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Volumn 103, Issue 4, 2012, Pages 777-785

Tyrosine replacement of PSGL-1 reduces association kinetics with P- and L-selectin on the cell membrane

Author keywords

[No Author keywords available]

Indexed keywords

L SELECTIN; MEMBRANE PROTEIN; P SELECTIN LIGAND PROTEIN; P-SELECTIN LIGAND PROTEIN; PADGEM PROTEIN; TYROSINE;

EID: 84865362693     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.07.028     Document Type: Article
Times cited : (14)

References (43)
  • 2
    • 41949098101 scopus 로고    scopus 로고
    • Mechanisms for flow-enhanced cell adhesion
    • C. Zhu, and T. Yago R.P. McEver Mechanisms for flow-enhanced cell adhesion Ann. Biomed. Eng. 36 2008 604 621
    • (2008) Ann. Biomed. Eng. , vol.36 , pp. 604-621
    • Zhu, C.1    Yagomcever, R.P.T.2
  • 3
    • 45949101608 scopus 로고    scopus 로고
    • The vessel wall and its interactions
    • D.D. Wagner, and P.S. Frenette The vessel wall and its interactions Blood 111 2008 5271 5281
    • (2008) Blood , vol.111 , pp. 5271-5281
    • Wagner, D.D.1    Frenette, P.S.2
  • 4
    • 0035986935 scopus 로고    scopus 로고
    • Measuring receptor/ligand interaction at the single-bond level: Experimental and interpretative issues
    • DOI 10.1114/1.1467923
    • C. Zhu, and M. Long P. Bongrand Measuring receptor/ligand interaction at the single-bond level: experimental and interpretative issues Ann. Biomed. Eng. 30 2002 305 314 (Pubitemid 34690555)
    • (2002) Annals of Biomedical Engineering , vol.30 , Issue.3 , pp. 305-314
    • Zhu, C.1    Long, M.2    Chesla, S.E.3    Bongrand, P.4
  • 5
    • 0026689285 scopus 로고
    • Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells
    • K.L. Moore, and N.L. Stults R.P. McEver Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells J. Cell Biol. 118 1992 445 456
    • (1992) J. Cell Biol. , vol.118 , pp. 445-456
    • Moore, K.L.1    Stults, N.L.2    McEver, R.P.3
  • 7
    • 0037698348 scopus 로고    scopus 로고
    • Model glycosulfopeptides from P-selectin glycoprotein ligand-1 require tyrosine sulfation and a core 2-branched O-glycan to bind to L-selectin
    • DOI 10.1074/jbc.M303551200
    • A. Leppänen, and T. Yago R.D. Cummings Model glycosulfopeptides from P-selectin glycoprotein ligand-1 require tyrosine sulfation and a core 2-branched O-glycan to bind to L-selectin J. Biol. Chem. 278 2003 26391 26400 (Pubitemid 36876778)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 26391-26400
    • Leppanen, A.1    Yago, T.2    Otto, V.I.3    McEver, R.P.4    Cummings, R.D.5
  • 9
    • 0034671746 scopus 로고    scopus 로고
    • Binding of glycosulfopeptides to P-selectin requires stereospecific contributions of individual tyrosine sulfate and sugar residues
    • DOI 10.1074/jbc.M005005200
    • A. Leppänen, and S.P. White R.D. Cummings Binding of glycosulfopeptides to P-selectin requires stereospecific contributions of individual tyrosine sulfate and sugar residues J. Biol. Chem. 275 2000 39569 39578 (Pubitemid 32058983)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.50 , pp. 39569-39578
    • Leppanen, A.1    White, S.P.2    Helin, J.3    McEver, R.P.4    Cummings, R.D.5
  • 10
    • 0033598750 scopus 로고    scopus 로고
    • Tyrosine replacement in P-selectin glycoprotein ligand-1 affects distinct kinetic and mechanical properties of bonds with P- and L-selectin
    • V. Ramachandran, and M.U. Nollert R.P. McEver Tyrosine replacement in P-selectin glycoprotein ligand-1 affects distinct kinetic and mechanical properties of bonds with P- and L-selectin Proc. Natl. Acad. Sci. USA 96 1999 13771 13776
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13771-13776
    • Ramachandran, V.1    Nollert, M.U.2    McEver, R.P.3
  • 11
    • 0040962320 scopus 로고    scopus 로고
    • A novel glycosulfopeptide binds to P-selectin and inhibits leukocyte adhesion to P-selectin
    • A. Leppänen, and P. Mehta R.D. Cummings A novel glycosulfopeptide binds to P-selectin and inhibits leukocyte adhesion to P-selectin J. Biol. Chem. 274 1999 24838 24848
    • (1999) J. Biol. Chem. , vol.274 , pp. 24838-24848
    • Leppänen, A.1    Mehtacummings, R.D.P.2
  • 13
    • 0030041932 scopus 로고    scopus 로고
    • Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin
    • DOI 10.1074/jbc.271.6.3255
    • F. Li, and P.P. Wilkins R.P. McEver Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin J. Biol. Chem. 271 1996 3255 3264 (Pubitemid 26055629)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.6 , pp. 3255-3264
    • Li, F.1    Wilkins, P.P.2    Crawley, S.3    Weinstein, J.4    Cummings, R.D.5    McEver, R.P.6
  • 14
    • 0028863479 scopus 로고
    • PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus
    • T. Pouyani, and B. Seed PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus Cell 83 1995 333 343
    • (1995) Cell , vol.83 , pp. 333-343
    • Pouyani, T.1    Seed, B.2
  • 15
    • 0029132217 scopus 로고
    • Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin
    • P.P. Wilkins, and K.L. Moore R.D. Cummings Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin J. Biol. Chem. 270 1995 22677 22680
    • (1995) J. Biol. Chem. , vol.270 , pp. 22677-22680
    • Wilkins, P.P.1    Moore, K.L.2    Cummings, R.D.3
  • 16
    • 0031985283 scopus 로고    scopus 로고
    • A novel P-selectin glycoprotein ligand-1 monoclonal antibody recognizes an epitope within the tyrosine sulfate motif of human PSGL-1 and blocks recognition of both P- and L-selectin
    • K.R. Snapp, and H. Ding G.S. Kansas A novel P-selectin glycoprotein ligand-1 monoclonal antibody recognizes an epitope within the tyrosine sulfate motif of human PSGL-1 and blocks recognition of both P- and L-selectin Blood 91 1998 154 164 (Pubitemid 28018740)
    • (1998) Blood , vol.91 , Issue.1 , pp. 154-164
    • Snapp, K.R.1    Ding, H.2    Atkins, K.3    Warnke, R.4    Luscinskas, F.W.5    Kansas, G.S.6
  • 18
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • G.I. Bell Models for the specific adhesion of cells to cells Science 200 1978 618 627
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 19
    • 0037653696 scopus 로고    scopus 로고
    • Direct observation of catch bonds involving cell-adhesion molecules
    • DOI 10.1038/nature01605
    • B.T. Marshall, and M. Long C. Zhu Direct observation of catch bonds involving cell-adhesion molecules Nature 423 2003 190 193 (Pubitemid 36569544)
    • (2003) Nature , vol.423 , Issue.6936 , pp. 190-193
    • Marshall, B.T.1    Long, M.2    Piper, J.W.3    Yago, T.4    McEver, R.P.5    Zhu, C.6
  • 21
    • 0031682733 scopus 로고    scopus 로고
    • Measuring two-dimensional receptor-ligand binding kinetics by micropipette
    • S.E. Chesla, P. Selvaraj, and C. Zhu Measuring two-dimensional receptor-ligand binding kinetics by micropipette Biophys. J. 75 1998 1553 1572 (Pubitemid 28397625)
    • (1998) Biophysical Journal , vol.75 , Issue.3 , pp. 1553-1572
    • Chesla, S.E.1    Selvaraj, P.2    Zhu, C.3
  • 23
    • 77950809538 scopus 로고    scopus 로고
    • The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness
    • J. Huang, and V.I. Zarnitsyna C. Zhu The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness Nature 464 2010 932 936
    • (2010) Nature , vol.464 , pp. 932-936
    • Huang, J.1    Zarnitsynazhu, C.V.I.2
  • 24
    • 0035544006 scopus 로고    scopus 로고
    • Kinetic measurements of cell surface E-selectin/carbohydrate ligand interactions
    • DOI 10.1114/1.1415529
    • M. Long, and H. Zhao C. Zhu Kinetic measurements of cell surface E-selectin/carbohydrate ligand interactions Ann. Biomed. Eng. 29 2001 935 946 (Pubitemid 34055195)
    • (2001) Annals of Biomedical Engineering , vol.29 , Issue.11 , pp. 935-946
    • Long, M.1    Zhao, H.2    Huang, K.-S.3    Zhu, C.4
  • 25
    • 34248222289 scopus 로고    scopus 로고
    • Impact of carrier stiffness and microtopology on two-dimensional kinetics of P-selectin and P-selectin glycoprotein ligand-1 (PSGL-1) interactions
    • DOI 10.1074/jbc.M609219200
    • L. Wu, and B.X. Xiao M. Long Impact of carrier stiffness and microtopology on two-dimensional kinetics of P-selectin and P-selectin glycoprotein ligand-1 (PSGL-1) interactions J. Biol. Chem. 282 2007 9846 9854 (Pubitemid 47104638)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.13 , pp. 9846-9854
    • Wu, L.1    Xiao, B.2    Jia, X.3    Zhang, Y.4    Lu, S.5    Chen, J.6    Long, M.7
  • 26
    • 0025115232 scopus 로고
    • Rapid neutrophil adhesion to activated endothelium mediated by GMP-140
    • J.G. Geng, and M.P. Bevilacqua R.P. McEver Rapid neutrophil adhesion to activated endothelium mediated by GMP-140 Nature 343 1990 757 760
    • (1990) Nature , vol.343 , pp. 757-760
    • Geng, J.G.1    Bevilacqua, M.P.2    McEver, R.P.3
  • 27
    • 0030801897 scopus 로고    scopus 로고
    • Soluble monomeric P-selectin containing only the lectin and epidermal growth factor domains binds to P-selectin glycoprotein ligand-1 on leukocytes
    • P. Mehta, and K.D. Patel R.P. McEver Soluble monomeric P-selectin containing only the lectin and epidermal growth factor domains binds to P-selectin glycoprotein ligand-1 on leukocytes Blood 90 1997 2381 2389 (Pubitemid 27392722)
    • (1997) Blood , vol.90 , Issue.6 , pp. 2381-2389
    • Mehta, P.1    Patel, K.D.2    Laue, T.M.3    Erickson, H.P.4    McEver, R.P.5
  • 28
    • 0029595303 scopus 로고
    • P-selectin must extend a sufficient length from the plasma membrane to mediate rolling of neutrophils
    • DOI 10.1083/jcb.131.6.1893
    • K.D. Patel, M.U. Nollert, and R.P. McEver P-selectin must extend a sufficient length from the plasma membrane to mediate rolling of neutrophils J. Cell Biol. 131 1995 1893 1902 (Pubitemid 26007984)
    • (1995) Journal of Cell Biology , vol.131 , Issue.6 , pp. 1893-1902
    • Patel, K.D.1    Nollert, M.U.2    McEver, R.P.3
  • 29
    • 0017401164 scopus 로고
    • Some methodologic aspects of the chromium chloride method for coupling antigen to erythrocytes
    • DOI 10.1016/0022-1759(77)90198-3
    • R. Kofler, and G. Wick Some methodologic aspects of the chromium chloride method for coupling antigen to erythrocytes J. Immunol. Methods 16 1977 201 209 (Pubitemid 8153152)
    • (1977) Journal of Immunological Methods , vol.16 , Issue.3 , pp. 201-209
    • Kofler, R.1    Wick, G.2
  • 30
    • 0023150401 scopus 로고
    • The T lymphocyte glycoprotein CD2 binds the cell surface ligand LFA-3
    • DOI 10.1038/326400a0
    • P. Selvaraj, and M.L. Plunkett T.A. Springer The T lymphocyte glycoprotein CD2 binds the cell surface ligand LFA-3 Nature 326 1987 400 403 (Pubitemid 17053770)
    • (1987) Nature , vol.326 , Issue.6111 , pp. 400-403
    • Selvaraj, P.1    Plunkett, M.L.2    Dustin, M.3
  • 31
    • 0033991340 scopus 로고    scopus 로고
    • Kinetics and mechanics of cell adhesion
    • C. Zhu Kinetics and mechanics of cell adhesion J. Biomech. 33 2000 23 33
    • (2000) J. Biomech. , vol.33 , pp. 23-33
    • Zhu, C.1
  • 32
    • 38349065134 scopus 로고    scopus 로고
    • Monitoring receptor-ligand interactions between surfaces by thermal fluctuations
    • W. Chen, and E.A. Evans C. Zhu Monitoring receptor-ligand interactions between surfaces by thermal fluctuations Biophys. J. 94 2008 694 701
    • (2008) Biophys. J. , vol.94 , pp. 694-701
    • Chen, W.1    Evanszhu, C.E.A.2
  • 34
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • A.D. MacKerell, and D. Bashford M. Karplus All-atom empirical potential for molecular modeling and dynamics studies of proteins J. Phys. Chem. B 102 1998 3586 3616
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1    Bashfordkarplus, M.D.2
  • 35
    • 33744461037 scopus 로고    scopus 로고
    • Forced dissociation of selectin-ligand complexes using steered molecular dynamics simulation
    • S.Q. Lü, and M. Long Forced dissociation of selectin-ligand complexes using steered molecular dynamics simulation Mol. Cell. Biomech. 2 2005 161 177 (Pubitemid 44794895)
    • (2005) MCB Molecular and Cellular Biomechanics , vol.2 , Issue.4 , pp. 161-177
    • Lu, S.1    Long, M.2
  • 37
    • 0034816999 scopus 로고    scopus 로고
    • Tyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin
    • S.D. Rodgers, R.T. Camphausen, and D.A. Hammer Tyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin Biophys. J. 81 2001 2001 2009 (Pubitemid 32917151)
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 2001-2009
    • Rodgers, S.D.1    Camphausen, R.T.2    Hammer, D.A.3
  • 39
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Z.S. Hendsch, and B. Tidor Do salt bridges stabilize proteins? A continuum electrostatic analysis Protein Sci. 3 1994 211 226 (Pubitemid 24086354)
    • (1994) Protein Science , vol.3 , Issue.2 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 40
    • 0032557503 scopus 로고    scopus 로고
    • Electrostatic enhancement of diffusion-controlled protein-protein association: Comparison of theory and experiment on barnase and barstar
    • DOI 10.1006/jmbi.1998.1747
    • M. Vijayakumar, and K.Y. Wong H.X. Zhou Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar J. Mol. Biol. 278 1998 1015 1024 (Pubitemid 28239701)
    • (1998) Journal of Molecular Biology , vol.278 , Issue.5 , pp. 1015-1024
    • Vijayakumar, M.1    Wong, K.-Y.2    Schreiber, G.3    Fersht, A.R.4    Szabo, A.5    Zhou, H.-X.6
  • 41
    • 0036082665 scopus 로고    scopus 로고
    • PIP(2) and proteins: Interactions, organization, and information flow
    • S. McLaughlin, and J. Wang D. Murray PIP(2) and proteins: interactions, organization, and information flow Annu. Rev. Biophys. Biomol. Struct. 31 2002 151 175
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 151-175
    • McLaughlin, S.1    Wangmurray, D.J.2
  • 42
    • 0029056922 scopus 로고
    • Energetics of protein-protein interactions: Analysis of the barnase-barstar interface by single mutations and double mutant cycles
    • G. Schreiber, and A.R. Fersht Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles J. Mol. Biol. 248 1995 478 486
    • (1995) J. Mol. Biol. , vol.248 , pp. 478-486
    • Schreiber, G.1    Fersht, A.R.2
  • 43
    • 58149359859 scopus 로고    scopus 로고
    • Low spring constant regulates P-selectin-PSGL-1 bond rupture
    • Y. Zhang, and G.Y. Sun M. Long Low spring constant regulates P-selectin-PSGL-1 bond rupture Biophys. J. 95 2008 5439 5448
    • (2008) Biophys. J. , vol.95 , pp. 5439-5448
    • Zhang, Y.1    Sunlong, M.G.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.