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  • 1
    Electronic Resource
    Electronic Resource
    End-label fingerprintings show that the N- and C-termini of actin are in the contact site with gelsolin (1989)
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 5269-5275 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00438a052
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  • 2
    Electronic Resource
    Electronic Resource
    Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking (1985)
    s.l. : American Chemical Society
    Biochemistry 24 (1985), S. 3714-3723 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00335a046
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  • 3
    Electronic Resource
    Electronic Resource
    PHOSPHOINOSITIDE REGULATION OF THE ACTIN CYTOSKELETON (2003)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Physiology 65 (2003), S. 761-789 
    Details
    ISSN: 0066-4278
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Medicine , Biology
    Notes: Abstract Phosphoinositides [PPIs, which collectively refer to phosphorylated derivatives of phosphatidylinositol (PI)] have a pivotal role as precursors to important second messengers and as bona fide signaling and scaffold targeting molecules. This review focuses on recent advances that elucidate how PPIs, particularly PI(4,5)P2 (PIP2), directly regulate the actin cytoskeleton in vivo by modulating the activity and targeting of actin regulatory proteins. The role of PIP2 in stimulating actin polymerization and in establishing cytoskeleton-plasma membrane linkages is emphasized. In addition, the review presents tantalizing evidence that suggests how binding of selected cytoskeletal proteins to membrane PPIs may promote PPI clustering into raft lipid microdomains, alter their accessibility to other proteins, and even distort the bilayer conformation. These actions have profound implications for many other PPI-regulated membrane functions that are beginning to be uncovered, and they suggest how PPIs can mediate crosstalk between the actin cytoskeleton and an expanding spectrum of essential cellular functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.physiol.65.092101.142517
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  • 4
    Electronic Resource
    Electronic Resource
    Control of cytoplasmic actin gel–sol transformation by gelsolin, a calcium-dependent regulatory protein (1979)
    [s.l.] : Nature Publishing Group
    Nature 281 (1979), S. 583-586 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Rabbit lung macrophage cytoplasmic extracts, prepared in buffered sucrose solution containing protease inhibitors12 and 5mM EGTA, solidified to form gels when warmed in the presence of 0.1 M KC1. Addition of calcium chloride to micro-molar-free calcium concentration inhibited gelation and caused ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/281583a0
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  • 5
    Electronic Resource
    Electronic Resource
    Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain (1986)
    [s.l.] : Nature Publishing Group
    Nature 323 (1986), S. 455-458 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The human hepatoma cell line HepG2 makes a large amount of plasma gelsolin2. We prepared a cDNA library from RNA isolated from confluent HepG2 cells and identified gelsolin clones by screening with labelled oligonucleotide probes. Rescreening with the original isolates led to the isolation of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/323455a0
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  • 6
    Electronic Resource
    Electronic Resource
    Gelsolin inhibition of fast axonal transport indicates a requirement for actin microfilaments (1984)
    [s.l.] : Nature Publishing Group
    Nature 310 (1984), S. 56-58 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fast axonal transport (FAT) can be inhibited in neurones by the injection of DNase I3"5 and filamin3. DNase I depolymerizes microfilaments by disrupting the F-actin/G-actin equilibrium9, whereas filamin inhibits activation of the myosin ATPase10. However, due to difficulties in controlling ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/310056a0
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  • 7
    Electronic Resource
    Electronic Resource
    Expression of gelsolin by cos cell secretion (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 14 (1989), S. 21-25 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970140106
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  • 8
    Electronic Resource
    Electronic Resource
    gCap39 is a nuclear and cytoplasmic protein (1993)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 26 (1993), S. 227-238 
    Details
    ISSN: 0886-1544
    Keywords: gelsolin ; actin binding proteins ; filament end capping ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: gCap39 is a newly identified member of the Ca2+- and polyphosphoinositidemodulated gelsolin family of actin binding proteins which is different from gelsolin in several important respects: it caps filament ends, it does not sever filaments, it binds reversibly to actin, it is phosphorylated in vivo, and it is also present in the nucleus. gCap39 and gelsolin coexist in a variety of cells. To better understand the roles of gCap39 and gelsolin, we have compared their relative amounts and intracellular distributions. We found that gCap39 is very abundant in macrophages (accounting for 0.6% of total macrophage proteins), and is present in 12-fold molar excess to gelsolin. Both proteins are highly induced during differentiation of the promyelocytic leukemia cell line into macrophages. gCap39 is less abundant in fibroblasts (0.04% total proteins) and is present in equal molar ratio to gelsolin. The two proteins are colocalized in the cytoplasm, but gCap39 is also found in the nucleus while gelsolin is not. Nuclear gCap39 redistributes throughout the cytoplasm during mitosis and is excluded from regions containing chromosomes. Our results demonstrate that gCap39 is a nuclear and cytoplasmic protein which has unique as well as common functions compared with gelsolin. © 1993 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970260306
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  • 9
    Electronic Resource
    Electronic Resource
    Effects of thymosin β4 and thymosin β10 on actin structures in living cells (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 27 (1994), S. 13-25 
    Details
    ISSN: 0886-1544
    Keywords: Tβ4 ; Tβ10 ; β-thymosins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The β-thymosins are a family of small proteins originally isolated from the thymus. Recently, two of the major mammalian isoforms, thymosin β4 (Tβ4) and thymosin β10 (Tβ10), are identified as significant actin monomer sequestering proteins which may be involved in regulating actin filament assembly. To study the cellular function of β-thymosins, we have used isoform-specific antibodies to determine their concentration and intracellular distribution, and examined the effects of inducing overexpression of Tβ4 and Tβ10 on actin filament structures. Immunofluorescence labeling of peritoneal macrophages showed that both β-thymosins are uniformly distributed within the cytoplasm. cDNA-mediated overexpression of β-thymosins in CV1 fibroblasts induced extensive loss of phalloidinstained actin stress fibers. Stress fibers in the cell center were more susceptible than those at the periphery. There was a decrease in the number of focal adhesions, as evidenced by a decrease in discrete vinculin staining and an increase in diffuse vinculin fluorescence. The majority of the transfected cells had normal shape in spite of extensive loss of actin filaments. Occasionally, cells overexpressing β-thymosin were observed to divide. In these cells, β-thymosin was excluded from the midbody which contains an actin filament-rich contractile ring. Our results indicate that Tβ4 and Tβ10 are functionally very similar and both are effective regulators of a large subset of actin filaments in living cells. © 1994 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970270103
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  • 10
    Electronic Resource
    Electronic Resource
    The organization and regulation of the macrophage actin skeleton (1988)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 10 (1988), S. 117-125 
    Details
    ISSN: 0886-1544
    Keywords: cytoskeleton ; actin-binding protein ; gelsolin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: To move, leukocytes extend portions of their cortical cytoplasm as pseudopods. These pseudopods are filled with a three-dimensional actin filament skeleton, the reversible assembly of which in response to receptor stimulation is thought to play a major role in providing the mechanical force for these protrusive movements. The organization of this actin skeleton occurs at different levels within the cell, and a number of macrophage proteins have been isolated and shown to affect the architecture, assembly, stability, and length of actin filaments in vitro. The architecture of cytoplasmic actin is regulated by proteins that cross-link filaments in higher-order structures. Actin-binding protein plays a major role in defining network structure by cross-linking actin filaments into orthogonal networks. Gelsolin may have a central role in regulating network structure. It binds to the sides of actin filaments and severs them, and binds the “barbed” filament end, thereby blocking monomer addition at this end. Gelsolin is activated to bind actin filaments by μM calcium. Dissociation of gelsolin bound on filament ends occurs in the presence of the polyphosphoinositides, PIP and PIP2. Calcium and PIP2 have been shown to be intracellular messengers of cell stimulation.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970100116
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