Abstract：
:Fibrin is a major component of atherosclerotic plaques, and there may also be situations in which intravascular fibrin is formed in contact with the endothelium. The studies to be presented describe the distribution of fibrinogen/fibrin I, fibrin II, and fragments D and D-dimer in normal vessels and atherosclerotic plaques of increasing severity and also describe some functional effects of fibrin on normal endothelium. Immunohistochemical studies using three specific monoclonal antibodies with the avidin-biotin complex immunoperoxidase technique demonstrated that little fibrinogen/fibrin I or fibrin II and no D/D-dimer were detected in normal aortas. In early lesions and in fibrous plaques, fibrinogen/fibrin I and fibrin II were distributed in long threads and around vessel wall cells. D/D-dimer was not seen in early lesions. In advanced plaques all three molecular forms were detected in areas of loose connective tissue, in thrombi, and around cholesterol crystals. Thus increased fibrin formation and degradation may be associated with progression of atherosclerotic disease. Additionally, the presence of fibrin II around vessel wall cells suggests that these cells may be involved in the fbgn to fibrin transition within the vessel wall. The second aspect of the work to be presented concerns effects of fibrin on vascular endothelium. Fibrin formed on the surface of cultured human umbilical vein endothelial cells stimulated production of prostacyclin and tissue plasminogen activator by the cells in a time- and dose-dependent manner. Stimulation of prostacyclin was completely inhibited by indomethacin and partially inhibited by actinomycin D, cycloheximide, and trifluoperazine, while stimulation of t-PA synthesis was completely inhibited by actinomycin D and cycloheximide and partially inhibited by cytochalasin D, vinblastine, and trifluoperazine.(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
Adv Exp Med Bioljournal_title
Advances in experimental medicine and biologyauthors
Kaplan KL,Bini A,Fenoglio J Jr,Kudryk Bdoi
10.1007/978-1-4615-3806-6_33subject
Has Abstractpub_date
1990-01-01 00:00:00pages
313-8eissn
0065-2598issn
2214-8019journal_volume
281pub_type
杂志文章,评审abstract：:In this paper we report the effect of sulfatides on rate constants of Factor XII activation by kallikrein and its isolated light chain. In free solution kallikrein and the light chain were equally effective in activating Factor XII and both enzymes had their pH optimum at pH 7.0 (k1 = 1.6 X 10(3) M-1 s-1). Sulfatides ...
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