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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.
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1991 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 266, no 23, 15240-3 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
1991. Vol. 266, no 23, 15240-3 p.
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Medical and Health Sciences
URN: urn:nbn:se:umu:diva-59900PubMedID: 1714455OAI: diva2:557001
Available from: 2012-09-26 Created: 2012-09-26 Last updated: 2012-09-26

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Ny, Tor
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Department of Medical Biochemistry and Biophysics
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