Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 430, Issue 1, Pages 144-149Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2012.11.056
Keywords
Anti-elastolytic factor; Apis cerana; Bee; Chymotrypsin inhibitor; Elastase inhibitor
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Funding
- Rural Development Administration (Next-Generation Biogreen 21 Program) of the Republic of Korea [PJ009031]
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The honeybee is an important insect species in global ecology, agriculture, and alternative medicine. While chymotrypsin and trypsin inhibitors from bees show activity against cathepsin G and plasmin, respectively, no anti-elastolytic role for these inhibitors has been elucidated. In this study, we identified an Asiatic honeybee (Apis cerana) chymotrypsin inhibitor (AcCI), which was shown to also act as an elastase inhibitor. AcCI was found to consist of a 65-amino acid mature peptide that displays ten cysteine residues. When expressed in baculovirus-infected insect cells, recombinant AcCI demonstrated inhibitory activity against chymotrypsin (K-i 11.27 nM), but not trypsin, defining a role for AcCI as a honeybee-derived chymotrypsin inhibitor. Additionally, AcCI showed no detectable inhibitory effects on factor Xa, thrombin, plasmin, or tissue plasminogen activator; however, AcCI inhibited human neutrophil elastase (K-i 61.05 nM), indicating that it acts as an anti-elastolytic factor. These findings constitute molecular evidence that AcCI acts as a chymotypsin/elastase inhibitor. (C) 2012 Elsevier Inc. All rights reserved.
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