메뉴 건너뛰기




Volumn 16, Issue 1, 2017, Pages 238-246

Surface Glycoproteins of Exosomes Shed by Myeloid-Derived Suppressor Cells Contribute to Function

Author keywords

cell surface capture; exosomes; myeloid derived suppressor cells; N glycoproteome

Indexed keywords

BETA1 INTEGRIN; CD11B ANTIGEN; CD157 ANTIGEN; CD172A ANTIGEN; CD177 ANTIGEN; CD18 ANTIGEN; CD39 ANTIGEN; CD4 ANTIGEN; CD47 ANTIGEN; CD82 ANTIGEN; CD97 ANTIGEN; CELL SURFACE PROTEIN; ENDOTHELIAL LIPASE; FIBRINOGEN RECEPTOR; FIBRONECTIN; GALECTIN 3; HERMES ANTIGEN; INTERLEUKIN 1BETA; JUNCTIONAL ADHESION MOLECULE A; KERATIN TYPE II CYTOSKELETAL 1B; MAST CELL EXPRESSED MEMBRANE PROTEIN 1; MEMBRANE PROTEIN; MYELOPEROXIDASE; OLFACTOMEDIN 4; PEPTIDES AND PROTEINS; REGULATOR PROTEIN; SIGNAL REGULATORY PROTEIN ALPHA; T LYMPHOCYTE RECEPTOR; THROMBOSPONDIN 1; TRANSMEMBRANE 9 SUPERFAMILY MEMBER 3; UNCLASSIFIED DRUG; CD47 PROTEIN, MOUSE; IMMUNOGLOBULIN RECEPTOR; PROTEOME; PTPNS1 PROTEIN, MOUSE; THROMBOSPONDIN-1, MOUSE;

EID: 85009877249     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/acs.jproteome.6b00811     Document Type: Article
Times cited : (57)

References (61)
  • 2
    • 84879711611 scopus 로고    scopus 로고
    • Perspectives on anti-CD47 antibody treatment for experimental cancer
    • Unanue, E. R. Perspectives on anti-CD47 antibody treatment for experimental cancer Proc. Natl. Acad. Sci. U. S. A. 2013, 110, 10886-10887 10.1073/pnas.1308463110
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 10886-10887
    • Unanue, E.R.1
  • 3
    • 84902097212 scopus 로고    scopus 로고
    • Protein-Centric N-Glycoproteomics Analysis of Membrane and Plasma Membrane Proteins
    • Sun, B.; Hood, L. Protein-Centric N-Glycoproteomics Analysis of Membrane and Plasma Membrane Proteins J. Proteomics Res. 2014, 13, 2705-2714 10.1021/pr500187g
    • (2014) J. Proteomics Res. , vol.13 , pp. 2705-2714
    • Sun, B.1    Hood, L.2
  • 5
    • 77956404647 scopus 로고    scopus 로고
    • Exosomes: Extracellular organelles important in intercellular communication
    • Mathivanan, S.; Ji, H.; Simpson, R. J. Exosomes: Extracellular organelles important in intercellular communication J. Proteomics 2010, 73, 1907-1920 10.1016/j.jprot.2010.06.006
    • (2010) J. Proteomics , vol.73 , pp. 1907-1920
    • Mathivanan, S.1    Ji, H.2    Simpson, R.J.3
  • 6
    • 84959386845 scopus 로고    scopus 로고
    • Proteomic comparison defines novel markers to characterize heterogeneous populations of extracellular vesicle subtypes
    • Kowal, J.; Arras, G.; Colombo, M.; Jouve, M.; Morath, J. P.; Primdal-bengtson, B. et al. Proteomic comparison defines novel markers to characterize heterogeneous populations of extracellular vesicle subtypes Proc. Natl. Acad. Sci. U. S. A. 2016, 113, E968-E977 10.1073/pnas.1521230113
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , pp. E968-E977
    • Kowal, J.1    Arras, G.2    Colombo, M.3    Jouve, M.4    Morath, J.P.5    Primdal-Bengtson, B.6
  • 7
    • 84919468543 scopus 로고    scopus 로고
    • Tetraspanins in extracellular vesicle formation and function
    • Andreu, Z.; Yáñez-Mó, M. Tetraspanins in extracellular vesicle formation and function Front. Immunol. 2014, 5, 442 10.3389/fimmu.2014.00442
    • (2014) Front. Immunol. , vol.5 , pp. 442
    • Andreu, Z.1    Yáñez-Mó, M.2
  • 9
    • 84866426167 scopus 로고    scopus 로고
    • Exosomes: Vehicles for the transfer of toxic proteins associated with neurodegenerative diseases?
    • Bellingham, S. A.; Guo, B. B.; Coleman, B. M.; Hill, A. F. Exosomes: Vehicles for the transfer of toxic proteins associated with neurodegenerative diseases? Front. Physiol. 2012, 3, 124 10.3389/fphys.2012.00124
    • (2012) Front. Physiol. , vol.3 , pp. 124
    • Bellingham, S.A.1    Guo, B.B.2    Coleman, B.M.3    Hill, A.F.4
  • 10
    • 84934759283 scopus 로고    scopus 로고
    • Exosomes and Their Role in the Life Cycle and Pathogenesis of RNA Viruses
    • Chahar, H.; Bao, X.; Casola, A. Exosomes and Their Role in the Life Cycle and Pathogenesis of RNA Viruses Viruses 2015, 7, 3204-3225 10.3390/v7062770
    • (2015) Viruses , vol.7 , pp. 3204-3225
    • Chahar, H.1    Bao, X.2    Casola, A.3
  • 13
    • 84941695057 scopus 로고    scopus 로고
    • Myeloid-derived suppressor cells in the tumor microenvironment: Expect the unexpected
    • Marvel, D.; Gabrilovich, D. I. Myeloid-derived suppressor cells in the tumor microenvironment: expect the unexpected J. Clin. Invest. 2015, 125, 3356-3364 10.1172/JCI80005
    • (2015) J. Clin. Invest. , vol.125 , pp. 3356-3364
    • Marvel, D.1    Gabrilovich, D.I.2
  • 14
    • 84952720594 scopus 로고    scopus 로고
    • Myeloid- Deived Suppressor Cells: Critical cells driving Immune Suppression in the Tumor Microenvironment
    • Parker, K. H.; Beury, D. W.; Ostrand-rosenberg, S. Myeloid- Deived Suppressor Cells: Critical cells driving Immune Suppression in the Tumor Microenvironment Adv. Cancer Res. 2015, 128, 95-139 10.1016/bs.acr.2015.04.002
    • (2015) Adv. Cancer Res. , vol.128 , pp. 95-139
    • Parker, K.H.1    Beury, D.W.2    Ostrand-Rosenberg, S.3
  • 15
    • 65249138393 scopus 로고    scopus 로고
    • Myeloid-derived suppressor cells: Linking inflammation and cancer
    • Ostrand-Rosenberg, S.; Sinha, P. et al. Myeloid-derived suppressor cells: linking inflammation and cancer J. Immunol. 2009, 182, 4499-4506 10.4049/jimmunol.0802740
    • (2009) J. Immunol. , vol.182 , pp. 4499-4506
    • Ostrand-Rosenberg, S.1    Sinha, P.2
  • 16
    • 34249300128 scopus 로고    scopus 로고
    • Prostaglandin E2 promotes tumor progression by inducing myeloid-derived suppressor cells
    • Sinha, P.; Clements, V. K.; Fulton, A. M.; Ostrand-Rosenberg, S. Prostaglandin E2 promotes tumor progression by inducing myeloid-derived suppressor cells Cancer Res. 2007, 67, 4507-4513 10.1158/0008-5472.CAN-06-4174
    • (2007) Cancer Res. , vol.67 , pp. 4507-4513
    • Sinha, P.1    Clements, V.K.2    Fulton, A.M.3    Ostrand-Rosenberg, S.4
  • 17
    • 84908054077 scopus 로고    scopus 로고
    • HMGB1 enhances immune suppression by facilitating the differentiation and suppressive activity of myeloid-derived suppressor cells
    • Parker, K. H.; Sinha, P.; Horn, L. A.; Clements, V. K.; Yang, H.; Li, J.; Tracey, K. J.; Ostrand-Rosenberg, S. HMGB1 enhances immune suppression by facilitating the differentiation and suppressive activity of myeloid-derived suppressor cells Cancer Res. 2014, 74, 5723-5733 10.1158/0008-5472.CAN-13-2347
    • (2014) Cancer Res. , vol.74 , pp. 5723-5733
    • Parker, K.H.1    Sinha, P.2    Horn, L.A.3    Clements, V.K.4    Yang, H.5    Li, J.6    Tracey, K.J.7    Ostrand-Rosenberg, S.8
  • 19
    • 84855573739 scopus 로고    scopus 로고
    • The roles of tumor-derived exosomes in cancer pathogenesis
    • Yang, C.; Robbins, P. D. The roles of tumor-derived exosomes in cancer pathogenesis Clin. Dev. Immunol. 2011, 2011, 842849 10.1155/2011/842849
    • (2011) Clin. Dev. Immunol. , vol.2011 , pp. 842849
    • Yang, C.1    Robbins, P.D.2
  • 20
    • 84893868499 scopus 로고    scopus 로고
    • Exosomes from Myeloid-Derived Suppressor Cells Carry Biologically Active Proteins
    • Burke, M.; Choksawangkarn, W.; Edwards, N.; Ostrand-Rosenberg, S.; Fenselau, C. Exosomes from Myeloid-Derived Suppressor Cells Carry Biologically Active Proteins J. Proteome Res. 2014, 13 (2) 836-843 10.1021/pr400879c
    • (2014) J. Proteome Res. , vol.13 , Issue.2 , pp. 836-843
    • Burke, M.1    Choksawangkarn, W.2    Edwards, N.3    Ostrand-Rosenberg, S.4    Fenselau, C.5
  • 21
    • 53349125963 scopus 로고    scopus 로고
    • Proinflammatory S100 Proteins Regulate the Accumulation of Myeloid-Derived Suppressor Cells
    • Sinha, P.; Okoro, C.; Foell, D.; Freeze, H. H.; Ostrand-Rosenberg, S.; Srikrishna, G. Proinflammatory S100 Proteins Regulate the Accumulation of Myeloid-Derived Suppressor Cells J. Immunol. 2008, 181, 4666-4675 10.4049/jimmunol.181.7.4666
    • (2008) J. Immunol. , vol.181 , pp. 4666-4675
    • Sinha, P.1    Okoro, C.2    Foell, D.3    Freeze, H.H.4    Ostrand-Rosenberg, S.5    Srikrishna, G.6
  • 22
    • 4444269513 scopus 로고    scopus 로고
    • Lectin Affinity as an Approach to the Proteomic Analysis of Membrane Glycoproteins research articles
    • Ghosh, D.; Krokhin, O.; Antonovici, M.; Ens, W.; Standing, K. G.; Beavis, R. C.; Wilkins, J. A. Lectin Affinity as an Approach to the Proteomic Analysis of Membrane Glycoproteins research articles J. Proteome Res. 2004, 3, 841-850 10.1021/pr049937f
    • (2004) J. Proteome Res. , vol.3 , pp. 841-850
    • Ghosh, D.1    Krokhin, O.2    Antonovici, M.3    Ens, W.4    Standing, K.G.5    Beavis, R.C.6    Wilkins, J.A.7
  • 23
    • 3543072968 scopus 로고    scopus 로고
    • Purification of biotinylated proteins on streptavidin resin: A protocol for quantitative elution
    • Rybak, J.-N.; Scheurer, S. B.; Neri, D.; Elia, G. Purification of biotinylated proteins on streptavidin resin: a protocol for quantitative elution Proteomics 2004, 4, 2296-2299 10.1002/pmic.200300780
    • (2004) Proteomics , vol.4 , pp. 2296-2299
    • Rybak, J.-N.1    Scheurer, S.B.2    Neri, D.3    Elia, G.4
  • 24
    • 0037470247 scopus 로고    scopus 로고
    • Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function
    • Shin, B. K.; Wang, H.; Yim, A. M.; Le Naour, F.; Brichory, F.; Jang, J. H.; Zhao, R.; Puravs, E.; Tra, J.; Michael, C. W. et al. Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function J. Biol. Chem. 2003, 278, 7607-7616 10.1074/jbc.M210455200
    • (2003) J. Biol. Chem. , vol.278 , pp. 7607-7616
    • Shin, B.K.1    Wang, H.2    Yim, A.M.3    Le Naour, F.4    Brichory, F.5    Jang, J.H.6    Zhao, R.7    Puravs, E.8    Tra, J.9    Michael, C.W.10
  • 25
    • 84874601536 scopus 로고    scopus 로고
    • Enrichment of Plasma Membrane Proteins Using Nanoparticle Pellicles: Comparison between Silica and Higher Density Nanoparticles
    • Choksawangkarn, W.; Kim, S.; Cannon, J. R.; Edwards, N. J.; Lee, S. B.; Fenselau, C. Enrichment of Plasma Membrane Proteins Using Nanoparticle Pellicles: Comparison between Silica and Higher Density Nanoparticles J. Proteome. Res. 2013, 12, 1134-1141 10.1021/pr301107x
    • (2013) J. Proteome. Res. , vol.12 , pp. 1134-1141
    • Choksawangkarn, W.1    Kim, S.2    Cannon, J.R.3    Edwards, N.J.4    Lee, S.B.5    Fenselau, C.6
  • 26
    • 77951637328 scopus 로고    scopus 로고
    • Isolation of cell surface proteins for mass spectrometry-based proteomics
    • Elschenbroich, S.; Kim, Y.; Medin, J. a; Kislinger, T. Isolation of cell surface proteins for mass spectrometry-based proteomics Expert Rev. Proteomics 2010, 7, 141-154 10.1586/epr.09.97
    • (2010) Expert Rev. Proteomics , vol.7 , pp. 141-154
    • Elschenbroich, S.1    Kim, Y.2    Medin, J.A.3    Kislinger, T.4
  • 27
    • 34347364743 scopus 로고    scopus 로고
    • Direct identification of nonreducing GlcNAc residues on N-glycans of glycoproteins using a novel chemoenzymatic method
    • Boeggeman, E.; Ramakrishnan, B.; Kilgore, C.; Khidekel, N.; Hsieh-Wilson, L. C.; Simpson, J. T.; Qasba, P. K. Direct identification of nonreducing GlcNAc residues on N-glycans of glycoproteins using a novel chemoenzymatic method Bioconjugate Chem. 2007, 18, 806-814 10.1021/bc060341n
    • (2007) Bioconjugate Chem. , vol.18 , pp. 806-814
    • Boeggeman, E.1    Ramakrishnan, B.2    Kilgore, C.3    Khidekel, N.4    Hsieh-Wilson, L.C.5    Simpson, J.T.6    Qasba, P.K.7
  • 28
    • 84871954135 scopus 로고    scopus 로고
    • Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans
    • Ramya, T. N. C.; Weerapana, E.; Cravatt, B. F.; Paulson, J. C. Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans Glycobiology 2013, 23, 211-221 10.1093/glycob/cws144
    • (2013) Glycobiology , vol.23 , pp. 211-221
    • Ramya, T.N.C.1    Weerapana, E.2    Cravatt, B.F.3    Paulson, J.C.4
  • 30
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang, H.; Li, X.-J.; Martin, D. B.; Aebersold, R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry Nat. Biotechnol. 2003, 21, 660-666 10.1038/nbt827
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.-J.2    Martin, D.B.3    Aebersold, R.4
  • 32
    • 79953192550 scopus 로고    scopus 로고
    • Proteomic pathway analysis reveals inflammation increases myeloid-derived suppressor cell resistance to apoptosis
    • M110.002980
    • Chornoguz, O.; Grmai, L.; Sinha, P.; Artemenko, K. A.; Zubarev, R. A.; Ostrand-Rosenberg, S. Proteomic pathway analysis reveals inflammation increases myeloid-derived suppressor cell resistance to apoptosis Mol. Cell. Proteomics 2011, 10, M110.002980 10.1074/mcp.M110.002980
    • (2011) Mol. Cell. Proteomics , vol.10
    • Chornoguz, O.1    Grmai, L.2    Sinha, P.3    Artemenko, K.A.4    Zubarev, R.A.5    Ostrand-Rosenberg, S.6
  • 33
    • 54949129419 scopus 로고    scopus 로고
    • ProteoWizard: Open source software for rapid proteomics tools development
    • Kessner, D.; Chambers, M.; Burke, R.; Agus, D.; Mallick, P. ProteoWizard: open source software for rapid proteomics tools development Bioinformatics 2008, 24, 2534-2536 10.1093/bioinformatics/btn323
    • (2008) Bioinformatics , vol.24 , pp. 2534-2536
    • Kessner, D.1    Chambers, M.2    Burke, R.3    Agus, D.4    Mallick, P.5
  • 34
    • 84896381869 scopus 로고    scopus 로고
    • PepArML: A Meta-Search Peptide Identification Platform for Tandem Mass Spectra
    • Edwards, N. J. PepArML: A Meta-Search Peptide Identification Platform for Tandem Mass Spectra Curr. Protoc Bioinformatics 2013, 13.23.1 10.1002/0471250953.bi1323s44
    • (2013) Curr. Protoc Bioinformatics , pp. 13231
    • Edwards, N.J.1
  • 35
    • 84923247212 scopus 로고    scopus 로고
    • MS-GF+ makes progress towards a universal database search tool for proteomics
    • Kim, S.; Pevzner, P. A. MS-GF+ makes progress towards a universal database search tool for proteomics Nat. Commun. 2014, 5, 5277 10.1038/ncomms6277
    • (2014) Nat. Commun. , vol.5 , pp. 5277
    • Kim, S.1    Pevzner, P.A.2
  • 37
    • 0036370537 scopus 로고    scopus 로고
    • Prediction of glycosylation across the human proteome and the correlation to protein function
    • Gupta, R.; Brunak, S. Prediction of glycosylation across the human proteome and the correlation to protein function Pac. Symp. Biocomput. 2002, 322, 310-322 10.1142/9789812799623-0029
    • (2002) Pac. Symp. Biocomput. , vol.322 , pp. 310-322
    • Gupta, R.1    Brunak, S.2
  • 38
    • 84897873840 scopus 로고    scopus 로고
    • Protter: Interactive protein feature visualization and integration with experimental proteomic data
    • Omasits, U.; Ahrens, C. H.; Muller, S.; Wollscheid, B. Protter: interactive protein feature visualization and integration with experimental proteomic data Bioinformatics 2014, 30, 884-886 10.1093/bioinformatics/btt607
    • (2014) Bioinformatics , vol.30 , pp. 884-886
    • Omasits, U.1    Ahrens, C.H.2    Muller, S.3    Wollscheid, B.4
  • 39
    • 84911390789 scopus 로고    scopus 로고
    • Exosome proteomics reveals transcriptional regulator proteins with potential to mediate downstream pathways
    • Ung, T. H.; Madsen, H. J.; Hellwinkel, J. E.; Lencioni, A. M.; Graner, M. W. Exosome proteomics reveals transcriptional regulator proteins with potential to mediate downstream pathways Cancer Sci. 2014, 105, 1384-1392 10.1111/cas.12534
    • (2014) Cancer Sci. , vol.105 , pp. 1384-1392
    • Ung, T.H.1    Madsen, H.J.2    Hellwinkel, J.E.3    Lencioni, A.M.4    Graner, M.W.5
  • 41
    • 84936804591 scopus 로고    scopus 로고
    • Loss of Cell Surface CD47 Clustering Formation and Binding Avidity to SIRPα Facilitate Apoptotic Cell Clearance by Macrophages
    • Lv, Z.; Bian, Z.; Shi, L.; Niu, S.; Ha, B.; Tremblay, A.; Li, L.; Zhang, X.; Paluszynski, J.; Liu, M. et al. Loss of Cell Surface CD47 Clustering Formation and Binding Avidity to SIRPα Facilitate Apoptotic Cell Clearance by Macrophages J. Immunol. 2015, 195, 661-671 10.4049/jimmunol.1401719
    • (2015) J. Immunol. , vol.195 , pp. 661-671
    • Lv, Z.1    Bian, Z.2    Shi, L.3    Niu, S.4    Ha, B.5    Tremblay, A.6    Li, L.7    Zhang, X.8    Paluszynski, J.9    Liu, M.10
  • 42
    • 0028024198 scopus 로고
    • Mouse Homologue of C33 Antigen (CD82), a member of the transmembrane 4 superfamily: Complementary DNA, genomic structure, and expression
    • Nagira, M.; Imai, T.; Ishikawa, I.; Uwabe, K.-I.; Yoshie, O. Mouse Homologue of C33 Antigen (CD82), a member of the transmembrane 4 superfamily: Complementary DNA, genomic structure, and expression Cell. Immunol. 1994, 157, 144-157 10.1006/cimm.1994.1212
    • (1994) Cell. Immunol. , vol.157 , pp. 144-157
    • Nagira, M.1    Imai, T.2    Ishikawa, I.3    Uwabe, K.-I.4    Yoshie, O.5
  • 43
    • 34249302620 scopus 로고    scopus 로고
    • Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells
    • Valadi, H.; Ekström, K.; Bossios, A.; Sjöstrand, M.; Lee, J. J.; Lötvall, J. O. Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells Nat. Cell Biol. 2007, 9, 654-659 10.1038/ncb1596
    • (2007) Nat. Cell Biol. , vol.9 , pp. 654-659
    • Valadi, H.1    Ekström, K.2    Bossios, A.3    Sjöstrand, M.4    Lee, J.J.5    Lötvall, J.O.6
  • 44
    • 45449093192 scopus 로고    scopus 로고
    • MicroRNA signatures of tumor-derived exosomes as diagnostic biomarkers of ovarian cancer
    • Taylor, D. D.; Gercel-Taylor, C. MicroRNA signatures of tumor-derived exosomes as diagnostic biomarkers of ovarian cancer Gynecol. Oncol. 2008, 110, 13-21 10.1016/j.ygyno.2008.04.033
    • (2008) Gynecol. Oncol. , vol.110 , pp. 13-21
    • Taylor, D.D.1    Gercel-Taylor, C.2
  • 46
    • 34548655590 scopus 로고    scopus 로고
    • CD8+ Dendritic Cells Use LFA-1 to Capture MHC-Peptide Complexes from Exosomes in Vivo
    • Segura, E.; Guerin, C.; Hogg, N.; Amigorena, S.; Thery, C. CD8+ Dendritic Cells Use LFA-1 to Capture MHC-Peptide Complexes from Exosomes In Vivo J. Immunol. 2007, 179, 1489-1496 10.4049/jimmunol.179.3.1489
    • (2007) J. Immunol. , vol.179 , pp. 1489-1496
    • Segura, E.1    Guerin, C.2    Hogg, N.3    Amigorena, S.4    Thery, C.5
  • 47
    • 47249144117 scopus 로고    scopus 로고
    • Human Tumor-Derived Exosomes Down-Modulate NKG2D Expression
    • Clayton, A.; Mitchell, J. P.; Court, J.; Linnane, S.; Mason, M. D.; Tabi, Z. Human Tumor-Derived Exosomes Down-Modulate NKG2D Expression J. Immunol. 2008, 180, 7249-7258 10.4049/jimmunol.180.11.7249
    • (2008) J. Immunol. , vol.180 , pp. 7249-7258
    • Clayton, A.1    Mitchell, J.P.2    Court, J.3    Linnane, S.4    Mason, M.D.5    Tabi, Z.6
  • 48
    • 6944253946 scopus 로고    scopus 로고
    • Adhesion and signaling by B cell-derived exosomes: The role of integrins
    • Clayton, A.; Turkes, A.; Dewitt, S.; Steadman, R.; Mason, M. D.; Hallett, M. B. Adhesion and signaling by B cell-derived exosomes: the role of integrins FASEB J. 2004, 18 (9) 977-979 10.1096/fj.03-1094fje
    • (2004) FASEB J. , vol.18 , Issue.9 , pp. 977-979
    • Clayton, A.1    Turkes, A.2    Dewitt, S.3    Steadman, R.4    Mason, M.D.5    Hallett, M.B.6
  • 49
    • 77953154769 scopus 로고    scopus 로고
    • Cellular internalization of exosomes occurs through phagocytosis
    • Feng, D.; Zhao, W. L.; Ye, Y. Y.; Bai, X. C.; Liu, R. Q.; Chang, L. F.; Zhou, Q.; Sui, S. F. Cellular internalization of exosomes occurs through phagocytosis Traffic 2010, 11, 675-687 10.1111/j.1600-0854.2010.01041.x
    • (2010) Traffic , vol.11 , pp. 675-687
    • Feng, D.1    Zhao, W.L.2    Ye, Y.Y.3    Bai, X.C.4    Liu, R.Q.5    Chang, L.F.6    Zhou, Q.7    Sui, S.F.8
  • 50
    • 84934939517 scopus 로고    scopus 로고
    • Exosome-mediated transfer of miR-10b promotes cell invasion in breast cancer
    • Singh, R.; Pochampally, R.; Watabe, K.; Lu, Z.; Mo, Y.-Y. Exosome-mediated transfer of miR-10b promotes cell invasion in breast cancer Mol. Cancer 2014, 13, 256 10.1186/1476-4598-13-256
    • (2014) Mol. Cancer , vol.13 , pp. 256
    • Singh, R.1    Pochampally, R.2    Watabe, K.3    Lu, Z.4    Mo, Y.-Y.5
  • 51
    • 0038712496 scopus 로고    scopus 로고
    • Thrombospondin-bound integrin-associated protein (CD47) physically and functionally modifies integrin αiIbβ3 by its extracellular domain
    • Fujimoto, T. T.; Katsutani, S.; Shimomura, T.; Fujimura, K. Thrombospondin-bound integrin-associated protein (CD47) physically and functionally modifies integrin αIIbβ3 by its extracellular domain J. Biol. Chem. 2003, 278, 26655-26665 10.1074/jbc.M302194200
    • (2003) J. Biol. Chem. , vol.278 , pp. 26655-26665
    • Fujimoto, T.T.1    Katsutani, S.2    Shimomura, T.3    Fujimura, K.4
  • 52
    • 0026557413 scopus 로고
    • Lymphocyte CD44 binds the COOH-terminal heparin-binding domain of fibronectin
    • Jalkanen, S.; Jalkanen, M. Lymphocyte CD44 binds the COOH-terminal heparin-binding domain of fibronectin J. Cell Biol. 1992, 116, 817-825 10.1083/jcb.116.3.817
    • (1992) J. Cell Biol. , vol.116 , pp. 817-825
    • Jalkanen, S.1    Jalkanen, M.2
  • 53
    • 13944267041 scopus 로고    scopus 로고
    • Inhibition of endothelial cell migration by thrombospondin-1 type-1 repeats is mediated by beta1 integrins
    • Short, S. M.; Derrien, A.; Narsimhan, R. P.; Lawler, J.; Ingber, D. E.; Zetter, B. R. Inhibition of endothelial cell migration by thrombospondin-1 type-1 repeats is mediated by beta1 integrins J. Cell Biol. 2005, 168, 643-653 10.1083/jcb.200407060
    • (2005) J. Cell Biol. , vol.168 , pp. 643-653
    • Short, S.M.1    Derrien, A.2    Narsimhan, R.P.3    Lawler, J.4    Ingber, D.E.5    Zetter, B.R.6
  • 54
    • 0035451118 scopus 로고    scopus 로고
    • Fibrinogen Stimulates Macrophage Chemokine Secretion Through Toll-Like Receptor 4
    • Smiley, S. T.; King, J. A.; Hancock, W. W. Fibrinogen Stimulates Macrophage Chemokine Secretion Through Toll-Like Receptor 4 J. Immunol. 2001, 167, 2887-2894 10.4049/jimmunol.167.5.2887
    • (2001) J. Immunol. , vol.167 , pp. 2887-2894
    • Smiley, S.T.1    King, J.A.2    Hancock, W.W.3
  • 56
    • 34147109358 scopus 로고    scopus 로고
    • A mechanism to safeguard platelet adhesion under high shear flow: Von Willebrand factor-glycoprotein Ib and integrin α2 β1-collagen interactions make complementary, collagen-type-specific contributions to adhesion
    • Moroi, M.; Jung, S. M. A mechanism to safeguard platelet adhesion under high shear flow: Von Willebrand factor-glycoprotein Ib and integrin α2 β1-collagen interactions make complementary, collagen-type-specific contributions to adhesion J. Thromb. Haemostasis 2007, 5, 797-803 10.1111/j.1538-7836.2007.02439.x
    • (2007) J. Thromb. Haemostasis , vol.5 , pp. 797-803
    • Moroi, M.1    Jung, S.M.2
  • 57
    • 0036565772 scopus 로고    scopus 로고
    • Association of thrombospondin-1 with the actin cytoskeleton of human thrombin-activated platelets through an αiIbβ3- or CD36-independent mechanism mechanism
    • Saumet, A.; Legrand, C.; Dubernard, V.; de Jesus, N. Association of thrombospondin-1 with the actin cytoskeleton of human thrombin-activated platelets through an αIIbβ3- or CD36-independent mechanism mechanism Biochem. J. 2002, 363, 473-482 10.1042/bj3630473
    • (2002) Biochem. J. , vol.363 , pp. 473-482
    • Saumet, A.1    Legrand, C.2    Dubernard, V.3    De Jesus, N.4
  • 59
    • 0038297125 scopus 로고    scopus 로고
    • Fibrinogen-CD11b/CD18 interaction activates the NF-κB pathway and delays apoptosis in human neutrophils
    • Rubel, C.; Gómez, S.; Fernández, G. C.; Isturiz, M. A.; Caamaño, J.; Palermo, M. S. Fibrinogen-CD11b/CD18 interaction activates the NF-κB pathway and delays apoptosis in human neutrophils Eur. J. Immunol. 2003, 33, 1429-1438 10.1002/eji.200323512
    • (2003) Eur. J. Immunol. , vol.33 , pp. 1429-1438
    • Rubel, C.1    Gómez, S.2    Fernández, G.C.3    Isturiz, M.A.4    Caamaño, J.5    Palermo, M.S.6
  • 60
    • 26444482058 scopus 로고    scopus 로고
    • Novel CD47-dependent intercellular adhesion modulates cell migration
    • Rebres, R. A.; Kajihara, K.; Brown, E. J. Novel CD47-dependent intercellular adhesion modulates cell migration J. Cell. Physiol. 2005, 205, 182-193 10.1002/jcp.20379
    • (2005) J. Cell. Physiol. , vol.205 , pp. 182-193
    • Rebres, R.A.1    Kajihara, K.2    Brown, E.J.3
  • 61
    • 84978725295 scopus 로고    scopus 로고
    • Oxford University, Stanford University ClinicalTrials.gov [Internet]. Bethesda (MD): National Library of Medicine (US). 2016- [cited 2016 Aug 22]. Available from
    • Oxford University, Stanford University. CAMELLIA: Anti-CD47 Antibody Therapy in Relapsed/Refractory Acute Myeloid Leukaemia. ClinicalTrials.gov [Internet]. Bethesda (MD): National Library of Medicine (US). 2016- [cited 2016 Aug 22]. Available from: https://clinicaltrials.gov/ct2/show/NCT02678338?term=CD47&rank=1.
    • CAMELLIA: Anti-CD47 Antibody Therapy in Relapsed/Refractory Acute Myeloid Leukaemia


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.