메뉴 건너뛰기




Volumn 49, Issue 8, 2008, Pages 1345-1352

99mTc-labeled duramycin as a novel phosphatidylethanolamine- binding molecular probe

Author keywords

imaging; 99mTc; Cardiology; Duramycin; Molecular imaging; Radiopharmaceuticals

Indexed keywords

DURAMYCIN; DURAMYCIN TC 99M; HYDRAZONE DERIVATIVE; LIPOSOME; PHOSPHATIDYLETHANOLAMINE; PHOSPHINE; PHOSPHOLIPID; RADIOPHARMACEUTICAL AGENT; SUCCINIMIDYL 6 HYDRAZINONICOTINATE ACETONE HYDRAZONE; TECHNETIUM 99M; TRACER; UNCLASSIFIED DRUG; BACTERIOCIN; ORGANOMETALLIC COMPOUND; PEPTIDE; TECHNETIUM;

EID: 48749103305     PISSN: 01615505     EISSN: None     Source Type: Journal    
DOI: 10.2967/jnumed.107.048603     Document Type: Article
Times cited : (114)

References (43)
  • 2
    • 0022181816 scopus 로고
    • Membrane lipid composition and cellular function
    • Spector AA, Yorek MA. Membrane lipid composition and cellular function. J Lipid Res. 1985;26:1015-1035.
    • (1985) J Lipid Res , vol.26 , pp. 1015-1035
    • Spector, A.A.1    Yorek, M.A.2
  • 3
    • 0032779519 scopus 로고    scopus 로고
    • Lipid translocation across the plasma membrane of mammalian cells
    • Bevers EM, Comfurius P, Dekkers DW, et al. Lipid translocation across the plasma membrane of mammalian cells. Biochim Biophys Acta. 1999;1439:317-330.
    • (1999) Biochim Biophys Acta , vol.1439 , pp. 317-330
    • Bevers, E.M.1    Comfurius, P.2    Dekkers, D.W.3
  • 4
    • 0031149132 scopus 로고    scopus 로고
    • Exposure of phosphatidylethanolamine on the surface of apoptotic cells
    • Emoto K, Toyama-Sorimachi N, Karasuyama H, et al. Exposure of phosphatidylethanolamine on the surface of apoptotic cells. Exp Cell Res. 1997;232:430-434.
    • (1997) Exp Cell Res , vol.232 , pp. 430-434
    • Emoto, K.1    Toyama-Sorimachi, N.2    Karasuyama, H.3
  • 5
    • 0032861193 scopus 로고    scopus 로고
    • Membrane phospholipid dynamics during cytokinesis: Regulation of actin filament assembly by redistribution of membrane surface phospholipid
    • Umeda M, Emoto K. Membrane phospholipid dynamics during cytokinesis: regulation of actin filament assembly by redistribution of membrane surface phospholipid. Chem Phys Lipids. 1999;101:81-91.
    • (1999) Chem Phys Lipids , vol.101 , pp. 81-91
    • Umeda, M.1    Emoto, K.2
  • 6
    • 0032498625 scopus 로고    scopus 로고
    • Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation
    • Mills JC, Stone NL, Erhardt J, et al. Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation. J Cell Biol. 1998;140:627-636.
    • (1998) J Cell Biol , vol.140 , pp. 627-636
    • Mills, J.C.1    Stone, N.L.2    Erhardt, J.3
  • 7
    • 0025151336 scopus 로고
    • The structure of PA48009: The revised structure of duramycin
    • Hayashi F, Nagashima K, Terui Y, et al. The structure of PA48009: the revised structure of duramycin. J Antibiot (Tokyo). 1990;43:1421-1430.
    • (1990) J Antibiot (Tokyo) , vol.43 , pp. 1421-1430
    • Hayashi, F.1    Nagashima, K.2    Terui, Y.3
  • 8
    • 0027248383 scopus 로고
    • Solution structures of the lantibiotics duramycin B and C
    • Zimmermann N, Freund S, Fredenhagen A, et al. Solution structures of the lantibiotics duramycin B and C. Eur J Biochem. 1993;216:419-428.
    • (1993) Eur J Biochem , vol.216 , pp. 419-428
    • Zimmermann, N.1    Freund, S.2    Fredenhagen, A.3
  • 9
    • 0026091089 scopus 로고
    • Mode of action of the lanthionine-containing peptide antibiotics duramycin, duramycin B and C, and cinnamycin as indirect inhibitors of phospholipase A2
    • Marki F, Hanni E, Fredenhagen A, et al. Mode of action of the lanthionine-containing peptide antibiotics duramycin, duramycin B and C, and cinnamycin as indirect inhibitors of phospholipase A2. Biochem Pharmacol. 1991;42:2027-2035.
    • (1991) Biochem Pharmacol , vol.42 , pp. 2027-2035
    • Marki, F.1    Hanni, E.2    Fredenhagen, A.3
  • 10
    • 34548637974 scopus 로고    scopus 로고
    • Curvature-dependent recognition of ethanolamine phospholipids by duramycin and cinnamycin
    • Iwamoto K, Hayakawa T, Murate M, et al. Curvature-dependent recognition of ethanolamine phospholipids by duramycin and cinnamycin. Biophys J. 2007;93:1608-1619.
    • (2007) Biophys J , vol.93 , pp. 1608-1619
    • Iwamoto, K.1    Hayakawa, T.2    Murate, M.3
  • 11
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • Seelig J. Thermodynamics of lipid-peptide interactions. Biochim Biophys Acta. 2004;1666:40-50.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 40-50
    • Seelig, J.1
  • 12
    • 0028101276 scopus 로고
    • A novel peptide probe for studying the transbilayer movement of phosphatidylethanolamine
    • Aoki Y, Uenaka T, Aoki J, et al. A novel peptide probe for studying the transbilayer movement of phosphatidylethanolamine. J Biochem (Tokyo). 1994;116:291-297.
    • (1994) J Biochem (Tokyo) , vol.116 , pp. 291-297
    • Aoki, Y.1    Uenaka, T.2    Aoki, J.3
  • 13
    • 0037065703 scopus 로고    scopus 로고
    • Specific binding of Ro 09-0198 (cinnamycin) to phosphatidylethanolamine: A thermodynamic analysis
    • Machaidze G, Ziegler A, Seelig J. Specific binding of Ro 09-0198 (cinnamycin) to phosphatidylethanolamine: a thermodynamic analysis. Biochemistry. 2002;41:1965-1971.
    • (2002) Biochemistry , vol.41 , pp. 1965-1971
    • Machaidze, G.1    Ziegler, A.2    Seelig, J.3
  • 14
    • 0033851437 scopus 로고    scopus 로고
    • Posttranslationally modified bacteriocins: The lantibiotics
    • Guder A, Wiedemann I, Sahl HG. Posttranslationally modified bacteriocins: the lantibiotics. Biopolymers. 2000;55:62-73.
    • (2000) Biopolymers , vol.55 , pp. 62-73
    • Guder, A.1    Wiedemann, I.2    Sahl, H.G.3
  • 16
    • 0025831674 scopus 로고
    • Prepeptide sequence of cinnamycin (Ro 09-0198): The first structural gene of a duramycin-type lantibiotic
    • Kaletta C, Entian KD, Jung G. Prepeptide sequence of cinnamycin (Ro 09-0198): the first structural gene of a duramycin-type lantibiotic. Eur J Biochem. 1991;199:411-415.
    • (1991) Eur J Biochem , vol.199 , pp. 411-415
    • Kaletta, C.1    Entian, K.D.2    Jung, G.3
  • 20
    • 0027432708 scopus 로고
    • Technetium-99m-labeled hydrazino nicotinamide derivatized chemotactic peptide analogs for imaging focal sites of bacterial infection
    • Babich JW, Solomon H, Pike MC, et al. Technetium-99m-labeled hydrazino nicotinamide derivatized chemotactic peptide analogs for imaging focal sites of bacterial infection. J Nucl Med. 1993;34:1964-1974.
    • (1993) J Nucl Med , vol.34 , pp. 1964-1974
    • Babich, J.W.1    Solomon, H.2    Pike, M.C.3
  • 21
    • 0028815077 scopus 로고
    • 99mTc-labeled hydrazino nicotinic acid derivatized chemotactic peptides
    • 99mTc-labeled hydrazino nicotinic acid derivatized chemotactic peptides. Nucl Med Biol. 1995;22:25-30.
    • (1995) Nucl Med Biol , vol.22 , pp. 25-30
    • Babich, J.W.1    Fischman, A.J.2
  • 23
    • 0037453585 scopus 로고    scopus 로고
    • Myocytes die by multiple mechanisms in failing human hearts
    • Kostin S, Pool L, Elsasser A, et al. Myocytes die by multiple mechanisms in failing human hearts. Circ Res. 2003;92:715-724.
    • (2003) Circ Res , vol.92 , pp. 715-724
    • Kostin, S.1    Pool, L.2    Elsasser, A.3
  • 24
    • 0031945404 scopus 로고    scopus 로고
    • Cardiomyocyte apoptosis in acute and chronic conditions
    • Freude B, Masters TN, Kostin S, et al. Cardiomyocyte apoptosis in acute and chronic conditions. Basic Res Cardiol. 1998;93:85-89.
    • (1998) Basic Res Cardiol , vol.93 , pp. 85-89
    • Freude, B.1    Masters, T.N.2    Kostin, S.3
  • 25
    • 0030454154 scopus 로고    scopus 로고
    • Myocardial Gd-DTPA kinetics determine MRI contrast enhancement and reflect the extent and severity of myocardial injury after acute reperfused infarction
    • Kim RJ, Chen EL, Lima JAC, et al. Myocardial Gd-DTPA kinetics determine MRI contrast enhancement and reflect the extent and severity of myocardial injury after acute reperfused infarction. Circulation. 1996;94:3318-3326.
    • (1996) Circulation , vol.94 , pp. 3318-3326
    • Kim, R.J.1    Chen, E.L.2    Lima, J.A.C.3
  • 26
    • 33745925575 scopus 로고    scopus 로고
    • Assessment of reperfused myocardial infarction in the hyper-acute phase with delayed enhancement magnetic resonance imaging
    • Zhu X, Zhang R, Campagna NF, et al. Assessment of reperfused myocardial infarction in the hyper-acute phase with delayed enhancement magnetic resonance imaging. J Cardiovasc Magn Reson. 2006;8:461-467.
    • (2006) J Cardiovasc Magn Reson , vol.8 , pp. 461-467
    • Zhu, X.1    Zhang, R.2    Campagna, N.F.3
  • 27
    • 33749049365 scopus 로고    scopus 로고
    • 99mTc-labeled C2A domain of synaptotagmin I as a target-specific molecular probe for noninvasive imaging of acute myocardial infarction
    • 99mTc-labeled C2A domain of synaptotagmin I as a target-specific molecular probe for noninvasive imaging of acute myocardial infarction. J Nucl Med. 2006;47:1367-1374.
    • (2006) J Nucl Med , vol.47 , pp. 1367-1374
    • Zhao, M.1    Zhu, X.2    Ji, S.3
  • 28
    • 34250304240 scopus 로고    scopus 로고
    • 99mTc-labeled C2A in the area at risk after myocardial ischemia and reperfusion
    • 99mTc-labeled C2A in the area at risk after myocardial ischemia and reperfusion. J Nucl Med. 2007;48:1031-1036.
    • (2007) J Nucl Med , vol.48 , pp. 1031-1036
    • Zhu, X.1    Li, Z.2    Zhao, M.3
  • 29
    • 35848938700 scopus 로고    scopus 로고
    • 99mTc-labeled C2A domain of synaptotagmin I in a rat model of ischemia and reperfusion
    • 99mTc-labeled C2A domain of synaptotagmin I in a rat model of ischemia and reperfusion. Nucl Med Biol. 2007;34:907-915.
    • (2007) Nucl Med Biol , vol.34 , pp. 907-915
    • Liu, Z.1    Zhao, M.2    Zhu, X.3
  • 30
    • 35848944663 scopus 로고    scopus 로고
    • 99mTc-C2A-GST distribution in the area at risk after myocardial ischemia and reperfusion using a compartmental model
    • 99mTc-C2A-GST distribution in the area at risk after myocardial ischemia and reperfusion using a compartmental model. Nucl Med Biol. 2007;34:897-905.
    • (2007) Nucl Med Biol , vol.34 , pp. 897-905
    • Audi, S.1    Poellmann, M.2    Zhu, X.3
  • 31
    • 0035173736 scopus 로고    scopus 로고
    • Non-invasive detection of apoptosis using magnetic resonance imaging and a targeted contrast agent
    • Zhao M, Beauregard DA, Loizou L, et al. Non-invasive detection of apoptosis using magnetic resonance imaging and a targeted contrast agent. Nat Med. 2001;7:1241-1244.
    • (2001) Nat Med , vol.7 , pp. 1241-1244
    • Zhao, M.1    Beauregard, D.A.2    Loizou, L.3
  • 32
    • 35848929261 scopus 로고    scopus 로고
    • 99mTc-labeled C2A domain of synaptotagmin I in a porcine-ischemia reperfusion model
    • 99mTc-labeled C2A domain of synaptotagmin I in a porcine-ischemia reperfusion model. Nucl Med Biol. 2007;34:917-923.
    • (2007) Nucl Med Biol , vol.34 , pp. 917-923
    • Fang, W.1    Wang, F.2    Ji, S.3
  • 33
    • 4644246936 scopus 로고    scopus 로고
    • Detection of apoptosis using the C2A domain of synaptotagmin I
    • Jung HI, Kettunen MI, Davletov B, et al. Detection of apoptosis using the C2A domain of synaptotagmin I. Bioconjug Chem. 2004;15:983-987.
    • (2004) Bioconjug Chem , vol.15 , pp. 983-987
    • Jung, H.I.1    Kettunen, M.I.2    Davletov, B.3
  • 34
    • 40949121437 scopus 로고    scopus 로고
    • Detection of cell death in tumors by using MR imaging and a gadolinium-based targeted contrast agent
    • Krishnan AS, Neves AA, de Backer MM, et al. Detection of cell death in tumors by using MR imaging and a gadolinium-based targeted contrast agent. Radiology. 2008;246:854-862.
    • (2008) Radiology , vol.246 , pp. 854-862
    • Krishnan, A.S.1    Neves, A.A.2    de Backer, M.M.3
  • 36
    • 0034661803 scopus 로고    scopus 로고
    • Visualisation of cell death in vivo in patients with acute myocardial infarction
    • Hofstra L, Liem IH, Dumont EA, et al. Visualisation of cell death in vivo in patients with acute myocardial infarction. Lancet. 2000;356:209-212.
    • (2000) Lancet , vol.356 , pp. 209-212
    • Hofstra, L.1    Liem, I.H.2    Dumont, E.A.3
  • 37
    • 13144305073 scopus 로고    scopus 로고
    • In vivo detection and imaging of phosphatidylserine expression during programmed cell death
    • Blankenberg FG, Katsikis PD, Tait JF, et al. In vivo detection and imaging of phosphatidylserine expression during programmed cell death. Proc Natl Acad Sci USA. 1998;95:6349-6354.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6349-6354
    • Blankenberg, F.G.1    Katsikis, P.D.2    Tait, J.F.3
  • 38
    • 0003074186 scopus 로고    scopus 로고
    • Technetium-99m HYNIC-annexin V: A potential radiopharmaceutical for the in-vivo detection of apoptosis
    • Ohtsuki K, Akashi K, Aoka Y, et al. Technetium-99m HYNIC-annexin V: a potential radiopharmaceutical for the in-vivo detection of apoptosis. Eur J Nucl Med. 1999;26:1251-1258.
    • (1999) Eur J Nucl Med , vol.26 , pp. 1251-1258
    • Ohtsuki, K.1    Akashi, K.2    Aoka, Y.3
  • 39
    • 0037447317 scopus 로고    scopus 로고
    • Near-infrared fluorescent imaging of tumor apoptosis
    • Petrovsky A, Schellenberger E, Josephson L, et al. Near-infrared fluorescent imaging of tumor apoptosis. Cancer Res. 2003;63:1936-1942.
    • (2003) Cancer Res , vol.63 , pp. 1936-1942
    • Petrovsky, A.1    Schellenberger, E.2    Josephson, L.3
  • 40
    • 2942657046 scopus 로고    scopus 로고
    • Apoptosis-detecting radioligands: Current state of the art and future perspectives
    • Lahorte CMM, VanderHeyden JL, Steinmetz N, et al. Apoptosis-detecting radioligands: current state of the art and future perspectives. Eur J Nucl Med Mol Imaging. 2004;31:887-919.
    • (2004) Eur J Nucl Med Mol Imaging , vol.31 , pp. 887-919
    • Lahorte, C.M.M.1    VanderHeyden, J.L.2    Steinmetz, N.3
  • 41
    • 24144479486 scopus 로고    scopus 로고
    • Magnetic resonance imaging of cardiomyocyte apoptosis with a novel magneto-optical nanoparticle
    • Sosnovik DE, Schellenberger EA, Nahrendorf M, et al. Magnetic resonance imaging of cardiomyocyte apoptosis with a novel magneto-optical nanoparticle. Magn Reson Med. 2005;54:718-724.
    • (2005) Magn Reson Med , vol.54 , pp. 718-724
    • Sosnovik, D.E.1    Schellenberger, E.A.2    Nahrendorf, M.3
  • 42
    • 0025000276 scopus 로고
    • The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes
    • Huber R, Romisch J, Paques EP. The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J. 1990;9:3867-3874.
    • (1990) EMBO J , vol.9 , pp. 3867-3874
    • Huber, R.1    Romisch, J.2    Paques, E.P.3
  • 43
    • 0028986240 scopus 로고
    • Structure of the first C2 domain of synaptotagmin I: A novel Ca2+/phospholipid-binding fold
    • Sutton RB, Davletov BA, Berghuis AM, Sudhof TC, Sprang SR. Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold. Cell. 1995;80:929-938.
    • (1995) Cell , vol.80 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3    Sudhof, T.C.4    Sprang, S.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.