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Role of polyamines in the stimulation of synthesis and secretion of plasminogen activator from bovine aortic endothelial cells

✍ Scribed by Be-Sheng Kuo; Gil Korner; Maciej Dryjski; Thorir D. Bjornsson


Publisher
John Wiley and Sons
Year
1988
Tongue
English
Weight
856 KB
Volume
137
Category
Article
ISSN
0021-9541

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✦ Synopsis


The effects of the polyamines putrescine (PUT), sperrnidine (SPD), and sperrnine (SPM) on the secretion of plasminogen activator (PA) and plasminogen activator inhibitor (PAl) were evaluated using cultured bovine aortic endothelial cells. All three polyarnines enhanced PA secretion in a time-and dosedependent manner, with a potency rank order of SPM > SPD > PUT. The PA stimulation required both RNA and protein synthesis, as evidenced by inhibition of polyamine-induced PA secretion by actinornycin D and cycloheximide. The inhibitors of polyamine biosynthesis methylglyoxal bis-(guanylhydrazone) (MGBG) and dl-(difluoromethyl) ornithine (DFMO) alone did not affect basal or polyamine-induced PA secretion, with the exception that MGBG reduced the effect of PUT. Polyamine-treated cells enhanced secretions of both tissue-type and urokinase-type PA. The results of the present study suggest that polyamines may play a role in the regulation of PA synthesis and secretion and that this function can be modified under pathophysiological conditions affecting cellular and tissue levels of polyamines.


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