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  • Electronic Resource  (3)
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  • Electronic Resource  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Role of ADP-ribosylation in wound repair. The contributions of Thomas K. Hunt, MD (2003)
    Malden, USA : Blackwell Science Inc
    Wound repair and regeneration 11 (2003), S. 0 
    Details
    ISSN: 1524-475X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Nearly 36 years ago Thomas K. Hunt, with Patrick Twomey, was the first to report that the level of lactate significantly increases in healing wounds. This observation convinced him that lactate, besides being the by-product of glycolysis, must have a regulatory role in the healing process. He set out to investigate this observation and found it to be so. This article is written in recognition of his foresight. It summarizes the salient findings emanating from this fundamental observation and describes the biochemical principles by which most of the lactate action may be explained. Down-regulation of the ubiquitous protein modification reaction called ADP-ribosylation turned out to be a basic signal behind the role of lactate in wound healing. (WOUND REP REG 2003;11:439–444)
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1524-475X.2003.11608.x
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  • 2
    Electronic Resource
    Electronic Resource
    Biochemical alterations in inflammatory periodontal diseases I. Poly (ADP-ribose) synthetase activity in gingiva and gingival fibroblasts from humans with periodontitis (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 31 (1996), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Periodontal diseases are characterized in part by generation of oxygen free radicals, which can cause breaks in cellular DNA strands. Repair of damaged DNA is dependent upon the synthesis of poly(ADP-ribose)(PADPR) catalyzed by PADPR synthetase, an enzyme known to be activated by the broken ends of DNA strands. We measured the activities of PADPR synthetase and of PADPR glycohydrolase. which degrades PADPRS, in gingival biopsy specimens from 16 sites with adult periodontitis and 12 clinically healthy control sites. The results indicated that sites with periodontitis displayed markedly reduced PADPR synthetase activity compared with healthy control sites, whereas PADPR glycohydrolase activity was not changed. The mean specific activity of PADPR synthetase for the diseased specimens was one-sixth of that of the healthy specimens (p 〈 0.001). The PADPR synthetase activity was negatively correlated with the Gingival Index (rs=-0.60), pocket depth (rs=-0.70) and bleeding upon probing (rs=-0.72). Cultured fibroblasts derived from clinically characterized healthy and diseased gingival sites reflected similar patterns of enzyme activity. The mean specific activity of PADPR synthetase for the diseased-site cultures (n=9) was 56±7% (p 〈 0.001) of the cultures from healthy control sites (n=6). These results suggest that a reduced level of PADPR synthetase activity is associated with increased inflammation and periodontal destruction, and that the ability to synthesize PADPR is compromised in adult periodontitis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1996.tb01408.x
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  • 3
    Electronic Resource
    Electronic Resource
    Oxygen enhances fusion of cultured chick embryo myoblasts (1981)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 106 (1981), S. 209-213 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Fusion of mononucleate myoblasts to form multinucleated myotubes increases when skeletal muscle cells are grown in progressively higher oxygen concentrations (5%, 20%, and 40% oxygen). At four days of growth fusion of myoblasts (as expressed by the percent of all muscle nuclei that are located in myotubes) is 57 ± 2% in 5% oxygen, 68 ± 1% in 20% oxygen, and 78 ± 2% in 40% oxygen (P〈0.001). However, at a concentration of 40%, oxygen depresses the rate of cell division and thereby affects the number of myoblasts available for fusion. Thus, oxygen concentration significantly modifies growth of skeletal muscle in vitro. Its net effect on myotube formation results from the interaction of its separate effects to enhance cell fusion and to depress cell proliferation.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041060206
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    Paper (German National Licenses)
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