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M D Lutsik

Publications and source records attributed to M D Lutsik.

At least 19 recordsLinked to original sources
PubMed2002

In vitro studies of activation of phagocytic cells by bioactive peptides.

The effect of formyl chemotactic peptide (fCTP, fMet-Leu-Phe), beta-amyloid peptides (beta-AP, 1-42, 1-16 and 25-35), and bradykinin (BK) on functional activity of phagocytic cells has been investigated. Wheat germ agglutinin (WGA) was also used as a model membrane binding agent of polypeptide nature. Murine monocyte-macrophage cell line J774.2 and normal human blood polymorphonuclear (PMN) cells were used as target phagocytic cells. Their activity was quantitatively estimated by measuring phagocytosis of killed yeast cells. Beta-AP (1-41) maximally stimulated phagocytosis at 0.1 microg/ml, BK--at 1.0 microg/ml, and fCTP--at 2.0 microg/ml. Beta-AP (1-16) and beta-AP (25-35) were inactive in used test-systems. Phagocytosis-inducing activity of beta-AP (1-42) and BK reached maximal levels in 2 h and decreased after 4-6 h of incubation. Phagocytosis numbers were compared with the indicators of phagocytic cell activation, such as absorption of neutral red dye, glucose utilization, production of super-oxide anion (NBT-test) and nitrite accumulation (indicator of NO production). NBT-test, which may be related to the killing ability of phagocytic cells towards the ingested objects, was positive only in stimulated PMN leukocytes, while the nitrite accumulation was detected only in stimulated macrophages. Nitrite accumulation in macrophages was markedly induced by lipopolysaccharide and to a lower extent by 0.5 microg/ml beta-AP (1-42). In high dose (5.0 microg/ml) beta-AP suppressed nitrite accumulation in macrophages stimulated by lipopolysaccharide. Other studied peptides were inactive in inducing nitrite accumulation. Transforming growth factor type beta suppressed phagocytic activity of PMN cells activated by beta-AP or WGA. The anti-inflammatory drugs (indomethacin and L-lysine aescinate) inhibited beta-AP (1-42)-induced phagocytosis. The interrelations between the regulatory pathways of BK, beta-AP and fCTP are discussed.

Amyloid beta-Peptides↗
PubMed1992

[Electron-cytochemical study of carbohydrate components in the surface membrane of cultured Helix pomatia neurons].

The structure and topography of carbohydrates on the surface of nerve cells of snail Helix pomatia cultured in vitro have been characterized with a series of colloidal gold-labelled lectins of different sugar specificity. The analysis of the lectin binding has shown substantial differences in the carbohydrate pattern between the soma of monoaminergic and peptidergic neurons. It has been found that the surface of monoaminergic and peptidergic neurons contains N-acetylglucosamine (WGA+) and N-acetyllactosamine (RCA-1-) determinants and does not contain neuraminic acid (LPA-) and complex branched N-glycosyl chains (PVA-). At the same time N-acetylgalactosamine (HPA+) was detected on the peptidergic neuron membrane only. It has been concluded that terminal residues of sialic acid are absent on the most of snail nerve cells. Differences in lectin binding between monoaminergic and peptidergic neurons can serve as a basis for formation of specific connections of cells by different types in the developing brain.

Acetylgalactosamine↗
PubMed1990

[Determination of lectin receptors on the surface membranes of lymphoid cells].

The authors describe a method for the detection of carbohydrate determinants contained by the cellular surface membrane glycosylated biopolymers, based on the use of horse radish peroxidase-conjugated Arachis, Helix pomatia, Ricinus communis, Lens, Glycine max, Sophora japonica lectins. The pattern of lectin receptor distribution on normal human blood lymphocytes, tonsillar lymphoid cells, and in some forms of leukemia and lymphoma is shown. The authors consider it essential that a lectin kit be used along with enzymochemical and immunocytochemical markers as an additional test for the diagnosis of various forms and types of malignant lymphoproliferative diseases.

Cell Membrane↗
PubMed1990

[The characteristics of lectin binding to the surface of differentiated neuroblastoma C 1300 cells].

Peculiarities of the binding of lectins of castor bean, cochlea, soya bean, lime bean and wheat germs to the surface of differential neuroblastoma C 1300 N 18 cells have been studied using the method electron cytochemistry. It is found that the quantity of the bound lectin conjugates with colloidal gold on the surface of differentiated cells varied considerably from that on the surface of nondifferentiated cells.

Animals↗
PubMed1989

[The relation of changes in the surface markers and the induction of thymocyte functional activity under the action of humoral thymic factors].

Mouse thymocytes were fractionated on PNA+- and PNA-cells. The PNA+-fraction was treated by tactivin--a preparation of thymic hormones. The treatment resulted in the loss of PNA-receptors from the surface of 10-12% of PNA+-cells. The treated suspension was again fractionated by the same method. PNA-thymocytes derived from both the first and the second procedure of fractionation expressed less Thy-1.2 antigen and SBA-receptors than PNA+-cells. Primary and induced PNA-thymocytes were able to produce IL-2 after mitogen stimulation. The data can be interpreted as an evidence of the ability of thymic hormones to induce not only a phenotypical but also a functional maturation of PNA+-thymocytes and of linkage of all the observed signs of maturation.

Adjuvants, Immunologic↗
PubMed1989

[Study of the carbohydrate components of the surface of S 1300 neuroblastoma cells with the use of cytochemical and lectin agglutination methods].

The carbohydrate determinants of the cell surface of neuroblastoma C 1300 clone N 18 have been investigated by light microscopy with a panel of 11 lectins as cytochemical reagents. The expression of N- and O-glycanes with a predominance of 3-4 antigenic N-glycosyl chains was revealed. The characteristic feature of neuroblastoma cells is an abundance of an antigen A surface determinant. A strong correlation is shown between the intensity of lectin binding and index of cell agglutination. After the binding of lectins with living cells the lectin-receptor complexes are clustered, endocytosed and for 4 hours are concentrated as microvesicles in the cytoplasm compact area. Heterogeneity of the neuroblastoma cell population on the binding of peanut and Lens culinaris lectins is revealed.

Agglutination Tests↗
PubMed1987

[Evaluation of the distribution of lectin receptors on the surface of tumor and transformed cells using methods of variation statistics].

Statistical procedures were used to estimate lectin receptor distribution on the surface of ascite lymphoma cells, neuroblastoma C-1300 cells and of transformed human T- and B-derived lymphoid cell lines. Relationships between the arithmetic means and mean square variances for sample populations from each cell and ferritin- or colloidal gold-lectin combination were used to define four types of topographical distributions: uniform-ordered, uniform-random, random and clustered.

Animals↗
PubMed1986

[Cell surface receptors in lymphoid lines studied using lectins].

The nature and distribution of some carbohydrate receptors on the cell membrane of transformed human B- and T-derived lymphocyte cell lines (RPMI-1788, Daudi, Jurkat, Molt-4) are studied by Ricinus communis agglutinin, soybean agglutinin, Helix pomatia lectin, peanut agglutinin and wheat germ agglutinin conjugated with ferritin and colloidal gold. The quality of receptors and the manner of their distribution detected by different lectins are considerably different.

Cells, Cultured↗
PubMed1986

[Lectin receptors in the salivary glands of the rat during postnatal ontogenesis].

Distribution of lectin-binding sites in rat submandibular and sublingual salivary glands during postnatal development has been investigated. Lectin preparations include con A, lentin lectin, castor beans agglutinin, peanut, soybean and Sophora japonica agglutinins, wheat germ agglutinin and lectin from the bark of Laburnum anagyroides. The direct and indirect peroxidase techniques are used. According to the similarities of histochemical patterns, all lectins are divided into four groups. Besides the general patterns of lectin binding sites, some details are noted. Lectins of peanut and Sophora japonica possess an extremely high affinity to mast cells, con A, lens lectin, castor beans and wheat germ agglutinins--to serous demilunes cells. Laburnum lectin--to salivary ducts epithelia in adult rat salivary glands. Lentin lectin, con A and Laburnum lectin preferentially stain cells with specific granularity in granular ducts at early stages of postnatal development. Considering the character of staining, we propose for further histochemical investigations of the salivary glands lentin lectin, peanut agglutinin, wheat germ agglutinin and Laburum anagyroides lectin.

Animals↗
PubMed1986

[Localization of lectin receptors on the surface of C1300 neuroblastoma cells].

D-mannose, D-galactose, N-acetyl-D-galactosamine, N-acetyl-D-glucosamine and L-fucose which are sugar determinants of receptors were found on the surface of neuroblastoma cells by means of four carbohydrate-specific lectin groups. Labeling of lectins was performed by horseradish peroxidase, ferritin and colloidal gold. Peculiarities of the lectin receptors distribution on the surface of immature neuroblastoma cells were detected.

Acetylgalactosamine↗
PubMed1982

[New fucose-specific lectin from the bark of dwarf almond golden rain Laburnum anagyroides Medik: purification, properties and immunochemical specificity].

A new lectin specific towards L-fucose has been purified from the bark of Laburnum anagyroides. The purification procedure included precipitation with ammonium sulfate (30-90% saturation), precipitation of the globuline fraction at pH 4.2, fractionation with rivanol, chromatography on Sephadex G-100 and DEAE-cellulose. Electrophoresis in SDS revealed one protein band with molecular weight of 33,000. The molecular weight of the native lectin is about 130,000, thus suggesting a tetrameric structure of the protein molecule. The lectin obtained contains 13.1% of carbohydrates; its amino acid composition is characterized by a high content of serine, threonine, glutamic and aspartic acids and by a lack of cystine and cysteine. The lectin activity is inhibited by L-fucose (2 mM). Lectin agglutinates native human erythrocytes with a preference for the O(H) blood group. The differences in the titre of hemagglutination of individual erythrocyte samples within a unique blood group were observed.

Amino Acids↗