메뉴 건너뛰기




Volumn 1830, Issue 3, 2013, Pages 2562-2573

Site-specifically 11C-labeled Sel-tagged annexin A5 and a size-matched control for dynamic in vivo PET imaging of protein distribution in tissues prior to and after induced cell death

Author keywords

Annexin A5; Carbon 11; Cell death; Molecular imaging; Positron emission tomography; Sel tag

Indexed keywords

CALCIUM; CARBON 11; CYSTEINE; GLYCINE; LIPOCORTIN 5; RECOMBINANT PROTEIN; TETRAPEPTIDE; CARBON; RADIOPHARMACEUTICAL AGENT;

EID: 84872826265     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2012.12.007     Document Type: Article
Times cited : (9)

References (59)
  • 1
    • 32944479631 scopus 로고    scopus 로고
    • Molecular imaging in the development of cancer therapeutics
    • J. Czernin, W.A. Weber, and H.R. Herschman Molecular imaging in the development of cancer therapeutics Annu. Rev. Med. 57 2006 99 118
    • (2006) Annu. Rev. Med. , vol.57 , pp. 99-118
    • Czernin, J.1    Weber, W.A.2    Herschman, H.R.3
  • 3
    • 78650394438 scopus 로고    scopus 로고
    • Molecular tracers for the PET and SPECT imaging of disease
    • S.L. Pimlott, and A. Sutherland Molecular tracers for the PET and SPECT imaging of disease Chem. Soc. Rev. 40 2011 149 162
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 149-162
    • Pimlott, S.L.1    Sutherland, A.2
  • 4
    • 78651298105 scopus 로고    scopus 로고
    • Beyond FDG: Many molecular imaging agents are in development
    • V. Brower Beyond FDG: many molecular imaging agents are in development J. Natl. Cancer Inst. 103 2011 13 15
    • (2011) J. Natl. Cancer Inst. , vol.103 , pp. 13-15
    • Brower, V.1
  • 5
    • 33645523763 scopus 로고    scopus 로고
    • Optimizing the affinity and specificity of proteins with molecular display
    • A.M. Levin, and G.A. Weiss Optimizing the affinity and specificity of proteins with molecular display Mol. Biosyst. 2 2006 49 57
    • (2006) Mol. Biosyst. , vol.2 , pp. 49-57
    • Levin, A.M.1    Weiss, G.A.2
  • 6
    • 33749328523 scopus 로고    scopus 로고
    • In vitro display technologies reveal novel biopharmaceutics
    • A. Rothe, R.J. Hosse, and B.E. Power In vitro display technologies reveal novel biopharmaceutics FASEB J. 20 2006 1599 1610
    • (2006) FASEB J. , vol.20 , pp. 1599-1610
    • Rothe, A.1    Hosse, R.J.2    Power, B.E.3
  • 7
    • 0032981989 scopus 로고    scopus 로고
    • Polypeptides from phage display. A superior source of in vivo imaging agents
    • R.C. Ladner Polypeptides from phage display. A superior source of in vivo imaging agents Q. J. Nucl. Med. 43 1999 119 124
    • (1999) Q. J. Nucl. Med. , vol.43 , pp. 119-124
    • Ladner, R.C.1
  • 8
    • 72949106918 scopus 로고    scopus 로고
    • Pharmacokinetics of biotech drugs: Peptides, proteins and monoclonal antibodies
    • J.H. Lin Pharmacokinetics of biotech drugs: peptides, proteins and monoclonal antibodies Curr. Drug Metab. 10 2009 661 691
    • (2009) Curr. Drug Metab. , vol.10 , pp. 661-691
    • Lin, J.H.1
  • 9
    • 27144550160 scopus 로고    scopus 로고
    • Arming antibodies: Prospects and challenges for immunoconjugates
    • A.M. Wu, and P.D. Senter Arming antibodies: prospects and challenges for immunoconjugates Nat. Biotechnol. 23 2005 1137 1146
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1137-1146
    • Wu, A.M.1    Senter, P.D.2
  • 11
  • 12
    • 0030696927 scopus 로고    scopus 로고
    • Alternative positron emission tomography with non-conventional positron emitters: Effects of their physical properties on image quality and potential clinical applications
    • M. Pagani, S. Stone-Elander, and S.A. Larsson Alternative positron emission tomography with non-conventional positron emitters: effects of their physical properties on image quality and potential clinical applications Eur. J. Nucl. Med. 24 1997 1301 1327
    • (1997) Eur. J. Nucl. Med. , vol.24 , pp. 1301-1327
    • Pagani, M.1    Stone-Elander, S.2    Larsson, S.A.3
  • 15
    • 77950457807 scopus 로고    scopus 로고
    • Radiolabelled proteins for positron emission tomography: Pros and cons of labelling methods
    • V. Tolmachev, and S. Stone-Elander Radiolabelled proteins for positron emission tomography: pros and cons of labelling methods Biochim. Biophys. Acta 1800 2010 487 510
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 487-510
    • Tolmachev, V.1    Stone-Elander, S.2
  • 16
    • 33845381207 scopus 로고    scopus 로고
    • Selenolthiol and dithiol C-terminal tetrapeptide motifs for one-step purification and labeling of recombinant proteins produced in E. coli
    • Q. Cheng, L. Johansson, J.-O. Thorell, A. Fredriksson, E. Samén, S. Stone-Elander, and E.S.J. Arnér Selenolthiol and dithiol C-terminal tetrapeptide motifs for one-step purification and labeling of recombinant proteins produced in E. coli Chembiochem 7 2006 1976 1981
    • (2006) Chembiochem , vol.7 , pp. 1976-1981
    • Cheng, Q.1    Johansson, L.2    Thorell, J.-O.3    Fredriksson, A.4    Samén, E.5    Stone-Elander, S.6    Arnér, E.S.J.7
  • 17
    • 33845405875 scopus 로고    scopus 로고
    • Tagging recombinant proteins with a Sel-tag for purification, labeling with electrophilic compounds or radiolabeling with carbon-11
    • Q. Cheng, S. Stone-Elander, and E.S.J. Arnér Tagging recombinant proteins with a Sel-tag for purification, labeling with electrophilic compounds or radiolabeling with carbon-11 Nat. Protoc. 1 2006 604 613
    • (2006) Nat. Protoc. , vol.1 , pp. 604-613
    • Cheng, Q.1    Stone-Elander, S.2    Arnér, E.S.J.3
  • 20
    • 46749092088 scopus 로고    scopus 로고
    • In vivo detection of apoptosis
    • F.G. Blankenberg In vivo detection of apoptosis J. Nucl. Med. 49 Suppl. 2 2008 81S 95S
    • (2008) J. Nucl. Med. , vol.49 , Issue.SUPPL. 2
    • Blankenberg, F.G.1
  • 24
    • 0036719790 scopus 로고    scopus 로고
    • To scan or not to scan, it is a question of timing: Technetium-99m- annexin v radionuclide imaging assessment of treatment efficacy after one course of chemotherapy
    • F. Blankenberg To scan or not to scan, it is a question of timing: technetium-99m-annexin V radionuclide imaging assessment of treatment efficacy after one course of chemotherapy Clin. Cancer Res. 8 2002 2757 2758
    • (2002) Clin. Cancer Res. , vol.8 , pp. 2757-2758
    • Blankenberg, F.1
  • 25
    • 1342322800 scopus 로고    scopus 로고
    • The imaging of apoptosis with the radiolabeled annexin V: Optimal timing for clinical feasibility
    • T. Belhocine, N. Steinmetz, C. Li, A. Green, and F.G. Blankenberg The imaging of apoptosis with the radiolabeled annexin V: optimal timing for clinical feasibility Technol. Cancer Res. Treat. 3 2004 23 32
    • (2004) Technol. Cancer Res. Treat. , vol.3 , pp. 23-32
    • Belhocine, T.1    Steinmetz, N.2    Li, C.3    Green, A.4    Blankenberg, F.G.5
  • 26
    • 0034000453 scopus 로고    scopus 로고
    • Tumor vascular permeability and the EPR effect in macromolecular therapeutics: A review
    • H. Maeda, J. Wu, T. Sawa, Y. Matsumura, and K. Hori Tumor vascular permeability and the EPR effect in macromolecular therapeutics: a review J. Control. Release 65 2000 271 284
    • (2000) J. Control. Release , vol.65 , pp. 271-284
    • Maeda, H.1    Wu, J.2    Sawa, T.3    Matsumura, Y.4    Hori, K.5
  • 27
    • 78650910950 scopus 로고    scopus 로고
    • Drug targeting strategies in cancer treatment: An overview
    • J.L. Arias Drug targeting strategies in cancer treatment: an overview Mini. Rev. Med. Chem. 11 2011 1 17
    • (2011) Mini. Rev. Med. Chem. , vol.11 , pp. 1-17
    • Arias, J.L.1
  • 28
    • 57749207052 scopus 로고    scopus 로고
    • Intravascular delivery of particulate systems: Does geometry really matter?
    • P. Decuzzi, R. Pasqualini, W. Arap, and M. Ferrari Intravascular delivery of particulate systems: does geometry really matter? Pharm. Res. 26 2009 235 243
    • (2009) Pharm. Res. , vol.26 , pp. 235-243
    • Decuzzi, P.1    Pasqualini, R.2    Arap, W.3    Ferrari, M.4
  • 29
    • 70350234894 scopus 로고    scopus 로고
    • A modeling analysis of the effects of molecular size and binding affinity on tumor targeting
    • M.M. Schmidt, and K.D. Wittrup A modeling analysis of the effects of molecular size and binding affinity on tumor targeting Mol. Cancer Ther. 8 2009 2861 2871
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 2861-2871
    • Schmidt, M.M.1    Wittrup, K.D.2
  • 30
    • 0025000276 scopus 로고
    • The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes
    • R. Huber, J. Romisch, and E.P. Paques The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes EMBO J. 9 1990 3867 3874
    • (1990) EMBO J. , vol.9 , pp. 3867-3874
    • Huber, R.1    Romisch, J.2    Paques, E.P.3
  • 33
    • 0033536575 scopus 로고    scopus 로고
    • High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes
    • E.S.J. Arnér, H. Sarioglu, F. Lottspeich, A. Holmgren, and A. Böck High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes J. Mol. Biol. 292 1999 1003 1016
    • (1999) J. Mol. Biol. , vol.292 , pp. 1003-1016
    • Arnér, E.S.J.1    Sarioglu, H.2    Lottspeich, F.3    Holmgren, A.4    Böck, A.5
  • 34
    • 4644224905 scopus 로고    scopus 로고
    • Assessment of production conditions for efficient use of Escherichia coli in high-yield heterologous recombinant selenoprotein synthesis
    • O. Rengby, L. Johansson, L.A. Carlson, E. Serini, A. Vlamis-Gardikas, P. Kårsnäs, and E.S.J. Arnér Assessment of production conditions for efficient use of Escherichia coli in high-yield heterologous recombinant selenoprotein synthesis Appl. Environ. Microbiol. 70 2004 5159 5167
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 5159-5167
    • Rengby, O.1    Johansson, L.2    Carlson, L.A.3    Serini, E.4    Vlamis-Gardikas, A.5    Kårsnäs, P.6    Arnér, E.S.J.7
  • 35
    • 33645409827 scopus 로고    scopus 로고
    • Single step protocol to purify recombinant proteins with low endotoxin contents
    • P. Reichelt, C. Schwarz, and M. Donzeau Single step protocol to purify recombinant proteins with low endotoxin contents Protein Expr. Purif. 46 2006 483 488
    • (2006) Protein Expr. Purif. , vol.46 , pp. 483-488
    • Reichelt, P.1    Schwarz, C.2    Donzeau, M.3
  • 36
    • 0026786146 scopus 로고
    • Enzymatic inverse PCR: A restriction site independent, single-fragment method for high-efficiency, site-directed mutagenesis
    • W.P. Stemmer, and S.K. Morris Enzymatic inverse PCR: a restriction site independent, single-fragment method for high-efficiency, site-directed mutagenesis Biotechniques 13 1992 214 220
    • (1992) Biotechniques , vol.13 , pp. 214-220
    • Stemmer, W.P.1    Morris, S.K.2
  • 39
    • 2342586664 scopus 로고    scopus 로고
    • Measurement of the affinity and cooperativity of annexin V-membrane binding under conditions of low membrane occupancy
    • J.F. Tait, D.F. Gibson, and C. Smith Measurement of the affinity and cooperativity of annexin V-membrane binding under conditions of low membrane occupancy Anal. Biochem. 329 2004 112 119
    • (2004) Anal. Biochem. , vol.329 , pp. 112-119
    • Tait, J.F.1    Gibson, D.F.2    Smith, C.3
  • 40
    • 79551616503 scopus 로고    scopus 로고
    • The use of alternative forms of graphical analysis to balance bias and precision in PET images
    • J. Logan, D. Alexoff, and J.S. Fowler The use of alternative forms of graphical analysis to balance bias and precision in PET images J. Cereb. Blood Flow Metab. 31 2011 535 546
    • (2011) J. Cereb. Blood Flow Metab. , vol.31 , pp. 535-546
    • Logan, J.1    Alexoff, D.2    Fowler, J.S.3
  • 41
    • 0031279782 scopus 로고    scopus 로고
    • Parametric imaging of ligand-receptor binding in PET using a simplified reference region model
    • R.N. Gunn, A.A. Lammertsma, S.P. Hume, and V.J. Cunningham Parametric imaging of ligand-receptor binding in PET using a simplified reference region model NeuroImage 6 1997 279 287
    • (1997) NeuroImage , vol.6 , pp. 279-287
    • Gunn, R.N.1    Lammertsma, A.A.2    Hume, S.P.3    Cunningham, V.J.4
  • 42
    • 0021364348 scopus 로고
    • A quantitative model for the in vivo assessment of drug binding sites with positron emission tomography
    • M.A. Mintun, M.E. Raichle, M.R. Kilbourn, G.F. Wooten, and M.J. Welch A quantitative model for the in vivo assessment of drug binding sites with positron emission tomography Ann. Neurol. 15 1984 217 227
    • (1984) Ann. Neurol. , vol.15 , pp. 217-227
    • Mintun, M.A.1    Raichle, M.E.2    Kilbourn, M.R.3    Wooten, G.F.4    Welch, M.J.5
  • 44
    • 20644432008 scopus 로고    scopus 로고
    • Structural requirements for in vivo detection of cell death wtih 99mTc-Annexin v
    • J.F. Tait, C. Smith, and F.G. Blankenberg Structural requirements for in vivo detection of cell death wtih 99mTc-Annexin V J. Nucl. Med. 46 2005 807 815
    • (2005) J. Nucl. Med. , vol.46 , pp. 807-815
    • Tait, J.F.1    Smith, C.2    Blankenberg, F.G.3
  • 45
  • 48
    • 20544460429 scopus 로고    scopus 로고
    • 99mTc-annexin A5 uptake and imaging to monitor chemosensitivity
    • 99mTc-annexin A5 uptake and imaging to monitor chemosensitivity Methods Mol. Med. 111 2005 363 380
    • (2005) Methods Mol. Med. , vol.111 , pp. 363-380
    • Belhocine, T.Z.1    Blankenberg, F.G.2
  • 54
    • 0019450585 scopus 로고
    • Receptor for albumin on the liver cell surface may mediate uptake of fatty acids and other albumin-bound substances
    • R. Weisiger, J. Gollan, and R. Ockner Receptor for albumin on the liver cell surface may mediate uptake of fatty acids and other albumin-bound substances Science 211 1981 1048 1051
    • (1981) Science , vol.211 , pp. 1048-1051
    • Weisiger, R.1    Gollan, J.2    Ockner, R.3
  • 59
    • 63649115838 scopus 로고    scopus 로고
    • Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1
    • Q. Cheng, T. Sandalova, Y. Lindqvist, and E.S.J. Arnér Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1 J. Biol. Chem. 284 2009 3998 4008
    • (2009) J. Biol. Chem. , vol.284 , pp. 3998-4008
    • Cheng, Q.1    Sandalova, T.2    Lindqvist, Y.3    Arnér, E.S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.