메뉴 건너뛰기




Volumn 157, Issue 1, 1996, Pages 321-325

The cytoplasmic domains of E- and P-selectin do not constitutively interact with α-actinin and are not essential for leukocyte adhesion

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA ACTININ; ENDOTHELIAL LEUKOCYTE ADHESION MOLECULE 1; PADGEM PROTEIN; VINCULIN;

EID: 0030010583     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (32)

References (37)
  • 1
    • 0026342111 scopus 로고
    • Leukocyte-endothelial cell recognition: Three (or more) steps to specificity and diversity
    • Butcher, E. C. 1991. Leukocyte-endothelial cell recognition: three (or more) steps to specificity and diversity. Cell 67:1033.
    • (1991) Cell , vol.67 , pp. 1033
    • Butcher, E.C.1
  • 2
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer, T. A. 1994. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 76:301.
    • (1994) Cell , vol.76 , pp. 301
    • Springer, T.A.1
  • 3
    • 0029074732 scopus 로고
    • The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via α-actinin: Receptor positioning in microvilli does not require interaction with α-actinin
    • Pavalko, F. M., D. M. Walker, L. Graham, M. Goheen, C. M. Doerschuk, and G. S. Kansas. 1995. The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via α-actinin: receptor positioning in microvilli does not require interaction with α-actinin. J. Cell Biol. 129:1155.
    • (1995) J. Cell Biol. , vol.129 , pp. 1155
    • Pavalko, F.M.1    Walker, D.M.2    Graham, L.3    Goheen, M.4    Doerschuk, C.M.5    Kansas, G.S.6
  • 4
    • 0027509819 scopus 로고
    • Regulation of leukocyte rolling and adhesion to HEV through the cytoplasmic domain of L-selectin
    • Kansas, G. S., K. Ley, J. M. Munro, and T. F. Tedder. 1993. Regulation of leukocyte rolling and adhesion to HEV through the cytoplasmic domain of L-selectin. J. Exp. Med. 177:833.
    • (1993) J. Exp. Med. , vol.177 , pp. 833
    • Kansas, G.S.1    Ley, K.2    Munro, J.M.3    Tedder, T.F.4
  • 6
    • 0025781222 scopus 로고
    • Molecular mapping of functional domains of the leukocyte receptor for endothelium, LAM-1
    • Kansas, G. S., O. Spertini, L. M. Stoolman, and T. F. Tedder. 1991. Molecular mapping of functional domains of the leukocyte receptor for endothelium, LAM-1. J. Cell Biol. 114:351.
    • (1991) J. Cell Biol. , vol.114 , pp. 351
    • Kansas, G.S.1    Spertini, O.2    Stoolman, L.M.3    Tedder, T.F.4
  • 7
    • 0027178702 scopus 로고
    • L-selectin can mediate rolling independent of E- and P-selectin in mesenteric venules in vivo
    • Ley, K., T. F. Tedder, and G. S. Kansas. 1993. L-selectin can mediate rolling independent of E- and P-selectin in mesenteric venules in vivo. Blood 82:1632.
    • (1993) Blood , vol.82 , pp. 1632
    • Ley, K.1    Tedder, T.F.2    Kansas, G.S.3
  • 9
    • 0022476208 scopus 로고
    • The requirement for lymphocyte function-associated antigen 1 in homotypic leukocyte adhesion stimulated by phorbol ester
    • Rothlein, R., and T. A. Springer. 1986. The requirement for lymphocyte function-associated antigen 1 in homotypic leukocyte adhesion stimulated by phorbol ester. J. Exp. Med. 163:1132.
    • (1986) J. Exp. Med. , vol.163 , pp. 1132
    • Rothlein, R.1    Springer, T.A.2
  • 10
    • 0022453692 scopus 로고
    • A human intercellular adhesion molecule (ICAM-1) distinct from LFA-1
    • Rothlein, R., M. L. Dustin, S. D. Marlin, and T. A. Springer. 1986. A human intercellular adhesion molecule (ICAM-1) distinct from LFA-1. J. Immunol. 137:1270.
    • (1986) J. Immunol. , vol.137 , pp. 1270
    • Rothlein, R.1    Dustin, M.L.2    Marlin, S.D.3    Springer, T.A.4
  • 11
    • 0026504051 scopus 로고
    • Lymphocyte adhesion through very late antigen-4: Evidence for a novel binding site in the alternatively spliced domain of vascular cell adhesion molecule-1 and an additional α4 integrin counterreceptor on stimulated endothelium
    • Vonderheide, R. H., and T. A. Springer. 1992. Lymphocyte adhesion through very late antigen-4: evidence for a novel binding site in the alternatively spliced domain of vascular cell adhesion molecule-1 and an additional α4 integrin counterreceptor on stimulated endothelium. J. Exp. Med. 175:1433.
    • (1992) J. Exp. Med. , vol.175 , pp. 1433
    • Vonderheide, R.H.1    Springer, T.A.2
  • 12
    • 0024818401 scopus 로고
    • Direct expression cloning of vascular cell adhesion molecule-1, a cytokine-induced endothelial protein that binds to lymphocytes
    • Osborn, L., C. Hession, R. Tizard, C. Vassallo, S. Luhowskyj, G. Chi-Rosso, and R. Lobb. 1989. Direct expression cloning of vascular cell adhesion molecule-1, a cytokine-induced endothelial protein that binds to lymphocytes. Cell 59:1203.
    • (1989) Cell , vol.59 , pp. 1203
    • Osborn, L.1    Hession, C.2    Tizard, R.3    Vassallo, C.4    Luhowskyj, S.5    Chi-Rosso, G.6    Lobb, R.7
  • 13
    • 0027931392 scopus 로고
    • Shear stress selectively upregulates intercellular adhesion molecule-1 expression in cultured human vascular endothelial cells
    • Nagel, T., N. Resnick, W. J. Atkinson, C. F. Dewey Jr., and M. A. Gimbrone Jr. 1994. Shear stress selectively upregulates intercellular adhesion molecule-1 expression in cultured human vascular endothelial cells. J. Clin. Invest. 94:885.
    • (1994) J. Clin. Invest. , vol.94 , pp. 885
    • Nagel, T.1    Resnick, N.2    Atkinson, W.J.3    Dewey Jr., C.F.4    Gimbrone Jr., M.A.5
  • 14
    • 0019320755 scopus 로고
    • A rapid purification of α-actinin, filamin, and a 130,000-dalton protein from smooth muscle
    • Feramisco, J. R., and K. Burridge. 1980. A rapid purification of α-actinin, filamin, and a 130,000-dalton protein from smooth muscle. J. Biol. Chem. 255:1194.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1194
    • Feramisco, J.R.1    Burridge, K.2
  • 15
    • 0017874586 scopus 로고
    • Protein and cell membrane iodinations with a sparingly soluble chloroamide
    • Fraker, P. J., and J. C. Speck. 1978. Protein and cell membrane iodinations with a sparingly soluble chloroamide. Biochem. Biophys. Res. Commun. 80:849.
    • (1978) Biochem. Biophys. Res. Commun. , vol.80 , pp. 849
    • Fraker, P.J.1    Speck, J.C.2
  • 16
    • 0027317933 scopus 로고
    • Activation of human neutrophils induces an interaction between the integrin β 2-subunit (CD18) and the actin binding protein α-actinin
    • Pavalko, F. M., and S. M. LaRoche. 1993. Activation of human neutrophils induces an interaction between the integrin β 2-subunit (CD18) and the actin binding protein α-actinin. J. Immunol. 151:3795.
    • (1993) J. Immunol. , vol.151 , pp. 3795
    • Pavalko, F.M.1    LaRoche, S.M.2
  • 17
    • 0022402201 scopus 로고
    • Pathways of protein secretion in eukaryotes
    • Kelly, R. B. 1985. Pathways of protein secretion in eukaryotes. Science 230:25.
    • (1985) Science , vol.230 , pp. 25
    • Kelly, R.B.1
  • 18
    • 0023463127 scopus 로고
    • Constitutive and regulated secretion of proteins
    • Burgess, T. L., and R. B. Kelly. 1987. Constitutive and regulated secretion of proteins. Annu. Rev. Cell Biol. 3:243.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 243
    • Burgess, T.L.1    Kelly, R.B.2
  • 19
    • 0026517633 scopus 로고
    • P-selectin, a granule membrane protein of platelets and endothelial cells, follows the regulated secretory pathway in AtT-20 cells
    • Koedam, J. A., E. M. Cramer. E. Briend, B. Furie, B. C. Furie, and D. A. Wagner. 1992. P-selectin, a granule membrane protein of platelets and endothelial cells, follows the regulated secretory pathway in AtT-20 cells. J. Cell Biol. 116:617.
    • (1992) J. Cell Biol. , vol.116 , pp. 617
    • Koedam, J.A.1    Cramer, E.M.2    Briend, E.3    Furie, B.4    Furie, B.C.5    Wagner, D.A.6
  • 20
    • 0025291522 scopus 로고
    • An interaction between alpha-actinin and the beta 1 integrin subunit in vitro
    • Otey, C. A., F. M. Pavalko, and K. Burridge. 1990. An interaction between alpha-actinin and the beta 1 integrin subunit in vitro. J. Cell Biol. 111:721.
    • (1990) J. Cell Biol. , vol.111 , pp. 721
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 21
    • 0028979956 scopus 로고
    • Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin
    • Knudsen, K. A., A. P. Soler, K. R. Johnson, and M. J. Wheelock. 1995. Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin. J. Cell Biol. 130:67.
    • (1995) J. Cell Biol. , vol.130 , pp. 67
    • Knudsen, K.A.1    Soler, A.P.2    Johnson, K.R.3    Wheelock, M.J.4
  • 22
    • 0028040474 scopus 로고
    • Cadherins and catenins: Interactions and functions in embryonic development
    • Ranscht, B. 1994. Cadherins and catenins: interactions and functions in embryonic development. Curr. Opin. Cell Biol. 6:740.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 740
    • Ranscht, B.1
  • 23
    • 0027938682 scopus 로고
    • A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated
    • Stappert, J., and R. Kemler. 1994. A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated. Cell Adh. Commun. 2:319.
    • (1994) Cell Adh. Commun. , vol.2 , pp. 319
    • Stappert, J.1    Kemler, R.2
  • 24
    • 0027185632 scopus 로고
    • From cadherins to catenins: Cytoplasmic protein interactions and regulation of cell adhesion
    • Kemler, R. 1993. From cadherins to catenins: cytoplasmic protein interactions and regulation of cell adhesion. Trends Genet. 9:317.
    • (1993) Trends Genet. , vol.9 , pp. 317
    • Kemler, R.1
  • 25
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cyloskeletons
    • Tsukita, S., K. Oishi, N. Sato, J. Sagara, A. Kawai, and S. Tsukita. 1994. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cyloskeletons. J. Cell Biol. 126:391.
    • (1994) J. Cell Biol. , vol.126 , pp. 391
    • Tsukita, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5    Tsukita, S.6
  • 26
    • 0028141591 scopus 로고
    • Ankyrin-binding domain of CD44 (GP85) is required for the expression of hyaluronic acid-mediated adhesion function
    • Lokeshwar, V. B., N. Fregien, and L. Y. Bourguignon. 1994. Ankyrin-binding domain of CD44 (GP85) is required for the expression of hyaluronic acid-mediated adhesion function. J. Cell Biol. 126:1099.
    • (1994) J. Cell Biol. , vol.126 , pp. 1099
    • Lokeshwar, V.B.1    Fregien, N.2    Bourguignon, L.Y.3
  • 27
    • 0027146485 scopus 로고
    • Hyaluronic acid-induced lymphocyte signal transduction and HA receptor (GP85/ CD44)-cytoskeleton interaction
    • Bourguignon, L. Y., V. B. Lokeshwar, X. Chen, and W. G. Kerrick. 1993. Hyaluronic acid-induced lymphocyte signal transduction and HA receptor (GP85/ CD44)-cytoskeleton interaction. J. Immunol. 151:6634.
    • (1993) J. Immunol. , vol.151 , pp. 6634
    • Bourguignon, L.Y.1    Lokeshwar, V.B.2    Chen, X.3    Kerrick, W.G.4
  • 28
    • 0026568543 scopus 로고
    • Antigen receptor complex stimulation triggers protein kinase C-dependent CD11a/CD18-cytoskeleton association in T lymphocytes
    • Pardi, R., L. Inverdi, C. Rugarli, and J. R. Bender. 1992. Antigen receptor complex stimulation triggers protein kinase C-dependent CD11a/CD18-cytoskeleton association in T lymphocytes. J. Cell Biol. 116:1211.
    • (1992) J. Cell Biol. , vol.116 , pp. 1211
    • Pardi, R.1    Inverdi, L.2    Rugarli, C.3    Bender, J.R.4
  • 29
    • 2342638940 scopus 로고
    • Association of E-selectin with components of the endothelial cytoskeleton during leukocyte adhesion
    • Yoshida, M., N. Resnick, A. Rosenzweig, and M. A. Gimbrone Jr. 1995. Association of E-selectin with components of the endothelial cytoskeleton during leukocyte adhesion. FASEB J. 9:A35.
    • (1995) FASEB J. , vol.9
    • Yoshida, M.1    Resnick, N.2    Rosenzweig, A.3    Gimbrone Jr., M.A.4
  • 31
    • 0022574146 scopus 로고
    • Induction by IL-1 and interferon-γ: Tissue distribution, biochemistry, and function of a natural adherence molecule (ICAM-1)
    • Dustin, M. L., R. Rothlein, A. K. Bhan, C A. Dinarello, and T. A. Springer. 1986. Induction by IL-1 and interferon-γ: tissue distribution, biochemistry, and function of a natural adherence molecule (ICAM-1). J. Immunol. 137:245.
    • (1986) J. Immunol. , vol.137 , pp. 245
    • Dustin, M.L.1    Rothlein, R.2    Bhan, A.K.3    Dinarello, C.A.4    Springer, T.A.5
  • 32
    • 0024436119 scopus 로고
    • Tumor necrosis factor and Interferon-γ induce distinct patterns of endothelial activation and associated leukocyte accumulation in skin of Papio anubis
    • Munro, J. M., J. S. Pober, and R. S. Cotran. 1989. Tumor necrosis factor and Interferon-γ induce distinct patterns of endothelial activation and associated leukocyte accumulation in skin of Papio anubis. Am. J. Pathol. 135:121.
    • (1989) Am. J. Pathol. , vol.135 , pp. 121
    • Munro, J.M.1    Pober, J.S.2    Cotran, R.S.3
  • 33
    • 0026672861 scopus 로고
    • Association of intercellular adhesion molecule-1 (ICAM-1) with actin-containing cytoskeleton and alpha-actinin
    • Carpen, O., P. Pallai, D. E. Staunton, and T. A. Springer. 1992. Association of intercellular adhesion molecule-1 (ICAM-1) with actin-containing cytoskeleton and alpha-actinin. J. Cell Biol. 118:1223.
    • (1992) J. Cell Biol. , vol.118 , pp. 1223
    • Carpen, O.1    Pallai, P.2    Staunton, D.E.3    Springer, T.A.4
  • 34
    • 0027067835 scopus 로고
    • Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway
    • Disdier, M., J. H. Morrissey, R. D. Fugate, D. F. Bainton, and R. P. McEver. 1992. Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway. Mol. Biol. Cell 3:309.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 309
    • Disdier, M.1    Morrissey, J.H.2    Fugate, R.D.3    Bainton, D.F.4    McEver, R.P.5
  • 35
    • 0028140035 scopus 로고
    • The cytoplasmic domain of P-selectin contains a sorting determinant that mediates rapid degradation in lysosomes
    • Green, S. A., H. Setiadi, R. P. McEver, and R. B. Kelly. 1994. The cytoplasmic domain of P-selectin contains a sorting determinant that mediates rapid degradation in lysosomes. J. Cell Biol. 124:435.
    • (1994) J. Cell Biol. , vol.124 , pp. 435
    • Green, S.A.1    Setiadi, H.2    McEver, R.P.3    Kelly, R.B.4
  • 36
    • 0027182466 scopus 로고
    • The cytoplasmic domain of P-selectin is phosphorylated on serine and threonine residues
    • Fujimoto, T., and R. P. McEver. 1993. The cytoplasmic domain of P-selectin is phosphorylated on serine and threonine residues. Blood 82:1758.
    • (1993) Blood , vol.82 , pp. 1758
    • Fujimoto, T.1    McEver, R.P.2
  • 37
    • 0029118628 scopus 로고
    • Histidine phosphorylation of P-selectin upon stimulation of human platelets: A novel pathway for activation-dependent signal transduction
    • Crovello, C. S., B. C. Furie, and B. Furie. 1995. Histidine phosphorylation of P-selectin upon stimulation of human platelets: a novel pathway for activation-dependent signal transduction. Cell 82:279.
    • (1995) Cell , vol.82 , pp. 279
    • Crovello, C.S.1    Furie, B.C.2    Furie, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.