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Volumn 92, Issue 6, 1998, Pages 809-818

Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN; L SELECTIN; PROTEINASE;

EID: 0032549712     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81408-7     Document Type: Article
Times cited : (178)

References (65)
  • 1
    • 0023644790 scopus 로고
    • Regulation of calmodulin binding to P-57. A neurospecific calmodulin binding protein
    • Alexander, K.A., Cimler, B.M., Meier, K.E., and Storm, D.R. (1987). Regulation of calmodulin binding to P-57. A neurospecific calmodulin binding protein. J. Biol. Chem. 262, 6108-6113.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6108-6113
    • Alexander, K.A.1    Cimler, B.M.2    Meier, K.E.3    Storm, D.R.4
  • 2
    • 0031134090 scopus 로고    scopus 로고
    • L-selectin shedding does not regulate human neutrophil attachment, rolling, or transmigration across human vascular endothelium in vitro
    • Allport, J.R., Ding, H.T., Ager, A., Steeber, D.A., Tedder, T.F., and Luscinskas, F.W. (1997). L-selectin shedding does not regulate human neutrophil attachment, rolling, or transmigration across human vascular endothelium in vitro. J. Immunol. 158, 4365-4372.
    • (1997) J. Immunol. , vol.158 , pp. 4365-4372
    • Allport, J.R.1    Ding, H.T.2    Ager, A.3    Steeber, D.A.4    Tedder, T.F.5    Luscinskas, F.W.6
  • 3
    • 0019503687 scopus 로고
    • Calmodulin antagonists modulate rabbit neutrophil degranulation, aggregation and stimulated oxygen consumption
    • Alobaidi, T., Naccache, P.H., and Sha'afi, R.I. (1981). Calmodulin antagonists modulate rabbit neutrophil degranulation, aggregation and stimulated oxygen consumption. Biochim. Biophys. Acta 675, 316-321.
    • (1981) Biochim. Biophys. Acta , vol.675 , pp. 316-321
    • Alobaidi, T.1    Naccache, P.H.2    Sha'afi, R.I.3
  • 4
    • 0029826160 scopus 로고    scopus 로고
    • Interactions through L-selectin between leukocytes and adherent leukocytes nucleate rolling adhesions on selectins and VCAM-1 in shear flow
    • Alon, R., Fuhlbrigge, R.C., Finger, E.B., and Springer, T.A. (1996). Interactions through L-selectin between leukocytes and adherent leukocytes nucleate rolling adhesions on selectins and VCAM-1 in shear flow. J. Cell Biol. 135, 849-865.
    • (1996) J. Cell Biol. , vol.135 , pp. 849-865
    • Alon, R.1    Fuhlbrigge, R.C.2    Finger, E.B.3    Springer, T.A.4
  • 5
    • 15844406752 scopus 로고    scopus 로고
    • Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors
    • Arribas, J., Coodly, L., Vollmer, P., Kishimoto, T.K., Rose-John, S., and Massague, J. (1996). Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors. J. Biol. Chem. 271, 11376-11382.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11376-11382
    • Arribas, J.1    Coodly, L.2    Vollmer, P.3    Kishimoto, T.K.4    Rose-John, S.5    Massague, J.6
  • 6
    • 0028143514 scopus 로고
    • Neutrophils roll on adherent neutrophils bound to cytokine-induced endothelial cells via L-selectin on the rolling cells
    • Bargatze, R.F., Kurk, S., Butcher, E.C., and Jutila, M.A. (1994). Neutrophils roll on adherent neutrophils bound to cytokine-induced endothelial cells via L-selectin on the rolling cells. J. Exp. Med. 180, 1785-1792.
    • (1994) J. Exp. Med. , vol.180 , pp. 1785-1792
    • Bargatze, R.F.1    Kurk, S.2    Butcher, E.C.3    Jutila, M.A.4
  • 8
    • 0029975125 scopus 로고    scopus 로고
    • Hydroxamate-based metalloprotease inhibitor blocks shedding of L-selectin adhesion molecule from leukocytes
    • Bennett, T.A., Lynam, E.B., Sklar, L.A., and Rogelj, S. (1996). Hydroxamate-based metalloprotease inhibitor blocks shedding of L-selectin adhesion molecule from leukocytes. J. Immunol. 156, 3093-3097.
    • (1996) J. Immunol. , vol.156 , pp. 3093-3097
    • Bennett, T.A.1    Lynam, E.B.2    Sklar, L.A.3    Rogelj, S.4
  • 9
    • 0022405825 scopus 로고
    • Calcium requirements for increased complement receptor expression during neutrophil activation
    • Berger, M., Birx, D.L., Wetzler, E.M., O'Shea, J.J., Brown, E.J., and Cross, A.S. (1985). Calcium requirements for increased complement receptor expression during neutrophil activation. J. Immunol. 135, 1342-1348.
    • (1985) J. Immunol. , vol.135 , pp. 1342-1348
    • Berger, M.1    Birx, D.L.2    Wetzler, E.M.3    O'Shea, J.J.4    Brown, E.J.5    Cross, A.S.6
  • 11
    • 0030834283 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNFα and Notch
    • Blobel, C.P. (1997). Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNFα and Notch. Cell 90, 589-592.
    • (1997) Cell , vol.90 , pp. 589-592
    • Blobel, C.P.1
  • 13
    • 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, 1033-1036.
    • (1991) Cell , vol.67 , pp. 1033-1036
    • Butcher, E.C.1
  • 14
    • 0029102738 scopus 로고
    • Structural requirements regulate endoproteolytic release of the L-selectin (CD62L) adhesion receptor from the cell surface of leukocytes
    • Chen, A., Engel, P., and Tedder, T.F. (1995). Structural requirements regulate endoproteolytic release of the L-selectin (CD62L) adhesion receptor from the cell surface of leukocytes. J. Exp. Med. 182, 519-530.
    • (1995) J. Exp. Med. , vol.182 , pp. 519-530
    • Chen, A.1    Engel, P.2    Tedder, T.F.3
  • 15
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici, A., and Ikura, M. (1995). Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24, 85-116.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 16
    • 0028926451 scopus 로고
    • Activation of human neutrophils through L-selectin and Mac-1 molecules
    • Crockett-Torabi, E., Sulenbarger, B., Smith, C.W., and Fantone, J.C. (1995). Activation of human neutrophils through L-selectin and Mac-1 molecules. J. Immunol. 154, 2291-2302.
    • (1995) J. Immunol. , vol.154 , pp. 2291-2302
    • Crockett-Torabi, E.1    Sulenbarger, B.2    Smith, C.W.3    Fantone, J.C.4
  • 17
    • 0024443411 scopus 로고
    • T cell receptor cross-linking transiently stimulates adhesiveness through LFA-1
    • Dustin, M.L., and Springer, T.A. (1989). T cell receptor cross-linking transiently stimulates adhesiveness through LFA-1. Nature 341, 619-624.
    • (1989) Nature , vol.341 , pp. 619-624
    • Dustin, M.L.1    Springer, T.A.2
  • 18
    • 0025721095 scopus 로고
    • Membrane proteins with soluble counterparts: Role of proteolysis in the release of transmembrane proteins
    • Ehlers, M.R.W., and Riordan, J.F. (1991). Membrane proteins with soluble counterparts: role of proteolysis in the release of transmembrane proteins. Biochem. 30, 10065-10074.
    • (1991) Biochem. , vol.30 , pp. 10065-10074
    • Ehlers, M.R.W.1    Riordan, J.F.2
  • 19
    • 0019932262 scopus 로고
    • Involvement of calmodulin in granulocyte chemotaxis: The effect of calmodulin inhibitors
    • Elferink, J.G., Deierkauf, M., and Riemersma, J.C. (1982). Involvement of calmodulin in granulocyte chemotaxis: the effect of calmodulin inhibitors. Res. Commun. Chem. Pathol. Pharmacol. 38, 77-84.
    • (1982) Res. Commun. Chem. Pathol. Pharmacol. , vol.38 , pp. 77-84
    • Elferink, J.G.1    Deierkauf, M.2    Riemersma, J.C.3
  • 20
    • 0029924173 scopus 로고    scopus 로고
    • Shedding of the lymphocyte L-selectin adhesion molecule is inhibited by a hydroxamic acid-based protease inhibitor
    • Feehan, C., Darlak, K., Kahn, J., Walcheck, B., Spatola, A.F., and Kishimoto, T.K. (1996). Shedding of the lymphocyte L-selectin adhesion molecule is inhibited by a hydroxamic acid-based protease inhibitor. J. Biol. Chem. 271, 7019-7024.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7019-7024
    • Feehan, C.1    Darlak, K.2    Kahn, J.3    Walcheck, B.4    Spatola, A.F.5    Kishimoto, T.K.6
  • 22
    • 0028791040 scopus 로고
    • Calmodulin: Effects of cell stimuli and drugs on cellular activation
    • Gnegy, M.E. (1995). Calmodulin: effects of cell stimuli and drugs on cellular activation. Prog. Drug Res. 45, 33-65.
    • (1995) Prog. Drug Res. , vol.45 , pp. 33-65
    • Gnegy, M.E.1
  • 23
    • 33749180170 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand (PSGL-1) is a ligand for L-selectin in neutrophil aggregation
    • Guyer, D.A., Moore, K.L., Lynam, E., McEver, R.P., and Sklar, L.A. (1996). P-selectin glycoprotein ligand (PSGL-1) is a ligand for L-selectin in neutrophil aggregation. Fed. Am. Soc. Exp. Biol. J. 10, A3536.
    • (1996) Fed. Am. Soc. Exp. Biol. J. , vol.10
    • Guyer, D.A.1    Moore, K.L.2    Lynam, E.3    McEver, R.P.4    Sklar, L.A.5
  • 25
    • 0026513601 scopus 로고
    • MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin
    • Hartwig, J.H., Thelen, M., Rosen, A., Janmey, P.A., Nairn, A.C., and Aderem, A. (1992). MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. Nature 356, 618-622.
    • (1992) Nature , vol.356 , pp. 618-622
    • Hartwig, J.H.1    Thelen, M.2    Rosen, A.3    Janmey, P.A.4    Nairn, A.C.5    Aderem, A.6
  • 26
    • 0028292223 scopus 로고
    • Identification of the sulfated monosaccharides of GlyCAM-1, an endothelial-derived ligand for L-selectin
    • Hemmerich, S., Bertozzi, C.R., Leffler, H., and Rosen, S.D. (1994). Identification of the sulfated monosaccharides of GlyCAM-1, an endothelial-derived ligand for L-selectin. Biochem. 33, 4820-4829.
    • (1994) Biochem. , vol.33 , pp. 4820-4829
    • Hemmerich, S.1    Bertozzi, C.R.2    Leffler, H.3    Rosen, S.D.4
  • 27
    • 0027180072 scopus 로고
    • Characterization of a 7.5-kDa protein kinase C substrate (RC3 protein, neurogranin) from rat brain
    • Huang, K.P., Huang, F.L., and Chen, H.C. (1993). Characterization of a 7.5-kDa protein kinase C substrate (RC3 protein, neurogranin) from rat brain. Arch. Biochem. Biophys. 305, 570-580.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 570-580
    • Huang, K.P.1    Huang, F.L.2    Chen, H.C.3
  • 28
    • 0029904693 scopus 로고    scopus 로고
    • Glycam-1, a physiologic ligand for L-selectin, activates β-2 integrins on naive peripheral lymphocytes
    • Hwang, S.T., Singer, M.S., Giblin, P.A., Yednock, T.A., Bacon, K.B., Simon, S.I., and Rosen, S.D. (1996). Glycam-1, a physiologic ligand for L-selectin, activates β-2 integrins on naive peripheral lymphocytes. J. Exp. Med. 184, 1343-1348.
    • (1996) J. Exp. Med. , vol.184 , pp. 1343-1348
    • Hwang, S.T.1    Singer, M.S.2    Giblin, P.A.3    Yednock, T.A.4    Bacon, K.B.5    Simon, S.I.6    Rosen, S.D.7
  • 29
    • 0021288852 scopus 로고
    • Calcium and calmodulin in neutrophil activation
    • Jones, H.P., and McCord, J.M. (1984). Calcium and calmodulin in neutrophil activation. Methods Enzymol. 105, 389-392.
    • (1984) Methods Enzymol. , vol.105 , pp. 389-392
    • Jones, H.P.1    McCord, J.M.2
  • 30
    • 0028269635 scopus 로고
    • Membrane proximal cleavage of L-selectin: Identification of the cleavage site and a 6-kDa transmembrane peptide fragment of L-selectin
    • Kahn, J., Ingraham, R.H., Shirley, F., Migaki, G.I., and Kishimoto, T.K. (1994). Membrane proximal cleavage of L-selectin: identification of the cleavage site and a 6-kDa transmembrane peptide fragment of L-selectin. J. Cell Biol. 125, 461-470.
    • (1994) J. Cell Biol. , vol.125 , pp. 461-470
    • Kahn, J.1    Ingraham, R.H.2    Shirley, F.3    Migaki, G.I.4    Kishimoto, T.K.5
  • 31
    • 0027509819 scopus 로고
    • Regulation of leukocyte rolling and adhesion to high endothelial venules through the cytoplasmic domain of L-selectin
    • Kansas, G.S., Ley, K., Munro, J.M., and Tedder, T.F. (1993). Regulation of leukocyte rolling and adhesion to high endothelial venules through the cytoplasmic domain of L-selectin. J. Exp. Med. 177, 833-838.
    • (1993) J. Exp. Med. , vol.177 , pp. 833-838
    • Kansas, G.S.1    Ley, K.2    Munro, J.M.3    Tedder, T.F.4
  • 32
    • 0024420563 scopus 로고
    • Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors
    • Kishimoto, T.K., Jutila, M.A., Berg, E.L., and Butcher, E.C. (1989). Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors. Science 245, 1238-1241.
    • (1989) Science , vol.245 , pp. 1238-1241
    • Kishimoto, T.K.1    Jutila, M.A.2    Berg, E.L.3    Butcher, E.C.4
  • 33
    • 0025210021 scopus 로고
    • Identification of a human peripheral lymph node homing receptor: A rapidly down-regulated adhesion molecule
    • Kishimoto, T.K., Jutila, M.A., and Butcher, E.C. (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
  • 36
    • 0027933127 scopus 로고
    • Sulfatides trigger increase of cytosolic free calcium and enhanced expression of tumor necrosis factor-α and interleukin-8 mRNA in human neutrophils. Evidence for a role of L-selectin as a signaling molecule
    • Laudanna, C., Constantin, G., Baron, P., Scarpini, E., Scarlato, G., Cabrini, G., Dechecchi, C., Rossi, F., Cassatella, M.A., and Berton, G. (1994). Sulfatides trigger increase of cytosolic free calcium and enhanced expression of tumor necrosis factor-α and interleukin-8 mRNA in human neutrophils. Evidence for a role of L-selectin as a signaling molecule. J. Biol. Chem. 269, 4021-4026.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4021-4026
    • Laudanna, C.1    Constantin, G.2    Baron, P.3    Scarpini, E.4    Scarlato, G.5    Cabrini, G.6    Dechecchi, C.7    Rossi, F.8    Cassatella, M.A.9    Berton, G.10
  • 37
    • 0028920951 scopus 로고
    • Rolling of lymphocytes and neutrophils on peripheral node addressin and subsequent arrest on ICAM-1 in shear flow
    • Lawrence, M.B., Berg, E.L., Butcher, E.G., and Springer, T.A. (1995). Rolling of lymphocytes and neutrophils on peripheral node addressin and subsequent arrest on ICAM-1 in shear flow. Eur. J. Immunol. 25, 1025-1031.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1025-1031
    • Lawrence, M.B.1    Berg, E.L.2    Butcher, E.G.3    Springer, T.A.4
  • 38
    • 0024337069 scopus 로고
    • 2+ and is phosphorylated in response to insulin and tumor-promoting phorbol esters
    • 2+ and is phosphorylated in response to insulin and tumor-promoting phorbol esters. J. Biol. Chem. 264, 9611-9618.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9611-9618
    • McDonald, J.R.1    Lawrence J.C., Jr.2
  • 39
    • 0029097546 scopus 로고
    • Mutational analysis of the membrane-proximal cleavage site of L-selectin: Relaxed sequence specifity surrounding the cleavage site
    • Migaki, G.I., Kahn, J., and Kishimoto, T.K. (1995). Mutational analysis of the membrane-proximal cleavage site of L-selectin: relaxed sequence specifity surrounding the cleavage site. J. Exp. Med. 182, 549-557.
    • (1995) J. Exp. Med. , vol.182 , pp. 549-557
    • Migaki, G.I.1    Kahn, J.2    Kishimoto, T.K.3
  • 42
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic α-helices
    • O'Neil, K.T., and DeGrado, W.F. (1990). How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices. Trends Biochem. Sci. 15, 59-64.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 59-64
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 43
    • 0026522926 scopus 로고
    • Rapid activation-independent shedding of leukocyte L-selectin induced by cross-linking of the surface antigen
    • Palecanda, A., Walcheck, B., Bishop, D.K., and Jutila, M.A. (1992). Rapid activation-independent shedding of leukocyte L-selectin induced by cross-linking of the surface antigen. Eur. J. Immunol. 22, 1279-1286.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1279-1286
    • Palecanda, A.1    Walcheck, B.2    Bishop, D.K.3    Jutila, M.A.4
  • 44
    • 0029074732 scopus 로고
    • Thecytoplasmic 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., Walker, D.M., Graham, L., Goheen, M., Doerschuk, C.M., and Kansas, G.S. (1995). Thecytoplasmic 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, 1155-1164.
    • (1995) J. Cell Biol. , vol.129 , pp. 1155-1164
    • Pavalko, F.M.1    Walker, D.M.2    Graham, L.3    Goheen, M.4    Doerschuk, C.M.5    Kansas, G.S.6
  • 45
    • 0025939215 scopus 로고
    • The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140
    • Picker, L.J., Warnock, R.A., Burns, A.R., Doerschuk, C.M., Berg, E.L., and Butcher, E.C. (1991). The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140. Cell 66, 921-933.
    • (1991) Cell , vol.66 , pp. 921-933
    • Picker, L.J.1    Warnock, R.A.2    Burns, A.R.3    Doerschuk, C.M.4    Berg, E.L.5    Butcher, E.C.6
  • 46
    • 17544382630 scopus 로고    scopus 로고
    • Metalloproteinase-mediated regulation of L-selectin levels on leukocytes
    • Preece, G., Murphy, G., and Ager, A. (1996). Metalloproteinase-mediated regulation of L-selectin levels on leukocytes. J. Biol. Chem. 271, 11634-11640.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11634-11640
    • Preece, G.1    Murphy, G.2    Ager, A.3
  • 47
    • 0029098409 scopus 로고
    • L-selectin (CD62L) cross-linking signals neutrophil adhesive functions via the Mac-1 (CD11b/CD18) β2-integrin
    • Simon, S.I., Burns, A.R., Taylor, A.D., Gopalan, P.K., Lynam, E.B., Sklar, L.A., and Smith, C.W. (1995). L-selectin (CD62L) cross-linking signals neutrophil adhesive functions via the Mac-1 (CD11b/CD18) β2-integrin. J. Immunol. 155, 1502-1514.
    • (1995) J. Immunol. , vol.155 , pp. 1502-1514
    • Simon, S.I.1    Burns, A.R.2    Taylor, A.D.3    Gopalan, P.K.4    Lynam, E.B.5    Sklar, L.A.6    Smith, C.W.7
  • 48
    • 0019417344 scopus 로고
    • Effects of trifluoperazine on human neutrophil function
    • Smith, R.J., Bowman, B.J., and Iden, S.S. (1981). Effects of trifluoperazine on human neutrophil function. Immunol. 44, 677-684.
    • (1981) Immunol. , vol.44 , pp. 677-684
    • Smith, R.J.1    Bowman, B.J.2    Iden, S.S.3
  • 50
    • 0026429124 scopus 로고
    • Regulation of leukocyte migration by activation of the leukocyte adhesion molecule-1 (LAM-1) selectin
    • Spertini, O., Kansas, G.S., Munro, J.M., Griffin, J.D., and Tedder, T.F. (1991). Regulation of leukocyte migration by activation of the leukocyte adhesion molecule-1 (LAM-1) selectin. Nature 349, 691-694.
    • (1991) Nature , vol.349 , pp. 691-694
    • Spertini, O.1    Kansas, G.S.2    Munro, J.M.3    Griffin, J.D.4    Tedder, T.F.5
  • 51
    • 0029987391 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand 1 is a ligand for L-selectin on neutrophils, monocytes, and CD34(+) hematopoietic progenitor cells
    • Spertini, O., Cordey, A.S., Monai, N., Giuffre, L., and Schapira, M. (1996). P-selectin glycoprotein ligand 1 is a ligand for L-selectin on neutrophils, monocytes, and CD34(+) hematopoietic progenitor cells. J. Cell Biol. 135, 523-531.
    • (1996) J. Cell Biol. , vol.135 , pp. 523-531
    • Spertini, O.1    Cordey, A.S.2    Monai, N.3    Giuffre, L.4    Schapira, M.5
  • 52
    • 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, 301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 53
    • 0031570940 scopus 로고    scopus 로고
    • Ligation of L-selectin through conserved regions within the lectin domain activates signal transduction pathways and integrin function in human, mouse, and rat leukocytes
    • Steeber, D.A., Engel, P., Miller, A.S., Sheetz, M.P., and Tedder, T.F. (1997). Ligation of L-selectin through conserved regions within the lectin domain activates signal transduction pathways and integrin function in human, mouse, and rat leukocytes. J. Immunol. 159, 952-963.
    • (1997) J. Immunol. , vol.159 , pp. 952-963
    • Steeber, D.A.1    Engel, P.2    Miller, A.S.3    Sheetz, M.P.4    Tedder, T.F.5
  • 54
    • 0024109988 scopus 로고
    • Immunohistologic and functional characterization of a vascular addressin involved in lymphocyte homing into peripheral lymph nodes
    • Streeter, P.R., Rouse, B.T., and Butcher, E.C. (1988). Immunohistologic and functional characterization of a vascular addressin involved in lymphocyte homing into peripheral lymph nodes. J. Cell Biol. 107, 1853-1862.
    • (1988) J. Cell Biol. , vol.107 , pp. 1853-1862
    • Streeter, P.R.1    Rouse, B.T.2    Butcher, E.C.3
  • 55
    • 0025924752 scopus 로고
    • 2+stimulates the Mg2(+)-ATPase activity of brush border myosin I with three or four calmodulin light chains but inhibits with less than two bound
    • 2+stimulates the Mg2(+)-ATPase activity of brush border myosin I with three or four calmodulin light chains but inhibits with less than two bound. J. Biol. Chem. 266, 1312-1319.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1312-1319
    • Swanljung-Collins, H.1    Collins, J.H.2
  • 56
    • 0030294239 scopus 로고    scopus 로고
    • L-selectin binds to P-selectin glycoprotein-1 on leukocyes - Interactions between the lectin, epidermal growth factor, and consensus repeat domains of the selectins determine ligand binding specificity
    • Tu, L.L., Chen, A.J., Delahunty, M.D., Moore, K.L., Watson, S.R., McEver, R.P., and Tedder, T.F. (1996). L-selectin binds to P-selectin glycoprotein-1 on leukocyes - interactions between the lectin, epidermal growth factor, and consensus repeat domains of the selectins determine ligand binding specificity. J. Immunol. 157, 3995-4004.
    • (1996) J. Immunol. , vol.157 , pp. 3995-4004
    • Tu, L.L.1    Chen, A.J.2    Delahunty, M.D.3    Moore, K.L.4    Watson, S.R.5    McEver, R.P.6    Tedder, T.F.7
  • 57
    • 0021739452 scopus 로고
    • Conditions for reproducible detection of calmodulin and S100 β in immunoblots
    • van Eldik, L.J., and Wolchok, S.R. (1984). Conditions for reproducible detection of calmodulin and S100 β in immunoblots. Biochem. Biophys. Res. Commun. 124, 752-759.
    • (1984) Biochem. Biophys. Res. Commun. , vol.124 , pp. 752-759
    • Van Eldik, L.J.1    Wolchok, S.R.2
  • 58
    • 0029086105 scopus 로고
    • A central role for microvillous receptor presentation in leukocyte adhesion under flow
    • von Andrian, D.H., Hasslen, S.R., Nelson, R.D., Erlandsen, S.L., and Butcher, E.C. (1995). A central role for microvillous receptor presentation in leukocyte adhesion under flow. Cell 82, 989-999.
    • (1995) Cell , vol.82 , pp. 989-999
    • Von Andrian, D.H.1    Hasslen, S.R.2    Nelson, R.D.3    Erlandsen, S.L.4    Butcher, E.C.5
  • 59
    • 0028065619 scopus 로고
    • Potentiation of the oxidative burst of human neutrophils. A signaling role for L-selectin
    • Waddell, T.K., Fialkow, L., Chan, C.K., Kishimoto, T.K., and Downey, G.P. (1994). Potentiation of the oxidative burst of human neutrophils. A signaling role for L-selectin. J. Biol. Chem. 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
  • 60
    • 0029075155 scopus 로고
    • Signaling functions of L-selectin - Enhancement of tyrosine phosphorylation and activation of MAP kinase
    • Waddell, T.K., Fialkow, L., Chan, C.K., Kishimoto, T.K., and Downey, G.P. (1995). Signaling functions of L-selectin - enhancement of tyrosine phosphorylation and activation of MAP kinase. J. Biol. Chem. 270, 15403-15411.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15403-15411
    • Waddell, T.K.1    Fialkow, L.2    Chan, C.K.3    Kishimoto, T.K.4    Downey, G.P.5
  • 62
    • 0029758146 scopus 로고    scopus 로고
    • Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1. A mechanism that amplifies initial leukocyte accumulation on P-selectin in vitro
    • Walcheck, B., Moore, K.L., McEver, R.P., and Kishimoto, T.K. (1996b). Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1. A mechanism that amplifies initial leukocyte accumulation on P-selectin in vitro. J. Clin. Invest. 98, 1081-1087.
    • (1996) J. Clin. Invest. , vol.98 , pp. 1081-1087
    • Walcheck, B.1    Moore, K.L.2    McEver, R.P.3    Kishimoto, T.K.4
  • 63
    • 0020471437 scopus 로고
    • Calmodulin binds to chick lens gap junction protein in a calcium-independent manner
    • Welsh, M.J., Aster, J.C., Ireland, M., Alcala, J., and Maisel, H. (1982). Calmodulin binds to chick lens gap junction protein in a calcium-independent manner. Science 216, 642-644.
    • (1982) Science , vol.216 , pp. 642-644
    • Welsh, M.J.1    Aster, J.C.2    Ireland, M.3    Alcala, J.4    Maisel, H.5
  • 64
    • 0023109832 scopus 로고
    • Comparison of the roles of calmodulin and protein kinase C in activation of the human neutrophil respiratory burst
    • Wright, C.D., and Hoffman, M.D. (1987). Comparison of the roles of calmodulin and protein kinase C in activation of the human neutrophil respiratory burst. Biochem. Biophys. Res. Commun. 142, 53-62.
    • (1987) Biochem. Biophys. Res. Commun. , vol.142 , pp. 53-62
    • Wright, C.D.1    Hoffman, M.D.2
  • 65
    • 0030818834 scopus 로고    scopus 로고
    • Prevention of in vitro neutrophil adhesion to endothelial cells through shedding of L-selectin by C-reactive protein and peptides derived from C-reactive protein
    • Zouki, C., Beauchamp, M., Baron, C., and Filep, J.G. (1997). Prevention of in vitro neutrophil adhesion to endothelial cells through shedding of L-selectin by C-reactive protein and peptides derived from C-reactive protein. J. Clin. Invest. 100, 522-529.
    • (1997) J. Clin. Invest. , vol.100 , pp. 522-529
    • Zouki, C.1    Beauchamp, M.2    Baron, C.3    Filep, J.G.4


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