PMID: 9531478Jun 11, 1998Paper

Functional effects of single amino acid substitutions in the region of Phe113 to Asp138 in the plasminogen activator inhibitor 1 molecule

The Biochemical Journal
G C Sui, Björn Wiman

Abstract

Thirteen amino acid substitutions have been introduced within the stretch Phe113 to Asp138 in the plasminogen activator inhibitor 1 (PAI-1) molecule by site-directed mutagenesis. The different proteins and wild-type (wt) PAI-1 have been overexpressed in Escherichia coli and purified by chromatography on heparin-Sepharose and on anhydrotrypsin-agarose. The PAI-1 variants have been characterized by their reactivity with tissue plasminogen activator (tPA), interactions with vitronectin or heparin, and stability. Most PAI-1 variants, except for Asp125-->Lys, Phe126-->Ser and Arg133-->Asp, displayed a high spontaneous inhibitory activity towards tPA, which did not change greatly on reactivation with 4 M guanidinium chloride, followed by dialysis at pH 5.5. The variants Asp125-->Lys and Arg133-->Asp became much more active after reactivation and they were also more rapidly transformed to inactive forms (t12 22-31 min) at physiological pH and temperature than the other variants. However, in the presence of vitronectin they were both almost equally stable (t12 2.3 h) as wtPAI-1 (t12 3.0 h). The mutant Glu130-->Lys showed an increased stability, both in the absence and in the presence of vitronectin compared with wtPAI-1. Nevertheless a...Continue Reading

Citations

Aug 10, 2000·Protein Science : a Publication of the Protein Society·P R ElliottD A Lomas
Jan 11, 2002·European Journal of Biochemistry·Nuria Arroyo De PradaViktor Magdolen
Jul 8, 2000·FEBS Letters·H MångsB Wiman
Dec 15, 2000·The Journal of Biological Chemistry·A ZhouD A Lomas
Nov 11, 1999·Biochimica Et Biophysica Acta·G C SuiB Wiman
Dec 22, 1999·Biochimica Et Biophysica Acta·N VleugelsP J Declerck

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