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Enhancement of catalytic activities of serine proteases by tripeptides compounds
Author(s) -
Hiwasa Takaki,
Ogawa Sachiko,
Kobayashi Hisashi,
Ike Yoshimasa
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00381-x
Subject(s) - proteases , chemistry , biochemistry , trypsin , chymotrypsin , thrombin , plasmin , serine , cathepsin c , tripeptide , exopeptidase , subtilisin , autolysis (biology) , cathepsin g , elastase , enzyme , peptide , biology , platelet , immunology
The tripeptide compounds, Glu‐Arg‐Pro‐amide (ERPm), d ‐Pro‐Thr‐Trp‐amide (dPTWm) and thioproline‐Thr‐Trp (tPTW), were obtained by screening of synthetic peptides for growth‐inhibitory activity toward cultured transformed cells. The effects of these peptide compounds on proteases were investigated and the results showed that these compounds enhanced the amidolytic activity of serine proteases despite the fact that each reaction was carried out under optimal conditions. ERPm stimulated the activities of trypsin, chymotrypsin, thrombin, plasmin urokinase and elastase. dPTWm also showed similar effects except that toward chymotrypsin. tPTW elevated the activity only of trypsin, chymotrypsin and thrombin. Stimulation of trypsin activity by these compounds was also confirmed by using casein as a substrate. None of these compounds affected the amidolytic activities of metalloproteinases (MMP‐1 and MMP‐9), cysteine proteinases (m‐ and μ‐calpains, cathepsin B and papain) or an exopeptidase (leucine aminopeptidase). The activation was at least partly due to the stabilization of the catalytic activity of proteases as well as prevention of autolysis.