메뉴 건너뛰기




Volumn 7, Issue 6, 2013, Pages 486-491

Neutrophil integrin affinity regulation in adhesion, migration, and bacterial clearance

Author keywords

Adhesion; Gelsolin; Integrin; Migration; Neutrophil; Phagocytosis; Reverse migration

Indexed keywords

ACTIN; ACTIN CAPPING PROTEIN; ADAPTOR PROTEIN; ALPHA ACTININ; BETA1 INTEGRIN; BETA3 INTEGRIN; CD18 ANTIGEN; COMPLEMENT COMPONENT C3B; CYTOCHALASIN D; ENDOTHELIAL LEUKOCYTE ADHESION MOLECULE 1; FIBRINOGEN; G PROTEIN COUPLED RECEPTOR; GELSOLIN; IMMUNOGLOBULIN G; INTEGRIN; INTERCELLULAR ADHESION MOLECULE 1; INTERLEUKIN 8; JASPAMIDE; KINDLIN 3; LEUKOTRIENE B4; P SELECTIN GLYCOPROTEIN LIGAND 1; PADGEM PROTEIN; PAXILLIN; PROTEIN KINASE SYK; PROTEIN SRC; PROTEIN TYROSINE KINASE; TALIN; TALIN 1; TYROSINE; UNCLASSIFIED DRUG; VINCULIN;

EID: 84894488327     PISSN: 19336918     EISSN: 19336926     Source Type: Journal    
DOI: 10.4161/cam.27293     Document Type: Review
Times cited : (37)

References (47)
  • 1
    • 33750453714 scopus 로고    scopus 로고
    • Integrin ligands at a glance
    • PMID:16988024
    • Humphries JD, Byron A, Humphries MJ. Integrin ligands at a glance. J Cell Sci 2006; 119:39013; PMID:16988024; http://dx.doi.org/10.1242/jcs.03098
    • (2006) J Cell Sci , vol.119 , pp. 39013
    • Humphries, J.D.1    Byron, A.2    Humphries, M.J.3
  • 2
    • 0141756175 scopus 로고    scopus 로고
    • Integrin avidity regulation: Are changes in affinity and conformation underemphasized?
    • DOI 10.1016/j.ceb.2003.08.003
    • Carman CV, Springer TA. Integrin avidity regulation: are changes in affinity and conformation underemphasized? Curr Opin Cell Biol 2003; 15:547-56; PMID:14519389; http://dx.doi.org/10.1016/j.ceb.2003.08.003 (Pubitemid 37176963)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.5 , pp. 547-556
    • Carman, C.V.1    Springer, T.A.2
  • 3
    • 79957621253 scopus 로고    scopus 로고
    • The insider's guide to leukocyte integrin signalling and function
    • PMID:21597477
    • Hogg N, Patzak I, Willenbrock F. The insider's guide to leukocyte integrin signalling and function. Nat Rev Immunol 2011; 11:416-26; PMID:21597477; http://dx.doi.org/10.1038/nri2986
    • (2011) Nat Rev Immunol , vol.11 , pp. 416-426
    • Hogg, N.1    Patzak, I.2    Willenbrock, F.3
  • 4
    • 21844450244 scopus 로고    scopus 로고
    • Intracellular signalling controlling integrin activation in lymphocytes
    • DOI 10.1038/nri1646
    • Kinashi T. Intracellular signalling controlling integrin activation in lymphocytes. Nat Rev Immunol 2005; 5:546-59; PMID:15965491; http://dx.doi.org/ 10.1038/nri1646 (Pubitemid 40961332)
    • (2005) Nature Reviews Immunology , vol.5 , Issue.7 , pp. 546-559
    • Kinashi, T.1
  • 5
    • 77951737987 scopus 로고    scopus 로고
    • The switchable integrin adhesome
    • PMID:20410370
    • Zaidel-Bar R, Geiger B. The switchable integrin adhesome. J Cell Sci 2010; 123:1385-8; PMID:20410370; http://dx.doi.org/10.1242/jcs.066183
    • (2010) J Cell Sci , vol.123 , pp. 1385-1388
    • Zaidel-Bar, R.1    Geiger, B.2
  • 6
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • PMID:18278053
    • Moser M, Nieswandt B, Ussar S, Pozgajova M, Fässler R. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat Med 2008; 14:32530; PMID:18278053; http://dx.doi.org/10.1038/nm1722
    • (2008) Nat Med , vol.14 , pp. 32530
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fässler, R.5
  • 7
    • 0033213922 scopus 로고    scopus 로고
    • The talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation
    • PMID:10497155
    • Calderwood DA, Zent R, Grant R, Rees DJ, Hynes RO, Ginsberg MH. The Talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation. J Biol Chem 1999; 274:280714; PMID:10497155; http://dx.doi.org/10.1074/jbc.274.40.28071
    • (1999) J Biol Chem , vol.274 , pp. 280714
    • Calderwood, D.A.1    Zent, R.2    Grant, R.3    Rees, D.J.4    Hynes, R.O.5    Ginsberg, M.H.6
  • 8
    • 0035958967 scopus 로고    scopus 로고
    • Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain
    • PMID:11382782
    • Yan B, Calderwood DA, Yaspan B, Ginsberg MH. Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain. J Biol Chem 2001; 276:28164-70; PMID:11382782; http://dx.doi.org/10.1074/jbc.M104161200
    • (2001) J Biol Chem , vol.276 , pp. 28164-28170
    • Yan, B.1    Calderwood, D.A.2    Yaspan, B.3    Ginsberg, M.H.4
  • 10
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate
    • DOI 10.1038/381531a0
    • Gilmore AP, Burridge K. Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate. Nature 1996; 381:531-5; PMID:8632828; http://dx.doi.org/10.1038/381531a0 (Pubitemid 26170933)
    • (1996) Nature , vol.381 , Issue.6582 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 11
    • 0037049555 scopus 로고    scopus 로고
    • Recruitment of the Arp2/3 complex to vinculin: Coupling membrane protrusion to matrix adhesion
    • DOI 10.1083/jcb.200206043
    • DeMali KA, Barlow CA, Burridge K. Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J Cell Biol 2002; 159:881-91; PMID:12473693; http://dx.doi.org/10.1083/jcb.200206043 (Pubitemid 36008369)
    • (2002) Journal of Cell Biology , vol.159 , Issue.5 , pp. 881-891
    • DeMali, K.A.1    Barlow, C.A.2    Burridge, K.3
  • 12
    • 61949352480 scopus 로고    scopus 로고
    • Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells
    • PMID:19234461
    • Moser M, Bauer M, Schmid S, Ruppert R, Schmidt S, Sixt M, Wang HV, Sperandio M, Fässler R. Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells. Nat Med 2009; 15:3005; PMID:19234461; http://dx.doi.org/10.1038/nm.1921
    • (2009) Nat Med , vol.15 , pp. 3005
    • Moser, M.1    Bauer, M.2    Schmid, S.3    Ruppert, R.4    Schmidt, S.5    Sixt, M.6    Wang, H.V.7    Sperandio, M.8    Fässler, R.9
  • 14
    • 42449160630 scopus 로고    scopus 로고
    • Integrin connections to the cytoskeleton through talin and vinculin
    • PMID:18363566
    • Ziegler WH, Gingras AR, Critchley DR, Emsley J. Integrin connections to the cytoskeleton through talin and vinculin. Biochem Soc Trans 2008; 36:2359; PMID:18363566; http://dx.doi.org/10.1042/BST0360235
    • (2008) Biochem Soc Trans , vol.36 , pp. 2359
    • Ziegler, W.H.1    Gingras, A.R.2    Critchley, D.R.3    Emsley, J.4
  • 15
    • 0033539801 scopus 로고    scopus 로고
    • 4 integrins modifies integrin-dependent biological responses
    • Liu S, Thomas SM, Woodside DG, Rose DM, Kiosses WB, Pfaff M, Ginsberg MH. Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses. Nature 1999; 402:676-81; PMID:10604475; http://dx.doi.org/10.1038/ 45264 (Pubitemid 129516339)
    • (1999) Nature , vol.402 , Issue.6762 , pp. 676-681
    • Liu, S.1    Thomas, S.M.2    Woodside, D.G.3    Rose, D.M.4    Klosses, W.B.5    Pfaff, M.6    Ginsberg, M.H.7
  • 16
    • 0032509204 scopus 로고    scopus 로고
    • Cytoskeletal interactions with the leukocyte integrin beta2 cytoplasmic tail. Activation-dependent regulation of associations with talin and alpha-actinin
    • PMID:9837942
    • Sampath R, Gallagher PJ, Pavalko FM. Cytoskeletal interactions with the leukocyte integrin beta2 cytoplasmic tail. Activation-dependent regulation of associations with talin and alpha-actinin. J Biol Chem 1998; 273:33588-94; PMID:9837942; http://dx.doi.org/10.1074/jbc.273.50.33588
    • (1998) J Biol Chem , vol.273 , pp. 33588-33594
    • Sampath, R.1    Gallagher, P.J.2    Pavalko, F.M.3
  • 17
    • 84880699172 scopus 로고    scopus 로고
    • Gelsolin expression increases ?1 -integrin affinity and l1210 cell adhesion
    • PMID:23595955
    • Langereis JD, Koenderman L, Huttenlocher A, Ulfman LH. Gelsolin expression increases ?1 -integrin affinity and L1210 cell adhesion. Cytoskeleton (Hoboken) 2013; 70:385-93; PMID:23595955; http://dx.doi.org/10.1002/cm.21112
    • (2013) Cytoskeleton (Hoboken) , vol.70 , pp. 385-393
    • Langereis, J.D.1    Koenderman, L.2    Huttenlocher, A.3    Ulfman, L.H.4
  • 19
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5 bisphosphate
    • DOI 10.1038/325362a0
    • Janmey PA, Stossel TP. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature 1987; 325:362-4; PMID:3027569; http://dx.doi.org/10.1038/325362a0 (Pubitemid 17053178)
    • (1987) Nature , vol.325 , Issue.6102 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 20
    • 0033520421 scopus 로고    scopus 로고
    • The platelet cytoskeleton regulates the affinity of the integrin alpha(iib)beta( 3) for fibrinogen
    • PMID:10464255
    • Bennett JS, Zigmond S, Vilaire G, Cunningham ME, Bednar B. The platelet cytoskeleton regulates the affinity of the integrin alpha(IIb)beta(3) for fibrinogen. J Biol Chem 1999; 274:25301-7; PMID:10464255; http://dx.doi.org/10. 1074/jbc.274.36.25301
    • (1999) J Biol Chem , vol.274 , pp. 25301-25307
    • Bennett, J.S.1    Zigmond, S.2    Vilaire, G.3    Cunningham, M.E.4    Bednar, B.5
  • 21
    • 0031590265 scopus 로고    scopus 로고
    • Actin polymerisation regulates integrin-mediated adhesion as well as rigidity of neutrophils
    • DOI 10.1006/bbrc.1997.7407
    • Sheikh S, Gratzer WB, Pinder JC, Nash GB. Actin polymerisation regulates integrin-mediated adhesion as well as rigidity of neutrophils. Biochem Biophys Res Commun 1997; 238:910-5; PMID:9325191; http://dx.doi.org/10.1006/bbrc.1997. 7407 (Pubitemid 27472676)
    • (1997) Biochemical and Biophysical Research Communications , vol.238 , Issue.3 , pp. 910-915
    • Sheikh, S.1    Gratzer, W.B.2    Pinder, J.C.3    Nash, G.B.4
  • 22
    • 0033578822 scopus 로고    scopus 로고
    • The actin cytoskeleton regulates lfa-1 ligand binding through avidity rather than affinity changes
    • PMID:10480895
    • van Kooyk Y, van Vliet SJ, Figdor CG. The actin cytoskeleton regulates LFA-1 ligand binding through avidity rather than affinity changes. J Biol Chem 1999; 274:26869-77; PMID:10480895; http://dx.doi.org/10.1074/jbc.274.38.26869
    • (1999) J Biol Chem , vol.274 , pp. 26869-26877
    • Van Kooyk, Y.1    Van Vliet, S.J.2    Figdor, C.G.3
  • 23
    • 0030840113 scopus 로고    scopus 로고
    • Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding
    • DOI 10.1084/jem.186.8.1347
    • Yauch RL, Felsenfeld DP, Kraeft SK, Chen LB, Sheetz MP, Hemler ME. Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding. J Exp Med 1997; 186:1347-55; PMID:9334374; http://dx.doi.org/10.1084/jem.186.8.1347 (Pubitemid 27469030)
    • (1997) Journal of Experimental Medicine , vol.186 , Issue.8 , pp. 1347-1355
    • Yauch, R.L.1    Felsenfeld, D.P.2    Kraeft, S.-K.3    Chen, L.B.4    Sheetz, M.P.5    Hemler, M.E.6
  • 25
    • 67649255876 scopus 로고    scopus 로고
    • A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish
    • PMID:19494811
    • Niethammer P, Grabher C, Look AT, Mitchison TJ. A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish. Nature 2009; 459:996-9; PMID:19494811; http://dx.doi.org/10.1038/nature08119
    • (2009) Nature , vol.459 , pp. 996-999
    • Niethammer, P.1    Grabher, C.2    Look, A.T.3    Mitchison, T.J.4
  • 28
    • 84875442814 scopus 로고    scopus 로고
    • Neutrophil recruitment and function in health and inflammation
    • PMID:23435331
    • Kolaczkowska E, Kubes P. Neutrophil recruitment and function in health and inflammation. Nat Rev Immunol 2013; 13:159-75; PMID:23435331; http://dx.doi.org/10.1038/nri3399
    • (2013) Nat Rev Immunol , vol.13 , pp. 159-175
    • Kolaczkowska, E.1    Kubes, P.2
  • 29
    • 0030614512 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and Fc receptor-mediated phagocytosis
    • DOI 10.1016/S0014-5793(96)01359-2, PII S0014579396013592
    • Strzelecka A, Kwiatkowska K, Sobota A. Tyrosine phosphorylation and Fcgamma receptor-mediated phagocytosis. FEBS Lett 1997; 400:11-4; PMID:9000504; http://dx.doi.org/10.1016/S0014-5793(96)01359-2 (Pubitemid 27046812)
    • (1997) FEBS Letters , vol.400 , Issue.1 , pp. 11-14
    • Strzelecka, A.1    Kwiatkowska, K.2    Sobota, A.3
  • 30
    • 0025001451 scopus 로고
    • Unusual expression of IgG Fc receptors on peripheral granulocytes from patients with leukocyte adhesion deficiency (CD11/CD18 deficiency)
    • Majima T, Minegishi N, Nagatomi R, Ohashi Y, Tsuchiya S, Kobayashi K, Konno T. Unusual expression of IgG Fc receptors on peripheral granulocytes from patients with leukocyte adhesion deficiency (CD11/CD18 deficiency). J Immunol 1990; 145:1694-9; PMID:2167908 (Pubitemid 20336731)
    • (1990) Journal of Immunology , vol.145 , Issue.6 , pp. 1694-1699
    • Majima, T.1    Minegishi, N.2    Nagatomi, R.3    Ohashi, Y.4    Tsuchiya, S.5    Kobayashi, K.6    Konno, T.7
  • 31
    • 0023850274 scopus 로고
    • Mechanism of inhibition of immunoglobulin g-mediated phagocytosis by monoclonal antibodies that recognize the mac-1 antigen
    • PMID:2963020
    • Brown EJ, Bohnsack JF, Gresham HD. Mechanism of inhibition of immunoglobulin G-mediated phagocytosis by monoclonal antibodies that recognize the Mac-1 antigen. J Clin Invest 1988; 81:36575; PMID:2963020; http://dx.doi.org/10.1172/JCI113328
    • (1988) J Clin Invest , vol.81 , pp. 36575
    • Brown, E.J.1    Bohnsack, J.F.2    Gresham, H.D.3
  • 32
    • 0242580737 scopus 로고    scopus 로고
    • Fc-receptors Induce Mac-1 (CD11b/CD18) Mobilization and Accumulation in the Phagocytic Cup for Optimal Phagocytosis
    • DOI 10.1074/jbc.M303704200
    • Jongstra-Bilen J, Harrison R, Grinstein S. Fcgammareceptors induce Mac-1 (CD11b/CD18) mobilization and accumulation in the phagocytic cup for optimal phagocytosis. J Biol Chem 2003; 278:45720-9; PMID:12941957; http://dx.doi.org/ 10.1074/jbc. M303704200 (Pubitemid 37432715)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45720-45729
    • Jongstra-Bilen, J.1    Harrison, R.2    Grinstein, S.3
  • 33
    • 33845383033 scopus 로고    scopus 로고
    • Resolution of inflammation by retrograde chemotaxis of neutrophils in transgenic zebrafish
    • DOI 10.1189/jlb.0506346
    • Mathias JR, Perrin BJ, Liu TX, Kanki J, Look AT, Huttenlocher A. Resolution of inflammation by retrograde chemotaxis of neutrophils in transgenic zebrafish. J Leukoc Biol 2006; 80:1281-8; PMID:16963624; http://dx.doi.org/10. 1189/jlb.0506346 (Pubitemid 44904967)
    • (2006) Journal of Leukocyte Biology , vol.80 , Issue.6 , pp. 1281-1288
    • Mathias, J.R.1    Perrin, B.J.2    Liu, T.-X.3    Kanki, J.4    Look, A.T.5    Huttenlocher, A.6
  • 34
    • 33646440505 scopus 로고    scopus 로고
    • Identification of a phenotypically and functionally distinct population of long-lived neutrophils in a model of reverse endothelial migration
    • PMID:16330528
    • Buckley CD, Ross EA, McGettrick HM, Osborne CE, Haworth O, Schmutz C, Stone PC, Salmon M, Matharu NM, Vohra RK, et al. Identification of a phenotypically and functionally distinct population of long-lived neutrophils in a model of reverse endothelial migration. J Leukoc Biol 2006; 79:30311; PMID:16330528; http://dx.doi.org/10.1189/jlb.0905496
    • (2006) J Leukoc Biol , vol.79 , pp. 30311
    • Buckley, C.D.1    Ross, E.A.2    McGettrick, H.M.3    Osborne, C.E.4    Haworth, O.5    Schmutz, C.6    Stone, P.C.7    Salmon, M.8    Matharu, N.M.9    Vohra, R.K.10
  • 37
    • 33751291963 scopus 로고    scopus 로고
    • Presence of neutrophil-bearing antigen in lymphoid organs of immune mice
    • DOI 10.1182/blood-2006-04-016659
    • Maletto BA, Ropolo AS, Alignani DO, Liscovsky MV, Ranocchia RP, Moron VG, Pistoresi-Palencia MC. Presence of neutrophil-bearing antigen in lymphoid organs of immune mice. Blood 2006; 108:3094-102; PMID:16835380; http://dx.doi.org/10.1182/blood-2006-04-016659 (Pubitemid 44794225)
    • (2006) Blood , vol.108 , Issue.9 , pp. 3094-3102
    • Maletto, B.A.1    Ropolo, A.S.2    Alignani, D.O.3    Liscovsky, M.V.4    Ranocchia, R.P.5    Moron, V.G.6    Pistoresi-Palencia, M.C.7
  • 38
    • 0018883785 scopus 로고
    • An inherited abnormality of neutrophil adhesion. Its genetic transmission and its association with a missing protein
    • Crowley CA, Curnutte JT, Rosin RE, AndreSchwartz J, Gallin JI, Klempner M, Snyderman R, Southwick FS, Stossel TP, Babior BM. An inherited abnormality of neutrophil adhesion. Its genetic transmission and its association with a missing protein. N Engl J Med 1980; 302:1163-8; PMID:7366657; http://dx.doi.org/10.1056/NEJM198005223022102 (Pubitemid 10109970)
    • (1980) New England Journal of Medicine , vol.302 , Issue.21 , pp. 1163-1168
    • Crowley, C.A.1    Curnutte, J.T.2    Rosin, R.E.3
  • 39
    • 0026448082 scopus 로고
    • Brief report: Recurrent severe infections caused by a novel leukocyte adhesion deficiency
    • PMID:1279426
    • Etzioni A, Frydman M, Pollack S, Avidor I, Phillips ML, Paulson JC, Gershoni-Baruch R. Brief report: recurrent severe infections caused by a novel leukocyte adhesion deficiency. N Engl J Med 1992; 327:178992; PMID:1279426; http://dx.doi.org/10.1056/NEJM199212173272505
    • (1992) N Engl J Med , vol.327 , pp. 178992
    • Etzioni, A.1    Frydman, M.2    Pollack, S.3    Avidor, I.4    Phillips, M.L.5    Paulson, J.C.6    Gershoni-Baruch, R.7
  • 43
    • 0026520089 scopus 로고
    • Leukocyte adhesion deficiency: Clinical and postmortem observations
    • PMID:1348581
    • Hawkins HK, Heffelfinger SC, Anderson DC. Leukocyte adhesion deficiency: clinical and postmortem observations. Pediatr Pathol 1992; 12:119-30; PMID:1348581; http://dx.doi.org/10.3109/15513819209023288
    • (1992) Pediatr Pathol , vol.20 , pp. 119-130
    • Hawkins, H.K.1    Heffelfinger, S.C.2    Anderson, D.C.3
  • 44
    • 0025230704 scopus 로고
    • CD18-dependent and -independent mechanisms of neutrophil emigration in the pulmonary and systemic microcirculation of rabbits
    • Doerschuk CM, Winn RK, Coxson HO, Harlan JM. CD18-dependent and -independent mechanisms of neutrophil emigration in the pulmonary and systemic microcirculation of rabbits. J Immunol 1990; 144:2327-33; PMID:1968927 (Pubitemid 20106576)
    • (1990) Journal of Immunology , vol.144 , Issue.6 , pp. 2327-2333
    • Doerschuk, C.M.1    Winn, R.K.2    Coxson, H.O.3    Harlan, J.M.4
  • 45
    • 0030731918 scopus 로고    scopus 로고
    • Neutrophil emigration in the skin, lungs, and peritoneum: Different requirements for CD11/CD18 revealed by CD18-deficient mice
    • DOI 10.1084/jem.186.8.1357
    • Mizgerd JP, Kubo H, Kutkoski GJ, Bhagwan SD, Scharffetter-Kochanek K, Beaudet AL, Doerschuk CM. Neutrophil emigration in the skin, lungs, and peritoneum: different requirements for CD11/CD18 revealed by CD18-deficient mice. J Exp Med 1997; 186:1357-64; PMID:9334375; http://dx.doi.org/10.1084/jem. 186.8.1357 (Pubitemid 27469031)
    • (1997) Journal of Experimental Medicine , vol.186 , Issue.8 , pp. 1357-1364
    • Mizgerd, J.P.1    Kubo, H.2    Kutkoski, G.J.3    Bhagwan, S.D.4    Scharffetter-Kochanek, K.5    Beaudet, A.L.6    Doerschuk, C.M.7
  • 46
    • 0021150435 scopus 로고
    • Abnormalities of polymorphonuclear leukocyte function associated with a heritable deficiency of high molecular weight surface glycoproteins (GP 138): Common relationship to diminished cell adherence
    • Anderson DC, Schmalstieg FC, Arnaout MA, Kohl S, Tosi MF, Dana N, Buffone GJ, Hughes BJ, Brinkley BR, Dickey WD, et al. Abnormalities of polymorphonuclear leukocyte function associated with a heritable deficiency of high molecular weight surface glycoproteins (GP138): common relationship to diminished cell adherence. J Clin Invest 1984; 74:536-51; PMID:6746906; http://dx.doi.org/10.1172/JCI111451 (Pubitemid 14054002)
    • (1984) Journal of Clinical Investigation , vol.74 , Issue.2 , pp. 536-551
    • Anderson, D.C.1    Schmalstieg, F.C.2    Arnaout, M.A.3
  • 47
    • 0025879691 scopus 로고
    • Leukocyte adhesion-deficient neutrophils fail to amplify phagocytic function in response to stimulation. Evidence for cd11b/cd18-dependent and -independent mechanisms of phagocytosis
    • PMID:1677946
    • Gresham HD, Graham IL, Anderson DC, Brown EJ. Leukocyte adhesion-deficient neutrophils fail to amplify phagocytic function in response to stimulation. Evidence for CD11b/CD18-dependent and -independent mechanisms of phagocytosis. J Clin Invest 1991; 88:588-97; PMID:1677946; http://dx.doi.org/ 10.1172/JCI115343
    • (1991) J Clin Invest , vol.88 , pp. 588-597
    • Gresham, H.D.1    Graham, I.L.2    Anderson, D.C.3    Brown, E.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.