Journal Image
Protein & Peptide Letters
ISSN (Print): 0929-8665
ISSN (Online): 1875-5305
DOI: 10.2174/092986612799789305      Price:  $58

Baupain, A Plant Cysteine Proteinase That Hinders Thrombin-Induced Human Platelet Aggregation

Author(s): Sheila S. Andrade, M. C.C. Silva, I. E. Gouvea, M. Y. Kondo, M. A. Juliano, M. U. Sampaio and Maria Luzia Oliva
Pages 474-477 (4)
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.
Bauhinia, cysteine proteinase, plant enzyme, platelet aggregation, thrombin, collagen, human proteinase-activated receptor, baupain, Phe-Leu
Department of Biochemistry, Universidade Federal de Sao Paulo-Escola Paulista de Medicina, 04044-020 Sao Paulo, SP, Brazil.