TAILIEUCHUNG - Báo cáo khoa học: Arg143 and Lys192 of the human mast cell chymase mediate the preference for acidic amino acids in position P2¢ of substrates

Chymases are chymotrypsin-like serine proteases that are found in large amounts in mast cell granules. So far, the extended cleavage specificities of eight such chymases have been determined, and four of these were shown to have a strong preference for acidic amino acids at position P2¢. These enzymes have basic amino acids in positions 143 and 192 (Arg and Lys, respectively). | ỊFEBS Journal Arg143 and Lys192 of the human mast cell chymase mediate the preference for acidic amino acids in position P2 of substrates Mattias K. Andersson Michael Thorpe and Lars Hellman Department of Celland Molecular Biology Uppsala University The BiomedicalCenter Sweden Keywords chymase cleavage specificity human chymase mast cell site-directed mutagenesis Correspondence L. Hellman Department of Cell and Molecular Biology Uppsala University The BiomedicalCenter Box 596 SE-751 24 Uppsala Sweden Fax 46 0 18 471 4382 Tel 46 0 18 471 4532 E-mail Website http immuno Received 29 December 2009 revised 2 March 2010 accepted 4 March 2010 doi Chymases are chymotrypsin-like serine proteases that are found in large amounts in mast cell granules. So far the extended cleavage specificities of eight such chymases have been determined and four of these were shown to have a strong preference for acidic amino acids at position P2 . These enzymes have basic amino acids in positions 143 and 192 Arg and Lys respectively . We therefore hypothesized that Arg143 and Lys192 of human chymase mediate the preference for acidic amino acids at position P2 of substrates. In order to address this question we performed site-directed mutagenesis of these two positions in human chymase. Analysis of the extended cleavage specificities of two single mutants Arg143 fi Gln and Lys192 fi Met and the combined double mutant revealed an altered specificity for P2 amino acids whereas all other positions were essentially unaffected. A weakened preference for acidic amino acids at position P2 was observed for the two single mutants whereas the double mutant lacked this preference. Therefore we conclude that positions 143 and 192 in human chymase contribute to the strong preference for negatively charged amino acids at position P2 . This is the first time that a similar combined effect has been shown to influence the cleavage .

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