Inhibition of human leukocyte elastase and cathepsin G by extended peptides and subunits derived from human C-reactive protein |
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| Authors: | Yavin Eran J. Yan Lin Desiderio Dominic M. Pontet Michel Fridkin Mati |
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| Affiliation: | (1) Department of Organic Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel;(2) Charles B. Stout Neuroscience Mass Spectrometry Laboratory, University of Tennessee-Memphis, 800 Madison Avenue, 38163 Memphis, TN, U.S.A.;(3) Departments of Neurology and Biochemistry, University of Tennessee-Memphis, 800 Madison Avenue, 38163 Memphis, TN, U.S.A.;(4) Laboratory of Biochemistry, Hospital Jean Verdier, F-93143 Bondy Cedex, France |
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| Abstract: | Summary 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=4.0μ M) 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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