메뉴 건너뛰기




Volumn 137, Issue 3, 1997, Pages 755-765

Tenascin supports lymphocyte rolling

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTHELIAL LEUKOCYTE ADHESION MOLECULE 1; GLYCOPROTEIN; TENASCIN;

EID: 0030943601     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.137.3.755     Document Type: Review
Times cited : (63)

References (67)
  • 1
    • 0028910904 scopus 로고
    • Lifetime of the P-selectin: Carbohydrate bond and its response to tensile force in hydrodynamic flow
    • Alon, R., D.A. Hammer, and T.A. Springer. 1995. Lifetime of the P-selectin: carbohydrate bond and its response to tensile force in hydrodynamic flow. Nature (Lond.). 374:539-542.
    • (1995) Nature (Lond.) , vol.374 , pp. 539-542
    • Alon, R.1    Hammer, D.A.2    Springer, T.A.3
  • 3
    • 0030884913 scopus 로고    scopus 로고
    • The kinetics of L-selectin tethers and the mechanics of selectin-mediated rolling
    • In press
    • Alon, R., S. Chen, K.D. Puri, E.B. Finger, and T.A. Springer. 1997. The kinetics of L-selectin tethers and the mechanics of selectin-mediated rolling. J. Cell Biol. In press.
    • (1997) J. Cell Biol.
    • Alon, R.1    Chen, S.2    Puri, K.D.3    Finger, E.B.4    Springer, T.A.5
  • 4
    • 0028783449 scopus 로고
    • The versican C-type lectin domain recognizes the adhesion protein tenascin-R
    • Aspberg, A., C. Binkert, and E. Ruoslahti. 1995. The versican C-type lectin domain recognizes the adhesion protein tenascin-R. Proc. Natl. Acad. Sci. USA. 92:10590-10594.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10590-10594
    • Aspberg, A.1    Binkert, C.2    Ruoslahti, E.3
  • 5
    • 0027474006 scopus 로고
    • Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins
    • Aukhil, I., P. Joshi, Y. Yan, and H.P. Erickson. 1993. Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins. J. Biol. Chem. 268:2542-2553.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2542-2553
    • Aukhil, I.1    Joshi, P.2    Yan, Y.3    Erickson, H.P.4
  • 6
    • 0028235153 scopus 로고
    • Receptor tyrosine phosphatase beta is expressed in the form of proteoglycan and binds to the extracellular matrix protein tenascin
    • Barnea, G., M. Grumet, P. Milev, O. Silvennoinen, J.B. Levy, J. Sap, and J. Schlessinger. 1994. Receptor tyrosine phosphatase beta is expressed in the form of proteoglycan and binds to the extracellular matrix protein tenascin. J. Biol. Chem. 269:14349-14352.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14349-14352
    • Barnea, G.1    Grumet, M.2    Milev, P.3    Silvennoinen, O.4    Levy, J.B.5    Sap, J.6    Schlessinger, J.7
  • 7
    • 0029257527 scopus 로고
    • Human thymic epithelial cells express an endogenous lectin, galectin-1, which binds to core 2 O-glycans on thymocytes and T lymphoblastoid cells
    • Baum, L.G., M. Pang, N.L. Perillo, T. Wu, A. Delegeane, C.H. Uittenbogaart, M. Fukuda, and J.J. Seilhamer. 1995. Human thymic epithelial cells express an endogenous lectin, galectin-1, which binds to core 2 O-glycans on thymocytes and T lymphoblastoid cells. J. Exp. Med. 181:877-887.
    • (1995) J. Exp. Med. , vol.181 , pp. 877-887
    • Baum, L.G.1    Pang, M.2    Perillo, N.L.3    Wu, T.4    Delegeane, A.5    Uittenbogaart, C.H.6    Fukuda, M.7    Seilhamer, J.J.8
  • 8
    • 1842387948 scopus 로고
    • Immunohistological characterization of 15 blind panel mAb with predominantly extrafollicular reactivity on a panel of B-cell neoplasias
    • W. Knapp, B. Dorken, E.P. Rieber, H. Stein, W.R. Gilks, R.E. Schmidt, and A.E.G.Kr. von dem Borne, editors. Oxford University Press, New York
    • Beiske, K., I.-L. Nordli, and P.F. Marton. 1989. Immunohistological characterization of 15 blind panel mAb with predominantly extrafollicular reactivity on a panel of B-cell neoplasias. In Leucocyte Typing IV: White Cell Differentiation Antigens. W. Knapp, B. Dorken, E.P. Rieber, H. Stein, W.R. Gilks, R.E. Schmidt, and A.E.G.Kr. von dem Borne, editors. Oxford University Press, New York. 197-199.
    • (1989) Leucocyte Typing IV: White Cell Differentiation Antigens , pp. 197-199
    • Beiske, K.1    Nordli, I.-L.2    Marton, P.F.3
  • 10
    • 0027231385 scopus 로고
    • Tenascin-X: A novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B
    • Bristow, J., M.K. Tee, S.E. Gitelman, S.H. Mellon, and W.L. Miller. 1993. Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B. J. Cell Biol. 122:265-278.
    • (1993) J. Cell Biol. , vol.122 , pp. 265-278
    • Bristow, J.1    Tee, M.K.2    Gitelman, S.E.3    Mellon, S.H.4    Miller, W.L.5
  • 12
    • 0028305739 scopus 로고
    • Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C
    • Chung, C.Y., and H.P. Erickson. 1994. Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J. Cell Biol. 126:539-548.
    • (1994) J. Cell Biol. , vol.126 , pp. 539-548
    • Chung, C.Y.1    Erickson, H.P.2
  • 13
    • 0028866433 scopus 로고
    • Binding of tenascin-C to soluble fibronectin and matrix fibrils
    • Chung, C.Y., L. Zardi, and H.P. Erickson. 1995. Binding of tenascin-C to soluble fibronectin and matrix fibrils. J. Biol. Chem. 270:29012-29017.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29012-29017
    • Chung, C.Y.1    Zardi, L.2    Erickson, H.P.3
  • 14
    • 0001107681 scopus 로고
    • The reticulum of lymph nodes in mice studied with the electron microscope
    • Clark, S.L., Jr. 1962. The reticulum of lymph nodes in mice studied with the electron microscope. Am. J. Anal. 110:217-258.
    • (1962) Am. J. Anal. , vol.110 , pp. 217-258
    • Clark Jr., S.L.1
  • 15
    • 0029799440 scopus 로고    scopus 로고
    • CD44 and hyaluronan-dependent rolling interactions of lymphocytes on tonsillar stroma
    • Clark, R.A., R. Alon, and T.A. Springer. 1996. CD44 and hyaluronan-dependent rolling interactions of lymphocytes on tonsillar stroma. J. Cell Biol. 134:1075-1087.
    • (1996) J. Cell Biol. , vol.134 , pp. 1075-1087
    • Clark, R.A.1    Alon, R.2    Springer, T.A.3
  • 17
    • 0029966274 scopus 로고    scopus 로고
    • CD44 and its ligand hyaluronate mediate rolling under physiologic flow: A novel lymphocyte-endothelial cell primary adhesion pathway
    • Degrendele, H.C., P. Estess, L.J. Picker, and M.H. Siegelman. 1996. CD44 and its ligand hyaluronate mediate rolling under physiologic flow: a novel lymphocyte-endothelial cell primary adhesion pathway. J. Exp. Med. 183:1119-1130.
    • (1996) J. Exp. Med. , vol.183 , pp. 1119-1130
    • Degrendele, H.C.1    Estess, P.2    Picker, L.J.3    Siegelman, M.H.4
  • 19
    • 0027227425 scopus 로고
    • Maximal migration of human smooth muscle cells on fibronectin and type IV collagen occurs at an intermediate attachment strength
    • DiMilla, P.A., J.A. Stone, J.A. Quinn, S.M. Albelda, and D.A. Lauffenburger. 1993. Maximal migration of human smooth muscle cells on fibronectin and type IV collagen occurs at an intermediate attachment strength. J. Cell Biol. 122:729-737.
    • (1993) J. Cell Biol. , vol.122 , pp. 729-737
    • DiMilla, P.A.1    Stone, J.A.2    Quinn, J.A.3    Albelda, S.M.4    Lauffenburger, D.A.5
  • 20
    • 0019778599 scopus 로고
    • Fibrinogen and fibrin
    • Doolittle, R.F. 1981. Fibrinogen and fibrin. Sci. Am. 245:126-135.
    • (1981) Sci. Am. , vol.245 , pp. 126-135
    • Doolittle, R.F.1
  • 21
    • 0001630685 scopus 로고
    • B-cell antigens: CD39
    • W. Knapp, B. Dorken, E.P. Rieber, H. Stein, W.R. Gilks, R.E. Schmidt, and A.E.G.Kr. von dem Borne, editors. Oxford University Press, New York
    • Dorken, B., P. Moller, A. Pezzutto, R. Schwartz-Albiez, and G. Moldenhauer. 1989. B-cell antigens: CD39. In Leucocyte Typing IV: White Cell Differentiation Antigens. W. Knapp, B. Dorken, E.P. Rieber, H. Stein, W.R. Gilks, R.E. Schmidt, and A.E.G.Kr. von dem Borne, editors. Oxford University Press, New York. 89-90.
    • (1989) Leucocyte Typing IV: White Cell Differentiation Antigens , pp. 89-90
    • Dorken, B.1    Moller, P.2    Pezzutto, A.3    Schwartz-Albiez, R.4    Moldenhauer, G.5
  • 22
    • 0029989478 scopus 로고    scopus 로고
    • Distinct effects of recombinant tenascin-C domains on neuronal cell adhesion, growth cone guidance, and neuronal polarity
    • Dorries, U., J. Taylor, Z. Xiao, A. Lochter, D. Montag, and M. Schachner. 1996. Distinct effects of recombinant tenascin-C domains on neuronal cell adhesion, growth cone guidance, and neuronal polarity. J. Neurosci. Res. 43:420-438.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 420-438
    • Dorries, U.1    Taylor, J.2    Xiao, Z.3    Lochter, A.4    Montag, D.5    Schachner, M.6
  • 23
    • 0024095296 scopus 로고
    • Fibronectin receptor exhibits high lateral mobility in embryonic locomoting cells but is immobile in focal contacts and fibrillar streaks in stationary cells
    • Duband, J.L., G.H. Nuckolls, A. Ishihara, and T. Hasegawa. 1988. Fibronectin receptor exhibits high lateral mobility in embryonic locomoting cells but is immobile in focal contacts and fibrillar streaks in stationary cells. J. Cell Biol. 107:1385-1396.
    • (1988) J. Cell Biol. , vol.107 , pp. 1385-1396
    • Duband, J.L.1    Nuckolls, G.H.2    Ishihara, A.3    Hasegawa, T.4
  • 24
    • 0024441046 scopus 로고
    • Tenascin: An extracellular matrix protein prominent in specialized embryonic tissues and tumors
    • Erickson, H.P. 1989. Tenascin: an extracellular matrix protein prominent in specialized embryonic tissues and tumors. Annu. Rev. Cell Biol. 5:71-92.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 71-92
    • Erickson, H.P.1
  • 25
    • 0028694581 scopus 로고
    • Evolution of the tenascin family: Implications for function of the C-terminal fibrinogen-like domain
    • Erickson, H.P. 1994. Evolution of the tenascin family: implications for function of the C-terminal fibrinogen-like domain. Perspect. Dev. Neurobiol. 2:9-19.
    • (1994) Perspect. Dev. Neurobiol. , vol.2 , pp. 9-19
    • Erickson, H.P.1
  • 26
    • 0021166341 scopus 로고
    • A six-armed oligomer isolated from cell surface fibronectin preparations
    • Erickson, H.P., and J.L. Iglesias. 1984. A six-armed oligomer isolated from cell surface fibronectin preparations. Nature (Lond.). 311:267-269.
    • (1984) Nature (Lond.) , vol.311 , pp. 267-269
    • Erickson, H.P.1    Iglesias, J.L.2
  • 27
    • 0030839023 scopus 로고    scopus 로고
    • Glycosamino glycans modulate fibronectin matrix assembly and are essential for matrix incorporation of tenascin-C
    • In press
    • 26a. Erickson, H.P, and C.Y. Chung. 1997. Glycosamino glycans modulate fibronectin matrix assembly and are essential for matrix incorporation of tenascin-C. J. Cell Sci. In press.
    • (1997) J. Cell Sci.
    • Erickson, H.P.1    Chung, C.Y.2
  • 28
    • 0028813381 scopus 로고
    • A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C
    • Fischer, D., R. Chiquet-Ehrismann, C. Bernasconi, and M. Chiquet. 1995. A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C. J. Biol. Chem. 270:3378-3384.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3378-3384
    • Fischer, D.1    Chiquet-Ehrismann, R.2    Bernasconi, C.3    Chiquet, M.4
  • 29
    • 0029844407 scopus 로고    scopus 로고
    • Sialylated, fucosylated ligands for L-selectin expressed on leukocytes mediate tethering and rolling adhesions in physiologic flow conditions
    • Fuhlbrigge, R.C., R. Alon, K.D. Puri, J.B. Lowe, and T.A. Springer. 1996. Sialylated, fucosylated ligands for L-selectin expressed on leukocytes mediate tethering and rolling adhesions in physiologic flow conditions. J. Cell Biol. 135:837-848.
    • (1996) J. Cell Biol. , vol.135 , pp. 837-848
    • Fuhlbrigge, R.C.1    Alon, R.2    Puri, K.D.3    Lowe, J.B.4    Springer, T.A.5
  • 30
    • 0027397492 scopus 로고
    • Molecular characterization and in situ mRNA localization of the neural recognition molecule J1-160/180: A modular structure similar to tenascin
    • Fuss, B., E.-S. Wintergerst, U. Bartsch, and M. Schachner. 1993. Molecular characterization and in situ mRNA localization of the neural recognition molecule J1-160/180: a modular structure similar to tenascin. J. Cell Biol. 120:1237-1249.
    • (1993) J. Cell Biol. , vol.120 , pp. 1237-1249
    • Fuss, B.1    Wintergerst, E.-S.2    Bartsch, U.3    Schachner, M.4
  • 32
    • 0028360757 scopus 로고
    • Interactions with tenascin and differential effects on cell adhesion of neurocan and phosphacan, two major chondroitin sulfate proteoglycans of nervous tissue
    • Grumet, M., P. Milev, T. Sakurai, L. Karthikeyan, M. Bourdon, R.K. Margolis, and R.U. Margolis. 1994. Interactions with tenascin and differential effects on cell adhesion of neurocan and phosphacan, two major chondroitin sulfate proteoglycans of nervous tissue. J. Biol. Chem. 269:12142-12146.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12142-12146
    • Grumet, M.1    Milev, P.2    Sakurai, T.3    Karthikeyan, L.4    Bourdon, M.5    Margolis, R.K.6    Margolis, R.U.7
  • 33
    • 0028196892 scopus 로고
    • Expression of tenascin in thymus and thymic nonlymphoid cells
    • Hemesath, T.J. and K. Stefansson. 1994. Expression of tenascin in thymus and thymic nonlymphoid cells. J. Immunol. 152:422-428.
    • (1994) J. Immunol. , vol.152 , pp. 422-428
    • Hemesath, T.J.1    Stefansson, K.2
  • 34
    • 0028318688 scopus 로고
    • Inhibition of T cell activation by the extracellular matrix protein tenascin
    • Hemesath, T.J., L.S. Marton, and K. Stefansson. 1994. Inhibition of T cell activation by the extracellular matrix protein tenascin. J. Immunol. 152: 5199-5207.
    • (1994) J. Immunol. , vol.152 , pp. 5199-5207
    • Hemesath, T.J.1    Marton, L.S.2    Stefansson, K.3
  • 35
    • 0027374172 scopus 로고
    • P-selectin mediates neutrophil rolling on histamine-stimulated endothelial cells
    • Jones, D.A., O. Abbassi, L.V. McIntire, R.P. McEver, and C.W. Smith. 1993. P-selectin mediates neutrophil rolling on histamine-stimulated endothelial cells. Biophys. J. 65:1560-1569.
    • (1993) Biophys. J. , vol.65 , pp. 1560-1569
    • Jones, D.A.1    Abbassi, O.2    McIntire, L.V.3    McEver, R.P.4    Smith, C.W.5
  • 36
    • 0027497077 scopus 로고
    • Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin
    • Joshi, P., C.-Y. Chung, I. Aukhil, and H.P. Erickson. 1993. Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin. J. Cell Sci. 106:389-400.
    • (1993) J. Cell Sci. , vol.106 , pp. 389-400
    • Joshi, P.1    Chung, C.-Y.2    Aukhil, I.3    Erickson, H.P.4
  • 37
    • 0025210021 scopus 로고
    • Identification of a human peripheral lymph node homing receptor: A rapidly down-regulated adhesion molecule
    • Kishimoto, T.K., M.A. Jutila, and E.C. Butcher. 1990. Identification of a human peripheral lymph node homing receptor: a rapidly down-regulated adhesion molecule. Proc. Natl. Acad. Sci. USA. 87:2244-2248.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2244-2248
    • Kishimoto, T.K.1    Jutila, M.A.2    Butcher, E.C.3
  • 38
    • 0027517137 scopus 로고
    • Tenascin is a cytoadhesive extracellular matrix component of the human hematopoietic microenvironment
    • Klein, G., S. Beck, and C.A. Muller. 1993. Tenascin is a cytoadhesive extracellular matrix component of the human hematopoietic microenvironment. J. Cell Biol. 123:1027-1035.
    • (1993) J. Cell Biol. , vol.123 , pp. 1027-1035
    • Klein, G.1    Beck, S.2    Muller, C.A.3
  • 39
    • 0023936681 scopus 로고
    • Basement-membrane components associated with the extracellular matrix of the lymph node
    • Kramer, R.H., S.D. Rosen, and K.A. McDonald. 1988. Basement-membrane components associated with the extracellular matrix of the lymph node. Cell Tissue Res. 252:367-375.
    • (1988) Cell Tissue Res. , vol.252 , pp. 367-375
    • Kramer, R.H.1    Rosen, S.D.2    McDonald, K.A.3
  • 40
    • 0027318675 scopus 로고
    • Fibrinogen mediates leukocyte adhesion to vascular endothelium through an ICAM-1-dependent pathway
    • Languino, L.R., J. Plescia, A. Duperray, A.A. Brian, E.F. Plow, J.E. Geltosky, and D.C. Altieri. 1993. Fibrinogen mediates leukocyte adhesion to vascular endothelium through an ICAM-1-dependent pathway. Cell. 73: 1423-1434.
    • (1993) Cell , vol.73 , pp. 1423-1434
    • Languino, L.R.1    Plescia, J.2    Duperray, A.3    Brian, A.A.4    Plow, E.F.5    Geltosky, J.E.6    Altieri, D.C.7
  • 41
    • 0025907837 scopus 로고
    • Models for receptor-mediated cell phenomena: Adhesion and migration
    • Lauffenburger, D.A. 1991. Models for receptor-mediated cell phenomena: adhesion and migration. Annu. Rev. Biophys. Biophys. Chem. 20:387-414.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 387-414
    • Lauffenburger, D.A.1
  • 42
    • 0025854524 scopus 로고
    • Leukocytes roll on a selcctin at physiologic flow rates: Distinction from and prerequisite for adhesion through integrins
    • Lawrence, M.B., and T.A. Springer. 1991. Leukocytes roll on a selcctin at physiologic flow rates: distinction from and prerequisite for adhesion through integrins. Cell. 65:859-873.
    • (1991) Cell , vol.65 , pp. 859-873
    • Lawrence, M.B.1    Springer, T.A.2
  • 43
    • 0028429944 scopus 로고
    • Neutrophil tethering to and rolling on E-selectin are separable by requirement for L-selectin
    • Lawrence, M.B., D.F. Bainton, and T.A. Springer. 1994. Neutrophil tethering to and rolling on E-selectin are separable by requirement for L-selectin. Immunity. 1:137-145.
    • (1994) Immunity , vol.1 , pp. 137-145
    • Lawrence, M.B.1    Bainton, D.F.2    Springer, T.A.3
  • 44
    • 0029135225 scopus 로고
    • Immuno-electron-microscopic localization of types III pN-collagen and IV collagen, laminin and tenascin in developing and adult human spleen
    • Liakka, A., H. Karjalainen, I. Virtanen, and H. Autio-Harmainen. 1995. Immuno-electron-microscopic localization of types III pN-collagen and IV collagen, laminin and tenascin in developing and adult human spleen. Cell Tissue Res. 282:117-127.
    • (1995) Cell Tissue Res. , vol.282 , pp. 117-127
    • Liakka, A.1    Karjalainen, H.2    Virtanen, I.3    Autio-Harmainen, H.4
  • 45
    • 0028879844 scopus 로고
    • Complex-type asparagine-like oligosaccharides on phosphacan and protein-tyrosine phosphatase-zeta/beta mediate their binding to neural cell adhesion molecules and tenascin
    • Milev, P., B. Meyer-Puttlitz, R.K. Margolis, and R.U. Margolis. 1995. Complex-type asparagine-like oligosaccharides on phosphacan and protein-tyrosine phosphatase-zeta/beta mediate their binding to neural cell adhesion molecules and tenascin. J. Biol. Chem. 270:24650-24653.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24650-24653
    • Milev, P.1    Meyer-Puttlitz, B.2    Margolis, R.K.3    Margolis, R.U.4
  • 46
    • 0026633247 scopus 로고
    • The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs
    • Norenberg, U., H. Wille, J.M. Wolff, R. Frank, and F.G. Rathjen. 1992. The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs. Neuron. 8: 849-863.
    • (1992) Neuron. , vol.8 , pp. 849-863
    • Norenberg, U.1    Wille, H.2    Wolff, J.M.3    Frank, R.4    Rathjen, F.G.5
  • 47
    • 0027364324 scopus 로고
    • Multiple integrins mediate cell attachment to cytotactin/tenascin
    • Prieto, A.L., G.M. Edelman, and K.L. Crossin. 1993. Multiple integrins mediate cell attachment to cytotactin/tenascin. Proc. Natl. Acad. Sci. USA. 90:10154-10158.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10154-10158
    • Prieto, A.L.1    Edelman, G.M.2    Crossin, K.L.3
  • 48
    • 0029095492 scopus 로고
    • Sialomucin CD34 is the major L-selectin ligand in human tonsil high endothelial venules
    • Puri, K.D., E.B. Finger, G. Gaudernack, and T.A. Springer. 1995. Sialomucin CD34 is the major L-selectin ligand in human tonsil high endothelial venules. J. Cell Biol. 131:261-270.
    • (1995) J. Cell Biol. , vol.131 , pp. 261-270
    • Puri, K.D.1    Finger, E.B.2    Gaudernack, G.3    Springer, T.A.4
  • 49
    • 0030636972 scopus 로고    scopus 로고
    • The faster kinetics of L-selectin than E-selectin and P-selectin rolling at comparable binding strength
    • Puri, K.D., E.B. Finger, and T.A. Springer. 1997. The faster kinetics of L-selectin than E-selectin and P-selectin rolling at comparable binding strength. J. Immunol. 158:405-413.
    • (1997) J. Immunol. , vol.158 , pp. 405-413
    • Puri, K.D.1    Finger, E.B.2    Springer, T.A.3
  • 50
    • 0029621171 scopus 로고
    • Characterization of transendothelial chemotaxis of T lymphocytes
    • Roth, S.J., M.W. Carr, S.S. Rose, and T.A. Springer. 1995. Characterization of transendothelial chemotaxis of T lymphocytes. J. Immunol. Methods. 100:97-116.
    • (1995) J. Immunol. Methods. , vol.100 , pp. 97-116
    • Roth, S.J.1    Carr, M.W.2    Rose, S.S.3    Springer, T.A.4
  • 51
    • 0344778246 scopus 로고
    • Tenascin, an extracellular matrix protein, exerts immunomodulatory activities
    • Ruegg, C.R., R. Chiquel-Ehrismann, and S.S. Alkan. 1989. Tenascin, an extracellular matrix protein, exerts immunomodulatory activities. Proc. Natl. Acad. Sci. USA. 86:7437-7441.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7437-7441
    • Ruegg, C.R.1    Chiquel-Ehrismann, R.2    Alkan, S.S.3
  • 53
    • 0028981367 scopus 로고
    • The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin
    • Schnapp, L.M., N. Hatch, D.M. Ramos, I.V. Klimanskaya, D. Sheppard, and R. Pytela. 1995. The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin. J. Biol. Chem. 270: 23196-23202.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23196-23202
    • Schnapp, L.M.1    Hatch, N.2    Ramos, D.M.3    Klimanskaya, I.V.4    Sheppard, D.5    Pytela, R.6
  • 54
    • 0002015284 scopus 로고
    • Leucocyte differentiation antigen database
    • S.F. Schlossman, L. Boumsell, W. Gilks, J. Harlan, T. Kishimoto, T. Morimoto, J. Ritz, S. Shaw, R. Silverstein, T. Springer, T. Tedder, and R. Todd, editors. Oxford University Press, New York
    • Shaw, S., G.G. Luce, W.R. Gilks, K. Anderson, K. Ault, B.S. Bochner, L. Boumsell, S.M. Denning, E.G. Engleman, T. Fleisher, et al. 1995. Leucocyte differentiation antigen database. In Leucocyte Typing V: White Cell Differentiation Antigens. S.F. Schlossman, L. Boumsell, W. Gilks, J. Harlan, T. Kishimoto, T. Morimoto, J. Ritz, S. Shaw, R. Silverstein, T. Springer, T. Tedder, and R. Todd, editors. Oxford University Press, New York. 16-198.
    • (1995) Leucocyte Typing V: White Cell Differentiation Antigens , pp. 16-198
    • Shaw, S.1    Luce, G.G.2    Gilks, W.R.3    Anderson, K.4    Ault, K.5    Bochner, B.S.6    Boumsell, L.7    Denning, S.M.8    Engleman, E.G.9    Fleisher, T.10
  • 55
    • 0028935791 scopus 로고
    • Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration
    • Springer, T.A. 1995. Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration. Annu. Rev. Physiol. 57:827-872.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 827-872
    • Springer, T.A.1
  • 56
    • 0018758819 scopus 로고
    • Mac-1: A macrophage differentiation antigen identified by monoclonal antibody
    • Springer, T., G. Galfre, D.S. Secher, and C. Milstein. 1979. Mac-1: a macrophage differentiation antigen identified by monoclonal antibody. Eur. J. Immunol. 9:301-306.
    • (1979) Eur. J. Immunol. , vol.9 , pp. 301-306
    • Springer, T.1    Galfre, G.2    Secher, D.S.3    Milstein, C.4
  • 58
    • 0026087677 scopus 로고
    • Leukocyte integrin p150,95 (CD11c/CD18) functions as an adhesion molecule binding to a counter-receptor on stimulated endothelium
    • Stacker, S.A., and T.A. Springer. 1991. Leukocyte integrin p150,95 (CD11c/CD18) functions as an adhesion molecule binding to a counter-receptor on stimulated endothelium. J. Immunol. 146:648-655.
    • (1991) J. Immunol. , vol.146 , pp. 648-655
    • Stacker, S.A.1    Springer, T.A.2
  • 59
    • 0001005471 scopus 로고
    • Cluster report: CD26
    • W. Knapp, B. Dorken, E.P. Rieber, H. Stein, W.R. Gilks, R.E. Schmidt, and A.E.G.Kr. von dem Borne, editors. Oxford University Press, New York
    • Stein, H., R. Schwarting, and G. Niedobitek. 1989. Cluster report: CD26. In Leucocyte Typing IV: White Cell Differentiation Antigens. W. Knapp, B. Dorken, E.P. Rieber, H. Stein, W.R. Gilks, R.E. Schmidt, and A.E.G.Kr. von dem Borne, editors. Oxford University Press, New York. 412-415.
    • (1989) Leucocyte Typing IV: White Cell Differentiation Antigens , pp. 412-415
    • Stein, H.1    Schwarting, R.2    Niedobitek, G.3
  • 61
    • 0028171789 scopus 로고
    • Integrin alpha 6 beta 4 mediates dynamic interactions with laminin
    • Tözeren, A., H.K. Kleinman, S. Wu, A.M. Mercurio, and S.W. Byers. 1994. Integrin alpha 6 beta 4 mediates dynamic interactions with laminin. J. Cell Sci. 107:3153-3163.
    • (1994) J. Cell Sci. , vol.107 , pp. 3153-3163
    • Tözeren, A.1    Kleinman, H.K.2    Wu, S.3    Mercurio, A.M.4    Byers, S.W.5
  • 62
    • 0028980730 scopus 로고
    • The integrin receptor alpha 8 beta 1 mediates interactions of embryonic chick motor and sensory neurons with tenascin-C
    • Varnum-Finney, B., K. Venstrom, U. Muller, R. Kypla, C. Backus, M. Chiquet, and L.F. Reichardt. 1995. The integrin receptor alpha 8 beta 1 mediates interactions of embryonic chick motor and sensory neurons with tenascin-C. Neuron. 14:1213-1222.
    • (1995) Neuron. , vol.14 , pp. 1213-1222
    • Varnum-Finney, B.1    Venstrom, K.2    Muller, U.3    Kypla, R.4    Backus, C.5    Chiquet, M.6    Reichardt, L.F.7
  • 64
    • 0028924268 scopus 로고
    • Tenascin-C binds heparin by its fibronectin type III domain five
    • Weber, P., D.R. Zimmermann, K.H. Winterhalter, and L. Vaughan. 1995. Tenascin-C binds heparin by its fibronectin type III domain five. J. Biol. Chem. 270:4619-4623.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4619-4623
    • Weber, P.1    Zimmermann, D.R.2    Winterhalter, K.H.3    Vaughan, L.4
  • 65
    • 0025847137 scopus 로고
    • The extracellular matrix of lip wounds in fetal, neonatal and adult mice
    • Whitby, D.J., and M.W.J. Ferguson. 1991. The extracellular matrix of lip wounds in fetal, neonatal and adult mice. Development. 112:651-668.
    • (1991) Development , vol.112 , pp. 651-668
    • Whitby, D.J.1    Ferguson, M.W.J.2
  • 66
    • 0025813411 scopus 로고
    • Rapid epithelialisation of fetal wounds is associated with the early deposition of tenascin
    • Whitby, D.J., M.T. Longaker, M.R. Harrison, N.S. Adzick, and M.W.J. Ferguson. 1991. Rapid epithelialisation of fetal wounds is associated with the early deposition of tenascin. J. Cell Sci. 99:583-586.
    • (1991) J. Cell Sci. , vol.99 , pp. 583-586
    • Whitby, D.J.1    Longaker, M.T.2    Harrison, M.R.3    Adzick, N.S.4    Ferguson, M.W.J.5
  • 67
    • 0028171068 scopus 로고
    • The integrin alpha 9 beta 1 mediates cell attachment to a non-RGD site in the third fibronectin type III repeat of tenascin
    • Yokosaki, Y., E.L. Palmer, A.L. Prieto, K.L. Crossin, M.A. Bourdon, R. Pytela, and D. Sheppard. 1994. The integrin alpha 9 beta 1 mediates cell attachment to a non-RGD site in the third fibronectin type III repeat of tenascin. J. Biol. Chem. 269:26691-26696.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26691-26696
    • Yokosaki, Y.1    Palmer, E.L.2    Prieto, A.L.3    Crossin, K.L.4    Bourdon, M.A.5    Pytela, R.6    Sheppard, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.