Differential proteomics analysis of the surface heterogeneity of dextran iron oxide nanoparticles and the implications for their in vivo clearance

Biomaterials

Volumn 30, Issue 23-24, 2009, Pages 3926-3933

  Simberg, Dmitri ^a,b   Park, Ji Ho ^c   Karmali, Priya P ^b   Zhang, Wan Ming ^d   Merkulov, Sergei ^d   McCrae, Keith ^d   Bhatia, Sangeeta N ^e   Sailor, Michael ^c   Ruoslahti, Erkki ^b  

^a UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

^b BURNHAM INSTITUTE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^e HARVARD MIT DIVISION OF HEALTH SCIENCES AND TECHNOLOGY   (United States)

Author keywords

Coagulation; Complement; Liver; Macrophage; Nanoparticle; Plasma

Indexed keywords

BIOINERT; BLOOD PROTEIN; COMPLEMENT; DEXTRAN COATING; DIFFERENTIAL PROTEOMICS; HISTIDINE-RICH GLYCOPROTEINS; IN-VIVO; IRON OXIDE NANOPARTICLE; KNOCKOUT MICE; MANNAN-BINDING LECTINS; NANOPARTICLE SURFACE; PLASMA PROTEIN; PROTEIN COATING; RATIONAL DESIGN; SUPERPARAMAGNETIC IRON OXIDES; SURFACE DOMAINS; SURFACE HETEROGENEITIES;

COAGULATION; DEXTRAN; GLUCOSE; IRON ANALYSIS; LIVER; MACROPHAGES; MASS SPECTROMETRY; MOLECULAR BIOLOGY; NANOPARTICLES; PLASMAS; PROTEINS; SUPERPARAMAGNETISM; SURFACE ANALYSIS; TWO DIMENSIONAL;

IRON OXIDES;

BLOOD CLOTTING FACTOR; GLYCOPROTEIN; IRON DEXTRAN; KININOGEN; MANNAN BINDING LECTIN; NANOPARTICLE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; MACROPHAGE; MASS SPECTROMETRY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN BLOOD LEVEL; PROTEOMICS;

ANIMALS; CELLS, CULTURED; IRON; KUPFFER CELLS; MICE; NANOPARTICLES; OXIDES; PLASMA; PROTEIN BINDING; PROTEINS; PROTEOMICS;

MUS;

EID: 67349133162     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2009.03.056     Document Type: Article

References (35)

1. Moghimi S.M., Hunter A.C., and Murray J.C. Long-circulating and target-specific nanoparticles: theory to practice. Pharmacol Rev 53 2 (2001) 283-318
2. Moghimi S.M., and Szebeni J. Stealth liposomes and long circulating nanoparticles: critical issues in pharmacokinetics, opsonization and protein-binding properties. Prog Lipid Res 42 6 (2003) 463-478
3. Chonn A., Semple S.C., and Cullis P.R. Association of blood proteins with large unilamellar liposomes in vivo. Relation to circulation lifetimes. J Biol Chem 267 26 (1992) 18759-18765
4. Yan X., Kuipers F., Havekes L.M., Havinga R., Dontje B., Poelstra K., et al. The role of apolipoprotein E in the elimination of liposomes from blood by hepatocytes in the mouse. Biochem Biophys Res Commun 328 1 (2005) 57-62
5. Weissleder R., Bogdanov Jr. A., Neuwelt E.A., and Papisov M. Long-circulating iron oxides for MR imaging. Adv Drug Deliv Rev 16 (1995) 321-334
6. Park J.H., von Maltzahn G., Zhang L., Derfus A.M., Simberg D., Harris T.J., et al. Systematic surface engineering of magnetic nanoworms for in vivo tumor targeting. Small 5 6 (2009) 694-700
7. Park J.H., von Maltzahn G., Zhang L., Schwartz M.P., Ruoslahti E., Bhatia S., et al. Magnetic iron oxide nanoworms for tumor targeting and imaging. Adv Mater 20 (2008) 1630-1635
8. Bulte J.W., and Kraitchman D.L. Iron oxide MR contrast agents for molecular and cellular imaging. NMR Biomed 17 7 (2004) 484-499
9. Kamps J.A., and Scherphof G.L. Receptor versus non-receptor mediated clearance of liposomes. Adv Drug Deliv Rev 32 1-2 (1998) 81-97
10. Bertholon I., Ponchel G., Labarre D., Couvreur P., and Vauthier C. Bioadhesive properties of poly(alkylcyanoacrylate) nanoparticles coated with polysaccharide. J Nanosci Nanotechnol 6 9-10 (2006) 3102-3109
11. Moore A., Weissleder R., and Bogdanov Jr. A. Uptake of dextran-coated monocrystalline iron oxides in tumor cells and macrophages. J Magn Reson Imaging 7 6 (1997) 1140-1145
12. Raynal I., Prigent P., Peyramaure S., Najid A., Rebuzzi C., and Corot C. Macrophage endocytosis of superparamagnetic iron oxide nanoparticles: mechanisms and comparison of ferumoxides and ferumoxtran-10. Invest Radiol 39 1 (2004) 56-63
13. Timmer J.C., Enoksson M., Wildfang E., Zhu W., Igarashi Y., Denault J.B., et al. Profiling constitutive proteolytic events in vivo. Biochem J 407 1 (2007) 41-48
14. Choi H., Fermin D., and Nesvizhskii A.I. Significance analysis of spectral count data in label-free shotgun proteomics. Mol Cell Proteomics 7 12 (2008) 2373-2385
15. Lepay D.A., Nathan C.F., Steinman R.M., Murray H.W., and Cohn Z.A. Murine Kupffer cells. Mononuclear phagocytes deficient in the generation of reactive oxygen intermediates. J Exp Med 161 5 (1985) 1079-1096
16. Cedervall T., Lynch I., Lindman S., Berggard T., Thulin E., Nilsson H., et al. Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci U S A 104 7 (2007) 2050-2055
17. Vollmer M., Nagele E., and Horth P. Differential proteome analysis: two-dimensional nano-LC/MS of E. coli proteome grown on different carbon sources. J Biomol Technol 14 2 (2003) 128-135
18. Colman R.W., and Schmaier A.H. Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes. Blood 90 10 (1997) 3819-3843
19. Jones A.L., Hulett M.D., and Parish C.R. Histidine-rich glycoprotein: a novel adaptor protein in plasma that modulates the immune, vascular and coagulation systems. Immunol Cell Biol 83 2 (2005) 106-118
20. Bornhorst J.A., and Falke J.J. Purification of proteins using polyhistidine affinity tags. Methods Enzymol 326 (2000) 245-254
21. Jung C.W. Surface properties of superparamagnetic iron oxide MR contrast agents: ferumoxides, ferumoxtran, ferumoxsil. Magn Reson Imaging 13 5 (1995) 675-691
22. Takahashi M., Iwaki D., Kanno K., Ishida Y., Xiong J., Matsushita M., et al. Mannose-binding lectin (MBL)-associated serine protease (MASP)-1 contributes to activation of the lectin complement pathway. J Immunol 180 9 (2008) 6132-6138
23. Van Rooijen N., and Sanders A. Liposome mediated depletion of macrophages: mechanism of action, preparation of liposomes and applications. J Immunol Methods 174 1-2 (1994) 83-93
24. Schousboe I. Beta 2-glycoprotein I: a plasma inhibitor of the contact activation of the intrinsic blood coagulation pathway. Blood 66 5 (1985) 1086-1091
25. Maher V.M., Kitano Y., Neuwirth C., Gallagher J.J., Thompson G.R., and Myant N.B. Effective reduction of plasma LDL levels by LDL apheresis in familial defective apolipoprotein B-100. Atherosclerosis 95 2-3 (1992) 231-234
26. Fujita T., Matsushita M., and Endo Y. The lectin-complement pathway - its role in innate immunity and evolution. Immunol Rev 198 (2004) 185-202
27. Chacko B.K., and Appukuttan P.S. Dextran-binding human plasma antibody recognizes bacterial and yeast antigens and is inhibited by glucose concentrations reached in diabetic sera. Mol Immunol 39 15 (2003) 933-939
28. Furumoto K., Nagayama S., Ogawara K., Takakura Y., Hashida M., Higaki K., et al. Hepatic uptake of negatively charged particles in rats: possible involvement of serum proteins in recognition by scavenger receptor. J Control Release 97 1 (2004) 133-141
29. Nagayama S., Ogawara K., Minato K., Fukuoka Y., Takakura Y., Hashida M., et al. Fetuin mediates hepatic uptake of negatively charged nanoparticles via scavenger receptor. Int J Pharm 329 1-2 (2007) 192-198
30. Rappleye C.A., and Goldman W.E. Fungal stealth technology. Trends Immunol 29 1 (2008) 18-24
31. Kanno S., Furuyama A., and Hirano S. A murine scavenger receptor MARCO recognizes polystyrene nanoparticles. Toxicol Sci 97 2 (2007) 398-406
32. Lemarchand C., Gref R., Passirani C., Garcion E., Petri B., Muller R., et al. Influence of polysaccharide coating on the interactions of nanoparticles with biological systems. Biomaterials 27 1 (2006) 108-118
33. Dobrovolskaia M.A., and McNeil S.E. Immunological properties of engineered nanomaterials. Nat Nanotechnol 2 8 (2007) 469-478
34. Simberg D., Duza T., Park J.H., Essler M., Pilch J., Zhang L., et al. Biomimetic amplification of nanoparticle homing to tumors. Proc Natl Acad Sci U S A 104 3 (2007) 932-936
35. Porkka K., Laakkonen P., Hoffman J.A., Bernasconi M., and Ruoslahti E. A fragment of the HMGN2 protein homes to the nuclei of tumor cells and tumor endothelial cells in vivo. Proc Natl Acad Sci U S A 99 11 (2002) 7444-7449