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  • 1
    ISSN: 1432-0568
    Keywords: Cytotactin ; Central nervous system ; J1-160/180 ; Restrictin ; Precartilaginous mesenchyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Rabbit antisera against tenascin, a large extracellular matrix protein, in conjunction with monoclonal antibodies of mouse origin against versican, a large hyaluronate-binding proteoglycan, were used to make a comparative study of the distribution of the two antigens in the same cryostat sections by double immunofluorescence. In the central nervous system, tenascin was invariably associated with versican, but the reverse was not true, in that versican was also found where tenascin was not detectable, particularly in gray matter. There were major species differences in the distribution of tenascin in the central nervous system. In the cow, tenascin was found in cerebral and spinal cord white matter and in the granule cell layer of the cerebellum. In the human brain, tenascin was found in cerebral white matter but not in the cerebellum. In the rat, tenascin was mainly confined to brain periventricular layer and spinal cord white matter. During the development of the cerebellum of the rat, the tenascin immunoreactivity decreased, and a lower molecular weight band appeared (J1-160/180/restrictin?) and persisted throughout adulthood. Tenascin expression was a relatively late event in the development of the rat central nervous system, immunoreactivity being first observed after birth. In the rat embryo, tenascin was found to co-localize with versican in precartilaginous mesenchyme and in connective tissue underlying epithelia. The colocalization of versican with tenascin suggests that versican may be the tenascin (cytotactin)-associated proteoglycan reported in the literature.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 10 (1979), S. 419-431 
    ISSN: 0091-7419
    Keywords: microtubules ; assembly ; protein-protein interactions ; electron microscopy ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Tubulin rings have been previously identified as composed of linear polymers of tubulin subunits, equivalent to a protofilament in the microtubule wall but in a curved rather than a straight conformation. We have examined and measured a number of different ring structures obtained under different conditions. The preferred curvature is indicated by a single ring of 380 Å outside diameter. Radially double rings consist of two coplanar rings of 460 Å and 350 Å outside diameter, held together by a pattern of eight identical contacts between the 40 Å subunits in the inner and outer rings. In some circumstances a larger ring, 570 Å diameter, can be added to the outside, or a smaller ring, 240 Å diameter, may be added to the inside of the radially double ring, in both cases repeating the pattern of eight radial contacts. The distortion of the filament from its relaxed 380 Å diameter curvature apparently can be made without disrupting the longitudinal bond between subunits in the filament, but must be stabilized by the energy of the radial contacts. All of these rings (single and radially double and triple) are observed to associate axially to form pairs or in some cases larger stacks. The radially double rings or an axially associated pair of these (quadruple ring) may also associate to form crystals. These are thin plates, up to 100 μm in extent and several μm thick which have been of limited use so far in diffraction studies because of irregularities in the packing of adjacent rings.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 2 (1974), S. 393-411 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Tubulin obtained from disassembly of microtubules at 0°C exists in two forms: 6-S tubulin and a larger, curved or ring-shaped filament. These two forms have been separated chromat ographically and their roles in assembly examined. The purified rings reassemble to microtubules with high efficiency by uncoiling and straightening out, to be incorporated directly as protofilaments in the microtubule wall, and are thus identified as preformed protofilaments. Purified 6-S tubulin has not been observed to reassemble into microtubules by itself but will contribute to assembly when mixed with rings. Addition of glycerol at 0°C induces the 6-S tubulin to form rings, and the treated fraction will then reassemble to microtubules. Electron microscope observations indicate that assembly begins with the formation and growth of an incomplete microtubule wall. This wall grows wider by the addition of new protofilaments until the intact, circular microtubule, with 13 protofilaments, is formed. It is suggested here that growth of this wall from individual 6-S tubulin subunits may be energetically unfavorable. The direct incorporation of preformed protofilaments may be much more favorable, in which case the rings would be required for this initial stage of assembly.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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