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Role of polyamines in the stimulation of synthesis and secretion of plasminogen activator from bovine aortic endothelial cells
Author(s) -
Kuo BeSheng,
Korner Gil,
Dryjski Maciej,
Bjornsson Thorir D.
Publication year - 1988
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041370124
Subject(s) - plasminogen activator , spermidine , polyamine , secretion , putrescine , cycloheximide , spermine , tissue plasminogen activator , stimulation , biochemistry , biology , ornithine decarboxylase , protein biosynthesis , chemistry , microbiology and biotechnology , endocrinology , enzyme
The effects of the polyamines putrescine (PUT), spermidine (SPD), and spermine (SPM) on the secretion of plasminogen activator (PA) and plasminogen activator inhibitor (PAI) were evaluated using cultured bovine aortic endothelial cells. All three polyamines enhanced PA secretion in a time‐ and dose‐dependent 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 actinomycin 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.