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Furin is a subtilisin-like proprotein processing enzyme in higher eukaryotes
W J van de Ven1, J Voorberg, R Fontijn
1Molecular Oncology Section, University of Leuven, Belgium.
Molecular Biology Reports
|November 1, 1990
Summary
The human fur gene product, furin, is a novel enzyme that cleaves proteins at paired basic residues. This discovery identifies furin as a key proprotein processing enzyme in higher eukaryotes.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- The human fur gene encodes the furin protein, featuring a transmembrane domain and similarity to subtilisin serine proteases.
- Furin's N-terminal domain suggests a role in proteolytic activity.
Purpose of the Study:
- To characterize the furin protein and its catalytic domain.
- To predict and validate furin's substrate specificity.
Main Methods:
- Three-dimensional modeling of the furin catalytic domain.
- Transfection and cotransfection experiments in COS-1 cells.
- Western blot analysis to detect furin polypeptides.
- Functional analysis using wild-type and mutant von Willebrand factor (pro-vWF) precursors.
Main Results:
- Furin protein synthesis confirmed, producing 100 kDa and 90 kDa polypeptides.
- Furin enhances proteolytic processing of wild-type pro-vWF.
- Furin does not process a mutant pro-vWF (provWFgly763) with a modified cleavage site.
Conclusions:
- Furin exhibits endoproteolytic cleavage selectivity at paired basic residues.
- Furin is identified as a prototype subtilisin-like proprotein processing enzyme in higher eukaryotes.