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Nature

Title:		Furin-dependent intracellular activation of the human stromelysin-3 zymogen
Author(s):		Pei D; Weiss SJ;
Address:		"Department of Internal Medicine, University of Michigan Comprehensive Cancer Center, Ann Arbor 48109-0640, USA"
Journal Title:		Nature
Year:		1995
Volume:		375
Issue:		6528
Page Number:		244 - 247
DOI:		10.1038/375244a0
ISSN/ISBN:		0028-0836 (Print) 0028-0836 (Linking)
Abstract:		"Human stromelysin-3, a new member of the matrix metalloproteinase family, is expressed in tissues undergoing the active remodelling associated with embryonic development, wound healing and tumour invasion. But like all other members of the matrix metalloproteinase gene family, stromelysin-3 is synthesized as an inactive precursor that must be processed to its mature form in order to express enzymic activity. Here we identify stromelysin-3 as the first matrix metalloproteinase to be discovered that can be processed directly to its enzymically active form by an obligate intracellular proteolytic event that occurs within the constitutive secretory pathway. Intracellular activation is regulated by an unusual 10-amino-acid insert sandwiched between the pro- and catalytic-domains of stromelysin-3, which is encrypted with an Arg-X-Arg-X-Lys-Arg recognition motif for the Golgi-associated proteinase, furin, a mammalian homologue of the yeast Kex2 pheromone convertase. A furin-stromelysin-3 processing axis not only differentiates the regulation of this enzyme from all previously characterized matrix metalloproteinases, but also identifies pro-protein convertases as potential targets for therapeutic intervention in matrix-destructive disease states"
Keywords:		"Amino Acid Sequence Base Sequence Cell Line DNA Primers Enzyme Activation Enzyme Precursors/genetics/*metabolism Furin Humans Matrix Metalloproteinase 11 Metalloendopeptidases/genetics/*metabolism Molecular Sequence Data Mutagenesis Protein Processing, Po;"
Notes:		"MedlinePei, D Weiss, S J eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. England 1995/05/18 Nature. 1995 May 18; 375(6528):244-7. doi: 10.1038/375244a0"