Abstract
Protease nexin I (PNI) is a potent anti–thrombin and anti–urokinase secreted by fibroblasts, and certain other extravascular cells. We describe the isolation, sequence, and expression of PNI cDNA cloned from a human foreskin fibroblast cDNA library. Two forms of PNI cDNA (designated α and β) have been identified. These differ only by the insertion of three nucleotides into the coding sequence, and apparently arise by utilization of an alternative splice acceptor site in the PNI gene. In the resulting proteins, αPNI contains an arg residue at position 310 where βPNI contains thr–gly residues. Both forms have been expressed in mammalian cells and inhibit thrombin and urokinase. The amino acid sequence of βPNI is identical to that of a recently described glial–derived neurite promoting factor.
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McGrogan, M., Kennedy, J., Ping Li, M. et al. Molecular Cloning and Expression of Two Forms of Human Protease Nexin I. Nat Biotechnol 6, 172–177 (1988). https://doi.org/10.1038/nbt0288-172
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DOI: https://doi.org/10.1038/nbt0288-172