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Related Experiment Video

Updated: Jun 23, 2026

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Published on: June 3, 2014

Structure-function analysis of factor VII activating protease (FSAP): sequence determinants for heparin binding and

Lars Muhl¹, Karin Hersemeyer, Klaus T Preissner

¹Institute for Biochemistry, Medical School, Justus-Liebig-University Giessen, Giessen, Germany.

|May 19, 2009

Summary

Factor VII activating protease (FSAP) activity is regulated by its structure, with active forms decreasing cell viability. Inactive FSAP variants are secreted effectively, highlighting structural importance in disease-associated protease function.

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Factor VII activating protease (FSAP) is implicated in cardiovascular diseases and liver fibrosis.
Understanding FSAP's proteolytic activity regulation is crucial for disease insights.

Purpose of the Study:

To characterize recombinant FSAP mutants and elucidate the regulation of its proteolytic activity.
To investigate the impact of FSAP variants on cell viability and secretion.

Main Methods:

Over-expression of recombinant FSAP mutants in HEK-293 cells.
Measurement of secreted FSAP protein concentration and enzymatic activity.
Assessment of cell viability following FSAP variant expression.

Main Results:

Secreted FSAP concentration inversely correlated with enzymatic activity.
Active FSAP over-expression reduced cell viability; inactive variants were secreted well.
The G534E variant showed reduced proteolytic activity, and DeltaEGF-3 mutant had impaired heparin binding/activation.

Conclusions:

FSAP activity regulation is dependent on its EGF-3 domain.
Over-expression of active FSAP variants induces cell death, suggesting a role in pathogenesis.