메뉴 건너뛰기




Volumn 21, Issue 1, 1992, Pages 25-37

Evidence for a gelsolin-rich, labile F-actin pool in human polymorphonuclear leukocytes

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; F ACTIN; GELSOLIN; PHALLACIDIN; REGULATOR PROTEIN; TRITON X 100;

EID: 0026584237     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/cm.970210104     Document Type: Article
Times cited : (49)

References (33)
  • 1
    • 0020290629 scopus 로고
    • Stress fibers in cells in situ: Immunofluorescence visualization with antiactin, antimyosin, and anti‐alpha‐actinin
    • Byers, H. R., Fujiwara, K. (1982): Stress fibers in cells in situ: Immunofluorescence visualization with antiactin, antimyosin, and anti‐alpha‐actinin. J. Cell Biol. 93: 804–811.
    • (1982) J. Cell Biol. , vol.93 , pp. 804-811
    • Byers, H.R.1    Fujiwara, K.2
  • 2
    • 0025219721 scopus 로고
    • Chemoattractant stimulated polymorphonuclear leukocytes contain two populations of actin filaments that differ in their spatial distributions and relative stabilities
    • Cassimeris, L., McNeill H., and Zigmond, S. H. (1990): Chemoattractant stimulated polymorphonuclear leukocytes contain two populations of actin filaments that differ in their spatial distributions and relative stabilities. J. Cell Biol. 110: 1067–1075.
    • (1990) J. Cell Biol. , vol.110 , pp. 1067-1075
    • Cassimeris, L.1    McNeill, H.2    Zigmond, S.H.3
  • 3
    • 0023008203 scopus 로고
    • The actin filament‐severing domain of plasma gelsolin
    • Chaponnier, C., Janmey, P. A., and Yin, H. L. (1981): The actin filament‐severing domain of plasma gelsolin. J. Cell Biol. 103: 1473–81.
    • (1981) J. Cell Biol. , vol.103 , pp. 1473-81
    • Chaponnier, C.1    Janmey, P.A.2    Yin, H.L.3
  • 4
    • 0023088797 scopus 로고
    • Reversibility of gelsolin/actin interaction in macrophages: Evidence of Ca2+ independent pathways
    • Chaponnier, C. H., Yin, H. L., and Stossel, T. P. (1987): Reversibility of gelsolin/actin interaction in macrophages: Evidence of Ca 2+ independent pathways. J. Exp. Med. 165: 97–106.
    • (1987) J. Exp. Med. , vol.165 , pp. 97-106
    • Chaponnier, C.H.1    Yin, H.L.2    Stossel, T.P.3
  • 5
    • 0023746711 scopus 로고
    • Two classes of actin microfilaments are associated with the inner cytoskeleton of axons
    • Fath, K. R., and Lasek, R. J. (1988): Two classes of actin microfilaments are associated with the inner cytoskeleton of axons. J. Cell Biol. 107: 613–621.
    • (1988) J. Cell Biol. , vol.107 , pp. 613-621
    • Fath, K.R.1    Lasek, R.J.2
  • 6
    • 0019867578 scopus 로고
    • Inhibition of actin polymerization in blood platelets by cytochalasins
    • Fox, J. E. B., and Phillips, D. R. (1981): Inhibition of actin polymerization in blood platelets by cytochalasins. Nature 292: 650–652.
    • (1981) Nature , vol.292 , pp. 650-652
    • Fox, J.E.B.1    Phillips, D.R.2
  • 7
    • 0023657143 scopus 로고
    • Kinetic heterogeneity of F‐actin polymers
    • Grazi, E., and Magri, E. (1987): Kinetic heterogeneity of F‐actin polymers. Biochem. J. 248: 721–25.
    • (1987) Biochem. J. , vol.248 , pp. 721-25
    • Grazi, E.1    Magri, E.2
  • 8
    • 0024548731 scopus 로고
    • Association of gelsolin with actin filaments and cell membranes of macrophages and platelets
    • Hartwig, J. H., Chambers, K. A., and Stossel, T. P. (1989): Association of gelsolin with actin filaments and cell membranes of macrophages and platelets. J. Cell Biol. 108: 467–479.
    • (1989) J. Cell Biol. , vol.108 , pp. 467-479
    • Hartwig, J.H.1    Chambers, K.A.2    Stossel, T.P.3
  • 9
    • 0025782209 scopus 로고
    • Cell locomotion: New research tests old ideas on membrane and cytoskeletal flow
    • Heath, J. P., and Holifield, B. F. (1991): Cell locomotion: New research tests old ideas on membrane and cytoskeletal flow. Cell Motil. Cytoskeleton 18: 245–257.
    • (1991) Cell Motil. Cytoskeleton , vol.18 , pp. 245-257
    • Heath, J.P.1    Holifield, B.F.2
  • 10
    • 85120515366 scopus 로고
    • Gelsolin regulates, but does not create, plus end nuclei during FMLP‐induced actin polymerization in neutrophils (PMNs)
    • Howard, T. H., and Chaponnier, C. (1990): Gelsolin regulates, but does not create, plus end nuclei during FMLP‐induced actin polymerization in neutrophils (PMNs). J. Cell Biol. 111 (5) (Part 2): 162a.
    • (1990) J. Cell Biol. , vol.111 , Issue.5 , pp. 162a
    • Howard, T.H.1    Chaponnier, C.2
  • 11
    • 0018594573 scopus 로고
    • Specific interaction of cytochalasins with muscle and platelet actin filaments in vitro
    • Howard, T. H., and Lin, S. (1979): Specific interaction of cytochalasins with muscle and platelet actin filaments in vitro. J. Supramol. Struct. 11: 283.
    • (1979) J. Supramol. Struct. , vol.11 , pp. 283
    • Howard, T.H.1    Lin, S.2
  • 12
    • 0021227906 scopus 로고
    • Chemotactic peptide modulation of actin assembly and locomotion in neutrophils
    • Howard, T. H., and Meyer, W. H. (1984): Chemotactic peptide modulation of actin assembly and locomotion in neutrophils. J. Cell Biol. 98: 1265–71.
    • (1984) J. Cell Biol. , vol.98 , pp. 1265-71
    • Howard, T.H.1    Meyer, W.H.2
  • 13
    • 0022293456 scopus 로고
    • A method for quantifying F‐actin in chemotactic peptide activated neutrophils: Study of the effect of tBOC peptide
    • Howard, T. H., and Oresajo, C. O. (1985a): A method for quantifying F‐actin in chemotactic peptide activated neutrophils: Study of the effect of tBOC peptide. Cell Motil. 5: 545–557.
    • (1985) Cell Motil. , vol.5 , pp. 545-557
    • Howard, T.H.1    Oresajo, C.O.2
  • 14
    • 0022181812 scopus 로고
    • The kinetics of chemotactic peptide‐induced change in F‐actin content, F‐actin distribution and the shape of neutrophils
    • Howard, T. H., and Oresajo, C. O. (1985b): The kinetics of chemotactic peptide‐induced change in F‐actin content, F‐actin distribution and the shape of neutrophils. J. Cell Biol. 101: 1078–85.
    • (1985) J. Cell Biol. , vol.101 , pp. 1078-85
    • Howard, T.H.1    Oresajo, C.O.2
  • 15
    • 0025367571 scopus 로고
    • Gelsolin‐actin interaction and actin polymerization in human neutrophils
    • Howard, T., Chaponnier, C., Yin, H., and Stossel, T., (1990a): Gelsolin‐actin interaction and actin polymerization in human neutrophils. J. Cell Biol. 110: 1983–1991.
    • (1990) J. Cell Biol. , vol.110 , pp. 1983-1991
    • Howard, T.1    Chaponnier, C.2    Yin, H.3    Stossel, T.4
  • 16
    • 0025020108 scopus 로고
    • Lipopolysac‐charide modulates chemotactic peptide induced actin polymerization in neutrophils
    • Howard, T. H., Wang, D., and Berkow, R. L. (1990b): Lipopolysac‐charide modulates chemotactic peptide induced actin polymerization in neutrophils. J. Leukocyte. Biol. 47: 13–24.
    • (1990) J. Leukocyte. Biol. , vol.47 , pp. 13-24
    • Howard, T.H.1    Wang, D.2    Berkow, R.L.3
  • 17
    • 0021801388 scopus 로고
    • Interactions of gelsolin and gelsolin‐actin complexes with actin: Effects of calcium on actin nucleation, filament severing and end blocking
    • Jammey, P. A., Chaponnier, C., Lind, S. E., Zaner, K. S., Tosssel, T. P., and Yin, H. L. (1985): Interactions of gelsolin and gelsolin‐actin complexes with actin: Effects of calcium on actin nucleation, filament severing and end blocking. Biochemistry 24: 3714–3723.
    • (1985) Biochemistry , vol.24 , pp. 3714-3723
    • Jammey, P.A.1    Chaponnier, C.2    Lind, S.E.3    Zaner, K.S.4    Tosssel, T.P.5    Yin, H.L.6
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970): Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0023875598 scopus 로고
    • Polymerization o. G‐actin by myosin subfragment I
    • Miller, L., Phillips, M., and Reisler, E. (1988): Polymerization o. G‐actin by myosin subfragment I. J. Biol. Chem. 263: 1996–2002.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1996-2002
    • Miller, L.1    Phillips, M.2    Reisler, E.3
  • 20
    • 0020669405 scopus 로고
    • Determination of total protein, in: Methods of Enzymology
    • Peterson, G. L., (1983): Determination of total protein. In Colowick, S. P., and Kaplan, N. O., (eds.); “ Methods of Enzymology,” Vol 91. San Diego ; Academic Press, Inc., pp. 95–99.
    • (1983) , vol.91 , pp. 95-99
    • Peterson, G.L.1
  • 21
    • 0019303302 scopus 로고
    • Identification of membrane proteins mediating the interaction of human platelets
    • Phillips, D. R., Jennings, L. K., and Edwards, H. H. (1980): Identification of membrane proteins mediating the interaction of human platelets. J. Cell Biol. 86: 77–86.
    • (1980) J. Cell Biol. , vol.86 , pp. 77-86
    • Phillips, D.R.1    Jennings, L.K.2    Edwards, H.H.3
  • 22
    • 0022555884 scopus 로고
    • Actin and actin binding proteins. A critical evaluation of mechanisms and functions
    • Pollard, T. D., and Cooper, J. A. (1986): Actin and actin binding proteins. A critical evaluation of mechanisms and functions. Ann. Rev. Biochem. 55: 987–1035.
    • (1986) Ann. Rev. Biochem. , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 23
    • 0021362583 scopus 로고
    • The organization of actin filaments in human polymorphonuclear leukocytes
    • Ryder, M. I., Weinreb, R. N., and Niederman, R. (1984): The organization of actin filaments in human polymorphonuclear leukocytes. Anat. Rec. 209: 7–20.
    • (1984) Anat. Rec. , vol.209 , pp. 7-20
    • Ryder, M.I.1    Weinreb, R.N.2    Niederman, R.3
  • 24
    • 0020836379 scopus 로고
    • Contractile proteins in leukocyte function
    • Southwick, F. S., and Stossel, T. P. (1983): Contractile proteins in leukocyte function. Semin. Hermatol. 20: 305–321.
    • (1983) Semin. Hermatol. , vol.20 , pp. 305-321
    • Southwick, F.S.1    Stossel, T.P.2
  • 25
    • 0025340881 scopus 로고
    • The actin released from profilin‐actin complexes is insufficient to account for the increase in F‐actin in chemoattractant stimulated polymorphonu clear leukocytes
    • Southwick, F. S., and Young, C. L. (1990): The actin released from profilin‐actin complexes is insufficient to account for the increase in F‐actin in chemoattractant stimulated polymorphonu clear leukocytes. J. Cell Biol. 110: 1965–73.
    • (1990) J. Cell Biol. , vol.110 , pp. 1965-73
    • Southwick, F.S.1    Young, C.L.2
  • 26
    • 0024454313 scopus 로고
    • PMN adherence induces actin polymerization by a transduction pathway which differs from that used by chemoattractants
    • Southwick, E. S., Dabiri, G. A., Paschetto, M., and Zigmond, S. H. (1990): PMN adherence induces actin polymerization by a transduction pathway which differs from that used by chemoattractants. J. Cell Biol. 109: 1561–69.
    • (1990) J. Cell Biol. , vol.109 , pp. 1561-69
    • Southwick, E.S.1    Dabiri, G.A.2    Paschetto, M.3    Zigmond, S.H.4
  • 27
    • 0015218407 scopus 로고
    • The regulation of rabbit muscle contraction: Biochemical studies of the interaction of the tropomyosin‐troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A., and Watt, S., (1971): The regulation of rabbit muscle contraction: Biochemical studies of the interaction of the tropomyosin‐troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246: 4866–4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 28
    • 84935776874 scopus 로고
    • The molecular biology of phagocytes and the molecular basis of non‐neoplastic phagocyte disorders, in: The Molecular Basis of Blood Diseases
    • Stossel, T. P., (1987): The molecular biology of phagocytes and the molecular basis of non‐neoplastic phagocyte disorders. In Stamatoyannopoulas, G., Nienhuis, A. W., Leder, P., Majerus, P. W., (eds.); “ The Molecular Basis of Blood Diseases.” Philadelphia: W.B. Saunders Co., pp. 499–533.
    • (1987) , pp. 499-533
    • Stossel, T.P.1
  • 29
    • 0343492953 scopus 로고
    • The mechanical responses of white blood cells, in: Inflammation: Basic Principles and Clinical Correlates
    • Stossel, T. P., (1988): The mechanical responses of white blood cells. In Gallin, J. I., Goldstein, I. M., Snyderman, R., (eds.); “ Inflammation: Basic Principles and Clinical Correlates.” New York: Raven Press, pp. 325–342.
    • (1988) , pp. 325-342
    • Stossel, T.P.1
  • 30
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Stachclin, T., and Gordon, J. (1979): Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. PNAS U.S.A. 76: 4350–4354.
    • (1979) PNAS U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Stachclin, T.2    Gordon, J.3
  • 31
    • 0023239714 scopus 로고
    • The effects of sulfhydryl inhibitors and cytochalasin on the cytoplasmic and cytoskeletal actin of human neutrophils
    • Wallace, P. J., Packman, C. H., Wersto, R. P., and Lichtman, M. A. (1987): The effects of sulfhydryl inhibitors and cytochalasin on the cytoplasmic and cytoskeletal actin of human neutrophils. J. Cell. Physiol. 132: 325–330.
    • (1987) J. Cell. Physiol. , vol.132 , pp. 325-330
    • Wallace, P.J.1    Packman, C.H.2    Wersto, R.P.3    Lichtman, M.A.4
  • 32
    • 0021020399 scopus 로고
    • Stimulation by chemotactic factor of actin association with the cytoskeleton in rabbit neutrophils
    • White, J. R., Naccache, P. H., and Sha'afi, R. I. (1983): Stimulation by chemotactic factor of actin association with the cytoskeleton in rabbit neutrophils. J. Biol. Chem. 258: 14041–14047.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14041-14047
    • White, J.R.1    Naccache, P.H.2    Sha'afi, R.I.3
  • 33
    • 0021888247 scopus 로고
    • Effects of chemotactic factors and other agents on the amounts of actin and a 65,000 molecular weight protein associated with the cytoskeleton of rabbit and human neutrophils
    • Yassin, R., Shefcyk, J., White, J. R., Tao, W., Volpi, M., Molski, T. F. P., Naccache, P. H., Feinstein, M. P., and Sha'afi, R. I. (1985): Effects of chemotactic factors and other agents on the amounts of actin and a 65,000 molecular weight protein associated with the cytoskeleton of rabbit and human neutrophils J. Cell Biol. 101: 182–188.
    • (1985) J. Cell Biol. , vol.101 , pp. 182-188
    • Yassin, R.1    Shefcyk, J.2    White, J.R.3    Tao, W.4    Volpi, M.5    Molski, T.F.P.6    Naccache, P.H.7    Feinstein, M.P.8    Sha'afi, R.I.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.