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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 24 (1985), S. 3926-3931 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 2135-2141 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0568
    Keywords: Key words Smooth muscle cells ; Arterial wall ; Endothelium ; Intima ; H-2Kb-tsA58 transgenic mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The presence of non-contractile smooth muscle cells within the arterial wall raises questions as to their origin and function. These cells abound within the aortae of murine and porcine neonates, but are also present within the intimal and medial layers of adult arteries. They are largely devoid of smooth muscle-associated proteins and manifest an epithelioid form. Their morphological resemblance to endothelial cells prompted us to explore this potential relationship and to investigate their angiogenic properties in three-dimensional collagen gels. Using well-characterized smooth muscle cell lines, displaying either the intima-like (epithelioid) or media-like (spindle-shaped) morphology, we were able to show that intima-like cells share several features in common with endothelial ones and can transform into a media-like phenotype, whereby they irreversibly lose their characteristic pattern of protein expression. Intima-like, but not media-like, vascular smooth muscle cells are capable of forming capillary tubes, and, in co-cultures, can induce media-like ones to participate in this process. Such capillaries consist of a randomly-organized, mixed population of endothelial cells with intima-like or media-like smooth muscle ones. The functional significance of this diversity in smooth muscle cell type is not well understood, but phenotypic plasticity could conceivably figure as an important adaptive response to changes in the local environment.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 22 (1992), S. 2-10 
    ISSN: 1059-910X
    Keywords: Hyaline layer ; Hyalin ; Echinonectin ; Morphogenesis ; Oogenesis ; Sea urchin embryo ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: The apical extracellular matrix of the sea urchin embryo, known as the hyaline layer (HL), is a multi-laminate organelle composed of at least 10 polypeptides. Although integrated into one ECM, HL proteins exhibit individual temporal and spatial dynamics throughout development. These molecules are stockpiled in the oocyte during vitellogenesis in at least four distinct vesicle populations. They are released onto the cell surface at fertilization in a specific order, and interact differentially with embryonic cells as development proceeds. Many experiments have suggested that the HL is vital for embryogenesis, but relatively little is known about the functions and interactions of its constituent molecules. The purpose of the present review has been to gather information on the basic characteristics of the known HL proteins together with data on their expression in the embryo, and where possible, their biological activities. Compiled, these observations may provide some insight into the workings of a uniquely embryonic organelle. © 1992 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 10 (1984), S. 267-281 
    ISSN: 0148-7280
    Keywords: sea urchin sperm ; catalase ; peroxidase ; phenylhydrazine ; 3-amino-1,2,4-triazole ; azide ; fertilization ; polyspermy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The release of hydrogen peroxide (H2O2) by the fertilized sea urchin egg has been shown to assist in the prevention of polyspermy [Coburn et al, 1981; Boldt et al, 1981]. Physiological data suggested that egg-derived H2O2 reacts with a phenylhydrazine-sensitive sperm peroxidase to inactivate sperm, while a 3-amino-1,2,4-triazole-sensitive catalase acts to protect sperm from H2O2 [Boldt et al, 1981]. Strongylocentrotus purpuratus sperm contain heat and pronase labile catalase and peroxidase activities. Differential extraction of sperm (hypotonic phosphate buffer for catalase and Triton X-100 at high ionic strength for peroxidase) results in complete separation of these enzyme activities. The catalase is highly sensitive to inhibition by azide and 3-amino-1,2,4-triazole, and less sensitive to inhibition by phenylhydrazine. The peroxidase is highly sensitive to inhibition by phenylhydrazine and relatively insensitive to 3-amino-1,2,4-triazole and azide. These results show that two distinct H2O2 reactive enzymes, catalase and peroxidase, are present in sea urchin sperm, and are consistent with our hypothesis concerning the biological functions of these enzymes in fertilization.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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