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J. Biol. Chem., Vol. 266, Issue 23, 15240-15243, Aug, 1991
G von Heijne, P Liljestrom, P Mikus, H Andersson and T Ny
Plasminogen-activator inhibitor type 2 (PAI-2) is a specific inhibitor of
plasminogen activators that belongs to the serine protease inhibitor
superfamily (SERPINS). PAI-2 exists in two molecular forms: an
intracellular, non-glycosylated form and a secreted, glycosylated form.
Like ovalbumin, PAI-2 contains an uncleaved internal secretion signal. By
deletion analysis, we have mapped the secretion signal to two mildly
hydrophobic regions near the NH2 terminus. We also show that both of these
regions become more efficient translocation signals when their
hydrophobicities are increased. The PAI-2 secretion signal provides a
unique example of a signal that, by virtue of its poor efficiency, allows
the synthesis of both an extracellular and an intracellular form of the
protein.
The efficiency of the uncleaved secretion signal in the plasminogen activator inhibitor type 2 protein can be enhanced by point mutations that increase its hydrophobicity
Department of Molecular Biology, Karolinska Institute, Huddinge, Sweden.
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