메뉴 건너뛰기




Volumn 27, Issue 4, 2007, Pages 241-245

Functional proteome analysis of human platelets;Funktionelle proteomanalyse humaner thrombozyten

Author keywords

Glycosylation; Mass spectrometry; Phosphorylation; Platelets; Proteome

Indexed keywords

CELL MEMBRANE; CONFERENCE PAPER; HUMAN; MASS SPECTROMETRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN ANALYSIS; PROTEIN GLYCOSYLATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEOMICS; THROMBOCYTE;

EID: 35348932235     PISSN: 07209355     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1617088     Document Type: Conference Paper
Times cited : (4)

References (38)
  • 1
    • 0030333694 scopus 로고    scopus 로고
    • Progress with proteome projects: Why all proteins expressed by a genome should be identified and how to do it
    • Wilkins MR, Sanchez JC, Gooley AA et al. Progress with proteome projects: why all proteins expressed by a genome should be identified and how to do it. Biotechnol Genet Eng Rev 1996; 13: 19-50.
    • (1996) Biotechnol Genet Eng Rev , vol.13 , pp. 19-50
    • Wilkins, M.R.1    Sanchez, J.C.2    Gooley, A.A.3
  • 2
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M, Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem 1988; 60: 2299-2301.
    • (1988) Anal Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 3
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK et al. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989; 246: 64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3
  • 4
    • 0034060037 scopus 로고    scopus 로고
    • The Human Genome Project - an overview
    • Bentley DR. The Human Genome Project - an overview. Med Res Rev 2000; 20: 189-196.
    • (2000) Med Res Rev , vol.20 , pp. 189-196
    • Bentley, D.R.1
  • 5
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM et al. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999; 20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3
  • 6
    • 58149115929 scopus 로고    scopus 로고
    • Platelet receptors
    • Michelson A ed, San Diego
    • Clementson K. Platelet receptors. In: Michelson A (ed). Platelets. San Diego: 2002, 64-84.
    • (2002) Platelets , pp. 64-84
    • Clementson, K.1
  • 7
    • 0033847019 scopus 로고    scopus 로고
    • Identification of platelet proteins separated by two-dimensional gel electrophoresis and analyzed by matrix assisted laser desorption/ionization-time of flight-mass spectrometry and detection of tyrosine-phosphorylated proteins
    • Marcus K, Immler D, Sternberger J et al. Identification of platelet proteins separated by two-dimensional gel electrophoresis and analyzed by matrix assisted laser desorption/ionization-time of flight-mass spectrometry and detection of tyrosine-phosphorylated proteins. Electrophoresis 2000, 21. 2622-2636.
    • (2000) Electrophoresis , vol.21 , pp. 2622-2636
    • Marcus, K.1    Immler, D.2    Sternberger, J.3
  • 8
    • 1542511097 scopus 로고    scopus 로고
    • Extensive analysis of the human platelet proteome by two-dimensional gel electrophoresis and mass spectrometry
    • Garcia A, Prabhakar S, Brock CJ et al. Extensive analysis of the human platelet proteome by two-dimensional gel electrophoresis and mass spectrometry. Proteomics 2004; 4: 656-668.
    • (2004) Proteomics , vol.4 , pp. 656-668
    • Garcia, A.1    Prabhakar, S.2    Brock, C.J.3
  • 9
    • 0036208705 scopus 로고    scopus 로고
    • Towards complete analysis of the platelet proteome
    • O'Neill EE, Brock CJ, von Kriegsheim AF et al. Towards complete analysis of the platelet proteome. Proteomics 2002; 2: 288-305.
    • (2002) Proteomics , vol.2 , pp. 288-305
    • O'Neill, E.E.1    Brock, C.J.2    von Kriegsheim, A.F.3
  • 10
    • 26844452187 scopus 로고    scopus 로고
    • The Platelet Microparticle Proteome
    • Garcia BA, Smalley DM, Cho H et al. The Platelet Microparticle Proteome. J Proteome Res 2005; 4. 1516-1521.
    • (2005) J Proteome Res , vol.4 , pp. 1516-1521
    • Garcia, B.A.1    Smalley, D.M.2    Cho, H.3
  • 11
    • 0026458937 scopus 로고
    • Isolation and characterization of platelet membranes prepared by free flow electrophoresis
    • Crawford N, Authi KS, Hack N. Isolation and characterization of platelet membranes prepared by free flow electrophoresis. Methods Enzymol 1992; 215: 5-20.
    • (1992) Methods Enzymol , vol.215 , pp. 5-20
    • Crawford, N.1    Authi, K.S.2    Hack, N.3
  • 12
    • 0018731408 scopus 로고
    • Isolation of human platelet plasma membranes with polylysine beads
    • Kinoshita T, Nachman RL, Minick R. Isolation of human platelet plasma membranes with polylysine beads. J Cell Biol 1979; 82: 688-696.
    • (1979) J Cell Biol , vol.82 , pp. 688-696
    • Kinoshita, T.1    Nachman, R.L.2    Minick, R.3
  • 13
    • 0014940777 scopus 로고
    • Isolation and characterization of plasma membranes from human blood platelets
    • Barber AJ, Jamieson GA. Isolation and characterization of plasma membranes from human blood platelets. J Biol Chem 1970; 245: 6357-6365.
    • (1970) J Biol Chem , vol.245 , pp. 6357-6365
    • Barber, A.J.1    Jamieson, G.A.2
  • 14
    • 0017284963 scopus 로고
    • Isolation of membranes from normal and thrombin-treated gel-filtered platelets using a lectin marker
    • Rittenhouse-Simmons S, Deykin D. Isolation of membranes from normal and thrombin-treated gel-filtered platelets using a lectin marker. Biochim Biophys Acta 1976; 426: 688-696.
    • (1976) Biochim Biophys Acta , vol.426 , pp. 688-696
    • Rittenhouse-Simmons, S.1    Deykin, D.2
  • 15
    • 0019874993 scopus 로고
    • Isolation, characterization and chemical composition of the membrane from sheep platelets
    • Lanillo M, Cabezas JA. Isolation, characterization and chemical composition of the membrane from sheep platelets. Biochim Biophys Acta 1981; 649: 229-238.
    • (1981) Biochim Biophys Acta , vol.649 , pp. 229-238
    • Lanillo, M.1    Cabezas, J.A.2
  • 16
    • 27844559478 scopus 로고    scopus 로고
    • The human platelet membrane proteome reveals several new potential membrane proteins
    • Moebius J, Zahedi RP, Lewandrowski U et al. The human platelet membrane proteome reveals several new potential membrane proteins. Mol Cell Proteomics 2005; 4: 1754-1761.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1754-1761
    • Moebius, J.1    Zahedi, R.P.2    Lewandrowski, U.3
  • 17
    • 0028892420 scopus 로고
    • The purification of membranes by affinity partitioning
    • Persson A, Jergil B. The purification of membranes by affinity partitioning. Faseb J 1995; 9: 1304-1310.
    • (1995) Faseb J , vol.9 , pp. 1304-1310
    • Persson, A.1    Jergil, B.2
  • 18
    • 33644663350 scopus 로고    scopus 로고
    • Proteomic analysis of brain plasma membranes isolated by affinity two-phase partitioning
    • Schindler J, Lewandrowski U, Sickmann A et al. Proteomic analysis of brain plasma membranes isolated by affinity two-phase partitioning. Mol Cell Proteomics 2006; 5: 390-400.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 390-400
    • Schindler, J.1    Lewandrowski, U.2    Sickmann, A.3
  • 19
    • 0030586426 scopus 로고    scopus 로고
    • 16-BAC/SDS-PAGE: A two-dimensional gel electrophoresis system suitable for the separation of integral membrane proteins
    • Hartinger J, Stenius K, Hogemann D et al. 16-BAC/SDS-PAGE: a two-dimensional gel electrophoresis system suitable for the separation of integral membrane proteins. Anal Biochem 1996; 240: 126-133.
    • (1996) Anal Biochem , vol.240 , pp. 126-133
    • Hartinger, J.1    Stenius, K.2    Hogemann, D.3
  • 20
    • 0035834629 scopus 로고    scopus 로고
    • G6b, a novel immunoglobulin superfamily member encoded in the human major histocompatibility complex, interacts with SHP-1 and SHP-2
    • De Vet EC, Aguado B, Campbell RD. G6b, a novel immunoglobulin superfamily member encoded in the human major histocompatibility complex, interacts with SHP-1 and SHP-2. J Biol Chem 2001; 276: 42070-42076.
    • (2001) J Biol Chem , vol.276 , pp. 42070-42076
    • De Vet, E.C.1    Aguado, B.2    Campbell, R.D.3
  • 21
    • 17644389891 scopus 로고    scopus 로고
    • The cell surface receptor G6b, a member of the immunoglobulin superfamily, binds heparin
    • De Vet EC, Newland SA, Lyons PA et al. The cell surface receptor G6b, a member of the immunoglobulin superfamily, binds heparin. FEBS Lett 2005; 579: 2355-2358.
    • (2005) FEBS Lett , vol.579 , pp. 2355-2358
    • De Vet, E.C.1    Newland, S.A.2    Lyons, P.A.3
  • 22
    • 34147183885 scopus 로고    scopus 로고
    • A comprehensive proteomics and genomics analysis reveals novel transmembrane proteins in human platelets and mouse megakaryocytes including G6b-B, a novel ITIM protein
    • Senis YA, Tomlinson MG, Garcia A et al. A comprehensive proteomics and genomics analysis reveals novel transmembrane proteins in human platelets and mouse megakaryocytes including G6b-B, a novel ITIM protein. Mol Cell Proteomics 2007; 6: 548-564.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 548-564
    • Senis, Y.A.1    Tomlinson, M.G.2    Garcia, A.3
  • 23
    • 33646921991 scopus 로고    scopus 로고
    • Profiling of the tetraspanin web of human colon cancer cells
    • Le Naour F, Andre M, Greco C et al. Profiling of the tetraspanin web of human colon cancer cells. Mol Cell Proteomics 2006; 5: 845-857.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 845-857
    • Le Naour, F.1    Andre, M.2    Greco, C.3
  • 24
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler ME. Tetraspanin functions and associated microdomains. Nat Rev Mol Cell Biol 2005; 6: 801-811.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 25
    • 4944252716 scopus 로고    scopus 로고
    • The tetraspanin superfamily member CD151 regulates outside-in integrin alphaIIbbeta3 signaling and platelet function
    • Lau LM, Wee JL, Wright MD et al. The tetraspanin superfamily member CD151 regulates outside-in integrin alphaIIbbeta3 signaling and platelet function. Blood 2004; 104: 2368-2375.
    • (2004) Blood , vol.104 , pp. 2368-2375
    • Lau, L.M.1    Wee, J.L.2    Wright, M.D.3
  • 26
    • 27744563093 scopus 로고    scopus 로고
    • State-of-the-art in phosphoproteomics
    • Reinders J, Sickmann A. State-of-the-art in phosphoproteomics. Proteomics 2005; 5: 4052-4061.
    • (2005) Proteomics , vol.5 , pp. 4052-4061
    • Reinders, J.1    Sickmann, A.2
  • 27
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse MW, Uitto PM, Hilhorst MJ et al. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal Chem 2004; 76: 3935-3943.
    • (2004) Anal Chem , vol.76 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3
  • 28
    • 5644259649 scopus 로고    scopus 로고
    • Phosphopeptide-selective column-switching RP-HPLC with a titania precolumn
    • Kuroda I, Shintani Y, Motokawa M et al. Phosphopeptide-selective column-switching RP-HPLC with a titania precolumn. Anal Sci 2004; 20: 1313-1319.
    • (2004) Anal Sci , vol.20 , pp. 1313-1319
    • Kuroda, I.1    Shintani, Y.2    Motokawa, M.3
  • 29
    • 4344574540 scopus 로고    scopus 로고
    • Large-scale characterization of HeLa cell nuclear phosphoproteins
    • Beausoleil SA, Jedrychowski M, Schwartz D et al. Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci USA 2004; 101: 12130-12135.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12130-12135
    • Beausoleil, S.A.1    Jedrychowski, M.2    Schwartz, D.3
  • 30
    • 5444266511 scopus 로고    scopus 로고
    • Regulation of integrin functions by N-glycans
    • Gu J, Taniguchi N. Regulation of integrin functions by N-glycans. Glycoconj J 2004; 21: 9-15.
    • (2004) Glycoconj J , vol.21 , pp. 9-15
    • Gu, J.1    Taniguchi, N.2
  • 31
    • 27144543207 scopus 로고    scopus 로고
    • The influence of N-linked glycosylation on the function of platelet glycoprotein VI
    • Kunicki TJ, Cheli Y, Moroi M et al. The influence of N-linked glycosylation on the function of platelet glycoprotein VI. Blood 2005; 106: 2744-2749.
    • (2005) Blood , vol.106 , pp. 2744-2749
    • Kunicki, T.J.1    Cheli, Y.2    Moroi, M.3
  • 32
    • 24044439159 scopus 로고    scopus 로고
    • The macrophage alphaMbeta2 integrin alphaM lectin domain mediates the phagocytosis of chilled platelets
    • Josefsson EC, Gebhard HH, Stossel TP et al. The macrophage alphaMbeta2 integrin alphaM lectin domain mediates the phagocytosis of chilled platelets. J Biol Chem 2005; 280: 18025-18032.
    • (2005) J Biol Chem , vol.280 , pp. 18025-18032
    • Josefsson, E.C.1    Gebhard, H.H.2    Stossel, T.P.3
  • 33
    • 33644690335 scopus 로고    scopus 로고
    • Elucidation of N-glycosylation sites on human platelet proteins: A glycoproteomic approach
    • Lewandrowski U, Moebius J, Walter U et al. Elucidation of N-glycosylation sites on human platelet proteins: A glycoproteomic approach. Mol Cell Proteomics 2006; 5: 226-233.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 226-233
    • Lewandrowski, U.1    Moebius, J.2    Walter, U.3
  • 34
    • 0037685263 scopus 로고    scopus 로고
    • Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins
    • Kaji H, Saito H, Yamauchi Y et al. Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins. Nat Biotechnol 2003; 21: 667-672.
    • (2003) Nat Biotechnol , vol.21 , pp. 667-672
    • Kaji, H.1    Saito, H.2    Yamauchi, Y.3
  • 35
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • Hagglund P, Bunkenborg J, Elortza F et al. A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation. J Proteome Res 2004; 3: 556-566.
    • (2004) J Proteome Res , vol.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3
  • 36
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang H, Li XJ, Martin DB et al. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol 2003; 21: 660-666.
    • (2003) Nat Biotechnol , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3
  • 37
    • 33845413316 scopus 로고    scopus 로고
    • Protein processing and other modifications analyzed by diagonal peptide chromatography
    • Gevaert K, van Damme P, Ghesquiere B et al. Protein processing and other modifications analyzed by diagonal peptide chromatography. Biochim Biophys Acta 2006; 1764: 1801-1810.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1801-1810
    • Gevaert, K.1    van Damme, P.2    Ghesquiere, B.3
  • 38
    • 0037250152 scopus 로고    scopus 로고
    • STRING: A database of predicted functional associations between proteins
    • Von Mering C, Huynen M, Jaeggi D et al. STRING: a database of predicted functional associations between proteins. Nucleic Acids Res 2003; 31: 258-261.
    • (2003) Nucleic Acids Res , vol.31 , pp. 258-261
    • Von Mering, C.1    Huynen, M.2    Jaeggi, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.