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Protease nexin I, thrombin- and urokinase-inhibiting serpin, concentrated in normal human cerebrospinal fluid

Neurobiology Research Laboratory (151), Veterans Affairs Medical Center, Kansas City, MO; and the Department of Neurology, University of Kansas Medical Center, Kansas City, KS.

Protease nexin I (PNI), a 43,000- to 50,000-dalton glycoprotein, is a potent thrombin and urokinase inhibitor produced by many mammalian cells, including human glia, in tissue culture. PNI is a member of the growing superfamily of serine protease inhibitors now known as serpins, but, unlike many others of this family, it has not yet been detected in normal human plasma. Of interest to neurobiology and neurologic disease, PNI is identical to a glia-derived neurite-promoting factor, glia-derived nexin (GDN). Antibody to PNI stains the periphery of senile amyloid plaques in brain tissue from patients with Alzheimer's disease (AD), along with another serpin, ₁-antichymotrypsin (₁-ACT). A soluble form of the ß-amyloid precursor protein (ßAPP), containing a Kunitz-type trypsin inhibitor domain, the ßAPP₇₅₁ form, is identical to protease nexin II (PNII), a 100,000-dalton serine protease inhibitor present in a number of tissues besides the brain. PNII/ßAPP is also found in normal and AD CSF. We found a 47,000-dalton PNI, a thrombin- and urokinase-inhibiting serpin, in normal human CSF by Western blotting using a monospecific antibody. We also demonstrated biologically active PNI capable of forming complexes with serine proteases ¹²⁵I-urokinase or ^l25I-thrombin.

Address correspondence and reprint requests to Dr. Barry W. Festoff, Neurobiology Research (151), DVA Medical Center, 4801 Linwood Boulevard. Kansas City, MO 64128

Supported by the American Health Assistance Foundation, the Alzheimer's Disease and Related Disorders Association, the Marion Merrell Dow Foundation, and by the Medical Research Service of the Department of Veterans Affairs.

Received October 25, 1991. Accepted for publication in final form December 27, 1991.

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