메뉴 건너뛰기




Volumn 39, Issue 3, 2007, Pages 586-596

Inhibition of plasma membrane Ca2+-ATPase by heparin is modulated by potassium

Author keywords

Ca2+ ATPase; Heparin; Plasma membrane; Potassium; Sulfated polysaccharides

Indexed keywords

4 NITROPHENOL; 4 NITROPHENYLPHOSPHATE; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; CALCIUM ION; HEPARIN; LITHIUM ION; PHOSPHATE; POLYSACCHARIDE SULFATE; POTASSIUM ION; UNCLASSIFIED DRUG; VANADIC ACID;

EID: 33846288324     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2006.10.010     Document Type: Article
Times cited : (7)

References (84)
  • 4
    • 0035817358 scopus 로고    scopus 로고
    • Slippage and uncoupling in P-type cation pumps: Implications for energy transduction mechanisms and regulation of metabolism
    • Berman M.C. Slippage and uncoupling in P-type cation pumps: Implications for energy transduction mechanisms and regulation of metabolism. Biochimica and Biophysica Acta 1513 (2001) 95-121
    • (2001) Biochimica and Biophysica Acta , vol.1513 , pp. 95-121
    • Berman, M.C.1
  • 6
    • 2942563927 scopus 로고    scopus 로고
    • Antitumor and antimethastatic effect of warfarin and heparin
    • Bobek B., and Kovarik J. Antitumor and antimethastatic effect of warfarin and heparin. Biomedicine and Pharmacotherapy 58 (2004) 213-219
    • (2004) Biomedicine and Pharmacotherapy , vol.58 , pp. 213-219
    • Bobek, B.1    Kovarik, J.2
  • 7
    • 0027418623 scopus 로고
    • Vascular derived growth factors: Cell biology, pathophysiology and pharmacology
    • Bobik A., and Campbell J.H. Vascular derived growth factors: Cell biology, pathophysiology and pharmacology. Pharmacological Reviews 45 (1993) 1-42
    • (1993) Pharmacological Reviews , vol.45 , pp. 1-42
    • Bobik, A.1    Campbell, J.H.2
  • 8
    • 0027509462 scopus 로고
    • Glycosaminoglycans and the regulation of blood coagulation
    • Bourin M.-C., and Lindahl U. Glycosaminoglycans and the regulation of blood coagulation. Biochemical Journal 289 (1993) 313-330
    • (1993) Biochemical Journal , vol.289 , pp. 313-330
    • Bourin, M.-C.1    Lindahl, U.2
  • 10
    • 0026074512 scopus 로고
    • Calcium pump of the plasma membrane
    • Carafoli E. Calcium pump of the plasma membrane. Physiological Reviews 71 (1991) 129-153
    • (1991) Physiological Reviews , vol.71 , pp. 129-153
    • Carafoli, E.1
  • 11
    • 0028113894 scopus 로고
    • Biogenesis: Plasma membrane calcium ATPase. 15 years of work on the purified enzyme
    • Carafoli E. Biogenesis: Plasma membrane calcium ATPase. 15 years of work on the purified enzyme. FASEB Journal 8 (1994) 993-1002
    • (1994) FASEB Journal , vol.8 , pp. 993-1002
    • Carafoli, E.1
  • 14
    • 0030012036 scopus 로고    scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum as revealed by thapsigargin stabilization
    • 2+-ATPase of sarcoplasmic reticulum as revealed by thapsigargin stabilization. Biochimica and Biophysica Acta 1289 (1996) 187-194
    • (1996) Biochimica and Biophysica Acta , vol.1289 , pp. 187-194
    • Davidson, G.A.1    Berman, M.C.2
  • 15
    • 0035877655 scopus 로고    scopus 로고
    • 2+-ATPase isoforms 2b and 4b interact promiscuously and selectively with members of the membrane-associated guanylate kinase family of PDZ (PSD95/Dlg/ZO-1) domain-containing proteins
    • 2+-ATPase isoforms 2b and 4b interact promiscuously and selectively with members of the membrane-associated guanylate kinase family of PDZ (PSD95/Dlg/ZO-1) domain-containing proteins. The Journal of Biological Chemistry 276 (2001) 21594-21600
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 21594-21600
    • De Marco, S.J.1    Strehler, E.E.2
  • 17
    • 0030908304 scopus 로고    scopus 로고
    • 2+-ATPase: ATP hydrolysis, ATP synthesis and heat production
    • 2+-ATPase: ATP hydrolysis, ATP synthesis and heat production. FEBS Letters 406 (1997) 201-204
    • (1997) FEBS Letters , vol.406 , pp. 201-204
    • De Meis, L.1    Bianconi, M.L.2    Suzano, V.A.3
  • 18
    • 0026505934 scopus 로고
    • 2+ transport ATPase of sarcoplasmic reticulum
    • 2+ transport ATPase of sarcoplasmic reticulum. FEBS Letters 299 (1992) 33-35
    • (1992) FEBS Letters , vol.299 , pp. 33-35
    • De Meis, L.1    Inesi, G.2
  • 20
    • 0025165373 scopus 로고
    • Functional interactions of catalytic site and transmembrane channel in the sarcoplasmic reticulum ATPase
    • De Meis L., Suzano V.A., and Inesi G. Functional interactions of catalytic site and transmembrane channel in the sarcoplasmic reticulum ATPase. The Journal of Biological Chemistry 265 (1990) 18848-18851
    • (1990) The Journal of Biological Chemistry , vol.265 , pp. 18848-18851
    • De Meis, L.1    Suzano, V.A.2    Inesi, G.3
  • 21
    • 0018733531 scopus 로고
    • Calculation programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato A., and Fabiato F. Calculation programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. Journal of Physiology 75 (1979) 463-505
    • (1979) Journal of Physiology , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 23
    • 0022616864 scopus 로고
    • A unique heparan sulfate in the nuclei of hepatocytes: Structural changes with the growth state of the cells
    • Fedarko N.S., and Conrad E. A unique heparan sulfate in the nuclei of hepatocytes: Structural changes with the growth state of the cells. The Journal of Cell Biology 102 (1986) 587-599
    • (1986) The Journal of Cell Biology , vol.102 , pp. 587-599
    • Fedarko, N.S.1    Conrad, E.2
  • 25
    • 0023157363 scopus 로고
    • Angiogenic factors
    • Folkman J., and Klagsbrum M. Angiogenic factors. Science 235 (1987) 442-447
    • (1987) Science , vol.235 , pp. 442-447
    • Folkman, J.1    Klagsbrum, M.2
  • 27
    • 0642346833 scopus 로고    scopus 로고
    • The potential of the molecular diversity of heparin and heparan sulfate for drug development
    • Fugedi P. The potential of the molecular diversity of heparin and heparan sulfate for drug development. Mini Reviews in Medicinal Chemistry 3 (2003) 659-667
    • (2003) Mini Reviews in Medicinal Chemistry , vol.3 , pp. 659-667
    • Fugedi, P.1
  • 28
    • 0023690141 scopus 로고
    • Competitive, reversible, and potent antagonism of inositol 1,4,5-triphosphate-activated calcium release by heparin
    • Ghosh T.K., Eis P.S., Mullaney J.M., Ebert C.L., and Gill D.L. Competitive, reversible, and potent antagonism of inositol 1,4,5-triphosphate-activated calcium release by heparin. The Journal of Biological Chemistry 263 (1988) 11075-11079
    • (1988) The Journal of Biological Chemistry , vol.263 , pp. 11075-11079
    • Ghosh, T.K.1    Eis, P.S.2    Mullaney, J.M.3    Ebert, C.L.4    Gill, D.L.5
  • 29
    • 0024519693 scopus 로고
    • Differential effects of heparin on inositol 1,4,5-triphosphate binding metabolism, and calcium release activity in the bovine adrenal cortex
    • Guillemette G., Lamontagne S., Boulay G., and Mouillac B. Differential effects of heparin on inositol 1,4,5-triphosphate binding metabolism, and calcium release activity in the bovine adrenal cortex. Molecular Pharmacology 35 (1989) 339-344
    • (1989) Molecular Pharmacology , vol.35 , pp. 339-344
    • Guillemette, G.1    Lamontagne, S.2    Boulay, G.3    Mouillac, B.4
  • 30
    • 0033008853 scopus 로고    scopus 로고
    • Heparinoids: Structure, biological activities and therapeutic applications
    • Gunay N.S., and Linhardt R.J. Heparinoids: Structure, biological activities and therapeutic applications. Planta Medica 65 (1999) 301-306
    • (1999) Planta Medica , vol.65 , pp. 301-306
    • Gunay, N.S.1    Linhardt, R.J.2
  • 34
    • 0023669720 scopus 로고
    • Heparin inhibits inositol triphosphate-induced calcium release from permeabilized rat liver cells
    • Hill T.D., Berggren P., and Boynton A.L. Heparin inhibits inositol triphosphate-induced calcium release from permeabilized rat liver cells. Biochemical and Biophysical Research Communications 149 (1987) 897-901
    • (1987) Biochemical and Biophysical Research Communications , vol.149 , pp. 897-901
    • Hill, T.D.1    Berggren, P.2    Boynton, A.L.3
  • 36
    • 0141609849 scopus 로고    scopus 로고
    • Mechanisms of glycosaminoglycan activation of the serpins in hemostasis
    • Huntington J.A. Mechanisms of glycosaminoglycan activation of the serpins in hemostasis. Journal of Thrombosis and Haemostasis 1 (2003) 1535-1549
    • (2003) Journal of Thrombosis and Haemostasis , vol.1 , pp. 1535-1549
    • Huntington, J.A.1
  • 37
    • 0023257520 scopus 로고
    • Involvement of phosphatidylinositol and insulin in the coordinate regulation of protoheparan sulfate metabolism and hepatocyte growth
    • Ishihara M., Fedarko N.S., and Conrad E. Involvement of phosphatidylinositol and insulin in the coordinate regulation of protoheparan sulfate metabolism and hepatocyte growth. The Journal of Biological Chemistry 262 (1987) 4708-4716
    • (1987) The Journal of Biological Chemistry , vol.262 , pp. 4708-4716
    • Ishihara, M.1    Fedarko, N.S.2    Conrad, E.3
  • 43
    • 0642345202 scopus 로고    scopus 로고
    • Regulation of smooth muscle cell growth, function and death in vitro by activated mast cells-A potential mechanism for the weakening and rupture of atherosclerotic plaques
    • Leskinen M.J., Kovanen P.T., and Lindstedt K.A. Regulation of smooth muscle cell growth, function and death in vitro by activated mast cells-A potential mechanism for the weakening and rupture of atherosclerotic plaques. Biochemical Pharmacology 66 (2003) 1493-1498
    • (2003) Biochemical Pharmacology , vol.66 , pp. 1493-1498
    • Leskinen, M.J.1    Kovanen, P.T.2    Lindstedt, K.A.3
  • 46
    • 2442608376 scopus 로고    scopus 로고
    • Lysophosphatidic acid regulates murine blastocyst development by transactivation of receptors for heparin-binding EGF-like growth factor
    • Liu Z., and Armant D.R. Lysophosphatidic acid regulates murine blastocyst development by transactivation of receptors for heparin-binding EGF-like growth factor. Experimental Cell Research 296 (2004) 317-326
    • (2004) Experimental Cell Research , vol.296 , pp. 317-326
    • Liu, Z.1    Armant, D.R.2
  • 48
    • 0000746932 scopus 로고
    • Lane D.A., and Lindahl U. (Eds), CRC Press Inc., Boca Raton, FL
    • Marcum J.A., and Rosennberg R.D. In: Lane D.A., and Lindahl U. (Eds). Heparin (1989), CRC Press Inc., Boca Raton, FL 275-294
    • (1989) Heparin , pp. 275-294
    • Marcum, J.A.1    Rosennberg, R.D.2
  • 49
  • 50
    • 0026776936 scopus 로고
    • Transforming growth factor-β1 is a heparin binding protein: Identification of putative heparin-binding and isolation of heparins with varying affinity for TGF-β1
    • McCaffrey T.A., Falcone D.J., and Du B. Transforming growth factor-β1 is a heparin binding protein: Identification of putative heparin-binding and isolation of heparins with varying affinity for TGF-β1. Journal of Cellular Physiology 152 (1992) 430-440
    • (1992) Journal of Cellular Physiology , vol.152 , pp. 430-440
    • McCaffrey, T.A.1    Falcone, D.J.2    Du, B.3
  • 51
    • 1242314690 scopus 로고    scopus 로고
    • 2+ store-operated and-independent ionic currents in insulin-secreting HIT-T15 cell mouse pancreatic beta-cells
    • 2+ store-operated and-independent ionic currents in insulin-secreting HIT-T15 cell mouse pancreatic beta-cells. Journal of Membrane Biology 197 (2004) 59-70
    • (2004) Journal of Membrane Biology , vol.197 , pp. 59-70
    • Mears, D.1    Zimliki, C.L.2
  • 56
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry e cols, which is more generally applicable
    • Peterson G.L. A simplification of the protein assay method of Lowry e cols, which is more generally applicable. Analytical Biochemistry 83 (1977) 346-356
    • (1977) Analytical Biochemistry , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 61
    • 0022273867 scopus 로고
    • 2+ release from the terminal cysterns of skeletal muscle sarcoplasmic reticulum
    • 2+ release from the terminal cysterns of skeletal muscle sarcoplasmic reticulum. FEBS Letters 188 (1985) 77-80
    • (1985) FEBS Letters , vol.188 , pp. 77-80
    • Ritov, V.B.1    Men'Shikova, E.V.2    Kozlov, Y.P.3
  • 64
    • 0028414107 scopus 로고
    • Increased calcium affinity of a fucosylated chondroitin sulfate from sea cucumber
    • Ruggiero J., Vieira R.P., and Mourão P.A.S. Increased calcium affinity of a fucosylated chondroitin sulfate from sea cucumber. Carbohydrate Research 256 (1994) 275-287
    • (1994) Carbohydrate Research , vol.256 , pp. 275-287
    • Ruggiero, J.1    Vieira, R.P.2    Mourão, P.A.S.3
  • 65
    • 0015848772 scopus 로고
    • Dependence on calcium concentration and stoichiometry of the calcium pump in human red cells
    • Schatzmann H.J. Dependence on calcium concentration and stoichiometry of the calcium pump in human red cells. Journal of Physiology (London) 235 (1973) 551-569
    • (1973) Journal of Physiology (London) , vol.235 , pp. 551-569
    • Schatzmann, H.J.1
  • 66
    • 0001989630 scopus 로고
    • The plasma membrane calcium pump of erythrocytes and other animal cells
    • Carafoli E. (Ed), Academic Press, New York
    • Schatzmann H.J. The plasma membrane calcium pump of erythrocytes and other animal cells. In: Carafoli E. (Ed). Membrane transport of calcium (1982), Academic Press, New York 41-88
    • (1982) Membrane transport of calcium , pp. 41-88
    • Schatzmann, H.J.1
  • 68
    • 0035889082 scopus 로고    scopus 로고
    • The plasma membrane calmodulin-dependent calcium pump: A major regulator of nitric oxide synthase I
    • Schuh K., Uldrijan S., Telkamp M., Rothlein N., and Neyses L. The plasma membrane calmodulin-dependent calcium pump: A major regulator of nitric oxide synthase I. The Journal of Cell Biology 155 (2001) 201-205
    • (2001) The Journal of Cell Biology , vol.155 , pp. 201-205
    • Schuh, K.1    Uldrijan, S.2    Telkamp, M.3    Rothlein, N.4    Neyses, L.5
  • 69
  • 72
    • 0022517661 scopus 로고
    • Caffeine inhibition of calcium accumulation by sarcoplasmic reticulum in mammalian skinned fibers
    • Sorenson M.M., Coelho H.S.L., and Reuben J.P. Caffeine inhibition of calcium accumulation by sarcoplasmic reticulum in mammalian skinned fibers. Journal of Membrane Biology 90 (1986) 219-230
    • (1986) Journal of Membrane Biology , vol.90 , pp. 219-230
    • Sorenson, M.M.1    Coelho, H.S.L.2    Reuben, J.P.3
  • 73
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler E.E., and Zacharias D.A. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiological Reviews 81 (2001) 21-50
    • (2001) Physiological Reviews , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 76
    • 0017684443 scopus 로고
    • Tissue specific distribution of sulfated mucopolysaccharides in mammals
    • Toledo O.M., and Dietrich C.P. Tissue specific distribution of sulfated mucopolysaccharides in mammals. Biochimica and Biophysica Acta 498 (1977) 114-122
    • (1977) Biochimica and Biophysica Acta , vol.498 , pp. 114-122
    • Toledo, O.M.1    Dietrich, C.P.2
  • 77
    • 0028972709 scopus 로고
    • Carbohydrate and heparin-binding proteins in mammalian fertilization
    • Töpfer-Petersen E., Calvette J.J., Sanz L., and Sinowatz F. Carbohydrate and heparin-binding proteins in mammalian fertilization. Andrologia 27 (1995) 303-324
    • (1995) Andrologia , vol.27 , pp. 303-324
    • Töpfer-Petersen, E.1    Calvette, J.J.2    Sanz, L.3    Sinowatz, F.4
  • 78
    • 0025895050 scopus 로고
    • Structure of a fucose branched chondroitin sulphate from sea cucumber: Evidence for the presence of 3-o-sulfo-beta-d-glucuronosyl residues
    • Vieira R.P., Mulloy B., and Mourão P.A.S. Structure of a fucose branched chondroitin sulphate from sea cucumber: Evidence for the presence of 3-o-sulfo-beta-d-glucuronosyl residues. The Journal of Biological Chemistry 266 (1991) 13530-13536
    • (1991) The Journal of Biological Chemistry , vol.266 , pp. 13530-13536
    • Vieira, R.P.1    Mulloy, B.2    Mourão, P.A.S.3
  • 81
    • 0025976838 scopus 로고
    • Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor
    • Yayon A., Klagsburn M., Esko J.D., Leder P., and Onitiz D.M. Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell 64 (1991) 841-848
    • (1991) Cell , vol.64 , pp. 841-848
    • Yayon, A.1    Klagsburn, M.2    Esko, J.D.3    Leder, P.4    Onitiz, D.M.5
  • 82
    • 0035805491 scopus 로고    scopus 로고
    • 2+-ATPase associates with the cytoskeleton in activated platelets through a PDZ-binding domain
    • 2+-ATPase associates with the cytoskeleton in activated platelets through a PDZ-binding domain. The Journal of Biological Chemistry 276 (2001) 14704-14709
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 14704-14709
    • Zabe, M.1    Dean, W.L.2
  • 83
    • 0346243796 scopus 로고    scopus 로고
    • 2+ ATPase from porcine brain synaptosome
    • 2+ ATPase from porcine brain synaptosome. Glycoconjugate Journal 19 (2003) 373-378
    • (2003) Glycoconjugate Journal , vol.19 , pp. 373-378
    • Zhao, Y.1    Zhang, X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.