Abstract
In the mouse submaxillary gland beta nerve growth factor (beta-NGF) forms a complex with two members of the kallikrein family of serine proteases, termed the alpha- and gamma-subunits of NGF. We demonstrate that the beta-NGF precursor produced in mammalian cells via a recombinant vaccinia virus can be cleaved by stoichiometric quantities of the gamma-subunit to produce beta-NGF. Trypsin in catalytic quantities also produces native beta-NGF. Proper cleavage depends critically on the conformation of the precursor. beta-NGF has at least 10-fold more biological activity than its precursor.
Highlights
From the $Departments of Biochemistryand Biophysics, and $Department of Neurology, Hormone Research Institute, University of California, Sun Francisco, CA 94143
The NGF precursor in mammalian cells using a vaccinia virus expression system.' We find that boththey-subunitand trypsin can cleave correctly the NGF precursor synthesized in vivo but not a precursor made by an i n vitro translation system
The NGF Precursor Produced by in Vitro Translation Is Degraded by the y-Subunit-To study cleavage of the NGF precursor in vitro, we first produced the precursor by translating SP6-derived NGF RNA in a cell-free wheat germ extract
Summary
0 1988by The American Society for Biochemistry and MolecularBiology, Inc. Vol 263,No., Issue of May 15, pp. 6810-6815, 1988 Printed in U.S.A. Factor (B-NGF) forms a complex with two members of In contrast, the longer precursor, which predominates in the the kallikrein family of serine proteases, termed the and y-subunits of NGF. 8-NGF has at least 10-fold more biological activity than its precursor. The non-NGF moiety of the precursor contains several sets of basic residues that may represent cleavage sites andcould generate other peptides from the NH, terminus of the NGF precursor. Cleavage of the precursor activatesthe biological function of NGF. In the mouse submaxillary gland, P-NGF forms a 7 S complex with two other proteins, both of which belong to the kallikrein family of serine proteases [4, 5]. The y-subunit of 7 S NGF exhibits proteolytic activity on artificial peptide substrates
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