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Volumn 156, Issue 3, 1996, Pages 1247-1254

Phosphorylation of MRP14, an S100 protein expressed during monocytic differentiation, modulates Ca2+-dependent translocation from cytoplasm to membranes and cytoskeleton

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[No Author keywords available]

Indexed keywords

CALCIUM;

EID: 0030030745     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (98)

References (41)
  • 3
    • 0023648813 scopus 로고
    • A clue to the basic defect in cystic fibrosis from cloning the CF antigen gene
    • Dorin, J R., M Novak, R. E. Hill, D J. Brock, D. S. Secher, and V. van Heyningen. 1987. A clue to the basic defect in cystic fibrosis from cloning the CF antigen gene. Nature 326:614.
    • (1987) Nature , vol.326 , pp. 614
    • Dorin, J.R.1    Novak, M.2    Hill, R.E.3    Brock, D.J.4    Secher, D.S.5    Van Heyningen, V.6
  • 5
    • 0023764583 scopus 로고
    • The leukocyte L1 protein: Identity with the cystic fibrosis antigen and the calcium-binding MRP-8 and MRP-14 macrophage components
    • Andersson, K. B., K. Sletten, H. B. Berntzen, I. Dale, P. Brandtzaeg, E Jellum, and M. K. Fagerhol. 1988. The leukocyte L1 protein: identity with the cystic fibrosis antigen and the calcium-binding MRP-8 and MRP-14 macrophage components. Scand J. Immunol 28.241.
    • (1988) Scand J. Immunol , vol.28 , pp. 241
    • Andersson, K.B.1    Sletten, K.2    Berntzen, H.B.3    Dale, I.4    Brandtzaeg, P.5    Jellum, E.6    Fagerhol, M.K.7
  • 6
    • 0024093392 scopus 로고
    • Expression pattern of two related cystic fibrosis-associated calcium-binding proteins in normal and abnormal tissues
    • Wilkinson, M. M , A. Busuttil, C. Hayward, D. J. Brock, J. R Dorin, and V. van Heyningen. 1988 Expression pattern of two related cystic fibrosis-associated calcium-binding proteins in normal and abnormal tissues. J. Cell Sci. 91.221.
    • (1988) J. Cell Sci. , vol.91 , pp. 221
    • Wilkinson, M.M.1    Busuttil, A.2    Hayward, C.3    Brock, D.J.4    Dorin, J.R.5    Van Heyningen, V.6
  • 7
    • 0024390899 scopus 로고
    • Monoclonal antibody 5.5 reacts with p8,14, a myeloid molecule associated with some vascular endothelium
    • Hogg, N., C. Allen, and J. Edgeworth. 1989. Monoclonal antibody 5.5 reacts with p8,14, a myeloid molecule associated with some vascular endothelium Eur. J Immunol. 19:1053.
    • (1989) Eur. J Immunol. , vol.19 , pp. 1053
    • Hogg, N.1    Allen, C.2    Edgeworth, J.3
  • 8
    • 0022470995 scopus 로고
    • A monoclonal antibody to a subset of human monocytes found only in the peripheral blood and inflammatory tissues
    • Zwadlo, G., R. Schlegel, and C. Sorg 1986. A monoclonal antibody to a subset of human monocytes found only in the peripheral blood and inflammatory tissues J. Immunol. 137:512.
    • (1986) J. Immunol. , vol.137 , pp. 512
    • Zwadlo, G.1    Schlegel, R.2    Sorg, C.3
  • 9
    • 0023944868 scopus 로고
    • Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation
    • Lagasse, E., and R. G. Clerc. 1988. Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation. Mol Cell. Biol. 8:2402.
    • (1988) Mol Cell. Biol. , vol.8 , pp. 2402
    • Lagasse, E.1    Clerc, R.G.2
  • 10
    • 0023917095 scopus 로고
    • Two calcium-binding proteins associated with specific stages of myeloid cell differentiation are expressed by subsets of macrophages in inflammatory tissues
    • Zwadlo, G., J Bruggen, G. Gerhards, R. Schlegel, and C. Sorg. 1988. Two calcium-binding proteins associated with specific stages of myeloid cell differentiation are expressed by subsets of macrophages in inflammatory tissues. Clin. Exp Immunol. 72.510.
    • (1988) Clin. Exp Immunol. , vol.72 , pp. 510
    • Zwadlo, G.1    Bruggen, J.2    Gerhards, G.3    Schlegel, R.4    Sorg, C.5
  • 11
    • 0027327718 scopus 로고
    • Expression of calcium-binding proteins MRPS and MRP14 is associated with distinct monocytic differentiation pathways in HL-60 cells
    • Roth, J., M. Goebeler, C. van den Bos, and C. Sorg. 1993. Expression of calcium-binding proteins MRPS and MRP14 is associated with distinct monocytic differentiation pathways in HL-60 cells. Biochem. Biophys. Res. Commun. 191:565.
    • (1993) Biochem. Biophys. Res. Commun. , vol.191 , pp. 565
    • Roth, J.1    Goebeler, M.2    Van Den Bos, C.3    Sorg, C.4
  • 12
    • 0025845953 scopus 로고
    • Cellular events associated with inflammatory angiogenesis in the mouse cornea
    • Sunderkotter, C., W. Beil, J Roth, and C. Sorg. 1991. Cellular events associated with inflammatory angiogenesis in the mouse cornea. Am. J Pathol. 138:931.
    • (1991) Am. J Pathol. , vol.138 , pp. 931
    • Sunderkotter, C.1    Beil, W.2    Roth, J.3    Sorg, C.4
  • 13
    • 0024421282 scopus 로고
    • Ionomycin-regulated phosphorylation of the myeloid calcium-binding protein p14
    • Edgeworth, J., P. Freemont, and N. Hogg. 1989. Ionomycin-regulated phosphorylation of the myeloid calcium-binding protein p14. Nature 342:189
    • (1989) Nature , vol.342 , pp. 189
    • Edgeworth, J.1    Freemont, P.2    Hogg, N.3
  • 14
    • 0025506195 scopus 로고
    • A protein complex expressed during terminal differentiation of monomyelocytic cells is an inhibitor of cell growth
    • Murao, S., F. Collart, and E Huberman. 1990 A protein complex expressed during terminal differentiation of monomyelocytic cells is an inhibitor of cell growth. Cell Growth Differ. 1 447
    • (1990) Cell Growth Differ. , vol.1 , pp. 447
    • Murao, S.1    Collart, F.2    Huberman, E.3
  • 15
    • 0023875705 scopus 로고
    • Interactions between the microtubule-associated tau proteins and S100b regulate tau phosphorylation by the Ca2+/calmodulin-dependent protein kinase II
    • Baudier, J., and R. D. Cole. 1988 Interactions between the microtubule-associated tau proteins and S100b regulate tau phosphorylation by the Ca2+/calmodulin-dependent protein kinase II. J. Biol Chem. 263.5876.
    • (1988) J. Biol Chem. , vol.263 , pp. 5876
    • Baudier, J.1    Cole, R.D.2
  • 16
    • 0023190008 scopus 로고
    • Comparison of S100b protein with calmodulin: Interactions with melittin and microtubule-associated tau proteins and inhibition of phosphorylation of tau proteins by protein kinase C
    • Baudier, J., D. Mochly Rosen, A. Newton, S. H. Lee, D. E. J. Koshland, and R. D. Cole. 1987. Comparison of S100b protein with calmodulin: interactions with melittin and microtubule-associated tau proteins and inhibition of phosphorylation of tau proteins by protein kinase C. Biochemistry 26:2886.
    • (1987) Biochemistry , vol.26 , pp. 2886
    • Baudier, J.1    Mochly Rosen, D.2    Newton, A.3    Lee, S.H.4    Koshland, D.E.J.5    Cole, R.D.6
  • 17
    • 0025772977 scopus 로고
    • Calcium-dependent complex assembly of the myeloic differentiation proteins MRP-8 and MRP-14
    • Teigelkamp, S., R. S. Bhardwaj, J. Roth, G. Meinardus Hager, M. Karas, and C Sorg. 1991. Calcium-dependent complex assembly of the myeloic differentiation proteins MRP-8 and MRP-14. J. Biol Chem 266:13462.
    • (1991) J. Biol Chem , vol.266 , pp. 13462
    • Teigelkamp, S.1    Bhardwaj, R.S.2    Roth, J.3    Meinardus Hager, G.4    Karas, M.5    Sorg, C.6
  • 18
    • 0027182472 scopus 로고
    • MRP8 and MRP14, S-100 like proteins associated with myeloid differentiation, are translocated to plasma membrane and intermediate filaments in a calcium-dependent manner
    • Roth, J., F Burwinkel, C. van den Bos, M. Goebeler, E. Vollmer, and C Sorg 1993. MRP8 and MRP14, S-100 like proteins associated with myeloid differentiation, are translocated to plasma membrane and intermediate filaments in a calcium-dependent manner Blood 82:1875.
    • (1993) Blood , vol.82 , pp. 1875
    • Roth, J.1    Burwinkel, F.2    Van Den Bos, C.3    Goebeler, M.4    Vollmer, E.5    Sorg, C.6
  • 19
    • 0020693430 scopus 로고
    • Endogenous protein phosphorylation by resting and activated human neutrophils
    • Andrews, P , and B. Babior 1983 Endogenous protein phosphorylation by resting and activated human neutrophils. Blood 61:333
    • (1983) Blood , vol.61 , pp. 333
    • Andrews, P.1    Babior, B.2
  • 20
    • 0025900907 scopus 로고
    • Identification of p8,14 as a highly abundant heterodimenc calcium binding protein complex of myeloid cells
    • Edgeworth, J., M Gorman, R Bennett, P. Freemont, and N. Hogg. 1991 Identification of p8,14 as a highly abundant heterodimenc calcium binding protein complex of myeloid cells. J. Biol. Chem 266:7706.
    • (1991) J. Biol. Chem , vol.266 , pp. 7706
    • Edgeworth, J.1    Gorman, M.2    Bennett, R.3    Freemont, P.4    Hogg, N.5
  • 21
    • 0024351958 scopus 로고
    • Regulation of casein kinase II activity by epidermal growth factor in human A-431 carcinoma cells
    • Ackerman, P., and N. Osheroff. 1989. Regulation of casein kinase II activity by epidermal growth factor in human A-431 carcinoma cells. J. Biol. Chem. 264 11958.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11958
    • Ackerman, P.1    Osheroff, N.2
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of dye-binding
    • Bradford, M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of dye-binding. Anal. Biochem 72;248
    • (1976) Anal. Biochem , vol.72 , pp. 248
    • Bradford, M.1
  • 23
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schaegger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368.
    • (1987) Anal. Biochem. , vol.166 , pp. 368
    • Schaegger, H.1    Von Jagow, G.2
  • 24
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H., 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007
    • O'Farrell, P.H.1
  • 25
    • 0020437026 scopus 로고
    • Casein kinases-multipotential protein kinases
    • Hathaway, G M., and J. A. Traugh. 1982. Casein kinases-multipotential protein kinases. Curr. Top. Cell Regul. 21:101
    • (1982) Curr. Top. Cell Regul. , vol.21 , pp. 101
    • Hathaway, G.M.1    Traugh, J.A.2
  • 26
    • 0015498927 scopus 로고
    • Isolation and characterization of lymphocyte plasma membranes
    • Ferber, E., K Resch, D. F. Wallach, and W. Imm. 1972 Isolation and characterization of lymphocyte plasma membranes. Biochim. Biophys. Acta 266:494
    • (1972) Biochim. Biophys. Acta , vol.266 , pp. 494
    • Ferber, E.1    Resch, K.2    Wallach, D.F.3    Imm, W.4
  • 27
    • 0344048011 scopus 로고
    • In vitro assembly of intermediate filaments from baby hamster kidney (BHK-21) cells
    • Zackroff, R. V , and R. D. Goldman 1979 In vitro assembly of intermediate filaments from baby hamster kidney (BHK-21) cells. Proc. Natl. Acad Sci. USA 76:6226.
    • (1979) Proc. Natl. Acad Sci. USA , vol.76 , pp. 6226
    • Zackroff, R.V.1    Goldman, R.D.2
  • 28
    • 0000969171 scopus 로고
    • Lactate dehydrogenase assay: UV-method with pyruvate and NADH
    • H U. Bergmeyer, ed. Academic Press, New York
    • Vasault, A. 1974. Lactate dehydrogenase assay: UV-method with pyruvate and NADH. In Methods of Enzymatic Analysis, 3rd Ed. H U. Bergmeyer, ed. Academic Press, New York, p. 607.
    • (1974) Methods of Enzymatic Analysis, 3rd Ed. , pp. 607
    • Vasault, A.1
  • 29
    • 0021379023 scopus 로고
    • Detection of calcium binding proteins by 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis
    • Maruyama, K , T. Mikawa, and S. Ebashi. 1984. Detection of calcium binding proteins by 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis. J. Biochem. (Tokyo) 95:511.
    • (1984) J. Biochem. (Tokyo) , vol.95 , pp. 511
    • Maruyama, K.1    Mikawa, T.2    Ebashi, S.3
  • 30
    • 0005817953 scopus 로고
    • One-dimensional electrophoresis
    • B. D. Hames and L Rickwood, eds IRL Press, Oxford, New York, and Tokyo
    • Hames, B. D. 1990. One-dimensional electrophoresis. In Gel Electrophoresis of Proteins-A Practical Approach, 2nd Ed B. D. Hames and L Rickwood, eds IRL Press, Oxford, New York, and Tokyo, p 119
    • (1990) Gel Electrophoresis of Proteins-A Practical Approach, 2nd Ed , pp. 119
    • Hames, B.D.1
  • 31
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak, M. 1987. An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs Nucleic Acids Res. 15:8125.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8125
    • Kozak, M.1
  • 32
    • 0025019946 scopus 로고
    • Subcellular fate of the int-2 oncoprotein is determined by choice of initiation codon
    • Acland, P., M. Dixon, G. Peters, and C. Dickson. 1990. Subcellular fate of the int-2 oncoprotein is determined by choice of initiation codon. Nature 343-662.
    • (1990) Nature , vol.343 , pp. 662
    • Acland, P.1    Dixon, M.2    Peters, G.3    Dickson, C.4
  • 33
    • 0026019439 scopus 로고
    • The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG
    • Saris, C J , J. Domen, and A Berns. 1991 The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG. EMBO J. 10:655.
    • (1991) EMBO J. , vol.10 , pp. 655
    • Saris, C.J.1    Domen, J.2    Berns, A.3
  • 34
    • 0026508612 scopus 로고
    • Alternative usage of initiation codons in mRNA encoding the cAMP-responsive element modulator generates regulators with opposite functions
    • Delmas, V., B M. Laoide, D Masquilier, R P. De Groot, N S. Foulkes, and Sassone-Corsi 1992. Alternative usage of initiation codons in mRNA encoding the cAMP-responsive element modulator generates regulators with opposite functions. Proc. Natl Acad. Sci. USA 89:4226.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 4226
    • Delmas, V.1    Laoide, B.M.2    Masquilier, D.3    De Groot, R.P.4    Foulkes, N.S.5    Sassone-Corsi6
  • 35
    • 0027301872 scopus 로고
    • Calcium-binding myeloid protein (P(8,14)) is phosphorylated in fMET-LEU-PHE stimulated neutrophils
    • Bengis-Garber, C., and N. Gruener. 1993 Calcium-binding myeloid protein (P(8,14)) is phosphorylated in fMET-LEU-PHE stimulated neutrophils. J. Leukocyte Biol. 54:114.
    • (1993) J. Leukocyte Biol. , vol.54 , pp. 114
    • Bengis-Garber, C.1    Gruener, N.2
  • 36
    • 0026688572 scopus 로고
    • Translocation of a small cytosolic calcium-binding protein (MRP8) to plasma membrane correlates with human neutrophil activation
    • Lemarchand, P., M Vagliot, J. Mauel, and M. Markert. 1992. Translocation of a small cytosolic calcium-binding protein (MRP8) to plasma membrane correlates with human neutrophil activation. J. Biol. Chem 267:19379.
    • (1992) J. Biol. Chem , vol.267 , pp. 19379
    • Lemarchand, P.1    Vagliot, M.2    Mauel, J.3    Markert, M.4
  • 37
    • 0026643040 scopus 로고
    • The calcium-binding proteins MRP8 and MRP14 form a membrane associated heterodimer in a subset of monocytes/macrophages present in acute but absent in chronic inflammation Eur
    • Bhardwaj, R S., C Zotz, G Zwadlo-Klarwasser, J Roth, M. Goebeler, K. Mahnke, M. Falk, G. Meinardus-Hager, and C. Sorg. 1992. The calcium-binding proteins MRP8 and MRP14 form a membrane associated heterodimer in a subset of monocytes/macrophages present in acute but absent in chronic inflammation Eur. J. Immunol. 22 1891.
    • (1992) J. Immunol. , vol.22 , pp. 1891
    • Bhardwaj, R.S.1    Zotz, C.2    Zwadlo-Klarwasser, G.3    Roth, J.4    Goebeler, M.5    Mahnke, K.6    Falk, M.7    Meinardus-Hager, G.8    Sorg, C.9
  • 38
    • 0027983558 scopus 로고
    • Expression of the calcium-binding proteins MRPS and MRP14 in monocytes is regulated by a calcium-induced suppressor mechanism
    • Roth, J., M. Goebeler, V. Wrocklage, C van den Bos, and C. Sorg 1994. Expression of the calcium-binding proteins MRPS and MRP14 in monocytes is regulated by a calcium-induced suppressor mechanism. Biochem. J. 301: 655.
    • (1994) Biochem. J. , vol.301 , pp. 655
    • Roth, J.1    Goebeler, M.2    Wrocklage, V.3    Van Den Bos, C.4    Sorg, C.5
  • 39
    • 0027991756 scopus 로고
    • Expression and complex formation of S100-like proteins MRP8 and MRP14 by macrophages during renal allograft rejection
    • Goebeler, M., J. Roth, F. Burwinkel, E. Vollmer, W. Bocker, and C. Sorg. 1994 Expression and complex formation of S100-like proteins MRP8 and MRP14 by macrophages during renal allograft rejection. Transplantation 58.355.
    • (1994) Transplantation , vol.58 , pp. 355
    • Goebeler, M.1    Roth, J.2    Burwinkel, F.3    Vollmer, E.4    Bocker, W.5    Sorg, C.6
  • 40
    • 0027431908 scopus 로고
    • Resistance of mice to experimental leishmaniasis is associated with more rapid appearance of mature macrophages in vitro and in vivo
    • Sunderkotter, C., M. Kunz, K. Steinbrink, G. Meinardus-Hager, M Goebeler, H. Bildau, and C. Sorg. 1993. Resistance of mice to experimental leishmaniasis is associated with more rapid appearance of mature macrophages in vitro and in vivo. J Immunol 151:4891.
    • (1993) J Immunol , vol.151 , pp. 4891
    • Sunderkotter, C.1    Kunz, M.2    Steinbrink, K.3    Meinardus-Hager, G.4    Goebeler, M.5    Bildau, H.6    Sorg, C.7
  • 41
    • 0026645680 scopus 로고
    • Expression of the calcium-binding proteins MRPS and MRP14 by early infiltrating cells in experimental contact dermatitis
    • Roth, J , C. Sunderkotter, M Goebeler, J Gutwald, and C. Sorg 1992. Expression of the calcium-binding proteins MRPS and MRP14 by early infiltrating cells in experimental contact dermatitis Int. Arch. Allergy Immunol. 98:130
    • (1992) Int. Arch. Allergy Immunol. , vol.98 , pp. 130
    • Roth, J.1    Sunderkotter, C.2    Goebeler, M.3    Gutwald, J.4    Sorg, C.5


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