Molecular cloning, expression, and partial characterization of a second human tissue-factor-pathway inhibitor

¹ZymoGenetics, Inc., Seattle, WA 98105.

Proceedings of the National Academy of Sciences of the United States of America

|April 12, 1994

Summary

A newly identified molecule, tissue-factor-pathway inhibitor-2 (TFPI-2), shares structural similarities with TFPI and inhibits trypsin and factor VIIa-tissue factor activity, with enhanced efficacy in the presence of heparin.

Area of Science:

Biochemistry
Molecular Biology
Hematology

Background:

Tissue-factor-pathway inhibitor (TFPI) regulates blood coagulation's extrinsic pathway.
TFPI inhibits factor Xa and factor VIIa-tissue factor activity.

Purpose of the Study:

To describe the molecular cloning and expression of a novel molecule, TFPI-2.
To characterize the structure and function of TFPI-2.

Main Methods:

Molecular cloning and expression of TFPI-2 cDNA.
Purification of recombinant TFPI-2 using chromatography techniques.
Analysis of TFPI-2 activity using amidolytic assays and SDS-PAGE.

Main Results:

TFPI-2 cDNA encodes a protein with structural homology to TFPI, featuring Kunitz-type domains.
TFPI-2 is transcribed in endothelial cells, liver, and placenta.
Purified recombinant TFPI-2 strongly inhibits trypsin and factor VIIa-tissue factor activity, enhanced by heparin.
TFPI-2 weakly inhibits factor Xa but not thrombin.

Conclusions:

TFPI-2 is a novel Kunitz-type serine protease inhibitor with distinct biochemical properties.
TFPI-2 represents a new regulator in the coagulation cascade or related protease systems.

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Molecular cloning, expression, and partial characterization of a second human tissue-factor-pathway inhibitor

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Background:

Purpose of the Study:

Main Methods:

Main Results:

Conclusions:

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