Isolation of Echimidine and Its C-7 Isomers from L. and Their Hepatotoxic Effect on Rat Hepatocytes.

Echimidine is the main pyrrolizidine alkaloid of L., a plant domesticated in many countries. Because of echimidine's toxicity, this alkaloid has become a target of the European Food Safety Authority regulations, especially in regard to honey contamination.

Health-Promoting of Polysaccharides Extracted from .

Medicinal mushrooms are rich sources of pharmacologically active compounds. One of the mushrooms commonly used in traditional Chinese medicine is (Leyss. Ex Fr.

Triterpenoid Acids as Important Antiproliferative Constituents of European Elderberry Fruits.

In Europe, both the fruits and flowers of Sambucus nigra L. have been used against cold, as well as laxative, diaphoretic, and diuretic remedies. There are also a number of commercially available food products that contain elderberry juice, puréed or dried elderberries.

Antibodies against Escherichia coli O24 and O56 O-Specific Polysaccharides Recognize Epitopes in Human Glandular Epithelium and Nervous Tissue.

Lipopolysaccharide (LPS), the major component of the outer membrane of Gram-negative bacteria, contains the O-polysaccharide, which is important to classify bacteria into different O-serological types within species. The O-polysaccharides of serotypes O24 and O56 of E. coli contain sialic acid in their structures, already established in our previous studies.

Cytotoxic effects of four aescin types on human colon adenocarcinoma cell lines.

Four types of aescin that are available on the pharmaceutical market, beta-aescin crystalline, beta-aescin amorphous, beta-aescin sodium and aescin polysulfate, have been analyzed for their cytotoxic effects on human colon adenocarcinoma (LoVo) and doxorubicin-resistant human colon adenocarcinoma cell lines (LoVo/Dx). Their cytotoxic activities were evaluated by sulforhodamine B (SRB) and methyl tetrazolium (MTT) assays. All four types of aescin exerted strong dose-dependent cytotoxicity to LoVo and, to a lesser degree, LoVo/Dx cell lines.

Enolase-like protein present on the outer membrane of Pseudomonas aeruginosa binds plasminogen.

Pseudomonas aeruginosa is one of the pathogenic bacteria which utilize binding of the host plasminogen (Plg) to promote their invasion throughout the host tissues. In the present study, we confirmed that P. aeruginosa exhibits binding affinity for human plasminogen.

Release of an ~55kDa fragment containing the actin-binding domain of β-spectrin by caspase-8 during FND-induced apoptosis depends on the presence of protein 4.1.

Analyses of the status of the membrane spectrin-based skeleton during fludarabine/mitoxantrone/dexamethasone-induced (FND-induced) apoptosis revealed proteolytic degradation of β-spectrin, with the prevalent appearance of a specific fragment with a molecular weight of ~55kDa, containing the actin-binding domain (ABD). Appearance of this fragment was dependent on induction of apoptosis. In silico proteolysis of spectrin identified caspase-8 as a candidate protease responsible for the generation of this ~55kDa ABD-containing fragment.

Estimation of the action of three different mechlorethamine doses on biochemical parameters during experimentally induced pleuritis in rats.

Nitrogranulogen (NTG) may modify the character of inflammatory reactions. These modifications are a result of cytotoxic and mutagenic effects. NTG has high affinity to DNA and causes disorders in the synthesis of acute phase proteins (e.

[The composition, biochemical properties and toxicity of snake venoms].

2.5 million cases of snake bites are noticed in the world every year (within 100,000 is mortal). These bites occur frequently in Asia and Africa.

Localization of enolase in the subfractions of a breast cancer cell line.

Enolase detected on the cell surface may be a receptor for certain ligands, especially for plasminogen. It is important for the pathogen invasiveness and in the development of a tumour. Therefore, we sought to preliminarily determine the enolase location and catalytic activity in the subfractions of MCF-7 cells.

[Amphibian skin secretions as a new source of antibiotics and biologically active substances].

So far, the main sources of biologically active substances used in medicine have been plants, molds, and propolis. The obtained compounds have either therapeutic features or require additional modification. They are sometimes combined with other pharmacological substances to intensify their therapeutic effect.

[Characterization of an inflammatory response].

The intensity of an inflammatory response in a tissue or an organ is dependent on the efficiency of the organism's homeostatic mechanisms, which restrict the extent of the reaction. The type of factor inducing a inflammatory response and its strength have significant influence on the dynamics of an inflammatory reaction. The prompt eradication of an inflammatory factor and its biologically adverse effects attest to the efficacious adaptive mechanisms of the organism.

Distribution of beta-enolase in normal and tumor rat cells.

Enolase - a glycolytic enzyme is also expressed on the surface of eukaryotic cells such as macrophages, neutrophils, endothelial, neuronal, tumor cells. Surface enolase as plasminogen receptor plays an important role in myogenesis, tumorgenesis and angiogenesis. Determination of enolase localization in the cell lines may give rise to the elucidation of its receptor function in tumor cells.

[Receptors for advanced glycation end products and their physiological and clinical significance].

The receptor for advanced glycation end products (RAGE) is a multiligand cell-surface protein and belongs to the immunoglobulin superfamily. RAGE is expressed by different cell types, including macrophages, lymphocytes, endothelial, neuronal, and smooth muscle cells. In addition to advanced glycation end products (AGEs), RAGE binds amphoterin, S100/calgranulin, amyloid, transthyretin, and a leukocyte integrin, Mac-1.

[Enolase on the surface of prockaryotic and eukaryotic cells is a receptor for human plasminogen].

Enolase was long considered an enzyme of the glycolytic pathway ubiquitously occurring in the cytosol of prokaryotic and eukaryotic cells. Results of extensive studies, especially those performed in the last ten years, indicate, however, that this protein is multifunctional. It plays several noncatalytic functions in various types of cells.