*nlm.life
			PubMed Journals: Biochem J

  Source:		PMID: 11237874


    		Biochem J. 2001 Mar 15;354(Pt 3):689-95.
     
			'Shed' furin: mapping of the cleavage determinants
			and identification of its C-terminus.

			Plaimauer B(1), Mohr G, Wernhart W, Himmelspach
			M, Dorner F, Schlokat U.

			Author Information
			(1) Biomedical Research Center, Hyland-Immuno
			Division, Baxter Healthcare, Uferstr. 15,
			2304 Orth/Donau, Austria.

			The human endoprotease furin is involved
			in the proteolytic maturation of the precursor
			molecules of a wide variety of bioactive
			proteins. Despite its localization in the
			membranes of the trans-Golgi system by means
			of a transmembrane domain, it has repeatedly
			been reported to form a C-terminally truncated,
			naturally secreted form referred to as 'shed'
			furin. In order to identify the cleavage
			site, internal deletion mutants of increasing
			size, N-terminal to Leu(708), and subsequently
			individual amino acid substitutions were
			introduced, and Arg(683) was identified
			as the prime determinant for shedding. MS
			analysis determined Ser(682) as the C-terminus
			of shed furin, suggesting that monobasic
			cleavage may occur N-terminal to Arg(683).
			Alteration of Arg(683) directs the shedding
			mechanism to alternative cleaving sites
			previously unused.

			PMCID: PMC1221701 PMID: 11237874 [Indexed
			for MEDLINE]

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