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1.
Biomed Pharmacother ; 135: 111141, 2021 Mar.
Article in English | MEDLINE | ID: mdl-33385857

ABSTRACT

Due to the richness of bioactive substances and easy accessibility, sea-buckthorn can be an ingredient of currently popular functional food supporting anti-cancer therapy. Low-polarity fractions from fruit (OL), twigs (GL) and leaves (LL) were investigated. Compared to the previous scientific reports a more detailed analysis of the chemical composition of individual fractions was performed. Cytotoxicity of low-polarity fractions has been investigated and activity compared in human tumor and normal cells cultured in vitro. The genotoxicity and pro-apoptotic properties of low-polarity fractions were also followed on selected cell lines that had proved to be the most sensitive. In the proposed research model being tested, low-polarity fractions act cytotoxically, even 3 times more strongly in cancer cells than normal ones. Measurement of caspase 3/7 activity indicated that cell death occurs through apoptosis. Furthermore, high concentrations of low-polarity fractions have moderate genotoxic properties. Data obtained on the biological properties of low-polarity fractions from sea-buckthorn show that these fractions can potentially support cancer cells elimination. Phytotochemical analysis indicates the key role of the triterpenoids in this process.


Subject(s)
Antineoplastic Agents, Phytogenic/pharmacology , Elaeagnaceae , Neoplasms/drug therapy , Plant Extracts/pharmacology , Antineoplastic Agents, Phytogenic/isolation & purification , Apoptosis/drug effects , Caspase 3/metabolism , Caspase 7/metabolism , DNA Damage , Elaeagnaceae/chemistry , HCT116 Cells , HT29 Cells , Humans , MCF-7 Cells , Neoplasms/metabolism , Neoplasms/pathology , PC-3 Cells , Plant Extracts/isolation & purification
2.
J Physiol Pharmacol ; 68(2): 223-229, 2017 Apr.
Article in English | MEDLINE | ID: mdl-28614772

ABSTRACT

Beneficial influence of fruits on human health may be their ability to prevent the hyperactivation of blood platelets and cardiovascular disorders. Effects of the phenolic fraction from Hippophae rhamnoides fruit on different stages of blood platelet activation (platelet adhesion and aggregation) were studied in vitro. We also examined effects of the H. rhamnoides fraction on metabolism of thiol groups, which plays an important role in platelet functions. The effects of the H. rhamnoides fraction on adhesion of blood platelets to collagen and fibrinogen were determined with Tuszynski's and Murphy's method. The platelet aggregation was determined with turbidimetry. The action of the H. rhamnoides fraction on the level of thiol groups in platelet proteins and a level of glutathione (GSH) in platelets was estimated with 5,5'-dithio-bis(2-nitro-benzoic acid). The tested fraction of H. rhamnoides (0.5 - 50 µg/ml; 30 min of the incubation time 30 min) inhibited blood platelets adhesion to collagen and fibrinogen. The effect of the tested fraction on blood platelet adhesion depended on concentration of fraction. In presence of the highest tested concentration which was 50 µg/ml, inhibition of platelet adhesion for thrombin-activated platelets was about 55%. On the other hand, tested plant fraction had no anti-aggregatory properties. Our results showed anti-adhesive properties of phenolic fraction from H. rhamnoides fruit and we suggest that it may be beneficial for prevention of cardiovascular diseases.


Subject(s)
Blood Platelets/drug effects , Fruit/chemistry , Hippophae , Phenols/pharmacology , Plant Extracts/chemistry , Platelet Adhesiveness/drug effects , Blood Platelets/physiology , Humans , Platelet Aggregation/drug effects
3.
Biochemistry (Mosc) ; 74(2): 226-30, 2009 Feb.
Article in English | MEDLINE | ID: mdl-19267680

ABSTRACT

Novel trypsin inhibitors from the white rot fungus Abortiporus biennis were isolated, partially purified, and characterized. The inhibitors were purified by heat treatment, anion-exchange chromatography, and gel filtration. SDS-PAGE of the purified preparation demonstrated the presence of two proteins with molecular masses of 20 and 21.5 kDa. The A. biennis inhibitors were most active against trypsin, while chymotrypsin alpha, proteinase K, and Carlsberg subtilisin were inhibited to a smaller extent. The inhibitors are acidic proteins with remarkably high heat stability.


Subject(s)
Coriolaceae/chemistry , Trypsin Inhibitors/isolation & purification , Anion Exchange Resins , Chromatography, Ion Exchange , Electrophoresis, Polyacrylamide Gel , Hot Temperature , Trypsin Inhibitors/chemistry
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