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  • *Apoptosis  (1)
  • Aspredo  (1)
  • Biological Science Disciplines/*methods  (1)
  • 1995-1999  (3)
  • 1955-1959
  • 1
    Electronic Resource
    Electronic Resource
    Comparative morphology of cotylephores in Platystacus and Solenostomus: modifications of the integument for egg attachment in skin-brooding fishes (1997)
    Springer
    Environmental biology of fishes 50 (1997), S. 13-25 
    Details
    ISSN: 1573-5133
    Keywords: cotylephore ; maternal-embryonic exchange ; ghost pipefish ; reproduction ; development ; Aspredo ; Aspredinichthys, Aspredini
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract External skin brooding evolved independently in several groups of fishes. Cotylephores, sites for the attachment of developing embryos, occur within the fused pelvic fins of the ghost pipefishes, Solenostomus, on the ventral surface of the South American catfish, Platystacus, and on other aspredinid cattfishes of the tribe Aspredini. Cotylephores are transient outgrowths of tissue that occur only on brooding fish. They consist of a pedicle that extends from the abdomen or fin and terminates in an apical calyx. The calyx supports and adheres to the egg envelope that encloses the developing embryo. The pedicle of the catfish cotylephore is a single, large structure (1615 ± 23.25 µm), while those of ghost pipefishes are small and branched (687 ± 3.89 µm; number of branches: 26 ± 0.63). In both instances, a simple cuboidal epithelium, whose cells bear microplicae, encloses an extensive connective tissue core that contains large blood vessels that ramify into a capillary plexus in the calyx. Cotylephores of Platystacus are more heavily vascularized than those of Solenostomus and contain 34.77% more blood vessel surface area at the calyx, to which the egg envelope adheres. In addition to their role in attachment, cotylephores may function in embryonic maintenance through the exchange of gas across the egg envelope, mediated by female circulatory vessels within the cotylephore calyx. Comparisons of morphology and development suggest that cotylephores are the result of convergent evolution of a reproductive adaptation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007309526982
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    Paper (German National Licenses)
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  • 2
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    Imaging molecular chemistry with infrared microscopy (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-09-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wetzel, D L -- LeVine, S M -- New York, N.Y. -- Science. 1999 Aug 20;285(5431):1224-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Microbeam Molecular Spectroscopy Lab, Kansas State University, Manhatten, KS 66506, USA. dwetzel@ksu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10484732" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biochemistry/*methods ; Biological Science Disciplines/*methods ; Forensic Medicine ; Humans ; Specimen Handling ; *Spectroscopy, Fourier Transform Infrared/instrumentation/methods ; Spectrum Analysis, Raman
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-21
    Description: In a cell-free apoptosis system, mitochondria spontaneously released cytochrome c, which activated DEVD-specific caspases, leading to fodrin cleavage and apoptotic nuclear morphology. Bcl-2 acted in situ on mitochondria to prevent the release of cytochrome c and thus caspase activation. During apoptosis in intact cells, cytochrome c translocation was similarly blocked by Bcl-2 but not by a caspase inhibitor, zVAD-fmk. In vitro, exogenous cytochrome c bypassed the inhibitory effect of Bcl-2. Cytochrome c release was unaccompanied by changes in mitochondrial membrane potential. Thus, Bcl-2 acts to inhibit cytochrome c translocation, thereby blocking caspase activation and the apoptotic process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kluck, R M -- Bossy-Wetzel, E -- Green, D R -- Newmeyer, D D -- CA69381/CA/NCI NIH HHS/ -- GM50284/GM/NIGMS NIH HHS/ -- GM52735/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Feb 21;275(5303):1132-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular Immunology, La Jolla Institute for Allergy and Immunology, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9027315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Chloromethyl Ketones/pharmacology ; Animals ; *Apoptosis ; Carrier Proteins/metabolism ; Cell Extracts ; Cell-Free System ; Cysteine Endopeptidases/metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Cytochrome c Group/*metabolism ; Cytosol/metabolism ; Membrane Potentials ; Microfilament Proteins/metabolism ; Mitochondria/*metabolism ; Ovum ; Proto-Oncogene Proteins c-bcl-2/*metabolism/pharmacology ; Recombinant Proteins ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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