Translocation of plasminogen activator inhibitor-1 during serum stimulated growth of mouse embryo fibroblasts.
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Date
1990-12
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Abstract
Serum-stimulated mouse embryo fibroblasts specifically secrete two proteins of
molecular weights 48,000 and 26,000. The 48 kDa protein showed affinity to concanavalin
A and was precipitated by antibody to plasminogen activator inhibitor. Immunoflowcytometry
using anti plasminogen activator inhibitor-1 serum indicate the presence of the
48 kDa protein in quiescent cells; this protein was virtually absent in serum-stimulated
cells. The presence of the plasminogen activator inhibitor-1 related protein in quiescent
cells and its absence in serum-stimulated cells in combination with the observation on the
absence of this protein, in the medium of quiescent cells and its presence in the medium of
stimulated cells indicate that the 48 kDa protein was transferred from the cells into the
medium upon serum-stimulation. The serum-mediated transfer of plasminogen activator
inhibitor-1 from the cells into the medium was inhibited by actinomycin-D suggesting that
the transfer process required actinomycin-D sensitive events. Treatment of pre-labelled
quiescent cells with medium containing 20% fetal calf serum resulted in the gradual
transfer of the labelled 48 kDa protein to the extra cellular matrix. These studies indicate
that exposure of quiescent cells to fetal calf serum results in the transfer of plasminogen
activator inhibitor-1 from the cells to the growth medium via extracellular matrix. The
translocation of the protease inhibitor from the cells to the matrix and medium may enable
the cellular and possibly the membrane proteases to act on growth factors or their
receptors thereby initiating the mitogenic response.
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Keywords
Plasminogen activator inhibitor, deposition, fibroblasts
Citation
Srinivas S, Nagashunmugam T, Shanmugam G. Translocation of plasminogen activator inhibitor-1 during serum stimulated growth of mouse embryo fibroblasts. Journal of Biosciences. 1990 Dec; 15(4): 351-359.