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Volumn 107, Issue 10, 2006, Pages 4149-4158

CD44 is a phagocytic receptor

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; FC RECEPTOR; GUANOSINE TRIPHOSPHATASE; HERMES ANTIGEN; HYALURONIC ACID; IMMUNOGLOBULIN G; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE SYK; RAC1 PROTEIN;

EID: 33646559230     PISSN: 00064971     EISSN: 00064971     Source Type: Journal    
DOI: 10.1182/blood-2005-09-3808     Document Type: Article
Times cited : (123)

References (90)
  • 2
    • 0025641883 scopus 로고
    • The hyaluronate receptor is a member of the CD44 (H-CAM) family of cell surface glycoproteins
    • Culty M, Miyake K, Kincade PW, et al. The hyaluronate receptor is a member of the CD44 (H-CAM) family of cell surface glycoproteins. J Cell Biol. 1990;111:2765-2774.
    • (1990) J Cell Biol , vol.111 , pp. 2765-2774
    • Culty, M.1    Miyake, K.2    Kincade, P.W.3
  • 3
    • 0037155805 scopus 로고    scopus 로고
    • A requirement for the CD44 cytoplasmic domain for hyaluronan binding, pericellular matrix assembly, and receptor-mediated endocytosis in COS-7 cells
    • Jiang H, Peterson RS, Wang W, Bartnik E, Knudson CB, Knudson W. A requirement for the CD44 cytoplasmic domain for hyaluronan binding, pericellular matrix assembly, and receptor-mediated endocytosis in COS-7 cells. J Biol Chem. 2002;277:10531-10538.
    • (2002) J Biol Chem , vol.277 , pp. 10531-10538
    • Jiang, H.1    Peterson, R.S.2    Wang, W.3    Bartnik, E.4    Knudson, C.B.5    Knudson, W.6
  • 4
    • 0027065573 scopus 로고
    • Genomic structure of DNA encoding the lymphocyte homing receptor CD44 reveals at least 12 alternatively spliced exons
    • U S A
    • Screaton GR, Bell MV, Jackson DG, Cornelis FB, Gerth U, Bell JI. Genomic structure of DNA encoding the lymphocyte homing receptor CD44 reveals at least 12 alternatively spliced exons. Proc Natl Acad Sci U S A. 1992;89:12160-12164.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 12160-12164
    • Screaton, G.R.1    Bell, M.V.2    Jackson, D.G.3    Cornelis, F.B.4    Gerth, U.5    Bell, J.I.6
  • 5
    • 0028985177 scopus 로고
    • CD44 isoforms containing exon V3 are responsible for the presentation of heparin-binding growth factor
    • Bennett KL, Jackson DG, Simon JC, et al. CD44 isoforms containing exon V3 are responsible for the presentation of heparin-binding growth factor. J Cell Biol. 1995;128:687-698.
    • (1995) J Cell Biol , vol.128 , pp. 687-698
    • Bennett, K.L.1    Jackson, D.G.2    Simon, J.C.3
  • 6
    • 0028809263 scopus 로고
    • Proteoglycan forms of the lymphocyte homing receptor CD44 are alternatively spliced variants containing the v3 exon
    • Jackson DG, Bell JI, Dickinson R, Timans J, Shields J, Whittle N. Proteoglycan forms of the lymphocyte homing receptor CD44 are alternatively spliced variants containing the v3 exon. J Cell Biol. 1995;128:673-685.
    • (1995) J Cell Biol , vol.128 , pp. 673-685
    • Jackson, D.G.1    Bell, J.I.2    Dickinson, R.3    Timans, J.4    Shields, J.5    Whittle, N.6
  • 7
    • 0025949195 scopus 로고
    • Post-translational protein modification and expression of ankyrin-binding site(s) in GP85 (Pgp-1/CD44) and its biosynthetic precursors during T-lymphoma membrane biosynthesis
    • Lokeshwar VB, Bourguignon LY. Post-translational protein modification and expression of ankyrin-binding site(s) in GP85 (Pgp-1/CD44) and its biosynthetic precursors during T-lymphoma membrane biosynthesis. J Biol Chem. 1991;266:17983-17989.
    • (1991) J Biol Chem , vol.266 , pp. 17983-17989
    • Lokeshwar, V.B.1    Bourguignon, L.Y.2
  • 8
    • 0032567715 scopus 로고    scopus 로고
    • Glycosylation provides both stimulatory and inhibitory effects on cell surface and soluble CD44 binding to hyaluronan
    • Skelton TP, Zeng C, Nocks A, Stamenkovic I. Glycosylation provides both stimulatory and inhibitory effects on cell surface and soluble CD44 binding to hyaluronan. J Cell Biol. 1998;140:431-446.
    • (1998) J Cell Biol , vol.140 , pp. 431-446
    • Skelton, T.P.1    Zeng, C.2    Nocks, A.3    Stamenkovic, I.4
  • 9
    • 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.
    • (1992) J Cell Biol , vol.116 , pp. 817-825
    • Jalkanen, S.1    Jalkanen, M.2
  • 10
    • 0026592507 scopus 로고
    • A cell surface chondroitin sulfate proteoglycan, immunologically related to CD44, is involved in type I collagen-mediated melanoma cell motility and invasion
    • Faassen AE, Schrager JA, Klein DJ, Oegema TR, Couchman JR, McCarthy JB. A cell surface chondroitin sulfate proteoglycan, immunologically related to CD44, is involved in type I collagen-mediated melanoma cell motility and invasion. J Cell Biol. 1992;116:521-531.
    • (1992) J Cell Biol , vol.116 , pp. 521-531
    • Faassen, A.E.1    Schrager, J.A.2    Klein, D.J.3    Oegema, T.R.4    Couchman, J.R.5    McCarthy, J.B.6
  • 11
    • 0029861970 scopus 로고    scopus 로고
    • Acute lung injury fibroblast migration and invasion of a fibrin matrix is mediated by CD44
    • Svee K, White J, Vaillant P, et al. Acute lung injury fibroblast migration and invasion of a fibrin matrix is mediated by CD44. J Clin Invest. 1996;98:1713-1727.
    • (1996) J Clin Invest , vol.98 , pp. 1713-1727
    • Svee, K.1    White, J.2    Vaillant, P.3
  • 12
    • 0029949785 scopus 로고    scopus 로고
    • CD44-related chondroitin sulfate proteoglycan, a cell surface receptor implicated with tumor cell invasion, mediates endothelial cell migration on fibrinogen and invasion into a fibrin matrix
    • Henke CA, Roongta U, Mickelson DJ, Knutson JR, McCarthy JB. CD44-related chondroitin sulfate proteoglycan, a cell surface receptor implicated with tumor cell invasion, mediates endothelial cell migration on fibrinogen and invasion into a fibrin matrix. J Clin Invest. 1996;97:2541-2552.
    • (1996) J Clin Invest , vol.97 , pp. 2541-2552
    • Henke, C.A.1    Roongta, U.2    Mickelson, D.J.3    Knutson, J.R.4    McCarthy, J.B.5
  • 13
    • 0028965095 scopus 로고
    • A novel ligand for CD44 is serglycin, a hematopoietic cell lineage-specific proteoglycan. Possible involvement in lymphoid cell adherence and activation
    • Toyama-Sorimachi N, Sorimachi H, Tobita Y, et al. A novel ligand for CD44 is serglycin, a hematopoietic cell lineage-specific proteoglycan. Possible involvement in lymphoid cell adherence and activation. J Biol Chem. 1995;270:7437-7444.
    • (1995) J Biol Chem , vol.270 , pp. 7437-7444
    • Toyama-Sorimachi, N.1    Sorimachi, H.2    Tobita, Y.3
  • 14
    • 0030064334 scopus 로고    scopus 로고
    • Receptor-ligand interaction between CD44 and osteopontin (Eta-1)
    • Weber GF, Ashkar S, Glimcher MJ, Cantor H. Receptor-ligand interaction between CD44 and osteopontin (Eta-1). Science. 1996;271:509-512.
    • (1996) Science , vol.271 , pp. 509-512
    • Weber, G.F.1    Ashkar, S.2    Glimcher, M.J.3    Cantor, H.4
  • 15
    • 0028999063 scopus 로고
    • Adhesive interactions between alternatively spliced CD44 isoforms
    • Droll A, Dougherty ST, Chiu RK, et al. Adhesive interactions between alternatively spliced CD44 isoforms. J Biol Chem. 1995;270:11567-11573.
    • (1995) J Biol Chem , vol.270 , pp. 11567-11573
    • Droll, A.1    Dougherty, S.T.2    Chiu, R.K.3
  • 16
    • 0027197441 scopus 로고
    • Antibody-induced activation of the hyaluronan receptor function of CD44 requires multivalent binding by antibody
    • Lesley J, Kincade PW, Hyman R. Antibody-induced activation of the hyaluronan receptor function of CD44 requires multivalent binding by antibody. Eur J Immunol. 1993;23:1902-1909.
    • (1993) Eur J Immunol , vol.23 , pp. 1902-1909
    • Lesley, J.1    Kincade, P.W.2    Hyman, R.3
  • 17
    • 0037023364 scopus 로고    scopus 로고
    • Resolution of lung inflammation by CD44
    • Teder P, Vandivier RW, Jiang D, et al. Resolution of lung inflammation by CD44. Science. 2002;296:155-158.
    • (2002) Science , vol.296 , pp. 155-158
    • Teder, P.1    Vandivier, R.W.2    Jiang, D.3
  • 18
    • 9544242738 scopus 로고    scopus 로고
    • Involvement of CD44 and the cytoskeletal linker protein ankyrin in human neutrophil bacterial phagocytosis
    • Moffat FL Jr, Han T, Li ZM, et al. Involvement of CD44 and the cytoskeletal linker protein ankyrin in human neutrophil bacterial phagocytosis. J Cell Physiol. 1996;168:638-647.
    • (1996) J Cell Physiol , vol.168 , pp. 638-647
    • Moffat Jr., F.L.1    Han, T.2    Li, Z.M.3
  • 19
    • 0031570880 scopus 로고    scopus 로고
    • CD44 regulates phagocytosis of apoptotic neutrophil granulocytes, but not apoptotic lymphocytes, by human macrophages
    • Hart SP, Dougherty GJ, Haslett C, Dransfield I. CD44 regulates phagocytosis of apoptotic neutrophil granulocytes, but not apoptotic lymphocytes, by human macrophages. J Immunol. 1997;159:919-925.
    • (1997) J Immunol , vol.159 , pp. 919-925
    • Hart, S.P.1    Dougherty, G.J.2    Haslett, C.3    Dransfield, I.4
  • 20
    • 6344258651 scopus 로고    scopus 로고
    • Phagocytosis of apoptotic eosinophils but not neutrophils by bronchial epithelial cells
    • Sexton DW, Al-Rabia M, Blaylock MG, Walsh GM. Phagocytosis of apoptotic eosinophils but not neutrophils by bronchial epithelial cells. Clin Exp Allergy. 2004;34:1514-1524.
    • (2004) Clin Exp Allergy , vol.34 , pp. 1514-1524
    • Sexton, D.W.1    Al-Rabia, M.2    Blaylock, M.G.3    Walsh, G.M.4
  • 21
    • 9644280855 scopus 로고    scopus 로고
    • Divalent cation-dependent and -independent augmentation of macrophage phagocytosis of apoptotic neutrophils by CD44 antibody
    • Vivers S, Heasman SJ, Hart SP, Dransfield I. Divalent cation-dependent and -independent augmentation of macrophage phagocytosis of apoptotic neutrophils by CD44 antibody. Clin Exp Immunol. 2004;138:447-452.
    • (2004) Clin Exp Immunol , vol.138 , pp. 447-452
    • Vivers, S.1    Heasman, S.J.2    Hart, S.P.3    Dransfield, I.4
  • 22
    • 0035969239 scopus 로고    scopus 로고
    • Tethering and tickling: A new role for the phosphatidylserine receptor
    • Somersan S, Bhardwaj N. Tethering and tickling: a new role for the phosphatidylserine receptor. J Cell Biol. 2001;155:501-504.
    • (2001) J Cell Biol , vol.155 , pp. 501-504
    • Somersan, S.1    Bhardwaj, N.2
  • 23
    • 0141452262 scopus 로고    scopus 로고
    • Phosphoinositide involvement in phagocytosis and phagosome maturation
    • Botelho RJ, Scott CC, Grinstein S. Phosphoinositide involvement in phagocytosis and phagosome maturation. Curr Top Microbiol Immunol. 2004;282:1-30.
    • (2004) Curr Top Microbiol Immunol , vol.282 , pp. 1-30
    • Botelho, R.J.1    Scott, C.C.2    Grinstein, S.3
  • 24
    • 3142514390 scopus 로고    scopus 로고
    • Signaling and membrane dynamics during phagocytosis: Many roads lead to the phagos(R)ome
    • Niedergang F, Chavrier P. Signaling and membrane dynamics during phagocytosis: many roads lead to the phagos(R)ome. Curr Opin Cell Biol. 2004;16:422-428.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 422-428
    • Niedergang, F.1    Chavrier, P.2
  • 25
    • 19344363325 scopus 로고    scopus 로고
    • Phagocytosis: Elegant complexity
    • Stuart LM, Ezekowitz RA. Phagocytosis: elegant complexity. Immunity. 2005;22:539-550.
    • (2005) Immunity , vol.22 , pp. 539-550
    • Stuart, L.M.1    Ezekowitz, R.A.2
  • 26
    • 0038373277 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase SHP-2 regulates interleukin-1-induced ERK activation in fibroblasts
    • MacGillivray M, Herrera-Abreu MT, Chow CW, et al. The protein tyrosine phosphatase SHP-2 regulates interleukin-1-induced ERK activation in fibroblasts. J Biol Chem. 2003;278:27190-27198.
    • (2003) J Biol Chem , vol.278 , pp. 27190-27198
    • MacGillivray, M.1    Herrera-Abreu, M.T.2    Chow, C.W.3
  • 27
    • 0035969234 scopus 로고    scopus 로고
    • Phosphatidylserine (PS) induces PS receptor-mediated macropinocytosis and promotes clearance of apoptotic cells
    • Hoffmann PR, deCathelineau AM, Ogden CA, et al. Phosphatidylserine (PS) induces PS receptor-mediated macropinocytosis and promotes clearance of apoptotic cells. J Cell Biol. 2001;155:649-659.
    • (2001) J Cell Biol , vol.155 , pp. 649-659
    • Hoffmann, P.R.1    Decathelineau, A.M.2    Ogden, C.A.3
  • 28
    • 9444238519 scopus 로고    scopus 로고
    • Rac1 is the small GTPase responsible for regulating the neutrophil chemotaxis compass
    • Sun CX, Downey GP, Zhu F, Koh AL, Thang H, Glogauer M. Rac1 is the small GTPase responsible for regulating the neutrophil chemotaxis compass. Blood. 2004;104:3758-3765.
    • (2004) Blood , vol.104 , pp. 3758-3765
    • Sun, C.X.1    Downey, G.P.2    Zhu, F.3    Koh, A.L.4    Thang, H.5    Glogauer, M.6
  • 29
    • 0033213982 scopus 로고    scopus 로고
    • Phagosomal maturation, acidification, and inhibition of bacterial growth in nonphagocytic cells transfected with FcgammaRIIA receptors
    • Downey GP, Botelho RJ, Butler JR, et al. Phagosomal maturation, acidification, and inhibition of bacterial growth in nonphagocytic cells transfected with FcgammaRIIA receptors. J Biol Chem. 1999;274:28436-28444.
    • (1999) J Biol Chem , vol.274 , pp. 28436-28444
    • Downey, G.P.1    Botelho, R.J.2    Butler, J.R.3
  • 30
    • 0034670005 scopus 로고    scopus 로고
    • Deficiency of Src homology 2-containing phosphatase 1 results in abnormalities in murine neutrophil function: Studies in motheaten mice
    • Kruger J, Butler JR, Cherapanov V, et al. Deficiency of Src homology 2-containing phosphatase 1 results in abnormalities in murine neutrophil function: studies in motheaten mice. J Immunol. 2000;165:5847-5859.
    • (2000) J Immunol , vol.165 , pp. 5847-5859
    • Kruger, J.1    Butler, J.R.2    Cherapanov, V.3
  • 31
    • 0028065619 scopus 로고
    • Potentiation of the oxidative burst of human neutrophils. A signaling role for L-selectin
    • Waddell TK, Fialkow L, Chan CK, Kishimoto TK, Downey GP. Potentiation of the oxidative burst of human neutrophils. A signaling role for L-selectin. J Biol Chem. 1994;269:18485-18491.
    • (1994) J Biol Chem , vol.269 , pp. 18485-18491
    • Waddell, T.K.1    Fialkow, L.2    Chan, C.K.3    Kishimoto, T.K.4    Downey, G.P.5
  • 33
    • 0035205569 scopus 로고    scopus 로고
    • Phagocytic signaling strategies: Fc(gamma)receptor-mediated phagocytosis as a model system
    • Cox D, Greenberg S. Phagocytic signaling strategies: Fc(gamma)receptor- mediated phagocytosis as a model system. Semin Immunol. 2001;13:339-345.
    • (2001) Semin Immunol , vol.13 , pp. 339-345
    • Cox, D.1    Greenberg, S.2
  • 34
    • 0842330365 scopus 로고    scopus 로고
    • Phagocytosis of opsonized apoptotic cells: Roles for 'old-fashioned' receptors for antibody and complement
    • Hart SP, Smith JR, Dransfield I. Phagocytosis of opsonized apoptotic cells: roles for 'old-fashioned' receptors for antibody and complement. Clin Exp Immunol. 2004;135:181-185.
    • (2004) Clin Exp Immunol , vol.135 , pp. 181-185
    • Hart, S.P.1    Smith, J.R.2    Dransfield, I.3
  • 36
    • 0035831463 scopus 로고    scopus 로고
    • CD44 interaction with c-Src kinase promotes cortactin-mediated cytoskeleton function and hyaluronic acid-dependent ovarian tumor cell migration
    • Bourguignon LY, Zhu H, Shao L, Chen YW. CD44 interaction with c-Src kinase promotes cortactin-mediated cytoskeleton function and hyaluronic acid-dependent ovarian tumor cell migration. J Biol Chem. 2001;276:7327-7336.
    • (2001) J Biol Chem , vol.276 , pp. 7327-7336
    • Bourguignon, L.Y.1    Zhu, H.2    Shao, L.3    Chen, Y.W.4
  • 37
    • 0031929182 scopus 로고    scopus 로고
    • The ankyrin-binding domain of CD44s is involved in regulating hyaluronic acid-mediated functions and prostate tumor cell transformation
    • Zhu D, Bourguignon LY. The ankyrin-binding domain of CD44s is involved in regulating hyaluronic acid-mediated functions and prostate tumor cell transformation. Cell Motil Cytoskeleton. 1998;39:209-222.
    • (1998) Cell Motil Cytoskeleton , vol.39 , pp. 209-222
    • Zhu, D.1    Bourguignon, L.Y.2
  • 38
    • 0032525106 scopus 로고    scopus 로고
    • CD44 selectively associates with active Src family protein tyrosine kinases Lck and Fyn in glycosphingolipid-rich plasma membrane domains of human peripheral blood lymphocytes
    • Ilangumaran S, Briol A, Hoessli DC. CD44 selectively associates with active Src family protein tyrosine kinases Lck and Fyn in glycosphingolipid-rich plasma membrane domains of human peripheral blood lymphocytes. Blood. 1998;91:3901-3908.
    • (1998) Blood , vol.91 , pp. 3901-3908
    • Ilangumaran, S.1    Briol, A.2    Hoessli, D.C.3
  • 39
    • 0037114153 scopus 로고    scopus 로고
    • Lyn and Syk kinases are sequentially engaged in phagocytosis mediated by Fc{gamma}R
    • Strzelecka-Kiliszek A, Kwiatkowska K, Sobota A. Lyn and Syk kinases are sequentially engaged in phagocytosis mediated by Fc{gamma}R. J Immunol. 2002;169:6787-6794.
    • (2002) J Immunol , vol.169 , pp. 6787-6794
    • Strzelecka-Kiliszek, A.1    Kwiatkowska, K.2    Sobota, A.3
  • 40
    • 3342938063 scopus 로고    scopus 로고
    • Cdc42, Rac1, and Rac2 display distinct patterns of activation during phagocytosis
    • Hoppe AD, Swanson JA. Cdc42, Rac1, and Rac2 display distinct patterns of activation during phagocytosis. Mol Biol Cell. 2004;15:3509-3519.
    • (2004) Mol Biol Cell , vol.15 , pp. 3509-3519
    • Hoppe, A.D.1    Swanson, J.A.2
  • 41
    • 0032534071 scopus 로고    scopus 로고
    • Syk- and Lyn-dependent phosphorylation of Syk on multiple tyrosines following B cell activation includes a site that negatively regulates signaling
    • Keshvara LM, Isaacson CC, Yankee TM, Sarac R, Harrison ML, Geahlen RL. Syk- and Lyn-dependent phosphorylation of Syk on multiple tyrosines following B cell activation includes a site that negatively regulates signaling. J Immunol. 1998;161:5276-5283.
    • (1998) J Immunol , vol.161 , pp. 5276-5283
    • Keshvara, L.M.1    Isaacson, C.C.2    Yankee, T.M.3    Sarac, R.4    Harrison, M.L.5    Geahlen, R.L.6
  • 42
    • 0034634638 scopus 로고    scopus 로고
    • Phosphorylation of Syk activation loop tyrosines is essential for Syk function. An in vivo study using a specific anti-Syk activation loop phosphotyrosine antibody
    • Zhang J, Billingsley ML, Kincaid RL, Siraganian RP. Phosphorylation of Syk activation loop tyrosines is essential for Syk function. An in vivo study using a specific anti-Syk activation loop phosphotyrosine antibody. J Biol Chem. 2000;275:35442-35447.
    • (2000) J Biol Chem , vol.275 , pp. 35442-35447
    • Zhang, J.1    Billingsley, M.L.2    Kincaid, R.L.3    Siraganian, R.P.4
  • 43
    • 0141532180 scopus 로고    scopus 로고
    • Class I phosphoinositide 3-kinase p110beta is required for apoptotic cell and Fcgamma receptor-mediated phagocytosis by macrophages
    • Leverrier Y, Okkenhaug K, Sawyer C, Bilancio A, Vanhaesebroeck B, Ridley AJ. Class I phosphoinositide 3-kinase p110beta is required for apoptotic cell and Fcgamma receptor-mediated phagocytosis by macrophages. J Biol Chem. 2003;278:38437-38442.
    • (2003) J Biol Chem , vol.278 , pp. 38437-38442
    • Leverrier, Y.1    Okkenhaug, K.2    Sawyer, C.3    Bilancio, A.4    Vanhaesebroeck, B.5    Ridley, A.J.6
  • 44
    • 0030829551 scopus 로고    scopus 로고
    • A critical role for Syk in signal transduction and phagocytosis mediated by Fcgamma receptors on macrophages
    • Crowley MT, Costello PS, Fitzer-Attas CJ, et al. A critical role for Syk in signal transduction and phagocytosis mediated by Fcgamma receptors on macrophages. J Exp Med. 1997;186:1027-1039.
    • (1997) J Exp Med , vol.186 , pp. 1027-1039
    • Crowley, M.T.1    Costello, P.S.2    Fitzer-Attas, C.J.3
  • 45
    • 0023897684 scopus 로고
    • Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate
    • Whitman M, Downes CP, Keeler M, Keller T, Cantley L. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature. 1988;332:644-646.
    • (1988) Nature , vol.332 , pp. 644-646
    • Whitman, M.1    Downes, C.P.2    Keeler, M.3    Keller, T.4    Cantley, L.5
  • 46
    • 0032562667 scopus 로고    scopus 로고
    • Specific detection of phosphatidylinositol 3,4,5-trisphosphate binding proteins by the PIP3 analogue beads: An application for rapid purification of the PIP3 binding proteins
    • Shirai T, Tanaka K, Terada Y, et al. Specific detection of phosphatidylinositol 3,4,5-trisphosphate binding proteins by the PIP3 analogue beads: an application for rapid purification of the PIP3 binding proteins. Biochim Biophys Acta. 1998;1402:292-302.
    • (1998) Biochim Biophys Acta , vol.1402 , pp. 292-302
    • Shirai, T.1    Tanaka, K.2    Terada, Y.3
  • 47
    • 0027432424 scopus 로고
    • Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: The role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses
    • Arcaro A, Wymann MP. Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses. Biochem J. 1993;296:297-301.
    • (1993) Biochem J , vol.296 , pp. 297-301
    • Arcaro, A.1    Wymann, M.P.2
  • 48
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos C, Matter W, Hui K, Brown R. A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J Biol Chem. 1994;269:5241-5248.
    • (1994) J Biol Chem , vol.269 , pp. 5241-5248
    • Vlahos, C.1    Matter, W.2    Hui, K.3    Brown, R.4
  • 50
    • 0032585635 scopus 로고    scopus 로고
    • Rac1 is required for the formation of three germ layers during gastrulation
    • Sugihara K, Nakatsuji N, Nakamura K, et al. Rac1 is required for the formation of three germ layers during gastrulation. Oncogene. 1998;17:3427-3433.
    • (1998) Oncogene , vol.17 , pp. 3427-3433
    • Sugihara, K.1    Nakatsuji, N.2    Nakamura, K.3
  • 51
    • 0024425981 scopus 로고
    • rac, a novel ras-related family of proteins that are botulinum toxin substrates
    • Didsbury J, Weber R, Bokoch G, Evans T, Snyderman R. rac, a novel ras-related family of proteins that are botulinum toxin substrates. J Biol Chem. 1989;264:16378-16382.
    • (1989) J Biol Chem , vol.264 , pp. 16378-16382
    • Didsbury, J.1    Weber, R.2    Bokoch, G.3    Evans, T.4    Snyderman, R.5
  • 52
    • 1342310842 scopus 로고    scopus 로고
    • Lysosome and lysosome-related organelles responsible for specialized functions in higher organisms, with special emphasis on vacuolar-type proton ATPase
    • Sun-Wada GH, Wada Y, Futai M. Lysosome and lysosome-related organelles responsible for specialized functions in higher organisms, with special emphasis on vacuolar-type proton ATPase. Cell Struct Funct. 2003;28:455-463.
    • (2003) Cell Struct Funct , vol.28 , pp. 455-463
    • Sun-Wada, G.H.1    Wada, Y.2    Futai, M.3
  • 53
    • 0025992764 scopus 로고
    • The superoxide-generating oxidase of phagocytic cells. Physiological, molecular and pathological aspects
    • Morel F, Doussiere J, Vignais PV. The superoxide-generating oxidase of phagocytic cells. Physiological, molecular and pathological aspects. Eur J Biochem. 1991;201:523-546.
    • (1991) Eur J Biochem , vol.201 , pp. 523-546
    • Morel, F.1    Doussiere, J.2    Vignais, P.V.3
  • 54
    • 33646570380 scopus 로고
    • Production of hyaluronic acid by Pseudomonas aeruginosa
    • Copenh
    • Bonde GJ, Carlsen FE, Jensen CE. Production of hyaluronic acid by Pseudomonas aeruginosa. Acta Pharmacol Toxicol (Copenh). 1957;13:205-212.
    • (1957) Acta Pharmacol Toxicol , vol.13 , pp. 205-212
    • Bonde, G.J.1    Carlsen, F.E.2    Jensen, C.E.3
  • 55
    • 0014518590 scopus 로고
    • Composition of Pseudomonas aeruginosa slime
    • Brown MR, Foster JH, Clamp JR. Composition of Pseudomonas aeruginosa slime. Biochem J. 1969;112:521-525.
    • (1969) Biochem J , vol.112 , pp. 521-525
    • Brown, M.R.1    Foster, J.H.2    Clamp, J.R.3
  • 56
    • 0032478626 scopus 로고    scopus 로고
    • Identification and molecular cloning of a unique hyaluronan synthase from Pasteurella multocida
    • DeAngelis PL, Jing W, Drake RR, Achyuthan AM. Identification and molecular cloning of a unique hyaluronan synthase from Pasteurella multocida. J Biol Chem. 1998;273:8454-8458.
    • (1998) J Biol Chem , vol.273 , pp. 8454-8458
    • DeAngelis, P.L.1    Jing, W.2    Drake, R.R.3    Achyuthan, A.M.4
  • 57
    • 0035818973 scopus 로고    scopus 로고
    • Group A Streptococcus tissue invasion by CD44-mediated cell signalling
    • Cywes C, Wessels MR. Group A Streptococcus tissue invasion by CD44-mediated cell signalling. Nature. 2001;414:648-652.
    • (2001) Nature , vol.414 , pp. 648-652
    • Cywes, C.1    Wessels, M.R.2
  • 58
    • 0022606167 scopus 로고
    • The role of extracellular matrix proteins in the control of phagocytosis
    • Brown EJ. The role of extracellular matrix proteins in the control of phagocytosis. J Leukoc Biol. 1986;39:579-591.
    • (1986) J Leukoc Biol , vol.39 , pp. 579-591
    • Brown, E.J.1
  • 59
    • 0025049546 scopus 로고
    • Neutrophil bactericidal activity against Staphylococcus aureus adherent on biological surfaces. Surface-bound extracellular matrix proteins activate intracellular killing by oxygen-dependent and -independent mechanisms
    • Hermann M, Jaconi ME, Dahlgren C, Waldvogel FA, Stendahl O, Lew DP. Neutrophil bactericidal activity against Staphylococcus aureus adherent on biological surfaces. Surface-bound extracellular matrix proteins activate intracellular killing by oxygen-dependent and -independent mechanisms. J Clin Invest. 1990;86:942-951.
    • (1990) J Clin Invest , vol.86 , pp. 942-951
    • Hermann, M.1    Jaconi, M.E.2    Dahlgren, C.3    Waldvogel, F.A.4    Stendahl, O.5    Lew, D.P.6
  • 60
    • 0029583337 scopus 로고
    • Distinct expression patterns of CD44 isoforms during human lung development and in pulmonary fibrosis
    • Kasper M, Gunthert U, Dall P, et al. Distinct expression patterns of CD44 isoforms during human lung development and in pulmonary fibrosis. Am J Respir Cell Mol Biol. 1995;13:648-656.
    • (1995) Am J Respir Cell Mol Biol , vol.13 , pp. 648-656
    • Kasper, M.1    Gunthert, U.2    Dall, P.3
  • 61
    • 0029808003 scopus 로고    scopus 로고
    • Hyaluronan (HA) fragments induce chemokine gene expression in alveolar macrophages. The role of HA size and CD44
    • McKee CM, Penno MB, Cowman M, et al. Hyaluronan (HA) fragments induce chemokine gene expression in alveolar macrophages. The role of HA size and CD44. J Clin Invest. 1996;98:2403-2413.
    • (1996) J Clin Invest , vol.98 , pp. 2403-2413
    • McKee, C.M.1    Penno, M.B.2    Cowman, M.3
  • 62
    • 0041423663 scopus 로고    scopus 로고
    • Apoptosis: Giving phosphatidylserine recognition an assist - With a twist
    • Fadok VA, Henson PM. Apoptosis: giving phosphatidylserine recognition an assist - with a twist. Curr Biol. 2003;13:r655-r657.
    • (2003) Curr Biol , vol.13
    • Fadok, V.A.1    Henson, P.M.2
  • 63
    • 0032400966 scopus 로고    scopus 로고
    • CD36 is required for phagocytosis of apoptotic cells by human macrophages that use either a phosphatidylserine receptor or the vitronectin receptor (alpha v beta 3)
    • Fadok VA, Warner ML, Bratton DL, Henson PM. CD36 is required for phagocytosis of apoptotic cells by human macrophages that use either a phosphatidylserine receptor or the vitronectin receptor (alpha v beta 3). J Immunol. 1998;161:6250-6257.
    • (1998) J Immunol , vol.161 , pp. 6250-6257
    • Fadok, V.A.1    Warner, M.L.2    Bratton, D.L.3    Henson, P.M.4
  • 64
    • 0141918823 scopus 로고    scopus 로고
    • By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation
    • Gardai SJ, Xiao YQ, Dickinson M, et al. By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation. Cell. 2003;115:13-23.
    • (2003) Cell , vol.115 , pp. 13-23
    • Gardai, S.J.1    Xiao, Y.Q.2    Dickinson, M.3
  • 65
    • 0344153281 scopus 로고    scopus 로고
    • The final step in programmed cell death: Phagocytes carry apoptotic cells to the grave
    • deCathelineau AM, Henson PM. The final step in programmed cell death: phagocytes carry apoptotic cells to the grave. Essays Biochem. 2003;39:105-117.
    • (2003) Essays Biochem , vol.39 , pp. 105-117
    • DeCathelineau, A.M.1    Henson, P.M.2
  • 66
    • 0027451274 scopus 로고
    • Receptor-receptor interactions of complement receptor type 3 in neutrophil membranes
    • Petty HR, Todd RF 3rd. Receptor-receptor interactions of complement receptor type 3 in neutrophil membranes. J Leukoc Biol. 1993;54:492-494.
    • (1993) J Leukoc Biol , vol.54 , pp. 492-494
    • Petty, H.R.1    Todd III, R.F.2
  • 67
    • 0030589322 scopus 로고    scopus 로고
    • CR3 (alphaM beta2; CD11b/CD18) restores IgG-dependent phagocytosis in transfectants expressing a phagocytosis-defective Fc gammaRIIA (CD32) tail-minus mutant
    • Worth RG, Mayo-Bond L, van de Winkel JG, Todd RF 3rd, Petty HR. CR3 (alphaM beta2; CD11b/CD18) restores IgG-dependent phagocytosis in transfectants expressing a phagocytosis-defective Fc gammaRIIA (CD32) tail-minus mutant. J Immunol. 1996;157:5660-5665.
    • (1996) J Immunol , vol.157 , pp. 5660-5665
    • Worth, R.G.1    Mayo-Bond, L.2    Van De Winkel, J.G.3    Todd III, R.F.4    Petty, H.R.5
  • 68
    • 0028308516 scopus 로고
    • Involvement of CD11b/CD18 in enhanced neutrophil adhesion by Fc gamma receptor stimulation
    • Kusunoki T, Tsuruta S, Higashi H, et al. Involvement of CD11b/CD18 in enhanced neutrophil adhesion by Fc gamma receptor stimulation. J Leukoc Biol. 1994;55:735-742.
    • (1994) J Leukoc Biol , vol.55 , pp. 735-742
    • Kusunoki, T.1    Tsuruta, S.2    Higashi, H.3
  • 69
    • 0028179557 scopus 로고
    • CR3 (Mac-1, alpha M beta 2, CD11b/CD18) and Fc gamma RIII cooperate in generation of a neutrophil respiratory burst: Requirement for Fc gamma RIII and tyrosine phosphorylation
    • Zhou MJ, Brown EJ. CR3 (Mac-1, alpha M beta 2, CD11b/CD18) and Fc gamma RIII cooperate in generation of a neutrophil respiratory burst: requirement for Fc gamma RIII and tyrosine phosphorylation. J Cell Biol. 1994;125:1407-1416.
    • (1994) J Cell Biol , vol.125 , pp. 1407-1416
    • Zhou, M.J.1    Brown, E.J.2
  • 70
    • 0242580737 scopus 로고    scopus 로고
    • Fcgamma-receptors induce Mac-1 (CD11b/CD18) mobilization and accumulation in the phagocytic cup for optimal phagocytosis
    • Jongstra-Bilen J, Harrison R, Grinstein S. Fcgamma-receptors induce Mac-1 (CD11b/CD18) mobilization and accumulation in the phagocytic cup for optimal phagocytosis. J Biol Chem. 2003;278:45720-45729.
    • (2003) J Biol Chem , vol.278 , pp. 45720-45729
    • Jongstra-Bilen, J.1    Harrison, R.2    Grinstein, S.3
  • 71
    • 0028793187 scopus 로고
    • Phosphorylated immunoreceptor signaling motifs (ITAMs) exhibit unique abilities to bind and activate Lyn and Syk tyrosine kinases
    • Johnson SA, Pleiman CM, Pao L, Schneringer J, Hippen K, Cambier JC. Phosphorylated immunoreceptor signaling motifs (ITAMs) exhibit unique abilities to bind and activate Lyn and Syk tyrosine kinases. J Immunol. 1995;155:4596-4603.
    • (1995) J Immunol , vol.155 , pp. 4596-4603
    • Johnson, S.A.1    Pleiman, C.M.2    Pao, L.3    Schneringer, J.4    Hippen, K.5    Cambier, J.C.6
  • 72
    • 0038558249 scopus 로고    scopus 로고
    • Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2
    • Gantner BN, Simmons RM, Canavera SJ, Akira S, Underhill DM. Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2. J Exp Med. 2003;197:1107-1117.
    • (2003) J Exp Med , vol.197 , pp. 1107-1117
    • Gantner, B.N.1    Simmons, R.M.2    Canavera, S.J.3    Akira, S.4    Underhill, D.M.5
  • 73
    • 0036347746 scopus 로고    scopus 로고
    • Fyn kinase initiates complementary signals required for IgE-dependent mast cell degranulation
    • Parravicini V, Gadina M, Kovarova M, et al. Fyn kinase initiates complementary signals required for IgE-dependent mast cell degranulation. Nat Immunol. 2002;3:741-748.
    • (2002) Nat Immunol , vol.3 , pp. 741-748
    • Parravicini, V.1    Gadina, M.2    Kovarova, M.3
  • 74
    • 20044363664 scopus 로고    scopus 로고
    • Src and Syk kinases: Key regulators of phagocytic cell activation
    • Berton G, Mocsai A, Lowell CA. Src and Syk kinases: key regulators of phagocytic cell activation. Trends Immunol. 2005;26:208-214.
    • (2005) Trends Immunol , vol.26 , pp. 208-214
    • Berton, G.1    Mocsai, A.2    Lowell, C.A.3
  • 75
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge K, Wennerberg K. Rho and Rac take center stage. Cell. 2004;116:167-179.
    • (2004) Cell , vol.116 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 76
    • 0043032859 scopus 로고    scopus 로고
    • Hyaluronan-mediated CD44 interaction with Rho-GEF and Rho kinase promotes Grb2-associated binder-1 phosphorylation and phosphatidylinositol 3-kinase signaling leading to cytokine (macrophage-colony stimulating factor) production and breast tumor progression
    • Bourguignon LY, Singleton PA, Zhu H, Diedrich F. Hyaluronan-mediated CD44 interaction with Rho-GEF and Rho kinase promotes Grb2-associated binder-1 phosphorylation and phosphatidylinositol 3-kinase signaling leading to cytokine (macrophage-colony stimulating factor) production and breast tumor progression. J Biol Chem. 2003;278:29420-29434.
    • (2003) J Biol Chem , vol.278 , pp. 29420-29434
    • Bourguignon, L.Y.1    Singleton, P.A.2    Zhu, H.3    Diedrich, F.4
  • 77
    • 0035966019 scopus 로고    scopus 로고
    • Hyaluronan promotes CD44v3-Vav2 interaction with Grb2-p185(HER2) and induces Rac1 and Ras signaling during ovarian tumor cell migration and growth
    • Bourguignon LY, Zhu H, Zhou B, Diedrich F, Singleton PA, Hung MC. Hyaluronan promotes CD44v3-Vav2 interaction with Grb2-p185(HER2) and induces Rac1 and Ras signaling during ovarian tumor cell migration and growth. J Biol Chem. 2001;276:48679-48692.
    • (2001) J Biol Chem , vol.276 , pp. 48679-48692
    • Bourguignon, L.Y.1    Zhu, H.2    Zhou, B.3    Diedrich, F.4    Singleton, P.A.5    Hung, M.C.6
  • 78
    • 0034695446 scopus 로고    scopus 로고
    • CD44 interaction with tiam1 promotes Rac1 signaling and hyaluronic acid-mediated breast tumor cell migration
    • Bourguignon LY, Zhu H, Shao L, Chen YW. CD44 interaction with tiam1 promotes Rac1 signaling and hyaluronic acid-mediated breast tumor cell migration. J Biol Chem. 2000;275:1829-1838.
    • (2000) J Biol Chem , vol.275 , pp. 1829-1838
    • Bourguignon, L.Y.1    Zhu, H.2    Shao, L.3    Chen, Y.W.4
  • 79
    • 0242384071 scopus 로고    scopus 로고
    • Vav proteins, masters of the world of cytoskeleton organization
    • Hornstein I, Alcover A, Katzav S. Vav proteins, masters of the world of cytoskeleton organization. Cell Signal. 2004;16:1-11.
    • (2004) Cell Signal , vol.16 , pp. 1-11
    • Hornstein, I.1    Alcover, A.2    Katzav, S.3
  • 80
    • 18944389626 scopus 로고    scopus 로고
    • Tiam1-IRSp53 complex formation directs specificity of rac-mediated actin cytoskeleton regulation
    • Connolly BA, Rice J, Feig LA, Buchsbaum RJ. Tiam1-IRSp53 complex formation directs specificity of rac-mediated actin cytoskeleton regulation. Mol Cell Biol. 2005;25:4602-4614.
    • (2005) Mol Cell Biol , vol.25 , pp. 4602-4614
    • Connolly, B.A.1    Rice, J.2    Feig, L.A.3    Buchsbaum, R.J.4
  • 81
    • 3342903325 scopus 로고    scopus 로고
    • Vav GEFs are required for beta2 integrin-dependent functions of neutrophils
    • Gakidis MA, Cullere X, Olson T, et al. Vav GEFs are required for beta2 integrin-dependent functions of neutrophils. J Cell Biol. 2004;166:273-282.
    • (2004) J Cell Biol , vol.166 , pp. 273-282
    • Gakidis, M.A.1    Cullere, X.2    Olson, T.3
  • 82
    • 13544261760 scopus 로고    scopus 로고
    • Activation of the phagocyte NADPH oxidase by Rac guanine nucleotide exchange factors in conjunction with ATP and nucleoside diphosphate kinase
    • Mizrahi A, Molshanski-Mor S, Weinbaum C, Zheng Y, Hirshberg M, Pick E. Activation of the phagocyte NADPH oxidase by Rac guanine nucleotide exchange factors in conjunction with ATP and nucleoside diphosphate kinase. J Biol Chem. 2005;280:3802-3811.
    • (2005) J Biol Chem , vol.280 , pp. 3802-3811
    • Mizrahi, A.1    Molshanski-Mor, S.2    Weinbaum, C.3    Zheng, Y.4    Hirshberg, M.5    Pick, E.6
  • 83
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
    • Tsukita S, Oishi K, Sato N, Sagara J, Kawai A. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J Cell Biol. 1994;126:391-401.
    • (1994) J Cell Biol , vol.126 , pp. 391-401
    • Tsukita, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5
  • 84
    • 0030966842 scopus 로고    scopus 로고
    • CD44: Structure, function, and association with the malignant process
    • Naor D, Sionov RV, Ish-Shalom D. CD44: structure, function, and association with the malignant process. Adv Cancer Res. 1997;71:241-319.
    • (1997) Adv Cancer Res , vol.71 , pp. 241-319
    • Naor, D.1    Sionov, R.V.2    Ish-Shalom, D.3
  • 85
  • 86
    • 0032812619 scopus 로고    scopus 로고
    • Rho-kinase (ROK) promotes CD44v(3,8-10)-ankyrin interaction and tumor cell migration in metastatic breast cancer cells
    • Bourguignon LY, Zhu H, Shao L, Zhu D, Chen YW. Rho-kinase (ROK) promotes CD44v(3,8-10)-ankyrin interaction and tumor cell migration in metastatic breast cancer cells. Cell Motil Cytoskeleton. 1999;43:269-287.
    • (1999) Cell Motil Cytoskeleton , vol.43 , pp. 269-287
    • Bourguignon, L.Y.1    Zhu, H.2    Shao, L.3    Zhu, D.4    Chen, Y.W.5
  • 87
    • 0037143448 scopus 로고    scopus 로고
    • Rho-kinase and myosin-II control phagocytic cup formation during CR, but not FcgammaR, phagocytosis
    • Olazabal IM, Caron E, May RC, Schilling K, Knecht DA, Machesky LM. Rho-kinase and myosin-II control phagocytic cup formation during CR, but not FcgammaR, phagocytosis. Curr Biol. 2002;12:1413-1418.
    • (2002) Curr Biol , vol.12 , pp. 1413-1418
    • Olazabal, I.M.1    Caron, E.2    May, R.C.3    Schilling, K.4    Knecht, D.A.5    Machesky, L.M.6
  • 88
    • 12344298862 scopus 로고    scopus 로고
    • Low-molecular collagen peptides have different effects on peritoneal macrophages and neutrophils
    • Kozlov IG, Yemelyanov AY, Davidova NV, Gorlina NK, Cheredeev AN. Low-molecular collagen peptides have different effects on peritoneal macrophages and neutrophils. Russ J Immunol. 1999;4:113-122.
    • (1999) Russ J Immunol , vol.4 , pp. 113-122
    • Kozlov, I.G.1    Yemelyanov, A.Y.2    Davidova, N.V.3    Gorlina, N.K.4    Cheredeev, A.N.5
  • 90
    • 0036900002 scopus 로고    scopus 로고
    • CD44 deficiency leads to enhanced neutrophil migration and lung injury in Escherichia coli pneumonia in mice
    • Wang Q, Teder P, Judd NP, Noble PW, Doerschuk CM. CD44 deficiency leads to enhanced neutrophil migration and lung injury in Escherichia coli pneumonia in mice. Am J Pathol. 2002;161:2219-2228.
    • (2002) Am J Pathol , vol.161 , pp. 2219-2228
    • Wang, Q.1    Teder, P.2    Judd, N.P.3    Noble, P.W.4    Doerschuk, C.M.5


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