Baupain, A Plant Cysteine Proteinase That Hinders Thrombin-Induced Human Platelet Aggregation
Authors: S. Andrade, Sheila; C.C. Silva, M.; E. Gouvea, I.; Y. Kondo, M.; A. Juliano, M.; U. Sampaio, M.; Luzia Oliva, Maria
Source: Protein and Peptide Letters, Volume 19, Number 4, February 2012 , pp. 474-477(4)
Publisher: Bentham Science Publishers
Abstract:Bauninia forficata is trivially known as cow paw, and popularly used in Brazil for treatment of diabetes mellitus. Denominated baupain a cysteine proteinase was purified from B. forficata leaves. In this study, we investigated the baupain effect on aggregation of isolated human platelets in vitro and the results show that baupain hinders thrombin - but not ADP- and collagen- induced platelet aggregation. With synthetic quenched-fluorescent peptides, the kinetics of the cleavage site of human proteinase-activated receptor 1 / 2 / 3 and 4 [PAR-1 / 2 / 3 and 4] by baupain was determined. In conclusion, similar to bromelain and papain, baupain hinders human platelets aggregation, probably through an unspecific cleavage in the Phe-Leu bond of PAR1.
Document Type: Research Article
Publication date: February 2012
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.