Pharmacol. , vol.123 , pp. 97-105
    • Sato, Y.1    Mariot, P.2    Detimary, P.3    Gilon, P.4    Henquin, J.C.5
  • 54
    • 0033954554 scopus 로고    scopus 로고
    • Effects of serine/threonine protein phosphatases on ion channels in excitable membranes
    • Herzig S, Neumann J. Effects of serine/threonine protein phosphatases on ion channels in excitable membranes. Physiol Rev 2000; 80:173-210.
    • (2000) Physiol. Rev. , vol.80 , pp. 173-210
    • Herzig, S.1    Neumann, J.2
  • 55
    • 0029164488 scopus 로고
    • Inhibition of serine/threonine protein phosphatases by secretagogues in insulin-secreting cells
    • Sjoholm A, Honkanen RE, Berggren PO. Inhibition of serine/threonine protein phosphatases by secretagogues in insulin-secreting cells. Endocrinology 1995; 136:3391-7.
    • (1995) Endocrinology , vol.136 , pp. 3391-3397
    • Sjoholm, A.1    Honkanen, R.E.2    Berggren, P.O.3
  • 56
    • 0036892130 scopus 로고    scopus 로고
    • Glucose metabolites inhibit protein phosphatases and directly promote insulin exocytosis in pancreatic beta-cells
    • Sjoholm A, Lehtihet M, Efanov AM, Zaitsev SV, Berggren PO, Honkanen RE. Glucose metabolites inhibit protein phosphatases and directly promote insulin exocytosis in pancreatic beta-cells. Endocrinology 2002; 143:4592-8.
    • (2002) Endocrinology , vol.143 , pp. 4592-4598
    • Sjoholm, A.1    Lehtihet, M.2    Efanov, A.M.3    Zaitsev, S.V.4    Berggren, P.O.5    Honkanen, R.E.6
  • 57
    • 0026713268 scopus 로고
    • Effects of fructose 2,6-bisphosphate and glucose 1,6-bisphosphate on porcine heart protein phosphatase 2A
    • Erickson AK, Killilea SD. Effects of fructose 2,6-bisphosphate and glucose 1,6-bisphosphate on porcine heart protein phosphatase 2A. Biochem Int 1992; 27:353-9.
    • (1992) Biochem. Int. , vol.27 , pp. 353-359
    • Erickson, A.K.1    Killilea, S.D.2
  • 59
    • 0034331359 scopus 로고    scopus 로고
    • Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits
    • Tolstykh T, Lee J, Vafai S, Stock JB. Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits. EMBO J 2000; 19:5682-91.
    • (2000) EMBO J. , vol.19 , pp. 5682-5691
    • Tolstykh, T.1    Lee, J.2    Vafai, S.3    Stock, J.B.4
  • 60
    • 0029887332 scopus 로고    scopus 로고
    • Carboxylmethylation of the catalytic subunit of protein phosphatase 2A in insulin-secreting cells: Evidence for functional consequences on enzyme activity and insulin secretion
    • Kowluru A, Seavey SE, Rabaglia ME, Nesher R, Metz SA. Carboxylmethylation of the catalytic subunit of protein phosphatase 2A in insulin-secreting cells: evidence for functional consequences on enzyme activity and insulin secretion. Endocrinology 1996; 137:2315-23.
    • (1996) Endocrinology , vol.137 , pp. 2315-2323
    • Kowluru, A.1    Seavey, S.E.2    Rabaglia, M.E.3    Nesher, R.4    Metz, S.A.5
  • 61
    • 0034331296 scopus 로고    scopus 로고
    • Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo
    • Wu J, Tolstykh T, Lee J, Boyd K, Stock JB, Broach JR. Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo. EMBO J 2000; 19:5672-81.
    • (2000) EMBO J. , vol.19 , pp. 5672-5681
    • Wu, J.1    Tolstykh, T.2    Lee, J.3    Boyd, K.4    Stock, J.B.5    Broach, J.R.6
  • 62
    • 0029059122 scopus 로고
    • Ceramide inhibits pancreatic beta-cell insulin production and mitogenesis and mimics the actions of interleukin-1 beta
    • Sjoholm A. Ceramide inhibits pancreatic beta-cell insulin production and mitogenesis and mimics the actions of interleukin-1 beta. FEBS Lett 1995; 367:283-6. t
    • (1995) FEBS Lett. , vol.367 , pp. 283-286
    • Sjoholm, A.1
  • 63
    • 0033554835 scopus 로고    scopus 로고
    • Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue
    • De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J. Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry. 1999; 38:16539-47.
    • (1999) Biochemistry , vol.38 , pp. 16539-16547
    • De Baere, I.1    Derua, R.2    Janssens, V.3    Van Hoof, C.4    Waelkens, E.5    Merlevede, W.6    Goris, J.7
  • 64
    • 0031105609 scopus 로고    scopus 로고
    • The interconversion of protein phosphatase 2A between PP2A1 and PP2A0 during retinoic acid-induced granulocytic differentiation and a modification on the catalytic subunit in S phase of HL-60 cells
    • Zhu T, Matsuzawa S, Mizuno Y, Kamibayashi C, Mumby MC, Andjelkovic N, et al. The interconversion of protein phosphatase 2A between PP2A1 and PP2A0 during retinoic acid-induced granulocytic differentiation and a modification on the catalytic subunit in S phase of HL-60 cells. Arch Biochem Biophys 1997; 339:210-7.
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 210-217
    • Zhu, T.1    Matsuzawa, S.2    Mizuno, Y.3    Kamibayashi, C.4    Mumby, M.C.5    Andjelkovic, N.6
  • 65
    • 0032159462 scopus 로고    scopus 로고
    • Physiologic importance of protein phosphatase inhibitors
    • Oliver CJ, Shenolikar S. Physiologic importance of protein phosphatase inhibitors. Front Biosci 1998; 3:D961-72.
    • (1998) Front Biosci. , vol.3
    • Oliver, C.J.1    Shenolikar, S.2
  • 66
    • 0034009389 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A panoply of enzymes
    • Virshup DM. Protein phosphatase 2A: a panoply of enzymes. Curr Opin Cell Biol 2000; 12:180-5.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 180-185
    • Virshup, D.M.1
  • 68
    • 0029975884 scopus 로고    scopus 로고
    • Characterization of the sphingomyelin content of isolated pancreatic islets. Evaluation of the role of sphingomyelin hydrolysis in the action of interleukin-1 to induce islet overproduction of nitric oxide
    • Kwon G, Bohrer A, Han X, Corbett JA, Ma Z, Gross RW, et al. Characterization of the sphingomyelin content of isolated pancreatic islets. Evaluation of the role of sphingomyelin hydrolysis in the action of interleukin-1 to induce islet overproduction of nitric oxide. Biochim Biophys Acta 1996; 1300:63-72.
    • (1996) Biochim. Biophys. Acta , vol.1300 , pp. 63-72
    • Kwon, G.1    Bohrer, A.2    Han, X.3    Corbett, J.A.4    Ma, Z.5    Gross, R.W.6
  • 69
    • 0030786078 scopus 로고    scopus 로고
    • Ceramide-activated protein phosphatase-2A activity in insulin-secreting cells
    • Kowluru A, Metz SA. Ceramide-activated protein phosphatase-2A activity in insulin-secreting cells. FEBS Lett 1997; 418:179-82.
    • (1997) FEBS Lett. , vol.418 , pp. 179-182
    • Kowluru, A.1    Metz, S.A.2
  • 70
    • 0038532298 scopus 로고    scopus 로고
    • A role for ceramide, but not diacylglycerol, in the antagonism of insulin signal transduction by saturated fatty acids
    • Chavez JA, Knotts TA, Wang LP, Li G, Dobrowsky RT, Florant GL, Summers SA. A role for ceramide, but not diacylglycerol, in the antagonism of insulin signal transduction by saturated fatty acids. J Biol Chem 2003; 278:10297-303.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10297-10303
    • Chavez, J.A.1    Knotts, T.A.2    Wang, L.P.3    Li, G.4    Dobrowsky, R.T.5    Florant, G.L.6    Summers, S.A.7
  • 71
    • 0032989112 scopus 로고    scopus 로고
    • Activation of the sphingomyelinase/ceramide signal transduction pathway in insulin-secreting beta-cells: Role in cytokine-induced beta-cell death
    • Major CD, Gao ZY, Wolf BA. Activation of the sphingomyelinase/ceramide signal transduction pathway in insulin-secreting beta-cells: role in cytokine-induced beta-cell death. Diabetes 1999; 48:1372-80.
    • (1999) Diabetes , vol.48 , pp. 1372-1380
    • Major, C.D.1    Gao, Z.Y.2    Wolf, B.A.3
  • 72
    • 0034523567 scopus 로고    scopus 로고
    • The acid sphingomyelinase inhibitor SR33557 counteracts TNF-alpha-mediated potentiation of IL-1beta-induced NF-kappaB activation in the insulin-producing cell line Rinm5F
    • Saldeen J, Jaffrezou JP, Welsh N. The acid sphingomyelinase inhibitor SR33557 counteracts TNF-alpha-mediated potentiation of IL-1beta-induced NF-kappaB activation in the insulin-producing cell line Rinm5F. Autoimmunity 2000; 32:241-54.
    • (2000) Autoimmunity , vol.32 , pp. 241-254
    • Saldeen, J.1    Jaffrezou, J.P.2    Welsh, N.3
  • 74
    • 0027477103 scopus 로고
    • Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A
    • Guo H, Damuni Z. Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A. Proc Natl Acad Sci U S A 1993; 90:2500-4.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2500-2504
    • Guo, H.1    Damuni, Z.2
  • 75
    • 0029349353 scopus 로고
    • Flicking the switches: Phosphorylation of serine/threonine protein phosphatases
    • Brautigan DL. Flicking the switches: phosphorylation of serine/threonine protein phosphatases. Semin Cancer Biol 1995; 6:211-7.
    • (1995) Semin. Cancer Biol. , vol.6 , pp. 211-217
    • Brautigan, D.L.1
  • 78
    • 0036010598 scopus 로고    scopus 로고
    • Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution
    • Ceulemans H, Stalmans W, Bollen M. Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution. Bioessays 2002; 24:371-81.
    • (2002) Bioessays , vol.24 , pp. 371-381
    • Ceulemans, H.1    Stalmans, W.2    Bollen, M.3
  • 79
    • 0035399464 scopus 로고    scopus 로고
    • Combinatorial control of protein phosphatase-1
    • Bollen M. Combinatorial control of protein phosphatase-1. Trends Biochem Sci 2001; 26:426-31.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 426-431
    • Bollen, M.1
  • 80
    • 0032518975 scopus 로고    scopus 로고
    • Dephosphorylation and deactivation of Ca2+/calmodulin-dependent protein kinase II in betaTC3-cells is mediated by Mg2+- and okadaic-acid-sensitive protein phosphatases
    • Easom RA, Tarpley JL, Filler NR, Bhatt H. Dephosphorylation and deactivation of Ca2+/calmodulin-dependent protein kinase II in betaTC3-cells is mediated by Mg2+- and okadaic-acid-sensitive protein phosphatases. Biochem J 1998; 329(Pt 2):283-8.
    • (1998) Biochem. J. , vol.329 , Issue.PART 2 , pp. 283-288
    • Easom, R.A.1    Tarpley, J.L.2    Filler, N.R.3    Bhatt, H.4
  • 82
    • 0001018554 scopus 로고
    • Calcineurin: A calcium- and calmodulin-binding protein of the nervous system
    • Klee CB, Crouch TH, Krinks MH. Calcineurin: a calcium- and calmodulin-binding protein of the nervous system. Proc Natl Acad Sci U S A 1979; 76:6270-3.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 6270-6273
    • Klee, C.B.1    Crouch, T.H.2    Krinks, M.H.3
  • 83
    • 0036234543 scopus 로고    scopus 로고
    • NFAT signaling: Choreographing the social lives of cells
    • Crabtree GR, Olson EN. NFAT signaling: choreographing the social lives of cells. Cell 2002; 109(Suppl):S67-79.
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Crabtree, G.R.1    Olson, E.N.2
  • 84
    • 0034796114 scopus 로고    scopus 로고
    • Regulation of insulin gene transcription by a Ca(2+)-responsive pathway involving calcineurin and nuclear factor of activated T cells
    • Lawrence MC, Bhatt HS, Watterson JM, Easom RA. Regulation of insulin gene transcription by a Ca(2+)-responsive pathway involving calcineurin and nuclear factor of activated T cells. Mol Endocrinol 2001; 15:1758-67.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 1758-1767
    • Lawrence, M.C.1    Bhatt, H.S.2    Watterson, J.M.3    Easom, R.A.4
  • 85
    • 0642344432 scopus 로고    scopus 로고
    • Calcineurin inhibitors and mechanisms that are responsible for the appearance of post-transplant diabetes mellitus
    • Ippoliti GB, Vigano M. Calcineurin inhibitors and mechanisms that are responsible for the appearance of post-transplant diabetes mellitus. G Ital Nefrol 2003; 20(Suppl 25):S11-4.
    • (2003) G. Ital. Nefrol. , vol.20 , Issue.SUPPL. 25
    • Ippoliti, G.B.1    Vigano, M.2
  • 86
    • 0030245732 scopus 로고    scopus 로고
    • Neurotransmitter-induced inhibition of exocytosis in insulin-secreting beta cells by activation of calcineurin
    • Renstrom E, Ding WG, Bokvist K, Rorsman P. Neurotransmitter-induced inhibition of exocytosis in insulin-secreting beta cells by activation of calcineurin. Neuron 1996; 17:513-22.
    • (1996) Neuron , vol.17 , pp. 513-522
    • Renstrom, E.1    Ding, W.G.2    Bokvist, K.3    Rorsman, P.4
  • 87
    • 0037024694 scopus 로고    scopus 로고
    • Ca2+-dependent dephosphorylation of kinesin heavy chain on beta-granules in pancreatic beta-cells. Implications for regulated beta-granule transport and insulin exocytosis
    • Donelan MJ, Morfini G, Julyan R, Sommers S, Hays L, Kajio H, et al. Ca2+-dependent dephosphorylation of kinesin heavy chain on beta-granules in pancreatic beta-cells. Implications for regulated beta-granule transport and insulin exocytosis. J Biol Chem 2002; 277:24232-42.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24232-24242
    • Donelan, M.J.1    Morfini, G.2    Julyan, R.3    Sommers, S.4    Hays, L.5    Kajio, H.6
  • 88
    • 0033605130 scopus 로고    scopus 로고
    • Purification and identification of a novel subunit of protein serine/threonine phosphatase 4
    • Kloeker S, Wadzinski BE. Purification and identification of a novel subunit of protein serine/threonine phosphatase 4. J Biol Chem 1999; 274:5339-47.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5339-5347
    • Kloeker, S.1    Wadzinski, B.E.2
  • 90
    • 0035234311 scopus 로고    scopus 로고
    • Protein phosphatase 5 in signal transduction
    • Chinkers M. Protein phosphatase 5 in signal transduction. Trends Endocrinol Metab 2001; 12:28-32.
    • (2001) Trends Endocrinol. Metab. , vol.12 , pp. 28-32
    • Chinkers, M.1
  • 91
    • 0028133445 scopus 로고
    • A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus
    • Chen MX, McPartlin AE, Brown L, Chen YH, Barker HM, Cohen PT. A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus. EMBO J 1994; 13:4278-90.
    • (1994) EMBO J. , vol.13 , pp. 4278-4290
    • Chen, M.X.1    McPartlin, A.E.2    Brown, L.3    Chen, Y.H.4    Barker, H.M.5    Cohen, P.T.6
  • 92
    • 0035914309 scopus 로고    scopus 로고
    • Interaction between protein phosphatase 5 and the A subunit of protein phosphatase 2A: Evidence for a heterotrimeric form of protein phosphatase 5
    • Lubert EJ, Hong Y, Sarge KD. Interaction between protein phosphatase 5 and the A subunit of protein phosphatase 2A: evidence for a heterotrimeric form of protein phosphatase 5. J Biol Chem 2001; 276:38582-7.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38582-38587
    • Lubert, E.J.1    Hong, Y.2    Sarge, K.D.3
  • 93
    • 0031569891 scopus 로고    scopus 로고
    • Localization of the novel serine/threonine protein phosphatase 6 gene (PPP6C) to human chromosome Xq22.3
    • Bastians H, Krebber H, Vetrie D, Hoheisel J, Lichter P, Ponstingl H, Joos S. Localization of the novel serine/threonine protein phosphatase 6 gene (PPP6C) to human chromosome Xq22.3. Genomics 1997; 41:296-7.
    • (1997) Genomics , vol.41 , pp. 296-297
    • Bastians, H.1    Krebber, H.2    Vetrie, D.3    Hoheisel, J.4    Lichter, P.5    Ponstingl, H.6    Joos, S.7
  • 94
    • 0033135523 scopus 로고    scopus 로고
    • Identification of a type 6 protein ser/thr phosphatase regulated by interleukin-2 stimulation
    • Filali M, Li S, Kim HW, Wadzinski B, Kamoun M. Identification of a type 6 protein ser/thr phosphatase regulated by interleukin-2 stimulation. J Cell Biochem 1999; 73:153-63.
    • (1999) J. Cell Biochem. , vol.73 , pp. 153-163
    • Filali, M.1    Li, S.2    Kim, H.W.3    Wadzinski, B.4    Kamoun, M.5
  • 96
    • 0038143218 scopus 로고    scopus 로고
    • Stress-induced protein phosphatase 2C is a negative regulator of a mitogen-activated protein kinase
    • Meskiene I, Baudouin E, Schweighofer A, Liwosz A, Jonak C, Rodriguez PL, et al. Stress-induced protein phosphatase 2C is a negative regulator of a mitogen-activated protein kinase. J Biol Chem 2003; 278:18945-52.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18945-18952
    • Meskiene, I.1    Baudouin, E.2    Schweighofer, A.3    Liwosz, A.4    Jonak, C.5    Rodriguez, P.L.6
  • 97
    • 17844396518 scopus 로고    scopus 로고
    • Inhibition of protein-tyrosine phosphatases stimulates insulin secretion in pancreatic islets of diabetic Goto-Kakizaki rats
    • Chen J, Ostenson CG. Inhibition of protein-tyrosine phosphatases stimulates insulin secretion in pancreatic islets of diabetic Goto-Kakizaki rats. Pancreas 2005; 30:314-7.
    • (2005) Pancreas , vol.30 , pp. 314-317
    • Chen, J.1    Ostenson, C.G.2
  • 99
    • 0036628009 scopus 로고    scopus 로고
    • Progression from IGT to type 2 diabetes mellitus: The central role of impaired early insulin secretion
    • Pratley RE, Weyer C. Progression from IGT to type 2 diabetes mellitus: the central role of impaired early insulin secretion. Curr Diab Rep 2002; 2:242-8.
    • (2002) Curr. Diab. Rep. , vol.2 , pp. 242-248
    • Pratley, R.E.1    Weyer, C.2


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