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      Regulation of the α‐secretase ADAM10 by its prodomain and proprotein convertases

      1 , 1 , 2 , 1 , 1
      The FASEB Journal
      Wiley

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          Beta-amyloid precursor protein cleavage by a membrane-bound protease.

          The principal component of amyloid plaques in Alzheimer disease is beta-amyloid protein, an approximately 4-kDa peptide derived from amyloid precursor proteins. Previous studies have established that amyloid precursor proteins are secreted after proteolytic cleavage within the beta-amyloid peptide. The present investigation documents that, in cultured cells, amyloid precursor protein is cleaved on the plasma membrane by a membrane-bound endoprotease and that the specificity of peptide bond hydrolysis is largely independent of the primary sequence of the precursor. The principal determinants of cleavage appear to be an alpha-helical conformation and the distance (12-13 residues) of the hydrolyzed bond from membrane.
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            Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'.

            The X-ray crystal structures of two zinc endopeptidases, astacin from crayfish, and adamalysin II from snake venom, reveal a strong overall topological equivalence and virtually identical extended HEXXHXXGXXH zinc-binding segments, but in addition a methionine-containing turn of similar conformation (the 'Met-turn'), which forms a hydrophobic basis for the zinc ion and the three liganding histidine residues. These two features are also present in a similar arrangement in the matrix metalloproteinases (matrixins) and in the large bacterial Serratia proteinase-like peptidases (serralysins). We suggest that these four proteinases represent members of distinct subfamilies which can be grouped together in a family, for which we propose the designation, metzincins.
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              Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide

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                Author and article information

                Journal
                The FASEB Journal
                FASEB j.
                Wiley
                0892-6638
                1530-6860
                August 2001
                August 2001
                June 27 2001
                August 2001
                : 15
                : 10
                : 1837-1839
                Affiliations
                [1 ]Institute of BiochemistryJohannes Gutenberg-University MainzBecherweg 30D-55128MainzGermany
                [2 ]Institute of VirologyPhilipps-University MarburgRobert-Koch-Str.17D-35037MarburgGermany
                Article
                10.1096/fj.01-0007fje
                11481247
                d6c51585-e8ad-49af-b5f0-5d96849ce173
                © 2001

                http://onlinelibrary.wiley.com/termsAndConditions#vor

                http://doi.wiley.com/10.1002/tdm_license_1.1

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