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The Spn4 gene from Drosophila melanogaster is a multipurpose defence tool directed against proteases from three different peptidase families
- Source :
- The Biochemical journal. 401(1)
- Publication Year :
- 2006
-
Abstract
- By alternative use of four RSL (reactive site loop) coding exon cassettes, the serpin (serine protease inhibitor) gene Spn4 from Drosophila melanogaster was proposed to enable the synthesis of multiple protease inhibitor isoforms, one of which has been shown to be a potent inhibitor of human furin. Here, we have investigated the inhibitory spectrum of all Spn4 RSL variants. The analyses indicate that the Spn4 gene encodes inhibitors that may inhibit serine proteases of the subtilase family (S8), the chymotrypsin family (S1), and the papain-like cysteine protease family (C1), most of them at high rates. Thus a cohort of different protease inhibitors is generated simply by grafting enzyme-adapted RSL sequences on to a single serpin scaffold, even though the target proteases contain different types and/or a varying order of catalytic residues and are descendents of different phylogenetic lineages. Since all of the Spn4 RSL isoforms are produced as intracellular residents and additionally as variants destined for export or associated with the secretory pathway, the Spn4 gene represents a versatile defence tool kit that may provide multiple antiproteolytic functions.
- Subjects :
- Proteases
Neutrophils
medicine.medical_treatment
cysteine protease inhibitor
Molecular Sequence Data
serine protease inhibitor
Serpin
Biochemistry
Subtilase
medicine
Animals
Drosophila Proteins
Humans
Protease Inhibitors
Amino Acid Sequence
Molecular Biology
Conserved Sequence
Serpins
Serine protease
Genetics
Protease
biology
Pancreatic Elastase
Sequence Homology, Amino Acid
serpin
Cell Biology
Cysteine protease
Protease inhibitor (biology)
Drosophila melanogaster
endoplasmic reticulum (ER) retention
biology.protein
signal
furin
Sequence Alignment
MASP1
medicine.drug
Peptide Hydrolases
Research Article
Subjects
Details
- ISSN :
- 14708728
- Volume :
- 401
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- The Biochemical journal
- Accession number :
- edsair.doi.dedup.....a57fc8d39543d823e92f3ee17e5f2cfb