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  • 1
    Electronic Resource
    Electronic Resource
    Properties of tropomyosin from the dual-regulated obliquely striated body wall muscle of the earthworm (Lumbricus terrestris L.) (1982)
    Springer
    Journal of muscle research and cell motility 3 (1982), S. 57-74 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The obliquely straited body wall muscle of the earthwormLumbricus terrestris L. possesses a dual actin-linked and myosin-linked regulatory system. Tropomyosin from this muscle has now been purified and its functional properties compared to tropomyosin from vertebrate skeletal muscle. Earthworm tropomyosin has a molecular weight of about 70 000 and is composed of two polypeptide chains of molecular weight of 34 000 and 37 000. Structural and functional similarities to skeletal muscle tropomyosin were demonstrated with respect to the formation and periodicity of paracrystals and nets and the potentiation of skeletal muscle acto-SF1 ATPase activity at low ATP concentration. Likewise, earthworm tropomyosin inhibited skeletal muscle acto-HMM ATPase activity at normal ATP concentrations but to a much greater extent than skeletal muscle tropomyosin; this inhibition was removed by skeletal muscle troponin, in the presence of Ca2+. In a system containing earthworm myosin and skeletal muscle actin, earthworm tropomyosin had no detectable influence on the actin-activated ATPase activity. It is concluded that earthworm tropomyosin plays an active role in the actin-linked troponin-dependent regulatory system and has no measurable effect on the regulation via myosin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00711880
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  • 2
    Electronic Resource
    Electronic Resource
    Metavinculin and vinculin from mammalian smooth muscle: Bulk isolation and characterization (1987)
    Springer
    Journal of muscle research and cell motility 8 (1987), S. 329-341 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Metavinculin, a vinculin related protein found only in muscle, has been prepared in bulk amounts from porcine stomach by a new procedure: the same procedure is applicable to the purification of vinculin from porcine stomach and avian gizzard. A comparison of the mammalian and avian proteins by peptide mapping showed them all to contain a common protease resistant 90 kDa core; however both avian and mammalian vinculins were notably more resistant to proteolysis down to this core than their respective metavinculins. Despite the close similarities in the peptide maps, in molecular weight and amino acid composition neither of the mammalian proteins exhibited the head and tail morphology formerly described for gizzard vinculin and metavinculin; both porcine proteins appeared globular under the electron microscope. From the gross variability in the ratios of metavinculin to vinculin among smooth muscles of different origin as well as from the common detergent-independent solubility properties of both proteins during isolation, it is concluded that vinculin and metavinculin perform duplicatory roles as peripheral membrane components. No definitive evidence for the interaction of either protein with actin filaments was obtained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01568889
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Actin and the coordination of protrusion, attachment and retraction in cell crawling (1996)
    Springer
    Bioscience reports 16 (1996), S. 351-368 
    Details
    ISSN: 1573-4935
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract To crawl over a substrate a cell must first protrude in front, establish new attachments to the substrate and then retract its rear. Protrusion and retraction utilise different subcompartments of the actin cytoskeleton and operate by different mechanisms, one involving actin polymerization and the other myosin-based contraction. Using as examples the rapidly locomoting keratocyte and the slowly moving fibroblast we illustrate how over expression of one or the other actin subcompartments leads to the observed differences in motility. We also propose, that despite these differences there is a common coordination mechanism underlying the genesis of the actin cytoskeleton that involves the nucleation of actin filaments at the protruding cell front, in the lamellipodium, and the relocation of these filaments, via polymerization and flow, to the more posterior actin filament compartments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01207261
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  • 4
    Electronic Resource
    Electronic Resource
    β-actin specific monoclonal antibody (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 27 (1994), S. 108-116 
    Details
    ISSN: 0886-1544
    Keywords: smooth muscle ; fibroblasts ; lamellipodia ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Using a synthetic peptide mimicking the NH2-terminus of β-actin we have raised a monoclonal antibody specific for this cytoplasmic actin isoform. Specificity of the antibody was demonstrated by its labelling of the actin polypeptide only in tissues containing the β isoform, by its exclusive recognition of the synthetic β-actin peptide amongst those mimicking all six vertebrate isoactins, and by its selective recognition of the β-actin spot in two-dimensional electrophoresis gels of smooth muscle extracts. The antibody bound to actin filaments in both living and fixed fibroblasts where it labelled the stress fiber bundles and, more predominantly, the peripheral actin rich lamellipodia. The characteristics of the antibody indicate that it should serve as a useful tool for studying isoactin distribution and function. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970270203
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  • 5
    Electronic Resource
    Electronic Resource
    Complex protein composition of isolated focal adhesions: A two-dimensional gel and database analysis (1994)
    Weinheim : Wiley-Blackwell
    Electrophoresis 15 (1994), S. 511-519 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Current ideas about the composition of the focal adhesion complexes in cultured cells are based mainly on indirect immunocytochemical data. We here report a two-dimensional (2-D) gel electrophoresis analysis of the focal adhesion associated-structures that remain in the growth substrate after removal of cells by mechanical shearing. Many proteins additional to the known adhesion proteins, and in higher abundance, could be identified. Using selective extraction procedures, employing detergent or gelsolin, these could be classified as either membrane-associated, actin-associated or both. Cross correlation of these polypeptode patterns with a 2-D gel database allowed identification of some proteins, not previously considered as resident of focal adhesions. The data point to a more complex make up of focal adhesions than formerly supposed.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150150169
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  • 6
    Electronic Resource
    Electronic Resource
    Structure-function relationships in smooth muscle: The missing links (1995)
    New York, NY : Wiley-Blackwell
    BioEssays 17 (1995), S. 785-792 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Smooth muscle cells have developed a contractile machinery that allows them to exert tension on the surrounding extracellular matrix over their entire length. This has been achieved by coupling obliquely organized contractile filaments to a more-or-less longitudinal framework of cytoskeletal elements. Earlier structural data suggested that the cytoskeleton was composed primarily of intermediate filaments and played only a passive role. More recent findings highlight the segregation of actin isotypes and of actin-associated proteins between the contractile and cytoskeletal domains and raise the possibility that the cytoskeleton performs a more active function. Current efforts focus on defining the relative contributions of myosin cross-bridge cycling and actin-associated protein interactions to the maintenance of tension in smooth muscle tissue.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950170908
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