Published June 11, 2010
| Version v1
Journal article
Bauhinia variegata var. variegata trypsin inhibitor: From isolation to potential medicinal applications
Creators
- 1. School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, Hong Kong SAR (China)
- 2. Department of Food Science, Division of Sciences, University of Otago (New Zealand)
- 3. Department of Anatomy, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Sassoon Road, Pokfulam, Hong Kong SAR (China)
Description
Here we report for the first time of a new Kunitz-type trypsin inhibitor (termed BvvTI) from seeds of the Camel's foot tree, Bauhinia variegata var. variegata. BvvTI shares the same reactive site residues (Arg, Ser) and exhibits a homology of N-terminal amino acid sequence to other Bauhinia protease inhibitors. The trypsin inhibitory activity (Ki, 0.1 x 10-9 M) of BvvTI ranks the highest among them. Besides anti-HIV-1 reverse transcriptase activity, BvvTI could significantly inhibit the proliferation of nasopharyngeal cancer CNE-1 cells in a selective way. This may partially be contributed by its induction of cytokines and apoptotic bodies. These results unveil potential medicinal applications of BvvTI.
Availability note (English)
Available from http://dx.doi.org/10.1016/j.bbrc.2010.04.140Additional details
Identifiers
- DOI
- 10.1016/j.bbrc.2010.04.140;
- PII
- S0006-291X(10)00835-1;
Publishing Information
- Journal Title
- Biochemical and Biophysical Research Communications
- Journal Volume
- 396
- Journal Issue
- 4
- Journal Page Range
- p. 806-811
- ISSN
- 0006-291X
- CODEN
- BBRCA9
INIS
- Country of Publication
- United States
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 45023549
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- AIDS VIRUS; AMINO ACID SEQUENCE; CARCINOMAS; LYMPHOKINES; MEDICINAL PLANTS; SEEDS; TREES; TRYPSIN
- Descriptors DEC
- DISEASES; ENZYMES; GROWTH FACTORS; HYDROLASES; MICROORGANISMS; MITOGENS; MOLECULAR STRUCTURE; NEOPLASMS; ORGANIC COMPOUNDS; PARASITES; PEPTIDE HYDROLASES; PLANTS; PROTEINS; SERINE PROTEINASES; VIRUSES
Optional Information
- Copyright
- Copyright (c) 2010 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.