Interaction of Wheat Germ Agglutinin with Porphyrin Compounds - Potential Anticancer Agents
نویسندگان
چکیده
Wheat germ agglutinin (WGA) is the first studied plant lectin shown to bind more strongly to tumour cells than to normal ones. WGA interacts with prostate cancer cells, human pancreatic cells and colon-cancer cells. Our results showed the interaction of WGA with two porphyrin compounds Fe porphyrin and Pd porphyrin. The dissociation constants for the porphyrin binding was kD (0.08-1.02 μM) showing high affinity for the two porphyrins for this protein. The hyperbolic titration curve indicated the presence of a single porphyrin binding site. In conclusion, we show that two photosentisizers with anticancer activity Fe porphyrin and Pd porphyrin, have high affinity for WGA. Since WGA binds to cancer cells, the results suggest that it may have utility in the targeted delivery of drugs for cancer.
منابع مشابه
New Activity of a Protein from Canavalia ensiformis
Concanavalin A is a legume lectin which preferentially agglutinates transformed cells and shows antitumor effects on human breast carcinoma cells in vitro and in vivo. It is considered as a new potential antineoplastic agent targeting apoptosis, autophagy, and anti-angiogenesis in preclinical or clinical trials for cancer therapeutics, which has recently become the object of intensive study. In...
متن کاملThe interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid.
The role of sialic acid in the interaction of sialoglycoproteins with wheat germ agglutinin was investigated by using several well characterized saccharides and sialoglycoconjugates. N-Acetylneuraminic acid and neuramin 2 + 3 lactose, in addition to N-acetyl-Dglucosamine and its fil-+ 4 oligomers were found to be inhibitors of wheat germ agglutinin-induced hemagglutination. Neuraminic acid-/?-m...
متن کاملThe Interaction of Wheat Germ Agglutinin with Sialoglycoproteins
The role of sialic acid in the interaction of sialoglycoproteins with wheat germ agglutinin was investigated by using several well characterized saccharides and sialoglycoconjugates. N-Acetylneuraminic acid and neuramin 2 + 3 lactose, in addition to N-acetyl-Dglucosamine and its fil-+ 4 oligomers were found to be inhibitors of wheat germ agglutinin-induced hemagglutination. Neuraminic acid-/?-m...
متن کاملAn Alkaline Phosphatase Lacking Wheat Germ Agglutinin Binding Sites Useful Enzyme for Lectin Assays with Comparable Activity to the Calf Enzyme
Despite the availability of various alkaline phosphatase (ALP) isoenzymes, the calf enzyme is being used in current enzyme assays as the detector enzyme. The glycosylation pattern of this enzyme makes it a suitable ligand for binding to wheat germ agglutinin lectin (WGA). As a result of this property, the enzyme can not be used as a conjugate with this lectin, and the calf enzyme conjugates can...
متن کاملIncrease in cell surface wheat germ agglutinin binding in a rat hepatoma cell line dRLa 74 treated with concanavalin A.
Wheat germ agglutinin binding to a rat hepatoma cell line dRLa 74 treated with concanavalin A was studied. It increased depending on the concanavalin A concentration in the culture medium. The cells exhibited about twofold increase in wheat germ agglutinin-binding when pretreated with 50 micrograms/ml of concanavalin A for 48 h. The wheat germ agglutinin binding sites were shown to be localized...
متن کامل