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Plasminogen activator inhibitor 1, the primary regulator of fibrinolysis, in normal human cerebrospinal fluid
Author(s) -
Rao Jasti S.,
Chen M.,
Festoff Barry W.
Publication year - 1993
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490340311
Subject(s) - cerebrospinal fluid , serpin , polyclonal antibodies , serine protease , plasminogen activator , microbiology and biotechnology , plasminogen activator inhibitor 1 , antigen , fibrinolysis , urokinase , chemistry , blot , protease inhibitor (pharmacology) , biology , protease , immunology , biochemistry , endocrinology , medicine , enzyme , virus , gene , genetics , neuroscience , antiretroviral therapy , viral load
The occurrence of type‐1 plasminogen activator inhibitor (PAI‐1) in human cerebrospinal fluid (CSF) has not previously been reported. As a member of the serpin superfamily of serine protease inhibitors and an acute phase response component, PAI‐1 has powerful potential roles in nervous system homeostasis. We have detected this serpin antigen using a polyclonal anti‐PAI‐1 antibody in normal human CSF. In Western blotting, PAI‐1 in several CSF samples appears as a two‐band antigen of Mr = 54 and 35 kDa, presumably the intact and proteolytic fragment, respectively. In vitro complex formation studies confirm that the 54 kDa form of PAI‐1 interacts with 125 I‐urokinase after activation with SDS, but the 35 kDa form does not. Quantification of total PAI‐1 antigen in 18 normal human CSF samples by ELISA reveals a mean value of 1.0 ± 0.07 (SEM) μg/dL, indicating that a relatively low concentration of the inhibitor occurs in normal human CSF. This information should now allow comparison of PAI‐1 levels and activity in various neurologic disorders. © 1993 Wiley‐Liss, Inc.