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A receptor for cathepsin G

₁-antichymotrypsin complexes on mouse spinal cord astrocytes

Neurobiology Research Laboratory (Drs. Chen and Festoff, and K.-J. Conn), Veterans Affairs Medical Center, Kansas City, MO; and the Departments of Physiology (Dr. Chen) and Neurology (Dr. Festoff), University of Kansas Medical Center, Kansas City, KS.

To determine whether there is a specific receptor for serpin:protease complexes on the astrocyte cell surface, we analyzed the cell-binding characteristics of an ¹²⁵I-cathepsin G:₁antichymotrypsin complex. Complex formation is maximal at a 1:1 molar ratio of cathepsin G to ₁-antichymotrypsin (₁-ACT) as revealed by sodium do-decyl sulfate-gel electrophoresis and autoradiography. Complex binding to mouse spinal cord astrocytes was inhibited by the presence of excess unlabeled complex, but not by the native protease, cathepsin G, or by the serpin, ₁ACT. Scatchard analysis of the binding curve showed the K_d to be 8 x 10^–8 M. We estimated receptor numbers on astrocytes to be about 2.2 x 10⁶ sites per cell. An -ACT-derived pentapeptide, Phe-Leu-Met-Ile-Ile (FLMII), homologous to a well-conserved segment in the serpin superfamily, did not inhibit the binding of complexes to cells. These data indicate that a specific receptor for ₁-ACT:cathepsin G exists on the CNS glial cell surface. Study of this receptor in astrocytes should facilitate understanding of the serpin:protease balance in the brain.

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

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

Received August 12,1992. Accepted for publication in final form October 27, 1992.

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