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LA Erickson, CM Hekman and DJ Loskutoff
Cultured bovine aortic endothelial cells and human serum contain
plasminogen activator inhibitors (PAIs) that are immunologically related.
In the present study, the electrophoretic mobilities, molecular weights
(mol wt), and activities of these PAIs were compared. When fractionated by
agarose zone electrophoresis, both PAIs migrated with beta mobility as
compared with the mobilities of human plasma/serum proteins.
Two-dimensional electrophoretic analysis, employing agarose zone
electrophoresis in the first dimension and sodium dodecyl
sulfate-polyacrylamide gel electrophoresis in the second dimension,
indicated that these beta-PAIs comigrated, both having a mol wt of
approximately 50,000. The activity of the PAI in endothelial cell-
conditioned medium is enhanced severalfold by treatment with either sodium
dodecyl sulfate or guanidine. In preliminary experiments, we were unable to
stimulate the PAI activity of undiluted serum by similar treatments.
However, the PAI activities in both diluted serum and gel- filtered or
electrophoretically fractionated serum were enhanced by treatment with
these denaturants. The gel filtration studies also revealed that serum
contains multiple forms of the beta-PAI. These forms may represent
polymeric PAI and/or complexes between the PAI and other serum components.
These findings indicate that the primary PAIs in bovine endothelial cells
and human serum are not only immunologically related but are also
biochemically similar.
This article has been cited by other articles:
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| Copyright © 1986 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
