Inhibition of human leukocyte elastase and cathepsin G by extended peptides and subunits derived from human C-reactive protein |
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| Authors: | Eran J. Yavin Lin Yan Dominic M. Desiderio Michel Pontet Mati Fridkin |
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| Affiliation: | (1) Department of Organic Chemistry, The Weizmann Institute of Science, Rehovot, 76100, Israel;(2) Charles B. Stout Neuroscience Mass Spectrometry Laboratory, University of Tennessee-Memphis, 800 Madison Avenue, Memphis, TN, 38163, U.S.A;(3) Departments of Neurology and Biochemistry, University of Tennessee-Memphis, 800 Madison Avenue, Memphis, TN, 38163, U.S.A;(4) Laboratory of Biochemistry, Hospital Jean Verdier, F-93143 Bondy Cedex, France |
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| Abstract: | Extended peptides that derive from the primary sequence of the acute phase reactant C-reactive protein (CRP) are shown to inhibit in vitro the enzymatic activities of human leukocyte elastase (hLE) and human leukocyte cathepsin G (hCG), which are associated with the tissue damage that occurs during the course of several chronic inflammatory conditions. Major inhibitory activity was observed in the peptides CRP70-98 and CRP50-98 towards hLE (Ki = 4.0 µM) and hCG (Ki = 1.4 µM), respectively. In contrast to the inability of intact CRP pentamers to inhibit both enzymes, CRP subunits (monomers) inhibited hLE (3.0 µM) and hCG (3.6 µM) activity. |
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| Keywords: | Acute phase proteins Inflammation Serine protease |
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