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  • Cell & Developmental Biology  (4)
  • 1975-1979  (2)
  • 1965-1969  (1)
  • 1890-1899  (1)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Morphology 149 (1976), S. 33-51 
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The mature annelid cuticle contains orthogonally oriented collagen in a matrix capped superficially by a dense epicuticle with external corpuscles. The underlying epidermis is a simple columnar epithelium with two major cell types, mucous-secreting cells which secrete through channels in the cuticle to the exterior of the worm, and “supportive” cells which presumably produce and increase the cuticle by secreting into it.The structures of supportive cells, previously interpreted as specialized for establishing interfibrillar collagen order, are revealed by glutaraldehyde fixation as common cellular components without the qualities deemed useful to align collagen. Cell processes which penetrate and sometimes pass completely through the cuticle are not stable, not in geometric order, and lack cilia-like structure. Cilia, unlike the ubiquitous cellular processes, are highly restricted to regions of the epidermis with specialized functions. Cellular control, or other control, of collagen fibrillogenesis remains unestablished.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Morphology 149 (1976), S. 53-71 
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Appearance of collagen fibrils in the cuticle was seen by electron microscopy to be preceded by fonnation of a finely filamentous matrix material. At first, the fine filaments of the matrix are unorganized. However, signs of orthogonal ordering soon appear in the most superficial portion of the cuticle, and subsequently appear more basally and closer to the underlying epidermis. Meanwhile, fibrils of different staining properties and identifiable as collagen begin to be deposited in the superficial portion of the cuticle, the same region which first showed organized fine filaments. Then, like the fine filaments before them, the collagen fibrils polymerize more basally. Collagen appears to polymerize on the preformed skeleton of fine filaments as though the fine filaments caused the collagen to assemble. Neither the polymerization nor ordering of collagen fibrils seems to require direct cellular intervention but occur first in that portion of the cuticle which is furthest away from the underlying epidermis. The fine filaments may be self ordering, extracellular macromolecules which in turn determine the polymerization of collagen fibrils.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Subunits of immunoglobulins have been prepared by two methods, both of which have contributed to our knowledge of the structural basis of antibody specificity. The first method is enzymic hydrolysis with either papain or pepsin and leads to the unequivocal conclusion that each combining site is contained in a fragment (Fab) of about 45,000 molecular weight and formed from the light chain and the N-terminal half of the heavy chain, the Fd fragment. The second method of preparing subunits is to reduce the interchain disulfide bonds and to isolate the chains. This should decide whether the combining site is in the Fd fragment, the light chain, or is formed jointly by both. In fact, considerable loss of affinity for the antigen follows, whatever technique is used to dissociate the peptide chains and, although many papers have been published on this subject, no definite answer has yet been obtained. Although the majority opinion probably favors the view that both chains are concerned in the formation of the combining site, our tentative conclusion is that the site is placed entirely in the heavy chain and that the light chain has only a semispecific role in facilitating the reformation of the native configuration of the heavy chain after its disruption under the conditions necessary for dissociation of the two chains.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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