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Volumn 1790, Issue 10, 2009, Pages 1274-1281

Calcium binding studies of peptides of human phospholipid scramblases 1 to 4 suggest that scramblases are new class of calcium binding proteins in the cell

Author keywords

Calcium binding; Isothermal titration calorimetry; Peptides; Phospholipids; Scramblase; Tryptophan fluorescence

Indexed keywords

CALCIUM ION; MAGNESIUM ION; PHOSPHOLIPID SCRAMBLASE 1; PHOSPHOLIPID SCRAMBLASE 2; PHOSPHOLIPID SCRAMBLASE 3; PHOSPHOLIPID SCRAMBLASE 4; SCRAMBLASE; UNCLASSIFIED DRUG;

EID: 69949092006     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2009.06.008     Document Type: Article
Times cited : (25)

References (51)
  • 1
    • 0034738623 scopus 로고    scopus 로고
    • Identification of three new members of the phospholipid scramblase gene family
    • Wiedmer T., Zhou Q., Kwoh D.Y., and Sims P.J. Identification of three new members of the phospholipid scramblase gene family. Biochim. Biophys. Acta 1467 (2000) 244-253
    • (2000) Biochim. Biophys. Acta , vol.1467 , pp. 244-253
    • Wiedmer, T.1    Zhou, Q.2    Kwoh, D.Y.3    Sims, P.J.4
  • 3
    • 0028820202 scopus 로고
    • Mechanisms of phosphatidyl serine exposure, on apoptotic T lymphocytes
    • Verhoven B., Schlegel R.A., and Willamson P. Mechanisms of phosphatidyl serine exposure, on apoptotic T lymphocytes. J. Exp. Med. 182 (1995) 1597-1601
    • (1995) J. Exp. Med. , vol.182 , pp. 1597-1601
    • Verhoven, B.1    Schlegel, R.A.2    Willamson, P.3
  • 4
    • 0025826481 scopus 로고
    • Platelet procoagulant activity: physiological significance and mechanism of PS exposure
    • Bevers E.M., Comfurius P., and Zwaal R.F. Platelet procoagulant activity: physiological significance and mechanism of PS exposure. Blood Rev. 5 (1991) 146-154
    • (1991) Blood Rev. , vol.5 , pp. 146-154
    • Bevers, E.M.1    Comfurius, P.2    Zwaal, R.F.3
  • 5
    • 0026508561 scopus 로고
    • Exposure of phosphatidyl serine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok V.A., Voelker D.R., Campbel P.A., Cohen J.J., Bratton D.L., and Henson P.M. Exposure of phosphatidyl serine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 148 (1992) 2207-2216
    • (1992) J. Immunol. , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbel, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 6
    • 0037215912 scopus 로고    scopus 로고
    • Exposure of anionic phospholipids serves as anti-inflammatory and immunosuppressive signal-implications for antiphospholipid syndrome and systemic lupus erythematosus
    • Gaipl U.S., Beyer T.D., Baumann I., Voll R.E., Stach C.M., Heydera P., Kalden J.R., Manfredi A., and Herrmann M. Exposure of anionic phospholipids serves as anti-inflammatory and immunosuppressive signal-implications for antiphospholipid syndrome and systemic lupus erythematosus. Immunobiol. 207 (2003) 73-81
    • (2003) Immunobiol. , vol.207 , pp. 73-81
    • Gaipl, U.S.1    Beyer, T.D.2    Baumann, I.3    Voll, R.E.4    Stach, C.M.5    Heydera, P.6    Kalden, J.R.7    Manfredi, A.8    Herrmann, M.9
  • 7
    • 0034725570 scopus 로고    scopus 로고
    • Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase C delta
    • Frasch S.C., Henson P.M., Kailey J.M., Richter D.A., Janes M.S., Fadok V.A., and Bratton D.L. Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase C delta. J. Biol. Chem. 275 (2000) 23065-23073
    • (2000) J. Biol. Chem. , vol.275 , pp. 23065-23073
    • Frasch, S.C.1    Henson, P.M.2    Kailey, J.M.3    Richter, D.A.4    Janes, M.S.5    Fadok, V.A.6    Bratton, D.L.7
  • 8
    • 0032549693 scopus 로고    scopus 로고
    • Level of expression of phospholipid scramblase regulates induced movement of phosphatidyl serine to the cell surface
    • Zhao J., Zhou Q., Wiedmer T., and Sims P.J. Level of expression of phospholipid scramblase regulates induced movement of phosphatidyl serine to the cell surface. J. Biol. Chem. 273 (1998) 6603-6606
    • (1998) J. Biol. Chem. , vol.273 , pp. 6603-6606
    • Zhao, J.1    Zhou, Q.2    Wiedmer, T.3    Sims, P.J.4
  • 9
    • 2942637935 scopus 로고    scopus 로고
    • Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids
    • Zwaal R.F.A., Comfurius P., and Bevers E.M. Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids. Biochim. Biophys. Acta 1636 (2004) 119-128
    • (2004) Biochim. Biophys. Acta , vol.1636 , pp. 119-128
    • Zwaal, R.F.A.1    Comfurius, P.2    Bevers, E.M.3
  • 12
    • 2942637935 scopus 로고    scopus 로고
    • Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids
    • Zwaal R.F.A., Comfurius P., and Bevers R.M. Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids. Biochim. Biophys. Acta 1636 (2004) 119-128
    • (2004) Biochim. Biophys. Acta , vol.1636 , pp. 119-128
    • Zwaal, R.F.A.1    Comfurius, P.2    Bevers, R.M.3
  • 15
    • 0030849152 scopus 로고    scopus 로고
    • Molecular cloning of human plasma membrane phospholipid scramblase
    • Zhou Q., Zhao J., Stout J.G., Luhm R.A., Wiedmer T., and Sims P.J. Molecular cloning of human plasma membrane phospholipid scramblase. J. Biol. Chem. 272 (1997) 18240-18244
    • (1997) 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
  • 16
    • 0141844576 scopus 로고    scopus 로고
    • Plasma membrane phospholipid scramblase 1 promotes EGF-dependent activation of c-Src through the epidermal growth factor receptor
    • Nanjundan M., Sun J., Zhao J., Zhou Q., Sims P.J., and Wiedmer T. Plasma membrane phospholipid scramblase 1 promotes EGF-dependent activation of c-Src through the epidermal growth factor receptor. J. Biol. Chem. 278 (2003) 37413-37418
    • (2003) J. Biol. Chem. , vol.278 , pp. 37413-37418
    • Nanjundan, M.1    Sun, J.2    Zhao, J.3    Zhou, Q.4    Sims, P.J.5    Wiedmer, T.6
  • 17
    • 0036258870 scopus 로고    scopus 로고
    • Role of Mm TRA1b/phospholipid scramblase 1 gene expression in the induction of differentiation of human myeloid leukemia cells into granulocytes
    • Nakamaki T., Okabe-Kado J., Yamamoto-Yamaguchi Y., Hino K., Tomoyasu S., Honma Y., and Kasukabe T. Role of Mm TRA1b/phospholipid scramblase 1 gene expression in the induction of differentiation of human myeloid leukemia cells into granulocytes. Exp. Hematol. 30 (2002) 421-429
    • (2002) Exp. Hematol. , vol.30 , pp. 421-429
    • Nakamaki, T.1    Okabe-Kado, J.2    Yamamoto-Yamaguchi, Y.3    Hino, K.4    Tomoyasu, S.5    Honma, Y.6    Kasukabe, T.7
  • 18
    • 27144480096 scopus 로고    scopus 로고
    • Phospholipid scramblase 1 binds to the promoter region of the inositol 1, 4, 5-triphosphate receptor type 1 gene to enhance its expression
    • Zhou Q., Ben-Efraim I., Bigcas J., Junqueira D., Wiedmer T., and Sims P.J. Phospholipid scramblase 1 binds to the promoter region of the inositol 1, 4, 5-triphosphate receptor type 1 gene to enhance its expression. J. Biol. Chem. 280 (2005) 35062-35068
    • (2005) J. Biol. Chem. , vol.280 , pp. 35062-35068
    • Zhou, Q.1    Ben-Efraim, I.2    Bigcas, J.3    Junqueira, D.4    Wiedmer, T.5    Sims, P.J.6
  • 19
    • 0036624776 scopus 로고    scopus 로고
    • Normal homeostasis but defective hematopoetic response to growth factors in mice deficient in phospholipid scramblase 1
    • Zhou Q., Zhao J., Wiedmer T., and Sims P.J. Normal homeostasis but defective hematopoetic response to growth factors in mice deficient in phospholipid scramblase 1. Blood 99 (2002) 4030-4038
    • (2002) Blood , vol.99 , pp. 4030-4038
    • Zhou, Q.1    Zhao, J.2    Wiedmer, T.3    Sims, P.J.4
  • 20
  • 21
    • 46549087800 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) induced mitochondrial pathway to apoptosis and caspase activation is potentiated by phospholipid scramblase-3
    • Ndebele K., Gona P., Jin T.G., Benhaga N., Chalah A., Degli-Esposti M., and Khosravi-Far R. Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) induced mitochondrial pathway to apoptosis and caspase activation is potentiated by phospholipid scramblase-3. Apoptosis 13 (2008) 845-856
    • (2008) Apoptosis , vol.13 , pp. 845-856
    • Ndebele, K.1    Gona, P.2    Jin, T.G.3    Benhaga, N.4    Chalah, A.5    Degli-Esposti, M.6    Khosravi-Far, R.7
  • 22
    • 44349188067 scopus 로고    scopus 로고
    • Identification of alix-type and non-alix type ALG-2-binding sites in human phospholipid scramblase 3
    • Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., and Maki M. Identification of alix-type and non-alix type ALG-2-binding sites in human phospholipid scramblase 3. J. Biol. Chem. 283 (2008) 9623-9632
    • (2008) J. Biol. Chem. , vol.283 , pp. 9623-9632
    • Shibata, H.1    Suzuki, H.2    Kakiuchi, T.3    Inuzuka, T.4    Yoshida, H.5    Mizuno, T.6    Maki, M.7
  • 23
    • 0032562186 scopus 로고    scopus 로고
    • 2+-accelerated transbilayer movement of membrane phospholipids
    • 2+-accelerated transbilayer movement of membrane phospholipids. Biochemistry 37 (1998) 2356-2360
    • (1998) Biochemistry , vol.37 , pp. 2356-2360
    • Zhou, Q.1    Sims, P.J.2    Wiedmer, T.3
  • 26
    • 34547729698 scopus 로고    scopus 로고
    • Calcium-binding to lens βB2- and βA3-crystallins suggests that all β-crystallins are calcium-binding proteins
    • Jobby M.K., and Sharma Y. Calcium-binding to lens βB2- and βA3-crystallins suggests that all β-crystallins are calcium-binding proteins. FEBS J. 274 (2007) 4135-4147
    • (2007) FEBS J. , vol.274 , pp. 4135-4147
    • Jobby, M.K.1    Sharma, Y.2
  • 29
    • 0021267421 scopus 로고
    • Heat capacity and entropy changes of calmodulin induced by calcium binding
    • Tanokura M., and Yamada K. Heat capacity and entropy changes of calmodulin induced by calcium binding. J. Biochem. 95 (1984) 643-649
    • (1984) J. Biochem. , vol.95 , pp. 643-649
    • Tanokura, M.1    Yamada, K.2
  • 30
    • 0014722597 scopus 로고    scopus 로고
    • Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous properly of water
    • Lumry R., and Rajender S. Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous properly of water. Biopolymers 9 (2004) 1125-1227
    • (2004) Biopolymers , vol.9 , pp. 1125-1227
    • Lumry, R.1    Rajender, S.2
  • 31
    • 3242808002 scopus 로고    scopus 로고
    • Thermodynamic properties of peptide folding
    • Sigman J.A. Thermodynamic properties of peptide folding. Biochem. Mol. Biol. Educ. 32 (2004) 265-268
    • (2004) Biochem. Mol. Biol. Educ. , vol.32 , pp. 265-268
    • Sigman, J.A.1
  • 32
    • 0033994803 scopus 로고    scopus 로고
    • Peptide analogs from E-cadherin with different calcium-binding affinities
    • Yang W., Tsai T., Kats M., and Yang J.J. Peptide analogs from E-cadherin with different calcium-binding affinities. J. Peptide Res. 55 (2000) 203-215
    • (2000) J. Peptide Res. , vol.55 , pp. 203-215
    • Yang, W.1    Tsai, T.2    Kats, M.3    Yang, J.J.4
  • 35
    • 85056046664 scopus 로고    scopus 로고
    • Calcium-induced conformational transition of trout ependymins monitored by tryptophan fluorescence
    • Ganss B., and Hoffmann W. Calcium-induced conformational transition of trout ependymins monitored by tryptophan fluorescence. Open Biochem. J. 3 (2009) 14-17
    • (2009) Open Biochem. J. , vol.3 , pp. 14-17
    • Ganss, B.1    Hoffmann, W.2
  • 38
    • 44049102957 scopus 로고    scopus 로고
    • Peptide sequence and conformation strongly influence tryptophan fluorescence
    • Alston R.W., Lasagna M., Grimsley G.R., Scholtz J.M., and Reinhart G.D. Peptide sequence and conformation strongly influence tryptophan fluorescence. Biophys. J. 94 (2008) 2280-2287
    • (2008) Biophys. J. , vol.94 , pp. 2280-2287
    • Alston, R.W.1    Lasagna, M.2    Grimsley, G.R.3    Scholtz, J.M.4    Reinhart, G.D.5
  • 40
    • 0038281274 scopus 로고    scopus 로고
    • Vibrational spectroscopic detection of beta- and gamma-turns in synthetic and natural peptides and proteins
    • Vass E., Hollosi M., Besson F., and Buchet R. Vibrational spectroscopic detection of beta- and gamma-turns in synthetic and natural peptides and proteins. Chem. Rev. 103 (2003) 1917-1954
    • (2003) Chem. Rev. , vol.103 , pp. 1917-1954
    • Vass, E.1    Hollosi, M.2    Besson, F.3    Buchet, R.4
  • 41
    • 33644533148 scopus 로고    scopus 로고
    • Random coils, β-sheet ribbons, and α-helical fibers: one peptide adopting three different secondary structures
    • Pagel K., Wagner S.C., Samedov K., von Berlepsch H., Bttcher C., and Kosch B. Random coils, β-sheet ribbons, and α-helical fibers: one peptide adopting three different secondary structures. J. Am. Chem. Soc. 128 (2006) 2196-2197
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2196-2197
    • Pagel, K.1    Wagner, S.C.2    Samedov, K.3    von Berlepsch, H.4    Bttcher, C.5    Kosch, B.6
  • 42
    • 0032797930 scopus 로고    scopus 로고
    • Weakly bound calcium ions involved in the thermostability of aqualysin I, a heat-stable subtilisin-type protease of Thermus aquaticus YT-1
    • Lin S., Yoshimura E., Hiroshi S., Takayoshi W., and Hiroshi M. Weakly bound calcium ions involved in the thermostability of aqualysin I, a heat-stable subtilisin-type protease of Thermus aquaticus YT-1. Biochim. Biophys. Acta 1433 (1999) 132-138
    • (1999) Biochim. Biophys. Acta , vol.1433 , pp. 132-138
    • Lin, S.1    Yoshimura, E.2    Hiroshi, S.3    Takayoshi, W.4    Hiroshi, M.5
  • 44
    • 33750046332 scopus 로고    scopus 로고
    • Prediction of EF-hand calcium-binding proteins and analysis of bacterial EF-hand proteins
    • Zhou Y., Yang Y., Kirberger M., Lee H., Ayalasomayajula G., and Yang J.J. Prediction of EF-hand calcium-binding proteins and analysis of bacterial EF-hand proteins. Proteins 65 (2006) 643-655
    • (2006) Proteins , vol.65 , pp. 643-655
    • Zhou, Y.1    Yang, Y.2    Kirberger, M.3    Lee, H.4    Ayalasomayajula, G.5    Yang, J.J.6
  • 45
    • 58349112969 scopus 로고    scopus 로고
    • Phospholipid scramblases and tubby-like proteins belong to a new superfamily of membrane tethered transcription factors
    • Bateman A., Finn R.D., Sims P.J., Wiedmer T., Biegert A., and Söding J. Phospholipid scramblases and tubby-like proteins belong to a new superfamily of membrane tethered transcription factors. Bioinformatics 25 (2009) 159-162
    • (2009) Bioinformatics , vol.25 , pp. 159-162
    • Bateman, A.1    Finn, R.D.2    Sims, P.J.3    Wiedmer, T.4    Biegert, A.5    Söding, J.6
  • 46
    • 0032825215 scopus 로고    scopus 로고
    • Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains
    • Paoli M., Anderson B.F., Baker H.M., Morgan W.T., Smith A., and Baker E.N. Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains. Nat. Struct. Biol. 6 (1999) 926-931
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 926-931
    • Paoli, M.1    Anderson, B.F.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 47
    • 0029919194 scopus 로고    scopus 로고
    • Purification and characterization of cytosolic and microsomal cyclophilins from maize (Zea mays)
    • Sheldon P.S., and Venis M.A. Purification and characterization of cytosolic and microsomal cyclophilins from maize (Zea mays). Biochem. J. 315 (1996) 965-970
    • (1996) Biochem. J. , vol.315 , pp. 965-970
    • Sheldon, P.S.1    Venis, M.A.2
  • 49
    • 44849125498 scopus 로고    scopus 로고
    • Engagement of phospholipid scramblase 1 in activated cells: implication for phosphatidyl serine externalization and exocytosis
    • Smrz D., Lebduska P., Draberova L., Korb J., and Draber P. Engagement of phospholipid scramblase 1 in activated cells: implication for phosphatidyl serine externalization and exocytosis. J. Biol. Chem. 283 (2008) 10904-10918
    • (2008) J. Biol. Chem. , vol.283 , pp. 10904-10918
    • Smrz, D.1    Lebduska, P.2    Draberova, L.3    Korb, J.4    Draber, P.5
  • 50
    • 0031711701 scopus 로고    scopus 로고
    • Transmembrane phospholipid distribution in blood cells: control mechanisms and pathophysiological significance
    • Bevers E.M., Comfurius P., Dekkers D.W., Harmsma M., and Zwaal R.F. Transmembrane phospholipid distribution in blood cells: control mechanisms and pathophysiological significance. Biol. Chem. 379 (1998) 973-986
    • (1998) Biol. Chem. , vol.379 , pp. 973-986
    • Bevers, E.M.1    Comfurius, P.2    Dekkers, D.W.3    Harmsma, M.4    Zwaal, R.F.5
  • 51
    • 57649210164 scopus 로고    scopus 로고
    • 2+-dependent neutral sphingomyelinase 1 as a mediator of heat stress-induced ceramide generation and apoptosis
    • 2+-dependent neutral sphingomyelinase 1 as a mediator of heat stress-induced ceramide generation and apoptosis. J. Biol. Chem. 283 (2008) 29971-29982
    • (2008) J. Biol. Chem. , vol.283 , pp. 29971-29982
    • Yabu, T.1    Imamura, S.2    Yamashita, M.3    Okazaki, T.4


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