메뉴 건너뛰기




Volumn 1853, Issue 10, 2015, Pages 2464-2480

Different states of integrin LFA-1 aggregation are controlled through its association with tetraspanin CD9

Author keywords

Adhesion; CD9; Cytotoxicity; Integrin; LFA 1; Tetraspanin

Indexed keywords

CD9 ANTIGEN; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; CD9 PROTEIN, HUMAN;

EID: 84938349481     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2015.05.018     Document Type: Article
Times cited : (33)

References (79)
  • 1
    • 0026575901 scopus 로고
    • Camptothecin induces differentiation and stimulates the expression of differentiation-related genes in U-937 human promonocytic leukemia cells
    • Aller P., Rius C., Mata F., Zorrilla A., Cabanas C., Bellon T., Bernabeu C. Camptothecin induces differentiation and stimulates the expression of differentiation-related genes in U-937 human promonocytic leukemia cells. Cancer Res. 1992, 52:1245-1251.
    • (1992) Cancer Res. , vol.52 , pp. 1245-1251
    • Aller, P.1    Rius, C.2    Mata, F.3    Zorrilla, A.4    Cabanas, C.5    Bellon, T.6    Bernabeu, C.7
  • 2
    • 18144426450 scopus 로고    scopus 로고
    • Distinct role of lymphocyte function-associated antigen-1 in mediating effective cytolytic activity by cytotoxic T lymphocytes
    • Anikeeva N., Somersalo K., Sims T.N., Thomas V.K., Dustin M.L., Sykulev Y. Distinct role of lymphocyte function-associated antigen-1 in mediating effective cytolytic activity by cytotoxic T lymphocytes. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:6437-6442.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6437-6442
    • Anikeeva, N.1    Somersalo, K.2    Sims, T.N.3    Thomas, V.K.4    Dustin, M.L.5    Sykulev, Y.6
  • 5
    • 23744514951 scopus 로고    scopus 로고
    • Aberrant expression of tetraspanin molecules in B-cell chronic lymphoproliferative disorders and its correlation with normal B-cell maturation
    • Barrena S., Almeida J., Yunta M., Lopez A., Fernandez-Mosteirin N., Giralt M., Romero M., Perdiguer L., Delgado M., Orfao A., et al. Aberrant expression of tetraspanin molecules in B-cell chronic lymphoproliferative disorders and its correlation with normal B-cell maturation. Leukemia 2005, 19:1376-1383.
    • (2005) Leukemia , vol.19 , pp. 1376-1383
    • Barrena, S.1    Almeida, J.2    Yunta, M.3    Lopez, A.4    Fernandez-Mosteirin, N.5    Giralt, M.6    Romero, M.7    Perdiguer, L.8    Delgado, M.9    Orfao, A.10
  • 6
    • 84859266427 scopus 로고    scopus 로고
    • Tetraspanins: interactions and interplay with integrins
    • Bassani S., Cingolani L.A. Tetraspanins: interactions and interplay with integrins. Int. J. Biochem. Cell Biol. 2012, 44:703-708.
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 703-708
    • Bassani, S.1    Cingolani, L.A.2
  • 7
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: more than meets the eye
    • Berditchevski F. Complexes of tetraspanins with integrins: more than meets the eye. J. Cell Sci. 2001, 114:4143-4151.
    • (2001) J. Cell Sci. , vol.114 , pp. 4143-4151
    • Berditchevski, F.1
  • 8
    • 0035798702 scopus 로고    scopus 로고
    • Analysis of the CD151-alpha3beta1 integrin and CD151-tetraspanin interactions by mutagenesis
    • Berditchevski F., Gilbert E., Griffiths M.R., Fitter S., Ashman L., Jenner S.J. Analysis of the CD151-alpha3beta1 integrin and CD151-tetraspanin interactions by mutagenesis. J. Biol. Chem. 2001, 276:41165-41174.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41165-41174
    • Berditchevski, F.1    Gilbert, E.2    Griffiths, M.R.3    Fitter, S.4    Ashman, L.5    Jenner, S.J.6
  • 9
    • 0026542081 scopus 로고
    • The binding site on ICAM-1 for Plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site
    • Berendt A.R., McDowall A., Craig A.G., Bates P.A., Sternberg M.J., Marsh K., Newbold C.I., Hogg N. The binding site on ICAM-1 for Plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site. Cell 1992, 68:71-81.
    • (1992) Cell , vol.68 , pp. 71-81
    • Berendt, A.R.1    McDowall, A.2    Craig, A.G.3    Bates, P.A.4    Sternberg, M.J.5    Marsh, K.6    Newbold, C.I.7    Hogg, N.8
  • 11
    • 0023136438 scopus 로고
    • The role of the T cell receptor, CD8, and LFA-1 in different stages of the cytolytic reaction mediated by alloreactive T lymphocyte clones
    • Blanchard D., van Els C., Borst J., Carrel S., Boylston A., de Vries J.E., Spits H. The role of the T cell receptor, CD8, and LFA-1 in different stages of the cytolytic reaction mediated by alloreactive T lymphocyte clones. J. Immunol. 1987, 138:2417-2421.
    • (1987) J. Immunol. , vol.138 , pp. 2417-2421
    • Blanchard, D.1    van Els, C.2    Borst, J.3    Carrel, S.4    Boylston, A.5    de Vries, J.E.6    Spits, H.7
  • 12
    • 0028171951 scopus 로고
    • Integrin alpha v beta 3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor alpha 5 beta 1
    • Blystone S.D., Graham I.L., Lindberg F.P., Brown E.J. Integrin alpha v beta 3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor alpha 5 beta 1. J. Cell Biol. 1994, 127:1129-1137.
    • (1994) J. Cell Biol. , vol.127 , pp. 1129-1137
    • Blystone, S.D.1    Graham, I.L.2    Lindberg, F.P.3    Brown, E.J.4
  • 13
    • 0028983057 scopus 로고
    • Integrin beta 3 cytoplasmic tail is necessary and sufficient for regulation of alpha 5 beta 1 phagocytosis by alpha v beta 3 and integrin-associated protein
    • Blystone S.D., Lindberg F.P., LaFlamme S.E., Brown E.J. Integrin beta 3 cytoplasmic tail is necessary and sufficient for regulation of alpha 5 beta 1 phagocytosis by alpha v beta 3 and integrin-associated protein. J. Cell Biol. 1995, 130:745-754.
    • (1995) J. Cell Biol. , vol.130 , pp. 745-754
    • Blystone, S.D.1    Lindberg, F.P.2    LaFlamme, S.E.3    Brown, E.J.4
  • 16
    • 0023947922 scopus 로고
    • Characterization of a CD11c-reactive monoclonal antibody (HC1/1) obtained by immunizing with phorbol ester differentiated U937 cells
    • Cabanas C., Sanchez-Madrid F., Acevedo A., Bellon T., Fernandez J.M., Larraga V., Bernabeu C. Characterization of a CD11c-reactive monoclonal antibody (HC1/1) obtained by immunizing with phorbol ester differentiated U937 cells. Hybridoma 1988, 7:167-176.
    • (1988) Hybridoma , vol.7 , pp. 167-176
    • Cabanas, C.1    Sanchez-Madrid, F.2    Acevedo, A.3    Bellon, T.4    Fernandez, J.M.5    Larraga, V.6    Bernabeu, C.7
  • 18
    • 0141756175 scopus 로고    scopus 로고
    • Integrin avidity regulation: are changes in affinity and conformation underemphasized?
    • Carman C.V., Springer T.A. Integrin avidity regulation: are changes in affinity and conformation underemphasized?. Curr. Opin. Cell Biol. 2003, 15:547-556.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 547-556
    • Carman, C.V.1    Springer, T.A.2
  • 19
    • 27544442354 scopus 로고    scopus 로고
    • The mechanisms and dynamics of (alpha)v(beta)3 integrin clustering in living cells
    • Cluzel C., Saltel F., Lussi J., Paulhe F., Imhof B.A., Wehrle-Haller B. The mechanisms and dynamics of (alpha)v(beta)3 integrin clustering in living cells. J. Cell Biol. 2005, 171:383-392.
    • (2005) J. Cell Biol. , vol.171 , pp. 383-392
    • Cluzel, C.1    Saltel, F.2    Lussi, J.3    Paulhe, F.4    Imhof, B.A.5    Wehrle-Haller, B.6
  • 22
    • 84874536522 scopus 로고    scopus 로고
    • Ezrin and moesin are required for efficient T cell adhesion and homing to lymphoid organs
    • Chen E.J., Shaffer M.H., Williamson E.K., Huang Y., Burkhardt J.K. Ezrin and moesin are required for efficient T cell adhesion and homing to lymphoid organs. PLoS ONE 2013, 8:e52368.
    • (2013) PLoS ONE , vol.8 , pp. e52368
    • Chen, E.J.1    Shaffer, M.H.2    Williamson, E.K.3    Huang, Y.4    Burkhardt, J.K.5
  • 24
    • 0024474320 scopus 로고
    • Interplay between the TCR/CD3 complex and CD4 or CD8 in the activation of cytotoxic T lymphocytes
    • de Vries J.E., Yssel H., Spits H. Interplay between the TCR/CD3 complex and CD4 or CD8 in the activation of cytotoxic T lymphocytes. Immunol. Rev. 1989, 109:119-141.
    • (1989) Immunol. Rev. , vol.109 , pp. 119-141
    • de Vries, J.E.1    Yssel, H.2    Spits, H.3
  • 25
    • 0026581198 scopus 로고
    • Interaction of leukocyte integrins with ligand is necessary but not sufficient for function
    • Dransfield I., Cabanas C., Barrett J., Hogg N. Interaction of leukocyte integrins with ligand is necessary but not sufficient for function. J. Cell Biol. 1992, 116:1527-1535.
    • (1992) J. Cell Biol. , vol.116 , pp. 1527-1535
    • Dransfield, I.1    Cabanas, C.2    Barrett, J.3    Hogg, N.4
  • 26
    • 0026601096 scopus 로고
    • Divalent cation regulation of the function of the leukocyte integrin LFA-1
    • Dransfield I., Cabanas C., Craig A., Hogg N. Divalent cation regulation of the function of the leukocyte integrin LFA-1. J. Cell Biol. 1992, 116:219-226.
    • (1992) J. Cell Biol. , vol.116 , pp. 219-226
    • Dransfield, I.1    Cabanas, C.2    Craig, A.3    Hogg, N.4
  • 27
    • 0024443411 scopus 로고
    • T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1
    • Dustin M.L., Springer T.A. T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1. Nature 1989, 341:619-624.
    • (1989) Nature , vol.341 , pp. 619-624
    • Dustin, M.L.1    Springer, T.A.2
  • 34
    • 0344708475 scopus 로고    scopus 로고
    • Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain
    • Hemler M.E. Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain. Annu. Rev. Cell Dev. Biol. 2003, 19:397-422.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 397-422
    • Hemler, M.E.1
  • 35
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler M.E. 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
  • 36
    • 84890933854 scopus 로고    scopus 로고
    • Tetraspanin proteins promote multiple cancer stages
    • Hemler M.E. Tetraspanin proteins promote multiple cancer stages. Nat. Rev. Cancer 2013, 14:49-60.
    • (2013) Nat. Rev. Cancer , vol.14 , pp. 49-60
    • Hemler, M.E.1
  • 38
    • 33745238967 scopus 로고    scopus 로고
    • Recombinant extracellular domains of tetraspanin proteins are potent inhibitors of the infection of macrophages by human immunodeficiency virus type 1
    • Ho S.H., Martin F., Higginbottom A., Partridge L.J., Parthasarathy V., Moseley G.W., Lopez P., Cheng-Mayer C., Monk P.N. Recombinant extracellular domains of tetraspanin proteins are potent inhibitors of the infection of macrophages by human immunodeficiency virus type 1. J. Virol. 2006, 80:6487-6496.
    • (2006) J. Virol. , vol.80 , pp. 6487-6496
    • Ho, S.H.1    Martin, F.2    Higginbottom, A.3    Partridge, L.J.4    Parthasarathy, V.5    Moseley, G.W.6    Lopez, P.7    Cheng-Mayer, C.8    Monk, P.N.9
  • 39
    • 79957621253 scopus 로고    scopus 로고
    • The insider's guide to leukocyte integrin signalling and function
    • Hogg N., Patzak I., Willenbrock F. The insider's guide to leukocyte integrin signalling and function. Nat. Rev. Immunol. 2011, 11:416-426.
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 416-426
    • Hogg, N.1    Patzak, I.2    Willenbrock, F.3
  • 40
    • 0348036122 scopus 로고    scopus 로고
    • T-cell integrins: more than just sticking points
    • Hogg N., Laschinger M., Giles K., McDowall A. T-cell integrins: more than just sticking points. J. Cell Sci. 2003, 116:4695-4705.
    • (2003) J. Cell Sci. , vol.116 , pp. 4695-4705
    • Hogg, N.1    Laschinger, M.2    Giles, K.3    McDowall, A.4
  • 41
    • 0022357790 scopus 로고
    • Biochemical and functional characteristics of the human leukocyte membrane antigen family LFA-1, Mo-1 and p150,95
    • Keizer G.D., Borst J., Figdor C.G., Spits H., Miedema F., Terhorst C., De Vries J.E. Biochemical and functional characteristics of the human leukocyte membrane antigen family LFA-1, Mo-1 and p150,95. Eur. J. Immunol. 1985, 15:1142-1148.
    • (1985) Eur. J. Immunol. , vol.15 , pp. 1142-1148
    • Keizer, G.D.1    Borst, J.2    Figdor, C.G.3    Spits, H.4    Miedema, F.5    Terhorst, C.6    De Vries, J.E.7
  • 42
    • 11244274075 scopus 로고    scopus 로고
    • The primacy of affinity over clustering in regulation of adhesiveness of the integrin {alpha}L{beta}2
    • Kim M., Carman C.V., Yang W., Salas A., Springer T.A. The primacy of affinity over clustering in regulation of adhesiveness of the integrin {alpha}L{beta}2. J. Cell Biol. 2004, 167:1241-1253.
    • (2004) J. Cell Biol. , vol.167 , pp. 1241-1253
    • Kim, M.1    Carman, C.V.2    Yang, W.3    Salas, A.4    Springer, T.A.5
  • 43
    • 0942279501 scopus 로고    scopus 로고
    • Evidence for specific tetraspanin homodimers: inhibition of palmitoylation makes cysteine residues available for cross-linking
    • Kovalenko O.V., Yang X., Kolesnikova T.V., Hemler M.E. Evidence for specific tetraspanin homodimers: inhibition of palmitoylation makes cysteine residues available for cross-linking. Biochem. J. 2004, 377:407-417.
    • (2004) Biochem. J. , vol.377 , pp. 407-417
    • Kovalenko, O.V.1    Yang, X.2    Kolesnikova, T.V.3    Hemler, M.E.4
  • 44
    • 0029913643 scopus 로고    scopus 로고
    • Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes
    • Kucik D.F., Dustin M.L., Miller J.M., Brown E.J. Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes. J. Clin. Invest. 1996, 97:2139-2144.
    • (1996) J. Clin. Invest. , vol.97 , pp. 2139-2144
    • Kucik, D.F.1    Dustin, M.L.2    Miller, J.M.3    Brown, E.J.4
  • 45
    • 33845975257 scopus 로고    scopus 로고
    • Membrane microdomains and proteomics: lessons from tetraspanin microdomains and comparison with lipid rafts
    • Le Naour F., Andre M., Boucheix C., Rubinstein E. Membrane microdomains and proteomics: lessons from tetraspanin microdomains and comparison with lipid rafts. Proteomics 2006, 6:6447-6454.
    • (2006) Proteomics , vol.6 , pp. 6447-6454
    • Le Naour, F.1    Andre, M.2    Boucheix, C.3    Rubinstein, E.4
  • 46
    • 13444259476 scopus 로고    scopus 로고
    • The tetraspanin web modulates immune-signalling complexes
    • Levy S., Shoham T. The tetraspanin web modulates immune-signalling complexes. Nat. Rev. Immunol. 2005, 5:136-148.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 136-148
    • Levy, S.1    Shoham, T.2
  • 47
    • 2142765951 scopus 로고    scopus 로고
    • A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: analysis by quantitative immunocolocalization
    • Li Q., Lau A., Morris T.J., Guo L., Fordyce C.B., Stanley E.F. A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: analysis by quantitative immunocolocalization. J. Neurosci. 2004, 24:4070-4081.
    • (2004) J. Neurosci. , vol.24 , pp. 4070-4081
    • Li, Q.1    Lau, A.2    Morris, T.J.3    Guo, L.4    Fordyce, C.B.5    Stanley, E.F.6
  • 48
    • 15844363687 scopus 로고    scopus 로고
    • Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region (355-425) of the common beta 1 chain
    • Luque A., Gomez M., Puzon W., Takada Y., Sanchez-Madrid F., Cabanas C. Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region (355-425) of the common beta 1 chain. J. Biol. Chem. 1996, 271:11067-11075.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11067-11075
    • Luque, A.1    Gomez, M.2    Puzon, W.3    Takada, Y.4    Sanchez-Madrid, F.5    Cabanas, C.6
  • 49
    • 0025837201 scopus 로고
    • Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility
    • Miyake M., Koyama M., Seno M., Ikeyama S. Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility. J. Exp. Med. 1991, 174:1347-1354.
    • (1991) J. Exp. Med. , vol.174 , pp. 1347-1354
    • Miyake, M.1    Koyama, M.2    Seno, M.3    Ikeyama, S.4
  • 52
    • 0030824577 scopus 로고    scopus 로고
    • Integrin cross talk: activation of lymphocyte function-associated antigen-1 on human T cells alters alpha4beta1- and alpha5beta1-mediated function
    • Porter J.C., Hogg N. Integrin cross talk: activation of lymphocyte function-associated antigen-1 on human T cells alters alpha4beta1- and alpha5beta1-mediated function. J. Cell Biol. 1997, 138:1437-1447.
    • (1997) J. Cell Biol. , vol.138 , pp. 1437-1447
    • Porter, J.C.1    Hogg, N.2
  • 53
    • 0025196196 scopus 로고
    • Human natural killer cell adhesion molecules. Differential expression after activation and participation in cytolysis
    • Robertson M.J., Caligiuri M.A., Manley T.J., Levine H., Ritz J. Human natural killer cell adhesion molecules. Differential expression after activation and participation in cytolysis. J. Immunol. 1990, 145:3194-3201.
    • (1990) J. Immunol. , vol.145 , pp. 3194-3201
    • Robertson, M.J.1    Caligiuri, M.A.2    Manley, T.J.3    Levine, H.4    Ritz, J.5
  • 54
    • 0242607362 scopus 로고    scopus 로고
    • The interaction of activated integrin lymphocyte function-associated antigen 1 with ligand intercellular adhesion molecule 1 induces activation and redistribution of focal adhesion kinase and proline-rich tyrosine kinase 2 in T lymphocytes
    • Rodriguez-Fernandez J.L., Gomez M., Luque A., Hogg N., Sanchez-Madrid F., Cabanas C. The interaction of activated integrin lymphocyte function-associated antigen 1 with ligand intercellular adhesion molecule 1 induces activation and redistribution of focal adhesion kinase and proline-rich tyrosine kinase 2 in T lymphocytes. Mol. Biol. Cell 1999, 10:1891-1907.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1891-1907
    • Rodriguez-Fernandez, J.L.1    Gomez, M.2    Luque, A.3    Hogg, N.4    Sanchez-Madrid, F.5    Cabanas, C.6
  • 56
    • 33745837412 scopus 로고    scopus 로고
    • EWI-2 and EWI-F link the tetraspanin web to the actin cytoskeleton through their direct association with ezrin-radixin-moesin proteins
    • Sala-Valdes M., Ursa A., Charrin S., Rubinstein E., Hemler M.E., Sanchez-Madrid F., Yanez-Mo M. EWI-2 and EWI-F link the tetraspanin web to the actin cytoskeleton through their direct association with ezrin-radixin-moesin proteins. J. Biol. Chem. 2006, 281:19665-19675.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19665-19675
    • Sala-Valdes, M.1    Ursa, A.2    Charrin, S.3    Rubinstein, E.4    Hemler, M.E.5    Sanchez-Madrid, F.6    Yanez-Mo, M.7
  • 57
    • 1842684991 scopus 로고    scopus 로고
    • Rolling adhesion through an extended conformation of integrin alphaLbeta2 and relation to alpha I and beta I-like domain interaction
    • Salas A., Shimaoka M., Kogan A.N., Harwood C., von Andrian U.H., Springer T.A. Rolling adhesion through an extended conformation of integrin alphaLbeta2 and relation to alpha I and beta I-like domain interaction. Immunity 2004, 20:393-406.
    • (2004) Immunity , vol.20 , pp. 393-406
    • Salas, A.1    Shimaoka, M.2    Kogan, A.N.3    Harwood, C.4    von Andrian, U.H.5    Springer, T.A.6
  • 58
    • 0021042037 scopus 로고
    • A human leukocyte differentiation antigen family with distinct alpha-subunits and a common beta-subunit: the lymphocyte function-associated antigen (LFA-1), the C3bi complement receptor (OKM1/Mac-1), and the p150,95 molecule
    • Sanchez-Madrid F., Nagy J.A., Robbins E., Simon P., Springer T.A. A human leukocyte differentiation antigen family with distinct alpha-subunits and a common beta-subunit: the lymphocyte function-associated antigen (LFA-1), the C3bi complement receptor (OKM1/Mac-1), and the p150,95 molecule. J. Exp. Med. 1983, 158:1785-1803.
    • (1983) J. Exp. Med. , vol.158 , pp. 1785-1803
    • Sanchez-Madrid, F.1    Nagy, J.A.2    Robbins, E.3    Simon, P.4    Springer, T.A.5
  • 61
    • 0030021514 scopus 로고    scopus 로고
    • CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the alpha 6/beta 1 integrin and the neural adhesion molecule L1
    • Schmidt C., Kunemund V., Wintergerst E.S., Schmitz B., Schachner M. CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the alpha 6/beta 1 integrin and the neural adhesion molecule L1. J. Neurosci. Res. 1996, 43:12-31.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 12-31
    • Schmidt, C.1    Kunemund, V.2    Wintergerst, E.S.3    Schmitz, B.4    Schachner, M.5
  • 62
    • 0032709802 scopus 로고    scopus 로고
    • Overexpression of CD82 on human T cells enhances LFA-1/ICAM-1-mediated cell-cell adhesion: functional association between CD82 and LFA-1 in T cell activation
    • Shibagaki N., Hanada K., Yamashita H., Shimada S., Hamada H. Overexpression of CD82 on human T cells enhances LFA-1/ICAM-1-mediated cell-cell adhesion: functional association between CD82 and LFA-1 in T cell activation. Eur. J. Immunol. 1999, 29:4081-4091.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 4081-4091
    • Shibagaki, N.1    Hanada, K.2    Yamashita, H.3    Shimada, S.4    Hamada, H.5
  • 63
    • 0036696174 scopus 로고    scopus 로고
    • The immunological synapse: integrins take the stage
    • Sims T.N., Dustin M.L. The immunological synapse: integrins take the stage. Immunol. Rev. 2002, 186:100-117.
    • (2002) Immunol. Rev. , vol.186 , pp. 100-117
    • Sims, T.N.1    Dustin, M.L.2
  • 64
    • 0030975429 scopus 로고    scopus 로고
    • Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin
    • Sincock P.M., Mayrhofer G., Ashman L.K. Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin. J. Histochem. Cytochem. 1997, 45:515-525.
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 515-525
    • Sincock, P.M.1    Mayrhofer, G.2    Ashman, L.K.3
  • 66
    • 0023069478 scopus 로고
    • The lymphocyte function-associated LFA-1, CD2, and LFA-3 molecules: cell adhesion receptors of the immune system
    • Springer T.A., Dustin M.L., Kishimoto T.K., Marlin S.D. The lymphocyte function-associated LFA-1, CD2, and LFA-3 molecules: cell adhesion receptors of the immune system. Annu. Rev. Immunol. 1987, 5:223-252.
    • (1987) Annu. Rev. Immunol. , vol.5 , pp. 223-252
    • Springer, T.A.1    Dustin, M.L.2    Kishimoto, T.K.3    Marlin, S.D.4
  • 68
    • 0033598128 scopus 로고    scopus 로고
    • Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance
    • Tachibana I., Hemler M.E. Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance. J. Cell Biol. 1999, 146:893-904.
    • (1999) J. Cell Biol. , vol.146 , pp. 893-904
    • Tachibana, I.1    Hemler, M.E.2
  • 70
    • 4344714152 scopus 로고    scopus 로고
    • Expression of tetraspanins in peripheral blood leukocytes: a comparison between normal and infectious conditions
    • Tohami T., Drucker L., Radnay J., Shapira H., Lishner M. Expression of tetraspanins in peripheral blood leukocytes: a comparison between normal and infectious conditions. Tissue Antigens 2004, 64:235-242.
    • (2004) Tissue Antigens , vol.64 , pp. 235-242
    • Tohami, T.1    Drucker, L.2    Radnay, J.3    Shapira, H.4    Lishner, M.5
  • 71
    • 0033824065 scopus 로고    scopus 로고
    • Avidity regulation of integrins: the driving force in leukocyte adhesion
    • van Kooyk Y., Figdor C.G. Avidity regulation of integrins: the driving force in leukocyte adhesion. Curr. Opin. Cell Biol. 2000, 12:542-547.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 542-547
    • van Kooyk, Y.1    Figdor, C.G.2
  • 72
    • 0024828456 scopus 로고
    • Enhancement of LFA-1-mediated cell adhesion by triggering through CD2 or CD3 on T lymphocytes
    • van Kooyk Y., van de Wiel-van Kemenade P., Weder P., Kuijpers T.W., Figdor C.G. Enhancement of LFA-1-mediated cell adhesion by triggering through CD2 or CD3 on T lymphocytes. Nature 1989, 342:811-813.
    • (1989) Nature , vol.342 , pp. 811-813
    • van Kooyk, Y.1    van de Wiel-van Kemenade, P.2    Weder, P.3    Kuijpers, T.W.4    Figdor, C.G.5
  • 73
    • 0027402368 scopus 로고
    • Lymphocyte function-associated antigen 1 dominates very late antigen 4 in binding of activated T cells to endothelium
    • van Kooyk Y., van de Wiel-van Kemenade E., Weder P., Huijbens R.J., Figdor C.G. Lymphocyte function-associated antigen 1 dominates very late antigen 4 in binding of activated T cells to endothelium. J. Exp. Med. 1993, 177:185-190.
    • (1993) J. Exp. Med. , vol.177 , pp. 185-190
    • van Kooyk, Y.1    van de Wiel-van Kemenade, E.2    Weder, P.3    Huijbens, R.J.4    Figdor, C.G.5
  • 75
    • 0035076601 scopus 로고    scopus 로고
    • Anti-CD81 activates LFA-1 on T cells and promotes T cell-B cell collaboration
    • VanCompernolle S.E., Levy S., Todd S.C. Anti-CD81 activates LFA-1 on T cells and promotes T cell-B cell collaboration. Eur. J. Immunol. 2001, 31:823-831.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 823-831
    • VanCompernolle, S.E.1    Levy, S.2    Todd, S.C.3
  • 78
    • 0032482216 scopus 로고    scopus 로고
    • Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with alpha3 beta1 integrin localized at endothelial lateral junctions
    • Yanez-Mo M., Alfranca A., Cabanas C., Marazuela M., Tejedor R., Ursa M.A., Ashman L.K., de Landazuri M.O., Sanchez-Madrid F. Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with alpha3 beta1 integrin localized at endothelial lateral junctions. J. Cell Biol. 1998, 141:791-804.
    • (1998) J. Cell Biol. , vol.141 , pp. 791-804
    • Yanez-Mo, M.1    Alfranca, A.2    Cabanas, C.3    Marazuela, M.4    Tejedor, R.5    Ursa, M.A.6    Ashman, L.K.7    de Landazuri, M.O.8    Sanchez-Madrid, F.9
  • 79
    • 0034331438 scopus 로고    scopus 로고
    • Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphoinositide 4-kinase
    • Yauch R.L., Hemler M.E. Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphoinositide 4-kinase. Biochem. J. 2000, 351(Pt 3):629-637.
    • (2000) Biochem. J. , vol.351 , pp. 629-637
    • Yauch, R.L.1    Hemler, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.