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Volumn 54, Issue 1, 2007, Pages 183-191

Overexpression in Escherichia coli and functional reconstitution of the liposome binding ferriheme protein nitrophorin 7 from the bloodsucking bug Rhodnius prolixus

Author keywords

Bloodsucking insects; Heme protein reconstitution; Lipocalin refolding; Liposome protein interaction; Nitrophorin; Phosphatidylserine; Rhodnius prolixus

Indexed keywords

HEMIN; HEMOPROTEIN; LIPOSOME; NITROPHORIN; RECOMBINANT PROTEIN; SALIVA PROTEIN; UNCLASSIFIED DRUG;

EID: 34247344940     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.02.017     Document Type: Article
Times cited : (30)

References (37)
  • 1
    • 0000064601 scopus 로고    scopus 로고
    • Mauk A.G., and Sykes A.G. (Eds), Academic Press, San Diego (United States)
    • Walker F.A., and Montfort W.R. In: Mauk A.G., and Sykes A.G. (Eds). Advances in Inorganic Chemistry (2001), Academic Press, San Diego (United States) 295-358
    • (2001) Advances in Inorganic Chemistry , pp. 295-358
    • Walker, F.A.1    Montfort, W.R.2
  • 2
    • 0037211411 scopus 로고    scopus 로고
    • Changes in salivary nitrophorin profile during the life cycle of the blood-sucking bug Rhodnius prolixus
    • Moreira M.F., Coelho H.S.L., Zingali R.B., Oliveira P.L., and Masuda H. Changes in salivary nitrophorin profile during the life cycle of the blood-sucking bug Rhodnius prolixus. Insect Biochem. Mol. Biol. 33 (2003) 23-28
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 23-28
    • Moreira, M.F.1    Coelho, H.S.L.2    Zingali, R.B.3    Oliveira, P.L.4    Masuda, H.5
  • 3
    • 2642565286 scopus 로고    scopus 로고
    • Recognition of anionic phospholipid membranes by an antihemostatic protein from a blood-feeding insect
    • Andersen J.F., Gudderra N.P., Francischetti I.M.B., Valenzuela J.G., and Ribeiro J.M.C. Recognition of anionic phospholipid membranes by an antihemostatic protein from a blood-feeding insect. Biochemistry 43 (2004) 6987-6994
    • (2004) Biochemistry , vol.43 , pp. 6987-6994
    • Andersen, J.F.1    Gudderra, N.P.2    Francischetti, I.M.B.3    Valenzuela, J.G.4    Ribeiro, J.M.C.5
  • 4
    • 0029294689 scopus 로고
    • Nitric oxide loading of the salivary nitric-oxide-carrying hemoproteins (nitrophorins) in the blood-sucking bug Rhodnius prolixus
    • Nussenzveig R.H., Bentley D.L., and Ribeiro J.M.C. Nitric oxide loading of the salivary nitric-oxide-carrying hemoproteins (nitrophorins) in the blood-sucking bug Rhodnius prolixus. J. Exp. Biol. 198 (1995) 1093-1098
    • (1995) J. Exp. Biol. , vol.198 , pp. 1093-1098
    • Nussenzveig, R.H.1    Bentley, D.L.2    Ribeiro, J.M.C.3
  • 6
    • 0027213409 scopus 로고
    • Reversible binding of nitric oxide by a salivary heme protein from a bloodsucking insect
    • Ribeiro J.M.C., Hazzard J.M., Nussenzveig R.H., Champagne D.E., and Walker F.A. Reversible binding of nitric oxide by a salivary heme protein from a bloodsucking insect. Science 260 (1993) 539-541
    • (1993) Science , vol.260 , pp. 539-541
    • Ribeiro, J.M.C.1    Hazzard, J.M.2    Nussenzveig, R.H.3    Champagne, D.E.4    Walker, F.A.5
  • 7
    • 31344449504 scopus 로고    scopus 로고
    • Characterization of histamine release by mast cells, basophils, and monocytes
    • Falus A., Grosman N., and Darvas Z. (Eds), SpringMed Publishing Ltd., Budapest (Hungary)
    • Watt A.P., and Ennis M. Characterization of histamine release by mast cells, basophils, and monocytes. In: Falus A., Grosman N., and Darvas Z. (Eds). Histamine: Biology and Medical Aspects (2004), SpringMed Publishing Ltd., Budapest (Hungary) 99-111
    • (2004) Histamine: Biology and Medical Aspects , pp. 99-111
    • Watt, A.P.1    Ennis, M.2
  • 8
    • 0028029463 scopus 로고
    • High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus
    • Ribeiro J.M.C., and Walker F.A. High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus. J. Exp. Med. 180 (1994) 2251-2257
    • (1994) J. Exp. Med. , vol.180 , pp. 2251-2257
    • Ribeiro, J.M.C.1    Walker, F.A.2
  • 10
    • 0027924584 scopus 로고
    • American trypanosomiasis (Chagas' disease)-a tropical disease now in the United States
    • Kirchhoff L.V. American trypanosomiasis (Chagas' disease)-a tropical disease now in the United States. N. Engl. J. Med. 329 (1993) 639-644
    • (1993) N. Engl. J. Med. , vol.329 , pp. 639-644
    • Kirchhoff, L.V.1
  • 12
    • 0034684238 scopus 로고    scopus 로고
    • Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods
    • Montfort W.R., Weichsel A., and Andersen J.F. Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods. Biochim. Biophys. Acta 1482 (2000) 110-118
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 110-118
    • Montfort, W.R.1    Weichsel, A.2    Andersen, J.F.3
  • 13
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: structure and function
    • Flower D.R. The lipocalin protein family: structure and function. Biochem. J. 318 (1996) 1-14
    • (1996) Biochem. J. , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 14
    • 0034684194 scopus 로고    scopus 로고
    • Immunocalins: a lipocalin subfamily that modulates immune and inflammatory responses
    • Logdberg L., and Wester L. Immunocalins: a lipocalin subfamily that modulates immune and inflammatory responses. Biochim. Biophys. Acta 1482 (2000) 284-297
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 284-297
    • Logdberg, L.1    Wester, L.2
  • 16
    • 33746721535 scopus 로고    scopus 로고
    • Asymmetric distribution of phospholipids in biomembranes
    • Yamaji-Hasegawa A., and Tsujimoto M. Asymmetric distribution of phospholipids in biomembranes. Biol. Pharmac. Bull. 29 (2006) 1547-1553
    • (2006) Biol. Pharmac. Bull. , vol.29 , pp. 1547-1553
    • Yamaji-Hasegawa, A.1    Tsujimoto, M.2
  • 17
    • 0033550489 scopus 로고    scopus 로고
    • Nitric oxide binding to the ferri- and ferroheme states of nitrophorin 1, a reversible NO-binding heme protein from the saliva of the blood-sucking insect, Rhodnius prolixus
    • Ding X.D., Weichsel A., Andersen J.F., Shokhireva T.Kh., Balfour C., Pierik A.J., Averill B.A., Montfort W.R., and Walker F.A. Nitric oxide binding to the ferri- and ferroheme states of nitrophorin 1, a reversible NO-binding heme protein from the saliva of the blood-sucking insect, Rhodnius prolixus. J. Am. Chem. Soc. 121 (1999) 128-138
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 128-138
    • Ding, X.D.1    Weichsel, A.2    Andersen, J.F.3    Shokhireva, T.Kh.4    Balfour, C.5    Pierik, A.J.6    Averill, B.A.7    Montfort, W.R.8    Walker, F.A.9
  • 19
    • 0030993345 scopus 로고    scopus 로고
    • Nitric oxide binding and crystallization of recombinant nitrophorin I, a nitric oxide transport protein from the blood-sucking bug Rhodnius prolixus
    • Andersen J.F., Champagne D.E., Weichsel A., Ribeiro J.M.C., Balfour C.A., Dress V., and Montfort W.R. Nitric oxide binding and crystallization of recombinant nitrophorin I, a nitric oxide transport protein from the blood-sucking bug Rhodnius prolixus. Biochemistry 36 (1997) 4423-4428
    • (1997) Biochemistry , vol.36 , pp. 4423-4428
    • Andersen, J.F.1    Champagne, D.E.2    Weichsel, A.3    Ribeiro, J.M.C.4    Balfour, C.A.5    Dress, V.6    Montfort, W.R.7
  • 20
    • 0032957639 scopus 로고    scopus 로고
    • Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange Site-Directed Mutagenesis
    • Wang W., and Malcolm B.A. Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange Site-Directed Mutagenesis. BioTechniques 26 (1999) 680-682
    • (1999) BioTechniques , vol.26 , pp. 680-682
    • Wang, W.1    Malcolm, B.A.2
  • 21
    • 0014199262 scopus 로고    scopus 로고
    • T. Yonetani, Studies on cytochrome c peroxidase. X. Crystalline apo- and reconstituted holoenzymes, 242 (1967) 5008-5013.
  • 22
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophane and tyrosine in proteins
    • Edelhoch H. Spectroscopic determination of tryptophane and tyrosine in proteins. Biochemistry 6 (1967) 1948-1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 23
    • 0017101625 scopus 로고
    • Large volume liposomes by an ether vaporization method
    • Deamer D., and Bangham A.D. Large volume liposomes by an ether vaporization method. Biochim. Biophys. Acta 448 (1976) 629-634
    • (1976) Biochim. Biophys. Acta , vol.448 , pp. 629-634
    • Deamer, D.1    Bangham, A.D.2
  • 24
    • 0030298255 scopus 로고    scopus 로고
    • Surface changes induced by osmotic shrinkage on large unilamellar vesicles
    • Disalvo E.A., Campos A.M., Abuin E., and Lissi E.A. Surface changes induced by osmotic shrinkage on large unilamellar vesicles. Chem. Phys. Lipids 84 (1996) 35-45
    • (1996) Chem. Phys. Lipids , vol.84 , pp. 35-45
    • Disalvo, E.A.1    Campos, A.M.2    Abuin, E.3    Lissi, E.A.4
  • 25
    • 0032532483 scopus 로고    scopus 로고
    • The crystal structure of nitrophorin 4 at 1.5 Å resolution: transport of nitric oxide by a lipocalin-based heme protein
    • Andersen J.F., Weichsel A., Balfour C.A., Champagne D.E., and Montfort W.R. The crystal structure of nitrophorin 4 at 1.5 Å resolution: transport of nitric oxide by a lipocalin-based heme protein. Structure 6 (1998) 1315-1327
    • (1998) Structure , vol.6 , pp. 1315-1327
    • Andersen, J.F.1    Weichsel, A.2    Balfour, C.A.3    Champagne, D.E.4    Montfort, W.R.5
  • 26
    • 0023274482 scopus 로고
    • Reaction of nitric oxide with heme proteins and model compounds of hemoglobin
    • Sharma V.S., Traylor T.G., Gardiner R., and Mizukami H. Reaction of nitric oxide with heme proteins and model compounds of hemoglobin. Biochemistry 26 (1987) 3837-3843
    • (1987) Biochemistry , vol.26 , pp. 3837-3843
    • Sharma, V.S.1    Traylor, T.G.2    Gardiner, R.3    Mizukami, H.4
  • 27
    • 0030036756 scopus 로고    scopus 로고
    • Studies on the reaction mechanism for reductive nitrosylation for ferrihemoproteins in buffer solutions
    • Hoshino M., Maeda M., Konishi R., Seki H., and Ford P.C. Studies on the reaction mechanism for reductive nitrosylation for ferrihemoproteins in buffer solutions. J. Am. Chem. Soc. 118 (1996) 5702-5707
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5702-5707
    • Hoshino, M.1    Maeda, M.2    Konishi, R.3    Seki, H.4    Ford, P.C.5
  • 29
    • 0024970454 scopus 로고
    • Fusion of phospholipid vesicles mediated by cytochrome c
    • Lee S., and Kim H. Fusion of phospholipid vesicles mediated by cytochrome c. Arch. Biochem. Biophys. 271 (1989) 188-199
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 188-199
    • Lee, S.1    Kim, H.2
  • 30
    • 0034911765 scopus 로고    scopus 로고
    • Unraveling the mysteries of phospholipid scrambling
    • Sims P.J., and Wiedmer T. Unraveling the mysteries of phospholipid scrambling. Thromb. Haemostasis 86 (2001) 266-275
    • (2001) Thromb. Haemostasis , vol.86 , pp. 266-275
    • Sims, P.J.1    Wiedmer, T.2
  • 31
    • 0033662871 scopus 로고    scopus 로고
    • Immunologic stimulation of mast cells leads to the reversible exposure of phosphatidylserine in the absence of apoptosis
    • Martin S., Pombo I., Poncet P., David B., Arock M., and Blank U. Immunologic stimulation of mast cells leads to the reversible exposure of phosphatidylserine in the absence of apoptosis. Int. Arch. Allergy Immunol. 123 (2000) 249-258
    • (2000) Int. Arch. Allergy Immunol. , vol.123 , pp. 249-258
    • Martin, S.1    Pombo, I.2    Poncet, P.3    David, B.4    Arock, M.5    Blank, U.6
  • 33
    • 0025045871 scopus 로고
    • Transbilayer distribution and mobility of phosphatidylinositol in human red blood cells
    • Bütikofer P., Lin Z.W., Chiu D.T.-Y., Lubin B., and Kuypers F.A. Transbilayer distribution and mobility of phosphatidylinositol in human red blood cells. J. Biol. Chem. 265 (1990) 16035-16038
    • (1990) J. Biol. Chem. , vol.265 , pp. 16035-16038
    • Bütikofer, P.1    Lin, Z.W.2    Chiu, D.T.-Y.3    Lubin, B.4    Kuypers, F.A.5
  • 34
    • 0142218366 scopus 로고    scopus 로고
    • Regulation of transbilayer plasma membrane phospholipid asymmetry
    • Daleke D.L. Regulation of transbilayer plasma membrane phospholipid asymmetry. J. Lipid Res. 44 (2003) 233-242
    • (2003) J. Lipid Res. , vol.44 , pp. 233-242
    • Daleke, D.L.1
  • 35
    • 0034730723 scopus 로고    scopus 로고
    • The crystal structure of nitrophorin 2. A trifunctional antihemostatic protein from the saliva of Rhodnius prolixus
    • Andersen J.F., and Montfort W.R. The crystal structure of nitrophorin 2. A trifunctional antihemostatic protein from the saliva of Rhodnius prolixus. J. Biol. Chem. 275 (2000) 30496-30503
    • (2000) J. Biol. Chem. , vol.275 , pp. 30496-30503
    • Andersen, J.F.1    Montfort, W.R.2
  • 36
    • 0024289505 scopus 로고
    • Micromolar protein concentrations and metalloprotein stoichiometries obtained by inductively coupled plasma atomic emission spectrometric determination of sulfur
    • Bongers J., Walton C.D., Richardson D.E., and Bell J.U. Micromolar protein concentrations and metalloprotein stoichiometries obtained by inductively coupled plasma atomic emission spectrometric determination of sulfur. Anal. Chem. 60 (1988) 2683-2686
    • (1988) Anal. Chem. , vol.60 , pp. 2683-2686
    • Bongers, J.1    Walton, C.D.2    Richardson, D.E.3    Bell, J.U.4
  • 37
    • 34250177977 scopus 로고    scopus 로고
    • R.E. Berry, T.Kh. Shokhireva, I. Filippov, M.N. Shokhirev, H. Zhang, F. A. Walker, The effect of the N-terminus on heme cavity structure, ligand equilibrium and rate constants and reduction potentials of nitrophorin 2 from Rhodnius prolixus. Biochemistry (2007) accepted for publication.


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