PMID: 18712106Aug 21, 2008Paper

Furin and its biological role

Ukrainskiĭ biokhimicheskiĭ zhurnal
V K KibirevIu L Radavskiĭ

Abstract

The survey deals with structure, properties and biological role of furin, the calcium-dependent serine endoprotease, which is expressed in all tissues and cell lines examined. It is the best-characterized representative of the mammalian subtilisin-like family of proprotein convertases, which is capable to cleave precursors of a wide variety of proteins, including hormones, growth factors, serum proteins, proteases of the blood-clotting system, matrix metalloproteinases, receptors, viral envelope glycoproteins, and bacterial exotoxins, and so on. The enzyme plays the essential role in embryogenesis, homeostasis; it is also involved in tumor metastasis, activation and virulence of many bacterial and viral pathogens and in neurodegenerative processes associated with Alzheimer's disease. Furin is a very specific enzyme: it recognizes the cleavage-site sequence Arg-Xaa-Lys/Arg-Arg and catalyzes the hydrolysis of the precursors, containing a pair of basic amino acids Arg-Arg or Lys-Arg. The enzyme is a multidomain protein which is initially synthesized as 100 kDa glycosylated profurin consisting of 794 amino acid residues (for human furin) and including a N-terminal signal peptide, propeptide, catalytic domain, possessing approximate...Continue Reading

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