Disease relevance of FURIN

• Activation of an influenza virus A/turkey/Oregon/71 HA insertion variant by the subtilisin-like endoprotease furin [1].

High impact information on FURIN

• Ubiquitous expression of furin and other proprotein convertases in the chick embryo indicated that proteolytic activation of HA was not responsible for restriction of infection to the endothelium [2].
• Deletion of the insert revealed that the amino acid sequence -1 to -4 predisposes the protein for furin recognition [1].
• Site-directed mutagenesis of the cleavage site indicated that the arginine in position -4 is critical for HA activation by furin [1].
• The open reading frame (ORF) of this cDNA encodes a 288-amino acid protein containing a predicted transmembrane domain and a putative furin protease cleavage site like chicken BAFF (cBAFF), human BAFF (hBAFF) and mouse BAFF (mBAFF) [3].
• Two polyclonal antisera directed against the predicted catalytic domain of furin showed the highest level of immunoreactivity in a microsomal fraction that had minimal proalbumin converting activity [4].

Anatomical context of FURIN

• Rat and chicken liver microsomal membranes were used to investigate the relationship between proalbumin processing activity and the predicted proteinase furin [4].

References