a1-ORD Protein

Furin is a member of the proprotein convertase (PC)2 family of calcium-dependent serine proteases that have structural homology to subtilisin/kexin-type proteases and are characterized by their recognition of a distinctive P4 Arg-X-Arg/Lys-P1 Arg consensus cleavage site. PCs perform the intracellular and pericellular processing of a large number of peptide and protein precursors transiting the constitutive […]

Contributors

Inventor Institute
Gonzalo Izaguirre University of Illinois Chicago
Cat. #: 156500
Tool sub type: Inhibitor
Research Fields: Cell biology;Cancer;Cell signaling and signal transduction;Drug development;Microbiology
Alternate name: PC, PCSK
Product description: Furin is a member of the proprotein convertase (PC)2 family of calcium-dependent serine proteases that have structural homology to subtilisin/kexin-type proteases and are characterized by their recognition of a distinctive P4 Arg-X-Arg/Lys-P1 Arg consensus cleavage site. PCs perform the intracellular and pericellular processing of a large number of peptide and protein precursors transiting the constitutive and regulated protein secretion pathways, including prohormones, growth factors, and their receptors, matrix metalloproteases and integrins. PCs are thus pivotal in the control of cell signaling, proliferation, motility, and adhesion. PC dysfunction is associated with a broad spectrum of diseases, including cancer, autoimmunity, and Alzheimer disease. In addition, a number of significant human infectious organisms take advantage of host PC activity to promote their growth. PCs have been considered promising therapeutic drug targets, and the development of specific inhibitors is being intensely pursued.
Additional notes: Furin specific inhibitor (a1-ORD) is invented by creating a chimeric protein containing a1-PDX and Serpin B8 P6-P5 segment. a1-ORD shows 140-400 fold higher reactivity with Furin than with non-furin PCs.
Function: Inhibitor
References:

Izaguirre et al. 2019. Biochemistry. 58(12):1679-1688. PMID: 30848586.

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