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      Histology and growth of the cetacean petro-tympanic bone complex

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      Journal of Zoology
      Cambridge University Press (CUP)

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          Type V collagen: molecular structure and fibrillar organization of the chicken alpha 1(V) NH2-terminal domain, a putative regulator of corneal fibrillogenesis

          Previous work from our laboratories has demonstrated that: (a) the striated collagen fibrils of the corneal stroma are heterotypic structures composed of type V collagen molecules coassembled along with those of type I collagen, (b) the high content of type V collagen within the corneal collagen fibrils is one factor responsible for the small, uniform fibrillar diameter (25 nm) characteristic of this tissue, (c) the completely processed form of type V collagen found within tissues retains a large noncollagenous region, termed the NH2- terminal domain, at the amino end of its alpha 1 chain, and (d) the NH2- terminal domain may contain at least some of the information for the observed regulation of fibril diameters. In the present investigation we have employed polyclonal antibodies against the retained NH2- terminal domain of the alpha 1(V) chain for immunohistochemical studies of embryonic avian corneas and for immunoscreening a chicken cDNA library. When combined with cDNA sequencing and molecular rotary shadowing, these approaches provide information on the molecular structure of the retained NH2-terminal domain as well as how this domain might function in the regulation of fibrillar structure. In immunofluorescence and immunoelectron microscopy analyses, the antibodies against the NH2-terminal domain react with type V molecules present within mature heterotypic fibrils of the corneal stroma. Thus, epitopes within at least a portion of this domain are exposed on the fibril surface. This is in marked contrast to mAbs which we have previously characterized as being directed against epitopes located in the major triple helical domain of the type V molecule. The helical epitopes recognized by these antibodies are antigenically masked on type V molecules that have been assembled into fibrils. Sequencing of the isolated cDNA clones has provided the conceptual amino acid sequence of the entire amino end of the alpha 1(V) procollagen chain. The sequence shows the location of what appear to be potential propeptidase cleavage sites. One of these, if preferentially used during processing of the type V procollagen molecule, can provide an explanation for the retention of the NH2-terminal domain in the completely processed molecule. The sequencing data also suggest that the NH2-terminal domain consists of several regions, providing a structure which fits well with that of the completely processed type V molecule as visualized by rotary shadowing.
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            Bone cell biology: the regulation of development, structure, and function in the skeleton.

            Bone cells compose a population of cells of heterogeneous origin but restricted function with respect to matrix formation, mineralization, and resorption. The local, mesenchymal origin of the cells which form the skeleton contrasts with their extraskeletal, hemopoietic relatives under which bone resorption takes place. However, the functions of these two diverse populations are remarkably related and interdependent. Bone cell regulation, presently in its infancy, is a complicated cascade involving a plethora of local and systemic factors, including some components of the skeletal matrices and other organ systems. Thus, any understanding of bone cell regulation is a key ingredient in understanding not only the development, maintenance, and repair of the skeleton but also the prevention and treatment of skeletal disorders.
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              On how the periosteal bone of the delphinid humerus becomes cancellous: ontogeny of a histological specialization.

              In cetaceans, the bones of the flippers lack a free medullary cavity and have a cancellous texture, with compact cortices reduced or absent. The present work discusses the ontogenetic basis of these characters in terms of the ontogeny of the structure and textural bone compactness (TBC) of the humeral diaphysis in a growth series of common dolphins (Delphinus delphis). The texture of the primary periosteal deposits is compact; soon after their accretion, the deposits undergo an extensive erosion that turns them into a cancellous tissue. A diffuse endosteal front of resorption expands in parallel with the growth of the cortex and acts as small units scattered within the cortices. Starting soon after birth and continuing throughout the life of the animals, the compactness of the periosteal cortex decreases at both general and local levels. This trend correlates strongly with the increase in size of the diaphyseal section and reflects the fact that relatively more bone is eroded than deposited during growth in the cancellous parts of the cortex. In the broad sense, this is basically an osteoporotic process, which is not identical, however, to senile or disuse osteoporoses.
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                Author and article information

                Journal
                Journal of Zoology
                J. Zoology
                Cambridge University Press (CUP)
                0952-8369
                1469-7998
                1999
                April 2004
                : 262
                : 4
                : 371-381
                Article
                10.1017/S0952836903004758
                56b7af33-bf48-43ce-9bab-ed7b8dcef2fd
                © 2004

                http://doi.wiley.com/10.1002/tdm_license_1.1

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