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Volumn 46, Issue 1, 2009, Pages 86-92

Protein kinase C mediated inhibition of endothelial l-arginine transport is mediated by MARCKS protein

Author keywords

Amino acid transport; Cationic Amino Acid Transporter 1; Endothelium; L arginine; Nitric oxide; Protein kinase C; Protein protein interaction

Indexed keywords

ANTIBODY; ARGININE; CAT 1 ANTIBODY; MARCKS PROTEIN; PHOSPHORUS 32; PROTEIN KINASE C; UNCLASSIFIED DRUG;

EID: 57149107970     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2008.09.712     Document Type: Article
Times cited : (12)

References (42)
  • 1
    • 0028043223 scopus 로고
    • Arginine supply for nitric oxide synthesis and arginase is mainly exogenous in elicited murine and rat macrophages
    • Hrabak A., Idei M., and Temesi A. Arginine supply for nitric oxide synthesis and arginase is mainly exogenous in elicited murine and rat macrophages. Life Sci. 55 (1994) 797-805
    • (1994) Life Sci. , vol.55 , pp. 797-805
    • Hrabak, A.1    Idei, M.2    Temesi, A.3
  • 3
    • 10844240824 scopus 로고    scopus 로고
    • Impaired l-arginine transport and endothelial function in hypertensive and genetically predisposed normotensive subjects
    • Schlaich M.P., Parnell M.M., Ahlers B.A., Finch S., Marshall T., Zhang W.Z., et al. Impaired l-arginine transport and endothelial function in hypertensive and genetically predisposed normotensive subjects. Circulation 110 (2004) 3680-3686
    • (2004) Circulation , vol.110 , pp. 3680-3686
    • Schlaich, M.P.1    Parnell, M.M.2    Ahlers, B.A.3    Finch, S.4    Marshall, T.5    Zhang, W.Z.6
  • 4
    • 0029993977 scopus 로고    scopus 로고
    • Randomized, double-blind, placebo-controlled study of supplemental oral l-arginine in patients with heart failure
    • Rector T.S., Bank A.J., Mullen K.A., Tschumperlin L.K., Sih R., Pillai K., et al. Randomized, double-blind, placebo-controlled study of supplemental oral l-arginine in patients with heart failure. Circulation 93 (1996) 2135-2141
    • (1996) Circulation , vol.93 , pp. 2135-2141
    • Rector, T.S.1    Bank, A.J.2    Mullen, K.A.3    Tschumperlin, L.K.4    Sih, R.5    Pillai, K.6
  • 5
    • 0031916983 scopus 로고    scopus 로고
    • Transporters for cationic amino acids in animal cells: discovery, structure, and function
    • Deves R., and Boyd C.A. Transporters for cationic amino acids in animal cells: discovery, structure, and function. Physiol. Rev. 78 (1998) 487-545
    • (1998) Physiol. Rev. , vol.78 , pp. 487-545
    • Deves, R.1    Boyd, C.A.2
  • 6
    • 0034727706 scopus 로고    scopus 로고
    • In vivo and in vitro evidence for impaired arginine transport in human heart failure
    • Kaye D.M., Ahlers B.A., Autelitano D.J., and Chin-Dusting J.P. In vivo and in vitro evidence for impaired arginine transport in human heart failure. Circulation 102 (2000) 2707-2712
    • (2000) Circulation , vol.102 , pp. 2707-2712
    • Kaye, D.M.1    Ahlers, B.A.2    Autelitano, D.J.3    Chin-Dusting, J.P.4
  • 7
    • 0035960677 scopus 로고    scopus 로고
    • Endothelial dysfunction, oxidative stress, and risk of cardiovascular events in patients with coronary artery disease
    • Heitzer T., Schlinzig T., Krohn K., Meinertz T., and Munzel T. Endothelial dysfunction, oxidative stress, and risk of cardiovascular events in patients with coronary artery disease. Circulation 104 (2001) 2673-2678
    • (2001) Circulation , vol.104 , pp. 2673-2678
    • Heitzer, T.1    Schlinzig, T.2    Krohn, K.3    Meinertz, T.4    Munzel, T.5
  • 8
    • 0037428211 scopus 로고    scopus 로고
    • Rapid stimulation of l-arginine transport by d-glucose involves p42/44(mapk) and nitric oxide in human umbilical vein endothelium
    • Flores C., Rojas S., Aguayo C., Parodi J., Mann G., Pearson J.D., et al. Rapid stimulation of l-arginine transport by d-glucose involves p42/44(mapk) and nitric oxide in human umbilical vein endothelium. Circ. Res. 92 (2003) 64-72
    • (2003) Circ. Res. , vol.92 , pp. 64-72
    • Flores, C.1    Rojas, S.2    Aguayo, C.3    Parodi, J.4    Mann, G.5    Pearson, J.D.6
  • 9
    • 0029096138 scopus 로고
    • Protein kinase C-dependent regulation of l-arginine transport activity in Caco-2 intestinal cells
    • Pan M., and Stevens B.R. Protein kinase C-dependent regulation of l-arginine transport activity in Caco-2 intestinal cells. Biochim. Biophys. Acta 1239 (1995) 27-32
    • (1995) Biochim. Biophys. Acta , vol.1239 , pp. 27-32
    • Pan, M.1    Stevens, B.R.2
  • 10
    • 0036836057 scopus 로고    scopus 로고
    • Activation of intestinal arginine transport by protein kinase C is mediated by mitogen-activated protein kinases
    • Pan M., Meng Q.H., Wolfgang C.L., Lin C.M., Karinch A.M., Vary T.C., et al. Activation of intestinal arginine transport by protein kinase C is mediated by mitogen-activated protein kinases. J. Gastrointest. Surg. 6 (2002) 876-882
    • (2002) J. Gastrointest. Surg. , vol.6 , pp. 876-882
    • Pan, M.1    Meng, Q.H.2    Wolfgang, C.L.3    Lin, C.M.4    Karinch, A.M.5    Vary, T.C.6
  • 11
    • 0035079905 scopus 로고    scopus 로고
    • The transport activity of the human cationic amino acid transporter hCAT-1 is downregulated by activation of protein kinase C
    • Graf P., Forstermann U., and Closs E.I. The transport activity of the human cationic amino acid transporter hCAT-1 is downregulated by activation of protein kinase C. Br. J. Pharmacol. 132 (2001) 1193-1200
    • (2001) Br. J. Pharmacol. , vol.132 , pp. 1193-1200
    • Graf, P.1    Forstermann, U.2    Closs, E.I.3
  • 12
    • 0037059549 scopus 로고    scopus 로고
    • Inhibition of protein kinase Cbeta prevents impaired endothelium-dependent vasodilation caused by hyperglycemia in humans
    • Beckman J.A., Goldfine A.B., Gordon M.B., Garrett L.A., and Creager M.A. Inhibition of protein kinase Cbeta prevents impaired endothelium-dependent vasodilation caused by hyperglycemia in humans. Circ. Res. 90 (2002) 107-111
    • (2002) Circ. Res. , vol.90 , pp. 107-111
    • Beckman, J.A.1    Goldfine, A.B.2    Gordon, M.B.3    Garrett, L.A.4    Creager, M.A.5
  • 13
    • 0023674315 scopus 로고
    • Tumor promoter induces reorganization of actin filaments and calspectin (fodrin or nonerythroid spectrin) in 3T3 cells
    • Sobue K., Fujio Y., and Kanda K. Tumor promoter induces reorganization of actin filaments and calspectin (fodrin or nonerythroid spectrin) in 3T3 cells. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 482-486
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 482-486
    • Sobue, K.1    Fujio, Y.2    Kanda, K.3
  • 14
    • 0033960571 scopus 로고    scopus 로고
    • Association of l-arginine transporters with fodrin: implications for hypoxic inhibition of arginine uptake
    • Zharikov S.I., and Block E.R. Association of l-arginine transporters with fodrin: implications for hypoxic inhibition of arginine uptake. Am. J. Physiol. Lung Cell Mol. Physiol. 278 (2000) L111-L117
    • (2000) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.278
    • Zharikov, S.I.1    Block, E.R.2
  • 15
    • 4744348466 scopus 로고    scopus 로고
    • Myristoylated alanine-rich C kinase substrate (MARCKS) is involved in myoblast fusion through its regulation by protein kinase Calpha and calpain proteolytic cleavage
    • Dulong S., Goudenege S., Vuillier-Devillers K., Manenti S., Poussard S., and Cottin P. Myristoylated alanine-rich C kinase substrate (MARCKS) is involved in myoblast fusion through its regulation by protein kinase Calpha and calpain proteolytic cleavage. Biochem. J. 382 (2004) 1015-1023
    • (2004) Biochem. J. , vol.382 , pp. 1015-1023
    • Dulong, S.1    Goudenege, S.2    Vuillier-Devillers, K.3    Manenti, S.4    Poussard, S.5    Cottin, P.6
  • 16
    • 0019605676 scopus 로고
    • The cluster-tray method for rapid measurement of solute fluxes in adherent cultured cells
    • Gazzola G.C., Dall'Asta V., Franchi-Gazzola R., and White M.F. The cluster-tray method for rapid measurement of solute fluxes in adherent cultured cells. Anal. Biochem. 115 (1981) 368-374
    • (1981) Anal. Biochem. , vol.115 , pp. 368-374
    • Gazzola, G.C.1    Dall'Asta, V.2    Franchi-Gazzola, R.3    White, M.F.4
  • 17
    • 0031452440 scopus 로고    scopus 로고
    • A caveolar complex between the cationic amino acid transporter1 and endothelial nitric-oxide synthase may explain the "arginine paradox"
    • McDonald K.K., Zharikov S., Block E.R., and Kilberg M.S. A caveolar complex between the cationic amino acid transporter1 and endothelial nitric-oxide synthase may explain the "arginine paradox". J. Biol. Chem. 272 (1997) 31213-31216
    • (1997) J. Biol. Chem. , vol.272 , pp. 31213-31216
    • McDonald, K.K.1    Zharikov, S.2    Block, E.R.3    Kilberg, M.S.4
  • 18
    • 0033153454 scopus 로고    scopus 로고
    • CAT2-mediated l-arginine transport and nitric oxide production in activated macrophages
    • Kakuda D.K., Sweet M.J., Mac Leod C.L., Hume D.A., and Markovich D. CAT2-mediated l-arginine transport and nitric oxide production in activated macrophages. Biochem. J. 340 (1999) 549-553
    • (1999) Biochem. J. , vol.340 , pp. 549-553
    • Kakuda, D.K.1    Sweet, M.J.2    Mac Leod, C.L.3    Hume, D.A.4    Markovich, D.5
  • 19
    • 0025221039 scopus 로고
    • Stimulation of glucose transport and glucose transporter phosphorylation by okadaic acid in rat adipocytes
    • Lawrence Jr. J.C., Hiken J.F., and James D.E. Stimulation of glucose transport and glucose transporter phosphorylation by okadaic acid in rat adipocytes. J. Biol. Chem. 265 (1990) 19768-19776
    • (1990) J. Biol. Chem. , vol.265 , pp. 19768-19776
    • Lawrence Jr., J.C.1    Hiken, J.F.2    James, D.E.3
  • 20
    • 0032583180 scopus 로고    scopus 로고
    • High-affinity arginine transport of bovine aortic endothelial cells is impaired by lysophosphatidylcholine
    • Kikuta K., Sawamura T., Miwa S., Hashimoto N., and Masaki T. High-affinity arginine transport of bovine aortic endothelial cells is impaired by lysophosphatidylcholine. Circ. Res. 83 (1998) 1088-1096
    • (1998) Circ. Res. , vol.83 , pp. 1088-1096
    • Kikuta, K.1    Sawamura, T.2    Miwa, S.3    Hashimoto, N.4    Masaki, T.5
  • 21
    • 0028961653 scopus 로고
    • Differential inhibition of cytosolic and membrane-derived protein kinase C activity by staurosporine and other kinase inhibitors
    • Budworth J., and Gescher A. Differential inhibition of cytosolic and membrane-derived protein kinase C activity by staurosporine and other kinase inhibitors. FEBS Lett. 362 (1995) 139-142
    • (1995) FEBS Lett. , vol.362 , pp. 139-142
    • Budworth, J.1    Gescher, A.2
  • 22
    • 0025942516 scopus 로고
    • The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C
    • Toullec D., Pianetti P., Coste H., Bellevergue P., Grand-Perret T., Ajakane M., et al. The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C. J. Biol. Chem. 266 (1991) 15771-15781
    • (1991) J. Biol. Chem. , vol.266 , pp. 15771-15781
    • Toullec, D.1    Pianetti, P.2    Coste, H.3    Bellevergue, P.4    Grand-Perret, T.5    Ajakane, M.6
  • 23
    • 0037424792 scopus 로고    scopus 로고
    • The impact of N- and O-glycosylation on the functions of Glut-1 transporter in human thyroid anaplastic cells
    • Samih N., Hovsepian S., Notel F., Prorok M., Zattara-Cannoni H., Mathieu S., et al. The impact of N- and O-glycosylation on the functions of Glut-1 transporter in human thyroid anaplastic cells. Biochim. Biophys. Acta 1621 (2003) 92-101
    • (2003) Biochim. Biophys. Acta , vol.1621 , pp. 92-101
    • Samih, N.1    Hovsepian, S.2    Notel, F.3    Prorok, M.4    Zattara-Cannoni, H.5    Mathieu, S.6
  • 24
    • 0032875453 scopus 로고    scopus 로고
    • Analysis of receptor usage by ecotropic murine retroviruses, using green fluorescent protein-tagged cationic amino acid transporters
    • Masuda M., Kakushima N., Wilt S.G., Ruscetti S.K., Hoffman P.M., and Iwamoto A. Analysis of receptor usage by ecotropic murine retroviruses, using green fluorescent protein-tagged cationic amino acid transporters. J. Virol. 73 (1999) 8623-8629
    • (1999) J. Virol. , vol.73 , pp. 8623-8629
    • Masuda, M.1    Kakushima, N.2    Wilt, S.G.3    Ruscetti, S.K.4    Hoffman, P.M.5    Iwamoto, A.6
  • 25
    • 0034715520 scopus 로고    scopus 로고
    • Ecotropic murine leukemia virus receptor is physically associated with caveolin and membrane rafts
    • Lu X., and Silver J. Ecotropic murine leukemia virus receptor is physically associated with caveolin and membrane rafts. Virology 276 (2000) 251-258
    • (2000) Virology , vol.276 , pp. 251-258
    • Lu, X.1    Silver, J.2
  • 26
    • 0028798319 scopus 로고
    • Inhibition of endothelial nitric oxide synthase activity by protein kinase C
    • Hirata K., Kuroda R., Sakoda T., Katayama M., Inoue N., Suematsu M., et al. Inhibition of endothelial nitric oxide synthase activity by protein kinase C. Hypertension 25 (1995) 180-185
    • (1995) Hypertension , vol.25 , pp. 180-185
    • Hirata, K.1    Kuroda, R.2    Sakoda, T.3    Katayama, M.4    Inoue, N.5    Suematsu, M.6
  • 27
    • 0037834879 scopus 로고    scopus 로고
    • Classical isoforms of PKC as regulators of CAT-1 transporter activity in pulmonary artery endothelial cells
    • Krotova K.Y., Zharikov S.I., and Block E.R. Classical isoforms of PKC as regulators of CAT-1 transporter activity in pulmonary artery endothelial cells. Am. J. Physiol. Lung Cell Mol. Physiol. 284 (2003) L1037-L1044
    • (2003) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.284
    • Krotova, K.Y.1    Zharikov, S.I.2    Block, E.R.3
  • 28
    • 0036298987 scopus 로고    scopus 로고
    • Interaction of the C-terminal region of the rat serotonin transporter with MacMARCKS modulates 5-HT uptake regulation by protein kinase C
    • Jess U., El Far O., Kirsch J., and Betz H. Interaction of the C-terminal region of the rat serotonin transporter with MacMARCKS modulates 5-HT uptake regulation by protein kinase C. Biochem. Biophys. Res. Commun. 294 (2002) 272-279
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 272-279
    • Jess, U.1    El Far, O.2    Kirsch, J.3    Betz, H.4
  • 29
    • 0033544844 scopus 로고    scopus 로고
    • Regulated trafficking of the human dopamine transporter. Clathrin-mediated internalization and lysosomal degradation in response to phorbol esters
    • Daniels G.M., and Amara S.G. Regulated trafficking of the human dopamine transporter. Clathrin-mediated internalization and lysosomal degradation in response to phorbol esters. J. Biol. Chem. 274 (1999) 35794-35801
    • (1999) J. Biol. Chem. , vol.274 , pp. 35794-35801
    • Daniels, G.M.1    Amara, S.G.2
  • 30
    • 11144228635 scopus 로고    scopus 로고
    • Protein kinase C activation promotes the internalization of the human cationic amino acid transporter hCAT-1. A new regulatory mechanism for hCAT-1 activity
    • Rotmann A., Strand D., Martine U., and Closs E.I. Protein kinase C activation promotes the internalization of the human cationic amino acid transporter hCAT-1. A new regulatory mechanism for hCAT-1 activity. J. Biol. Chem. 279 (2004) 54185-54192
    • (2004) J. Biol. Chem. , vol.279 , pp. 54185-54192
    • Rotmann, A.1    Strand, D.2    Martine, U.3    Closs, E.I.4
  • 32
    • 0027532369 scopus 로고
    • Envelope-binding domain in the cationic amino acid transporter determines the host range of ecotropic murine retroviruses
    • Albritton L.M., Kim J.W., Tseng L., and Cunningham J.M. Envelope-binding domain in the cationic amino acid transporter determines the host range of ecotropic murine retroviruses. J. Virol. 67 (1993) 2091-2096
    • (1993) J. Virol. , vol.67 , pp. 2091-2096
    • Albritton, L.M.1    Kim, J.W.2    Tseng, L.3    Cunningham, J.M.4
  • 33
    • 0037195777 scopus 로고    scopus 로고
    • Protein kinase C activation decreases cell surface expression of the GLT-1 subtype of glutamate transporter. Requirement of a carboxyl-terminal domain and partial dependence on serine 486
    • Kalandadze A., Wu Y., and Robinson M.B. Protein kinase C activation decreases cell surface expression of the GLT-1 subtype of glutamate transporter. Requirement of a carboxyl-terminal domain and partial dependence on serine 486. J. Biol. Chem. 277 (2002) 45741-45750
    • (2002) J. Biol. Chem. , vol.277 , pp. 45741-45750
    • Kalandadze, A.1    Wu, Y.2    Robinson, M.B.3
  • 34
    • 0030965452 scopus 로고    scopus 로고
    • Phosphorylation of a vesicular monoamine transporter by casein kinase II
    • Krantz D.E., Peter D., Liu Y., and Edwards R.H. Phosphorylation of a vesicular monoamine transporter by casein kinase II. J. Biol. Chem. 272 (1997) 6752-6759
    • (1997) J. Biol. Chem. , vol.272 , pp. 6752-6759
    • Krantz, D.E.1    Peter, D.2    Liu, Y.3    Edwards, R.H.4
  • 35
    • 0033568870 scopus 로고    scopus 로고
    • Membrane trafficking regulates the activity of the human dopamine transporter
    • Melikian H.E., and Buckley K.M. Membrane trafficking regulates the activity of the human dopamine transporter. J. Neurosci. 19 (1999) 7699-7710
    • (1999) J. Neurosci. , vol.19 , pp. 7699-7710
    • Melikian, H.E.1    Buckley, K.M.2
  • 36
    • 0035910501 scopus 로고    scopus 로고
    • A novel casein kinase 2 alpha-subunit regulates membrane protein traffic in the human hepatoma cell line HuH-7
    • Shi X., Potvin B., Huang T., Hilgard P., Spray D.C., Suadicani S.O., et al. A novel casein kinase 2 alpha-subunit regulates membrane protein traffic in the human hepatoma cell line HuH-7. J. Biol. Chem. 276 (2001) 2075-2082
    • (2001) J. Biol. Chem. , vol.276 , pp. 2075-2082
    • Shi, X.1    Potvin, B.2    Huang, T.3    Hilgard, P.4    Spray, D.C.5    Suadicani, S.O.6
  • 38
    • 0024560660 scopus 로고
    • Effects of forskolin and phorbol-myristate-acetate on cytoskeleton, extracellular matrix and protein phosphorylation in human endothelial cells
    • Smirnov V.N., Antonov A.S., Antonova G.N., Romanov Y.A., Kabaeva N.V., Tchertikhina I.V., et al. Effects of forskolin and phorbol-myristate-acetate on cytoskeleton, extracellular matrix and protein phosphorylation in human endothelial cells. J. Mol. Cell. Cardiol. 21 Suppl 1 (1989) 3-11
    • (1989) J. Mol. Cell. Cardiol. , vol.21 , Issue.SUPPL. 1 , pp. 3-11
    • Smirnov, V.N.1    Antonov, A.S.2    Antonova, G.N.3    Romanov, Y.A.4    Kabaeva, N.V.5    Tchertikhina, I.V.6
  • 40
    • 0026513601 scopus 로고
    • MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin
    • Hartwig J.H., Thelen M., Rosen A., Janmey P.A., Nairn A.C., and Aderem A. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. Nature 356 (1992) 618-622
    • (1992) Nature , vol.356 , pp. 618-622
    • Hartwig, J.H.1    Thelen, M.2    Rosen, A.3    Janmey, P.A.4    Nairn, A.C.5    Aderem, A.6
  • 41
    • 0025907984 scopus 로고
    • Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane
    • Thelen M., Rosen A., Nairn A.C., and Aderem A. Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane. Nature 351 (1991) 320-322
    • (1991) Nature , vol.351 , pp. 320-322
    • Thelen, M.1    Rosen, A.2    Nairn, A.C.3    Aderem, A.4
  • 42
    • 0345540626 scopus 로고    scopus 로고
    • Translocation of MARCKS and reorganization of the cytoskeleton by PMA correlates with the ion selectivity, the confluence, and transformation state of kidney epithelial cell lines
    • Vaaraniemi J., Palovuori R., Lehto V.P., and Eskelinen S. Translocation of MARCKS and reorganization of the cytoskeleton by PMA correlates with the ion selectivity, the confluence, and transformation state of kidney epithelial cell lines. J. Cell. Physiol. 181 (1999) 83-95
    • (1999) J. Cell. Physiol. , vol.181 , pp. 83-95
    • Vaaraniemi, J.1    Palovuori, R.2    Lehto, V.P.3    Eskelinen, S.4


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