메뉴 건너뛰기




Volumn 100, Issue 9, 2002, Pages 3392-3399

Phorbol ester stimulates a protein kinase C-mediated agatoxin-TK-sensitive calcium permeability pathway in human red blood cells

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM CHANNEL; CALYCULIN A; CHELERYTHRINE; OKADAIC ACID; OMEGA AGATOXIN; PHORBOL 13 ACETATE 12 MYRISTATE; PHORBOL ESTER; PHOSPHATASE; PHOSPHOLIPASE C; PHOSPHOTRANSFERASE; PROTEIN KINASE C; SCRAMBLASE; STAUROSPORINE;

EID: 0036838529     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.V100.9.3392     Document Type: Article
Times cited : (100)

References (75)
  • 1
    • 0030970954 scopus 로고    scopus 로고
    • Erythrocyte signal transduction pathways and their possible functions
    • Minetti G, Low PS. Erythrocyte signal transduction pathways and their possible functions. Curr Opin Hematol. 1998;4:116-121.
    • (1998) Curr Opin Hematol , vol.4 , pp. 116-121
    • Minetti, G.1    Low, P.S.2
  • 2
    • 0035252076 scopus 로고    scopus 로고
    • Export by red blood cells of nitric oxide bioactivity
    • Pawloski JR, Hess DT, Stamler JS. Export by red blood cells of nitric oxide bioactivity. Nature. 2001;409:622-626.
    • (2001) Nature , vol.409 , pp. 622-626
    • Pawloski, J.R.1    Hess, D.T.2    Stamler, J.S.3
  • 3
    • 0029558622 scopus 로고
    • Effect of L-NAME on pressure-flow relationships in isolated rabbit lungs: Role of red blood cells
    • Sprague RS, Stephenson AH, Dimmitt RA, et al. Effect of L-NAME on pressure-flow relationships in isolated rabbit lungs: Role of red blood cells. Am J Physiol Heart Circ Physiol. 1995;269: H1941-H1948.
    • (1995) Am J Physiol Heart Circ Physiol , vol.269
    • Sprague, R.S.1    Stephenson, A.H.2    Dimmitt, R.A.3
  • 6
    • 0032811978 scopus 로고    scopus 로고
    • Role of red blood cells in thrombosis
    • Andrews DA, Low PS. Role of red blood cells in thrombosis. Curr Opin Hematol. 1999;6:76-82.
    • (1999) Curr Opin Hematol , vol.6 , pp. 76-82
    • Andrews, D.A.1    Low, P.S.2
  • 7
    • 0032570313 scopus 로고    scopus 로고
    • Cellfree and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation
    • Pawloski JR, Swaminathan RV, Stamler JS. Cellfree and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation. Circulation. 1998;97:263-267.
    • (1998) Circulation , vol.97 , pp. 263-267
    • Pawloski, J.R.1    Swaminathan, R.V.2    Stamler, J.S.3
  • 8
    • 85047676379 scopus 로고
    • Release of ATP from human erythrocytes in response to a brief period of hypoxia and hypercapnia
    • Bergfeld GR, Forrester T. Release of ATP from human erythrocytes in response to a brief period of hypoxia and hypercapnia. Cardiovasc Res. 1992;26:40-47.
    • (1992) Cardiovasc Res , vol.26 , pp. 40-47
    • Bergfeld, G.R.1    Forrester, T.2
  • 9
    • 0023694777 scopus 로고
    • Demonstration of a novel ecto-enzyme on human erythrocytes, capable of degrading ADP and of inhibiting ADP-induced platelet aggregation
    • Luthje J, Schornburg A, Ogilvie A. Demonstration of a novel ecto-enzyme on human erythrocytes, capable of degrading ADP and of inhibiting ADP-induced platelet aggregation. Eur J Biochem. 1988;175:285-289.
    • (1988) Eur J Biochem , vol.175 , pp. 285-289
    • Luthje, J.1    Schornburg, A.2    Ogilvie, A.3
  • 10
    • 0345131724 scopus 로고    scopus 로고
    • Erythrocyte promotion of platelet reactivity decreases the effectiveness of aspirin as an antithrombotic therapeutic modality: The effect of low-dose aspirin is less than optimal in patients with vascular disease due to prothrombotic effects of erythrocytes on platelet reactivity
    • Valles J, Santos MT, Aznar J, et al. Erythrocyte promotion of platelet reactivity decreases the effectiveness of aspirin as an antithrombotic therapeutic modality: The effect of low-dose aspirin is less than optimal in patients with vascular disease due to prothrombotic effects of erythrocytes on platelet reactivity. Circulation. 1998;97:350-355.
    • (1998) Circulation , vol.97 , pp. 350-355
    • Valles, J.1    Santos, M.T.2    Aznar, J.3
  • 11
    • 0022374265 scopus 로고
    • Role of adenosine uptake and metabolism by blood cells in the antiplatelet actions of dipyridamole, dilazep and nitrobenzylthioinosine
    • Dawicki DD, Agarwal KC, Parks RE Jr. Role of adenosine uptake and metabolism by blood cells in the antiplatelet actions of dipyridamole, dilazep and nitrobenzylthioinosine. Biochem Pharmacol. 1985;34:3965-3972.
    • (1985) Biochem Pharmacol , vol.34 , pp. 3965-3972
    • Dawicki, D.D.1    Agarwal, K.C.2    Parks R.E., Jr.3
  • 12
    • 9844250198 scopus 로고    scopus 로고
    • Retrospective analysis of long-term hemorheologic effects of pentoxifylline in diabetic patients with angiopathic complications
    • Solerte SB, Fioravanti M, Cerutti N, et al. Retrospective analysis of long-term hemorheologic effects of pentoxifylline in diabetic patients with angiopathic complications. Acta Diabetol. 1997;34:67-74.
    • (1997) Acta Diabetol , vol.34 , pp. 67-74
    • Solerte, S.B.1    Fioravanti, M.2    Cerutti, N.3
  • 14
    • 0027275040 scopus 로고
    • + transport and cell dehydration in sickle erythrocytes by clotrimazole and other imidazole derivatives
    • + transport and cell dehydration in sickle erythrocytes by clotrimazole and other imidazole derivatives. J Clin Invest. 1993;92:520-526.
    • (1993) J Clin Invest , vol.92 , pp. 520-526
    • Brugnara, C.1    De Franceschi, L.2    Alper, S.L.3
  • 15
    • 0000659323 scopus 로고
    • The function of calcium in the potassium permeability of human erythrocytes
    • Gardos G. The function of calcium in the potassium permeability of human erythrocytes. Biochim Biophys Acta. 1958;30:654-655.
    • (1958) Biochim Biophys Acta , vol.30 , pp. 654-655
    • Gardos, G.1
  • 16
    • 0029257716 scopus 로고
    • Erythrocyte dehydration in pathophysiology and treatment of sickle cell disease
    • Brugnara C. Erythrocyte dehydration in pathophysiology and treatment of sickle cell disease. Curr Opin Hematol. 1995;2:132-138.
    • (1995) Curr Opin Hematol , vol.2 , pp. 132-138
    • Brugnara, C.1
  • 17
    • 0028965796 scopus 로고
    • Calcium stimulation of procoagulant activity in human erythrocytes
    • Martin DW, Jesty J. Calcium stimulation of procoagulant activity in human erythrocytes. J Biol Chem. 1995;270:10468-10474.
    • (1995) J Biol Chem , vol.270 , pp. 10468-10474
    • Martin, D.W.1    Jesty, J.2
  • 18
    • 0030849152 scopus 로고    scopus 로고
    • Molecular cloning of human plasma membrane phospholipid scramblase: A protein mediating transbilayer movement of plasma membrane phospholipids
    • Zhou Q, Zhao J, Stout JG, Luhm RA, Wiedmer T, Sims PJ. Molecular cloning of human plasma membrane phospholipid scramblase: a protein mediating transbilayer movement of plasma membrane phospholipids. J Biol Chem. 1998;272:18240-18244.
    • (1998) J Biol Chem , vol.272 , pp. 18240-18244
    • Zhou, Q.1    Zhao, J.2    Stout, J.G.3    Luhm, R.A.4    Wiedmer, T.5    Sims, P.J.6
  • 19
    • 0030730935 scopus 로고    scopus 로고
    • Regulation of CD44-protein 4.1 interaction by Ca2+ and calmodulin. Implications for modulation of CD44-ankyrin interaction
    • Nunomura W, Takakuwa Y, Tokimitsu R, Krauss SW, Kawashima M, Mohandas N. Regulation of CD44-protein 4.1 interaction by Ca2+ and calmodulin. Implications for modulation of CD44-ankyrin interaction. J Biol Chem. 1997;272:30322-30328.
    • (1997) J Biol Chem , vol.272 , pp. 30322-30328
    • Nunomura, W.1    Takakuwa, Y.2    Tokimitsu, R.3    Krauss, S.W.4    Kawashima, M.5    Mohandas, N.6
  • 20
    • 0025924751 scopus 로고
    • 2+-dependent regulation of the spectrin/actin interaction by calmodulin: Implications for their role in regulation of skeletal protein interactions
    • 2+-dependent regulation of the spectrin/actin interaction by calmodulin: Implications for their role in regulation of skeletal protein interactions. J Biol Chem. 1991;266:1134-1140.
    • (1991) J Biol Chem , vol.266 , pp. 1134-1140
    • Tanaka, T.1    Kadowaki, K.2    Lazarides, E.3    Sobue, K.4
  • 21
    • 0023687847 scopus 로고
    • 2+ and calmodulin: Implications for their role in regulation of skeletal protein interactions
    • 2+ and calmodulin: Implications for their role in regulation of skeletal protein interactions. J Clin Invest. 1988;82:394-400.
    • (1988) J Clin Invest , vol.82 , pp. 394-400
    • Takakuwa, Y.1    Mohandas, N.2
  • 22
    • 0017746962 scopus 로고
    • Calcium-promoted changes of the human erythrocyte membrane: Involvement of spectrin, transglutaminase, and a membrane-bound protease
    • Anderson DR, Davis JL, Carraway KL. Calcium-promoted changes of the human erythrocyte membrane: Involvement of spectrin, transglutaminase, and a membrane-bound protease. J Biol Chem. 1977;252:6617-6623.
    • (1977) J Biol Chem , vol.252 , pp. 6617-6623
    • Anderson, D.R.1    Davis, J.L.2    Carraway, K.L.3
  • 24
    • 0017156531 scopus 로고
    • Production of 1,2-diacylglycerol and phosphatidate in human erythrocytes treated with calcium ions and ionophore A23187
    • Allan D, Watts R, Michell RH. Production of 1,2-diacylglycerol and phosphatidate in human erythrocytes treated with calcium ions and ionophore A23187. Biochem J. 1976;156:225-232.
    • (1976) Biochem J , vol.156 , pp. 225-232
    • Allan, D.1    Watts, R.2    Michell, R.H.3
  • 27
    • 0026739575 scopus 로고
    • Regulation and post-translational modification of erythrocyte membrane-skeletal proteins
    • Cohen CM, Gascard P. Regulation and post-translational modification of erythrocyte membrane-skeletal proteins. Semin Hematol. 1992;29:244-292.
    • (1992) Semin Hematol , vol.29 , pp. 244-292
    • Cohen, C.M.1    Gascard, P.2
  • 28
    • 0025911561 scopus 로고
    • Evidence for a voltage-gated, non-selective cation channel in the human red cell membrane
    • Christophersen P, Bennekou P. Evidence for a voltage-gated, non-selective cation channel in the human red cell membrane. Biochim Biophys Acta. 1991;1065:103-106.
    • (1991) Biochim Biophys Acta , vol.1065 , pp. 103-106
    • Christophersen, P.1    Bennekou, P.2
  • 31
    • 0028337456 scopus 로고
    • In vitro effects of nifedipine on human red cell metabolism and blood coagulation
    • Meky N. In vitro effects of nifedipine on human red cell metabolism and blood coagulation, J Med. 1994;25:17-22.
    • (1994) J Med , vol.25 , pp. 17-22
    • Meky, N.1
  • 33
    • 0031591691 scopus 로고    scopus 로고
    • Characterization of voltage-dependent calcium influx in human erythrocytes by fura-2
    • Soldati L, Spaventa R, Vezzoli G, et al. Characterization of voltage-dependent calcium influx in human erythrocytes by fura-2. Biochem Biophys Res Commun. 1997;236:549-554.
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 549-554
    • Soldati, L.1    Spaventa, R.2    Vezzoli, G.3
  • 35
    • 0031021981 scopus 로고    scopus 로고
    • Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate
    • Zhang M, Zhou M, Van Etten RL, Stauffacher CV. Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate. Biochemistry. 1997;36:15-23.
    • (1997) Biochemistry , vol.36 , pp. 15-23
    • Zhang, M.1    Zhou, M.2    Van Etten, R.L.3    Stauffacher, C.V.4
  • 38
    • 0028957270 scopus 로고
    • Protein kinase C modulates calcium channels in isolated presynaptic nerve terminals of rat hippocampus
    • Bartschat DK, Rhodes TE. Protein kinase C modulates calcium channels in isolated presynaptic nerve terminals of rat hippocampus. J Neurochem. 1995;64:2064-2072.
    • (1995) J Neurochem , vol.64 , pp. 2064-2072
    • Bartschat, D.K.1    Rhodes, T.E.2
  • 39
    • 0032935787 scopus 로고    scopus 로고
    • 2+ channel current in rat pinealocytes: Role of basal phosphorylation
    • 2+ channel current in rat pinealocytes: Role of basal phosphorylation. J Neurochem. 1999;72:73-80.
    • (1999) J Neurochem , vol.72 , pp. 73-80
    • Chik, C.L.1    Li, B.2    Karpinski, E.3    Ho, A.K.4
  • 40
    • 0022381636 scopus 로고
    • Protein kinase C in the human erythrocyte. Translocation to the plasma membrane and phosphorylation of bands 4.1 and 4.9 and other membrane proteins
    • Palfrey HC, Waseem A. Protein kinase C in the human erythrocyte. Translocation to the plasma membrane and phosphorylation of bands 4.1 and 4.9 and other membrane proteins. J Biol Chem. 1985;260:16021-16029.
    • (1985) J Biol Chem , vol.260 , pp. 16021-16029
    • Palfrey, H.C.1    Waseem, A.2
  • 41
    • 0027764538 scopus 로고
    • Phorbol 12-myristate 13-acetate stimulated phosphorylation of erythrocyte membrane skeletal proteins is blocked by calpain inhibitors: Possible role of protein kinase M
    • Al Z, Cohen CM. Phorbol 12-myristate 13-acetate stimulated phosphorylation of erythrocyte membrane skeletal proteins is blocked by calpain inhibitors: Possible role of protein kinase M. Biochem J. 1993;296:675-683.
    • (1993) Biochem J , vol.296 , pp. 675-683
    • Al, Z.1    Cohen, C.M.2
  • 42
    • 0025320809 scopus 로고
    • Selective modulation of band 4.1 binding to erythrocyte membranes by protein kinase C
    • Danilov YN, Fennell R, Ling E, Cohen CM. Selective modulation of band 4.1 binding to erythrocyte membranes by protein kinase C. J Biol Chem. 1990;265:2556-2562.
    • (1990) J Biol Chem , vol.265 , pp. 2556-2562
    • Danilov, Y.N.1    Fennell, R.2    Ling, E.3    Cohen, C.M.4
  • 45
    • 0021241536 scopus 로고
    • Irreversible ATP depletion caused by low concentrations of formaldehyde and of calcium-chelator esters in intact human cells
    • Tiffert T, Garcia-Sancho J, Lew VL. Irreversible ATP depletion caused by low concentrations of formaldehyde and of calcium-chelator esters in intact human cells. Biochim Biophys Acta. 1984;773:143-156.
    • (1984) Biochim Biophys Acta , vol.773 , pp. 143-156
    • Tiffert, T.1    Garcia-Sancho, J.2    Lew, V.L.3
  • 46
    • 0021991233 scopus 로고
    • Pyruvate prevents the ATP depletion caused by formaldehyde or calcium-chelator esters in the human red cell
    • Garcia-Sancho J. Pyruvate prevents the ATP depletion caused by formaldehyde or calcium-chelator esters in the human red cell. Biochim Biophys Acta. 1985;813:148-150.
    • (1985) Biochim Biophys Acta , vol.813 , pp. 148-150
    • Garcia-Sancho, J.1
  • 47
    • 0030062076 scopus 로고    scopus 로고
    • Calcium-independent binding to interfacial phorbol esters causes protein kinase C to associate with membranes in the absence of acidic lipids
    • Mosior M, Newton AC. Calcium-independent binding to interfacial phorbol esters causes protein kinase C to associate with membranes in the absence of acidic lipids. Biochemistry. 1996;35:1612-1623.
    • (1996) Biochemistry , vol.35 , pp. 1612-1623
    • Mosior, M.1    Newton, A.C.2
  • 49
    • 0021962050 scopus 로고
    • Exogenous sn-1,2-diacylglycerols containing saturated fatty acids function as bioregulators of protein kinase C in human platelets
    • Lapetina EG, Reep B, Ganong BR, Bell RM. Exogenous sn-1,2-diacylglycerols containing saturated fatty acids function as bioregulators of protein kinase C in human platelets. J Biol Chem. 1985;260:1358-1361.
    • (1985) J Biol Chem , vol.260 , pp. 1358-1361
    • Lapetina, E.G.1    Reep, B.2    Ganong, B.R.3    Bell, R.M.4
  • 51
    • 0026763873 scopus 로고
    • P-type calcium channels in rat central and peripheral neurons
    • Mintz IM, Adams ME, Bean BP. P-type calcium channels in rat central and peripheral neurons. Neuron. 1992;9:85-95.
    • (1992) Neuron , vol.9 , pp. 85-95
    • Mintz, I.M.1    Adams, M.E.2    Bean, B.P.3
  • 52
    • 0022575573 scopus 로고
    • Nitrendipine, nifedipine, and verapamil inhibit the in vitro formation of irreversibly sickled cells
    • Ohnishi ST, Horiuchi KY, Jurman ME, Sadanaga KK. Nitrendipine, nifedipine, and verapamil inhibit the in vitro formation of irreversibly sickled cells. Pharmacology. 1986;32:248-256.
    • (1986) Pharmacology , vol.32 , pp. 248-256
    • Ohnishi, S.T.1    Horiuchi, K.Y.2    Jurman, M.E.3    Sadanaga, K.K.4
  • 54
    • 0032549693 scopus 로고    scopus 로고
    • Level of expression of phospholipid scramblase regulates induced movement of phosphatidyiserine to the cell surface
    • Zhao J, Zhou Q, Wiedmer T, Sims PJ. Level of expression of phospholipid scramblase regulates induced movement of phosphatidyiserine to the cell surface. J Biol Chem. 1998;273:6603-6606.
    • (1998) J Biol Chem , vol.273 , pp. 6603-6606
    • Zhao, J.1    Zhou, Q.2    Wiedmer, T.3    Sims, P.J.4
  • 55
    • 0001492765 scopus 로고
    • Blocking and isolation of a calcium channel from neurons in mammals and cephalopods utilizing a toxin fraction (FTX) from funnel-web spider poison
    • Llinas R, Sugimori M, Lin J-W, Cherksey B. Blocking and isolation of a calcium channel from neurons in mammals and cephalopods utilizing a toxin fraction (FTX) from funnel-web spider poison. Proc Natl Acad Sci U S A. 1989;86:1689-1693.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 1689-1693
    • Llinas, R.1    Sugimori, M.2    Lin, J.-W.3    Cherksey, B.4
  • 60
    • 0027502079 scopus 로고
    • The voltage-gated non-selective cation channel from human red cells is sensitive to acetylcholine
    • Bennekou P. The voltage-gated non-selective cation channel from human red cells is sensitive to acetylcholine. Biochim Biophys Acta. 1993;1147:165-167.
    • (1993) Biochim Biophys Acta , vol.1147 , pp. 165-167
    • Bennekou, P.1
  • 62
    • 0035437137 scopus 로고    scopus 로고
    • Characterization of the phosphatidylserine-exposing subpopulation of sickle cells
    • de Jong K, Larkin SK, Styles LA, Bookchin RM, Kuypers FA. Characterization of the phosphatidylserine-exposing subpopulation of sickle cells. Blood. 2001;98:860-867.
    • (2001) Blood , vol.98 , pp. 860-867
    • De Jong, K.1    Larkin, S.K.2    Styles, L.A.3    Bookchin, R.M.4    Kuypers, F.A.5
  • 64
    • 0029865706 scopus 로고
    • Therapy with oral clotrimazole induces inhibition of the Gardos channel and reduction of erythrocyte dehydration in patients with sickle cell disease
    • Brugnara C, Gee B, Armsby CC, et al. Therapy with oral clotrimazole induces inhibition of the Gardos channel and reduction of erythrocyte dehydration in patients with sickle cell disease. J Clin Invest. 1986;97:1227-1243.
    • (1986) J Clin Invest , vol.97 , pp. 1227-1243
    • Brugnara, C.1    Gee, B.2    Armsby, C.C.3
  • 65
    • 0022549289 scopus 로고
    • Regulation of erythrocyte cation and water content in sickle cell anemia
    • Brugnara C, Bunn HF, Tosteson DC. Regulation of erythrocyte cation and water content in sickle cell anemia. Science. 1986;232:388-390.
    • (1986) Science , vol.232 , pp. 388-390
    • Brugnara, C.1    Bunn, H.F.2    Tosteson, D.C.3
  • 66
    • 0034161506 scopus 로고    scopus 로고
    • Volume control in sickle cells is facilitated by the novel anion conductance inhibitor NS 1652
    • , Bennekou P, Pedersen O, Molier A, Christophersen P. Volume control in sickle cells is facilitated by the novel anion conductance inhibitor NS 1652. Blood. 2000;95:1842-1848.
    • (2000) Blood , vol.95 , pp. 1842-1848
    • Bennekou, P.1    Pedersen, O.2    Molier, A.3    Christophersen, P.4
  • 67
    • 0019390504 scopus 로고
    • Effect of a sickling pulse on calcium and potassium transport in sickle cell trait red cells
    • Bookchin RM, Lew VL. Effect of a sickling pulse on calcium and potassium transport in sickle cell trait red cells. J Physiol. 1981;312:265-280.
    • (1981) J Physiol , vol.312 , pp. 265-280
    • Bookchin, R.M.1    Lew, V.L.2
  • 69
    • 0027527368 scopus 로고
    • Increased cytosolic free calcium in red blood cells is associated with essential hypertension in humans
    • Lindner A, Hinds TR, Davidson RC, Vincenzi FF. Increased cytosolic free calcium in red blood cells is associated with essential hypertension in humans. Am J Hypertens. 1993;6:771-779.
    • (1993) Am J Hypertens , vol.6 , pp. 771-779
    • Lindner, A.1    Hinds, T.R.2    Davidson, R.C.3    Vincenzi, F.F.4
  • 71
    • 0028145314 scopus 로고
    • Erythrocyte membrane calcium transport in patients with primary hyperparathyroidism
    • Vezzoli G, Reina MC, Cusi D, et al. Erythrocyte membrane calcium transport in patients with primary hyperparathyroidism. Biochem Biophys Res Commun. 1994;202:1505-1510.
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 1505-1510
    • Vezzoli, G.1    Reina, M.C.2    Cusi, D.3
  • 72
    • 0029586076 scopus 로고
    • (Ca+Mg)ATPase and calcium influx in erythrocytes of patients with idiopathic hypercalciuria
    • Vezzoli G, Reina MC, Zerbi S, et al. (Ca+Mg)ATPase and calcium influx in erythrocytes of patients with idiopathic hypercalciuria. Biochem Biophys Res Commun. 1995;217:1099-1104.
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 1099-1104
    • Vezzoli, G.1    Reina, M.C.2    Zerbi, S.3
  • 73
    • 0031825691 scopus 로고    scopus 로고
    • 2+ content during incubation, in normals and in subjects with vascular atherosclerotic disease and non-insulin-dependent diabetes mellitus
    • 2+ content during incubation, in normals and in subjects with vascular atherosclerotic disease and non-insulin-dependent diabetes mellitus. Clin Hemorheol Microcirc. 1998;18:195-197.
    • (1998) Clin Hemorheol Microcirc , vol.18 , pp. 195-197
    • Caimi, G.1    Canino, B.2    Montana, M.3    Lo Presti, R.4
  • 74
    • 0028270793 scopus 로고
    • The effect of endotoxin on neonatal erythrocyte intracellular calcium concentration
    • Todd JC III, Poulos ND, Mollitt DL. The effect of endotoxin on neonatal erythrocyte intracellular calcium concentration. J Pediatr Surg. 1994;29:805-807.
    • (1994) J Pediatr Surg , vol.29 , pp. 805-807
    • Todd J.C. III1    Poulos, N.D.2    Mollitt, D.L.3
  • 75
    • 0028953796 scopus 로고
    • Effect of sepsis on erythrocyte intracellular calcium homeostasis
    • Todd JC III, Mollitt DL, Effect of sepsis on erythrocyte intracellular calcium homeostasis. Crit Care Med. 1995;23:459-465.
    • (1995) Crit Care Med , vol.23 , pp. 459-465
    • Todd J.C. III1    Mollitt, D.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.