Title
Synthesis, storage and regulated secretion of tissue-type plasminogen activator by cultured rat heart endothelial cells
Author
Emeis, J.J.
van den Hoogen, C.M.
Diglio, C.A.
Gaubius Instituut TNO
Publication year
1998
Abstract
The synthesis, storage and regulated secretion (acute release) of tissue-type plasminogen activator (tPA) were studied in cultured rat heart endothelial (RHE) cells. In this study, special attention was paid to the correspondence between tPA metabolism in RHE cells in vitro and tPA metabolism in rats in vivo. RHE cells synthetized tPA, as shown by a spectrophotometric activity assay, by fibrin autography and by an ELISA for tPA antigen. The synthesis of tPA was strongly enhanced by phorbol myristate acetate, by all-trans-retinoic acid, by 8-bromoadenosine 3':5' cyclic- monophosphate (8-br-cAMP) and by compounds that enhance cAMP synthesis, such as cholera toxin and forskolin. Urokinase-type plasminogen activator and plasminogen activator inhibitor were not detected. tPA was constitutively secreted by RHE cells, but was also present in an intracellular pool of small dense granules, from which it could be acutely released by stimulating the cells with thrombin or the calcium ionophore A-23187. This release was maximal during the first minutes after stimulation. In all these aspects of tPA metabolism, RHE cells closely resembled rat endothelial cells in vivo. It is concluded that cultured RHE rat heart endothelial cells constitute a relevant in vitro model for studying endothelial tPA metabolism.
Subject
Health
8 bromo cyclic amp
calcimycin
cholera toxin
forskolin
phorbol 13 acetate 12 myristate
plasminogen activator inhibitor
retinoic acid
thrombin
tissue plasminogen activator
urokinase
animal cell
article
controlled study
heart
nonhuman
priority journal
protein secretion
protein synthesis
rat
vascular endothelium
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DOI
https://doi.org/10.1016/s0268-9499(98)80003-9
TNO identifier
234465
ISSN
1369-0191
Source
Fibrinolysis and Proteolysis, 12 (1), 9-16
Document type
article