The glioma cell-derived neurite promoting activity protein is functionally and immunologically related to human protease nexin-I
✍ Scribed by Daniel J. Knauer; Robert A. Orlando; Dorrie Rosenblatt
- Book ID
- 102884001
- Publisher
- John Wiley and Sons
- Year
- 1987
- Tongue
- English
- Weight
- 713 KB
- Volume
- 132
- Category
- Article
- ISSN
- 0021-9541
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✦ Synopsis
Protease nexin-l (PN-I, M, -43,000) is representative of a newly described class of cell-secreted protease inhibitors. PN-I has been purified to apparent homogeneity, partially sequenced, and monospecific antibodies have been raised against it. PN-I is a potent inhibitor of urokinase, thombin, plasmin, and trypsin. In addition, cells have specific receptors that mediate the uptake of covalently linked complexes formed between PN-I and its protease substrates. In the present studies, we have investigated the relationship between human PN-I and a protease inhibitor derived from C6 glioma cells in culture that has neurite-promoting activity. On t h e basis of co-purification on heparin-Sepharose, identical molecular weight, antibody cross-reactivity, and receptor cross-reactivity, we conclude that PN-I and the glioma-cell-derived inhibitor are equivalent molecules.