ABSTRACT
Senna occidentalis (sin. Cassia occidentalis) é um arbusto perene nativo da América do Sul e distribuída em regiões tropicais ao redor do mundo, frequentemente contaminando pastos e culturas de cereais. Inúmeros estudos demonstraram que esta planta é tóxica para animais. Na medicina popular, tribos americanas, africanas e indianas usam preparações da S. occidentalis como tônico, estomáquico, febrífugo, laxante e antimicrobiano. Diversas propriedades biológicas da espécie já foram comprovadas, tais como a antibacteriana, antifúngica, antimalárica, antitumoral e hepatoprotetora. As análises fitoquímicas evidenciaram que as antraquinonas, os flavonóides e outros derivados fenólicos são os seus principais constituintes. Esta revisão apresenta dados etnofarmacológicos, químicos e biológicos publicados na literatura sobre S. occidentalis.
Senna occidentalis (syn. Cassia occidentalis) is a perennial shrub, native to South America and indigenous to tropical regions throughout the world, often contaminating pastures and cereal crops. There have been many reports showing that S. occidentalis is toxic to animals. In traditional medicine, some American, African and Indian ethnic groups use S. occidentalis preparations in stomach treatments and as a tonic, febrifuge, laxative and topical antimicrobial agent. Several biological properties of this species have been proved, such as antibacterial, antifungal, antimalarial, antitumor and hepatoprotective activity. Phytochemical analysis has shown that anthraquinones, flavonols and other phenolics are its major constituents. In this paper we present an overview of the ethnopharmacological, chemical and biological data published in the literature on S. occidentalis.
Subject(s)
Caesalpinia/chemistry , Caesalpinia/toxicity , Cassia/chemistry , Cassia/toxicity , /chemistry , /toxicity , Fabaceae , Plants, MedicinalABSTRACT
We describe some structural requirements od the fibroblast growth factor (FGF) signaling system for the stimulation of the mitogenic response in terms of the design, synthesis and mitogenic activity of linear peptides related to the human FGF-1 sequence and the structural requirements of heparin for the potentiation of the mitogenic activity of FGF-1. The best mitogenic peptide we have synthesized so far is Ac-WFVGLKKNGSSKRGPRT-NH2, that has been shown: 1)to bind to heparin-Sepharose columns with moderate affinity, requiring about 0.5 M NaCl to be eluted from the resin; 2) to be mitogenic upon BALB/c 3T3 fibroblasts in culture (ED50=10-20 muM) and 3)to compete with human FGF-1 for cellular binding (ID50=30-50 muM). The potentiating activity of heparin upon FGF-1 has shown to be dependent on the oligosaccharide size, degree of sulfation and carboxylation. Apparently, these same requirements hold for the heparan sulfate molecules. Based on the reported studies, ee propose some important requirements of an oligosaccharide to potentiate FGF-1 mitogenic activity: 1) to have a minimum of twelve units, organized as disaccharides where one of the units is a uronic acid and the second is glycosamine; 2) to have at least one iduronic acid sulfated at position 2 and 3) to have N-sulfated glycosamines, preferentially 6-O-sulfated. To have groups of negative charges is not enough: they need to be localized in a correct conformation.