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  • 1
    Online Resource
    Online Resource
    Molecular Basis for the Association of Group IIA Phospholipase A 2 and Decorin in Human Atherosclerotic Lesions
    Ovid Technologies (Wolters Kluwer Health) ; 2000
    In:  Circulation Research Vol. 86, No. 6 ( 2000-03-31), p. 707-714
    Details
    In: Circulation Research, Ovid Technologies (Wolters Kluwer Health), Vol. 86, No. 6 ( 2000-03-31), p. 707-714
    Abstract: Abstract —Group IIA secretory nonpancreatic phospholipase A 2 (snpPLA 2 ) is associated with collagen fibers in the extracellular matrix of human atherosclerotic plaques. Decorin, a small proteoglycan (PG) carrying chondroitin/dermatan sulfate glycosaminoglycans (GAGs), forms part of the collagen network in human arteries. To explore whether snpPLA 2 may be associated with collagen fibers via interaction with decorin, we performed (1) immunohistochemistry to compare the relative in vivo localization of snpPLA 2 and decorin in human atherosclerotic tissue and (2) in vitro experiments to study the interaction between snpPLA 2 and decorin. In atherosclerotic lesions, decorin was detected within the snpPLA 2 -positive part of the intima close to the media. Electrophoretic mobility shift assay showed that snpPLA 2 binds to decorin synthesized by human fibroblasts. Native and GAG-depleted decorin enhanced the association of snpPLA 2 to collagen types I and VI in a solid-phase binding assay. Furthermore, snpPLA 2 bound efficiently to a recombinant decorin core protein fragment B/E (Asp45-Lys359). This binding was competed with soluble decorin and inhibited at NaCl concentrations 〉 150 mmol/L. The decorin core protein fragment B/E competed better than dermatan sulfate for binding of snpPLA 2 to decorin-coated microtiter wells. The enzymatic activity of snpPLA 2 increased 2- to 3-fold in the presence of decorin or GAG-depleted decorin. The results show that snpPLA 2 binds preferentially to the decorin protein core rather than to the GAG chain and that this interaction enhances snpPLA 2 activity. As a consequence, this active extracellular enzyme may contribute to the pathogenesis of atherosclerosis by modifying lipoproteins and releasing inflammatory lipid mediators at places of lipoprotein retention in the arterial wall.
    Type of Medium: Online Resource
    ISSN: 0009-7330 , 1524-4571
    URL: Article
    DOI: 10.1161/01.RES.86.6.707
    RVK:
    XA 10000
    Language: English
    Publisher: Ovid Technologies (Wolters Kluwer Health)
    Publication Date: 2000
    detail.hit.zdb_id: 1467838-X
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  • 2
    Online Resource
    Online Resource
    Molecular basis for the association of group IIA phospholipase A2 and decorin in atherosclerotic lesions
    Elsevier BV ; 2000
    In:  Atherosclerosis Vol. 151, No. 1 ( 2000-07), p. 87-88
    Details
    In: Atherosclerosis, Elsevier BV, Vol. 151, No. 1 ( 2000-07), p. 87-88
    Type of Medium: Online Resource
    ISSN: 0021-9150
    URL: Article
    DOI: 10.1016/S0021-9150(00)80397-4
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2000
    detail.hit.zdb_id: 1499887-7
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  • 3
    Online Resource
    Online Resource
    Selective Inhibitors of Cytosolic or Secretory Phospholipase A2 Block TNF-Induced Activation of Transcription Factor Nuclear Factor-κB and Expression of ICAM-1
    The American Association of Immunologists ; 1998
    In:  The Journal of Immunology Vol. 161, No. 7 ( 1998-10-01), p. 3421-3430
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 161, No. 7 ( 1998-10-01), p. 3421-3430
    Abstract: TNF signaling mechanisms involved in activation of transcription factor NF-κB were studied in the human keratinocyte cell line HaCaT. We show that TNF-induced activation of NF-κB was inhibited by the well-known selective inhibitors of cytosolic phospholipase A2 (cPLA2): the trifluoromethyl ketone analogue of arachidonic acid (AACOCF3) and methyl arachidonyl fluorophosphate. The trifluoromethyl ketone analogue of eicosapentaenoic acid (EPACOCF3) also suppressed TNF-induced NF-κB activation and inhibited in vitro cPLA2 enzyme activity with a similar potency as AACOCF3. The arachidonyl methyl ketone analogue (AACOCH3) and the eicosapentanoyl analogue (EPACHOHCF3), which both failed to inhibit cPLA2 enzyme activity in vitro, had no effect on TNF-induced NF-κB activation. TNF-induced NF-κB activation was also strongly reduced in cells stimulated in the presence of the secretory PLA2 (sPLA2) inhibitors 12-epi-scalaradial and LY311727. Addition of excess arachidonic acid suppressed the inhibitory effect of 12-epi-scalaradial and LY311727. Moreover, both methyl arachidonyl fluorophosphate and 12-epi-scalaradial blocked TNF-mediated enhancement of expression of ICAM-1. Activation of NF-κB by IL-1β was markedly less sensitive to both cPLA2 and sPLA2 inhibitors. The results indicate that both cPLA2 and sPLA2 may be involved in the TNF signal transduction pathway leading to nuclear translocation of NF-κB and to NF-κB-activated gene expression in HaCaT cells.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.161.7.3421
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1998
    detail.hit.zdb_id: 1475085-5
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