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Volumn 68, Issue 4, 2004, Pages 894-902

Characterization of murine grancalcin specifically expressed in leukocytes and its possible role in host defense against bacterial infection

Author keywords

Cytoskeleton; Grancalcin; Macrophage; p65 L plastin; Penta EF hand

Indexed keywords

ANTIBODY; CALCIUM; CALCIUM BINDING PROTEIN; CD11B ANTIGEN; COMPLEMENTARY DNA; GCA PROTEIN, HUMAN; GCA PROTEIN, MOUSE; HYDROGEN PEROXIDE; LIPOPOLYSACCHARIDE; RECOMBINANT PROTEIN;

EID: 4544277841     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.68.894     Document Type: Article
Times cited : (20)

References (35)
  • 1
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov, R., and Janeway Jr., C. A., Innate immunity: the virtues of a nonclonal system of recognition. Cell, 91, 295-298 (1997).
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway Jr., C.A.2
  • 2
    • 0034680145 scopus 로고    scopus 로고
    • Toll-like receptors in the induction of the innate immune response
    • Aderem, A., and Ulevitch, R. J., Toll-like receptors in the induction of the innate immune response. Nature, 406, 782-787 (2000).
    • (2000) Nature , vol.406 , pp. 782-787
    • Aderem, A.1    Ulevitch, R.J.2
  • 3
  • 4
    • 0025909326 scopus 로고
    • Purification and characterization of the 65-kDa protein phosphorylated in murine macrophages by stimulation with bacterial lipopolysaccharide
    • Shinomiya, H., Hirata, H., and Nakano, M., Purification and characterization of the 65-kDa protein phosphorylated in murine macrophages by stimulation with bacterial lipopolysaccharide. J. Immunol., 146, 3617-3625 (1991).
    • (1991) J. Immunol. , vol.146 , pp. 3617-3625
    • Shinomiya, H.1    Hirata, H.2    Nakano, M.3
  • 5
    • 0028030747 scopus 로고
    • Identification of the 65-kDa phosphoprotein in murine macrophages as a novel protein: Homology with human L-plastin
    • Shinomiya, H., Hirata, H., Saito, S., Yagisawa, H., and Nakano, M., Identification of the 65-kDa phosphoprotein in murine macrophages as a novel protein: homology with human L-plastin. Biochem. Biophys. Res. Commun., 202, 1631-1638 (1994).
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 1631-1638
    • Shinomiya, H.1    Hirata, H.2    Saito, S.3    Yagisawa, H.4    Nakano, M.5
  • 6
    • 0028933571 scopus 로고
    • Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide
    • Shinomiya, H., Hagi, A., Fukuzumi, M., Mizobuchi, M., Hirata, H., and Utsumi, S., Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide. J. Immunol., 154, 3471-3478 (1995).
    • (1995) J. Immunol. , vol.154 , pp. 3471-3478
    • Shinomiya, H.1    Hagi, A.2    Fukuzumi, M.3    Mizobuchi, M.4    Hirata, H.5    Utsumi, S.6
  • 7
    • 2142857233 scopus 로고    scopus 로고
    • Preparation and characterization of recombinant murine p65/L-plastin expressed in Escherichia coli and high-liter antibodies against the protein
    • Shinomiya, H., Nagai, K., Hirata, H., Kobayashi, N., Hasegawa, H., Liu, F., Sumita, K., and Asano, Y., Preparation and characterization of recombinant murine p65/L-plastin expressed in Escherichia coli and high-liter antibodies against the protein. Biosci. Biotechnol. Biochem., 67, 1368-1375 (2003).
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 1368-1375
    • Shinomiya, H.1    Nagai, K.2    Hirata, H.3    Kobayashi, N.4    Hasegawa, H.5    Liu, F.6    Sumita, K.7    Asano, Y.8
  • 8
    • 0032483008 scopus 로고    scopus 로고
    • A role for the actin-bundling protein L-plastin in the regulation of leukocyte integrin function
    • Jones, S. L., Wang, J., Turck, C. W., and Brown, E. J., A role for the actin-bundling protein L-plastin in the regulation of leukocyte integrin function. Proc. Natl. Acad. Sci. U.S.A., 95, 9331-9336 (1998).
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 9331-9336
    • Jones, S.L.1    Wang, J.2    Turck, C.W.3    Brown, E.J.4
  • 9
    • 0035947576 scopus 로고    scopus 로고
    • Biochemical characterization of the penta-EF-hand protein grancalcin and identification of L-plastin as a binding partner
    • Lollike, K., Johnsen, A. H., Durussel, I., Borregaard, N., and Cox, J. A., Biochemical characterization of the penta-EF-hand protein grancalcin and identification of L-plastin as a binding partner. J. Biol. Chem., 276, 17762-17769 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 17762-17769
    • Lollike, K.1    Johnsen, A.H.2    Durussel, I.3    Borregaard, N.4    Cox, J.A.5
  • 11
    • 0029671219 scopus 로고    scopus 로고
    • 2+-binding protein ALG-2 and Alzheimer's disease gene ALG-3
    • 2+-binding protein ALG-2 and Alzheimer's disease gene ALG-3. Science, 271, 521-525 (1996).
    • (1996) Science , vol.271 , pp. 521-525
    • Vito, P.1    Lacana, E.2    D'Adamio, L.3
  • 12
    • 0022990809 scopus 로고
    • A 22-kD protein (sorcin/V19) encoded by an amplified gene in multidrug-resistant cells is homologous to the calcium-binding light chain of calpain
    • Van der Bliek, A. M., Meyers, M. B., Biedler, J. L., Mes, E., and Borst, P., A 22-kD protein (sorcin/V19) encoded by an amplified gene in multidrug-resistant cells is homologous to the calcium-binding light chain of calpain. EMBO J., 5, 3201-3208 (1986).
    • (1986) EMBO J. , vol.5 , pp. 3201-3208
    • Van Der Bliek, A.M.1    Meyers, M.B.2    Biedler, J.L.3    Mes, E.4    Borst, P.5
  • 13
    • 0001920056 scopus 로고
    • Screening recombinant DNA libraries
    • eds. Ausubel, F. M., et al., John Wiley & Sons, New York
    • Strauss, W. M., Screening recombinant DNA libraries. In "Current Protocols in Molecular Biology", eds. Ausubel, F. M., et al., John Wiley & Sons, New York, pp. 6.0.1-6.6.1 (1987).
    • (1987) Current Protocols in Molecular Biology
    • Strauss, W.M.1
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0023151099 scopus 로고
    • Preparation and characterization of polyclonal and monoclonal antibodies against human interleukin 1 α (IL 1 α)
    • Kasahara, T., Mukaida, N., Shinomiya, H., Imai, M., Matsushima, K., Wakasugi, H., and Nakano, K., Preparation and characterization of polyclonal and monoclonal antibodies against human interleukin 1 α (IL 1 α). J. Immunol., 138, 1804-1812 (1987).
    • (1987) J. Immunol. , vol.138 , pp. 1804-1812
    • Kasahara, T.1    Mukaida, N.2    Shinomiya, H.3    Imai, M.4    Matsushima, K.5    Wakasugi, H.6    Nakano, K.7
  • 16
    • 0025924279 scopus 로고
    • Assessment of cytokines by immunofluorescence and the paraformaldehyde-saponin procedure
    • Sander, B., Andersson, J., and Andersson, U., Assessment of cytokines by immunofluorescence and the paraformaldehyde-saponin procedure. Immunol. Rev., 119, 65-93 (1991).
    • (1991) Immunol. Rev. , vol.119 , pp. 65-93
    • Sander, B.1    Andersson, J.2    Andersson, U.3
  • 17
    • 0035083218 scopus 로고    scopus 로고
    • Process formation of podocytes: Morphogenetic activity of microtubules and regulation by protein serine/threonine phosphatase PP2A
    • Kobayashi, N., Reiser, J., Schwarz, K., Sakai, T., Kriz, W., and Mundel, P., Process formation of podocytes: morphogenetic activity of microtubules and regulation by protein serine/threonine phosphatase PP2A. Histochem. Cell. Biol., 115, 255-266 (2001).
    • (2001) Histochem. Cell. Biol. , vol.115 , pp. 255-266
    • Kobayashi, N.1    Reiser, J.2    Schwarz, K.3    Sakai, T.4    Kriz, W.5    Mundel, P.6
  • 22
    • 0030069967 scopus 로고    scopus 로고
    • Characterization of the M(r) 65,000 lymphokine-activated killer proteins phosphorylated after tumor target binding: Evidence that pp65a and pp65b are phosphorylated forms of L-plastin
    • Frederick, M. J., Rodriguez, L. V., Johnston, D. A., Darnay, B. G., and Grimm, E. A., Characterization of the M(r) 65,000 lymphokine-activated killer proteins phosphorylated after tumor target binding: evidence that pp65a and pp65b are phosphorylated forms of L-plastin. Cancer Res., 56, 138-144 (1996).
    • (1996) Cancer Res. , vol.56 , pp. 138-144
    • Frederick, M.J.1    Rodriguez, L.V.2    Johnston, D.A.3    Darnay, B.G.4    Grimm, E.A.5
  • 23
    • 0028351807 scopus 로고
    • Serine phosphorylation of a 67-kDa protein in human T lymphocytes represents an accessory receptor-mediated signaling event
    • Henning, S. W., Meuer, S. C., and Samstag, Y., Serine phosphorylation of a 67-kDa protein in human T lymphocytes represents an accessory receptor-mediated signaling event. J. Immunol., 152, 4808-4815 (1994).
    • (1994) J. Immunol. , vol.152 , pp. 4808-4815
    • Henning, S.W.1    Meuer, S.C.2    Samstag, Y.3
  • 24
    • 0027216620 scopus 로고
    • Characterization of a 64-kD protein phosphorylated during chemotactic activation with IL-8 and fMLP of human polymorphonuclear leukocytes. I. Phosphorylation of a 64-kD protein and other proteins
    • Shibata, M., Ohoka, T., Mizuno, S., and Suzuki, K., Characterization of a 64-kD protein phosphorylated during chemotactic activation with IL-8 and fMLP of human polymorphonuclear leukocytes. I. Phosphorylation of a 64-kD protein and other proteins. J. Leukoc. Biol., 54, 1-9 (1993).
    • (1993) J. Leukoc. Biol. , vol.54 , pp. 1-9
    • Shibata, M.1    Ohoka, T.2    Mizuno, S.3    Suzuki, K.4
  • 25
    • 0027511422 scopus 로고
    • Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells
    • Lin, C. S., Park, T., Chen, Z. P., and Leavitt, J., Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells. J. Biol. Chem., 268, 2781-2792 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 2781-2792
    • Lin, C.S.1    Park, T.2    Chen, Z.P.3    Leavitt, J.4
  • 27
    • 0024616167 scopus 로고
    • Molecular interactions in macrophage activation
    • Adams, D. O., Molecular interactions in macrophage activation. Immunol. Today, 10, 33-35 (1989).
    • (1989) Immunol. Today , vol.10 , pp. 33-35
    • Adams, D.O.1
  • 28
    • 0037304551 scopus 로고    scopus 로고
    • Granulocyte function in grancalcin-deficient mice
    • Roes, J., Choi, B. K., Power, D., Xu, P., and Segal, A. W., Granulocyte function in grancalcin-deficient mice. Mol. Cell. Biol., 23, 826-830 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 826-830
    • Roes, J.1    Choi, B.K.2    Power, D.3    Xu, P.4    Segal, A.W.5
  • 30
    • 0036230129 scopus 로고    scopus 로고
    • Microbial killing: Hold the bleach and pass the salt!
    • Bokoch, G. M., Microbial killing: hold the bleach and pass the salt! Nat. Immunol., 3, 340-342 (2002).
    • (2002) Nat. Immunol. , vol.3 , pp. 340-342
    • Bokoch, G.M.1
  • 31
    • 0037108109 scopus 로고    scopus 로고
    • Current molecular models for NADPH oxidase regulation by Rac GTPase
    • Bokoch, G. M., and Diebold, B. A., Current molecular models for NADPH oxidase regulation by Rac GTPase. Blood, 100, 2692-2696 (2002).
    • (2002) Blood , vol.100 , pp. 2692-2696
    • Bokoch, G.M.1    Diebold, B.A.2
  • 33
    • 0037304542 scopus 로고    scopus 로고
    • All roads lead to actin: The intimate relationship between TCR signaling and the cytoskeleton
    • Fuller, C. L., Braciale, V. L., and Samelson, L. E., All roads lead to actin: the intimate relationship between TCR signaling and the cytoskeleton. Immunol. Rev., 191, 220-236 (2003).
    • (2003) Immunol. Rev. , vol.191 , pp. 220-236
    • Fuller, C.L.1    Braciale, V.L.2    Samelson, L.E.3
  • 34
    • 0038433238 scopus 로고    scopus 로고
    • Podosomes: Adhesion hot-spots of invasive cells
    • Linder, S., and Aepfelbacher, M., Podosomes: adhesion hot-spots of invasive cells. Trends Cell. Biol., 13, 376-385 (2003).
    • (2003) Trends Cell. Biol. , vol.13 , pp. 376-385
    • Linder, S.1    Aepfelbacher, M.2
  • 35
    • 0036178447 scopus 로고    scopus 로고
    • Signal transduction by cell adhesion receptors and the cytoskeleton
    • Juliano, R. L., Signal transduction by cell adhesion receptors and the cytoskeleton. Annu. Rev. Pharmacol. Toxicol., 42, 283-323 (2002).
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 283-323
    • Juliano, R.L.1


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