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Biomedical subjects

V P Goncharova

Publications and source records attributed to V P Goncharova.

At least 19 recordsLinked to original sources
PubMed1994

[Fibroblast growth factors (a short review)].

Some features of structure and expression of bFGF gene and FGF receptors genes, unique secretion property of bFGF, as well as FGF's interactions with heparin-containing components of the cell and extracellular matrix are briefly observed. These special features may underlie the multifunctionality of members of ubiquitously distributed fibroblast growth factor family which recently have been filled up with two new members: androgen-induced growth factor--FGF-8 (Tanaka A., Miyamoto K., Minamino N. at al., 1992) and glia-activating factor--FGF-9 (Naruo K., Seco C., Kuroshima K. at al. 1993).

Amino Acid Sequence↗
PubMed1991

[A comparative analysis of the biological activity of an acid-extractable brain protein and fibroblast growth factors].

An acid-soluble protein was isolated from bovine brain tissue using a combination of 5% HClO4 acidic extraction, cation-exchange chromatography and heparin-Sepharose affinity chromatography. This preparation had a biological activity similar to that of the fibroblast growth factor (FGF). It has stimulated neurite outgrowth in organotypic culture of chicken embryo dorsal root ganglia and also has stimulated a proliferation of human embryonic fibroblasts in the culture. The biological activity of isolated preparation was totally inhibited by anti-bFGF antibodies, while anti-aFGF antibodies had no effect. The bFGF showed a neurite stimulating activity in the organotypic culture that was completely abolished by the anti-bFGF, IgG, while the aFGF was inactive. This data, as well as cationic properties of isolated protein and its heparin-binding ability, enable us to postulate a high degree of homology of the brain acid-soluble protein and the bFGF. At the same time the relations of the isolated growth factor and other brain-derived heparin-binding growth factors are yet to be established.

Animals↗
PubMed1989

[The growth and morphophysiological study of the bushy tissue receptor in a nerve tissue culture].

The conditions for growing bush receptors on collagen substrate in presence of 2-4 ng/ml highly purified brain neurite stimulating protein were determined in the study of spinal ganglia cultures of 10-11-day chicken embryos. The degree of neurite branching and sinuosity and the distribution density of preterminals of cultured bush-like receptors are like those of chicken embryos' natural interoceptors. The ultrastructure of end receptor plates in culture resembles that of natural mechanoreceptor terminals. Cultural receptors are characterized by spontaneous electrophysiological activity. They respond to tactile irritation with bursts of discharges.

Animals↗
PubMed1989

[Effect of neurite-stimulating protein on the growth and proliferation of peripheral glia cells].

Proliferative activity of peripheral glia was investigated in the organotypic culture of peripheral nerves of 9-10-day old chick embryos. The neurite-stimulating protein, a stimulator of the neurite growth in the organotypic culture of spinal ganglia, being added to the culture media sharply increased the mitotic activity of glia: on the 3d day its level was 3.5 times higher as compared with the control one.

Animals↗
PubMed1988

[Comparative analysis of brain neurite-stimulating protein and nerve growth factor by using a culture of chick embryo sensory neurons].

The effect of brain neurite-stimulating protein (BNSP) on growth and differentiation of nerve cells was studied in cultured chick embryo neurons BNSP stimulated axon growth. Its chemical characteristics were different from those of neurotrophic factor (NGF). The effect of NGF antiserum was not blocked by the BNSP action. The neurite-stimulating effect of BNSP can be used for stimulation of regenerating processes in the nervous tissue.

Animals↗
PubMed1987

[Brain neurite-stimulating protein].

A protein possessing the neurite-stimulating activity in organotypic cultures of chicken embryo spinal ganglia was isolated and purified from bovine brain tissue. The isolation and purification procedures included acid extraction, ultrafiltration, preparative polyacrylamide gel electrophoresis and chromatography on heparin-Sepharose. The molecular weight of the protein is about 15000 Da. The neurite-stimulating activity of the purified protein manifests itself at a protein concentration of about 10(-9) M.

Animals↗
PubMed1986

[Effect of a cerebral neurite-stimulating protein on the morphogenesis of an organotypical culture of spinal ganglia].

Cationic protein with molecular mass of 15,000 kDa has been extracted from the hemispheres of the rat and bovine brain. Addition of the protein into nutritive medium of the organo-typical culture of the chick embryo spinal ganglia results in a considerable (by 2-2.5 times) increase of the growth zone in the explants. Neurite-stimulating effect of the protein is demonstrate dat concentration of 10 ng/ml. An intensive longitudinal growth of neurites is observed, increase of their amount per area unit, an essential intensification of ramification, formation of powerful anastomoses, numerous dense plexuses and arcades. Fasciculi of neurites covered with glia are formed. The cerebral neurite-stimulating protein is, evidently, one of neuron-growing factors, regulating development of the nervous system in the organism.

Animals↗
PubMed1979

[Proteinase activity of nuclei from various tissues towards endogenous histones].

The proteinase activities of nuclei isolated from tissues differing in their mitotic activities (brain, thymus, liver, ascite lymphoma) towards the histones and non-histone acid -- extractable proteins were studied. The sensitivity of different histone fractions to nuclear proteinase depends on temperature and time of nuclei incubation under conditions providing for complete dissociation of chromatin proteins from DNA (2 M NaCl--5 M urea). The proteinase activity in the brain and thymus nuclei is revealed only under prolonged (43 hrs) incubation of the nuclei at 25 degrees C, which is accompanied by partial proteolysis of histone H1. Histone H4 from brain nuclei and histone H2a from thymus nuclei are preferably degraded. In the nuclei isolated from the mice ascite cell lymphoma NK/ly and from rat liver the enzyme activity is revealed mainly towards the arginine-enriched histones H3 and H4. The proteolysis of the arginine-enriched histones in tumour cell nuclei is more complete. A high sensitivity to proteolysis was observed for non-histone acid-extractable proteins with low electrophoretic mobility, which were found in brain and tumour cell nuclei.

Animals↗
PubMedDate not supplied

Effect of cerebral neurite-stimulating protein on morphogenesis of organotypical culture of spinal ganglia.

We have extracted a cationic protein with a molecular weight of 15,000 kdalton from the hemispheres of rat and bovine brain. Addition of the protein to the nutrient medium of the organotypical culture of chick embryo spinal ganglia results in a considerable (2-2.5 fold) increase in the growth zone of the explants. The neurite-stimulating effect of the protein is observed at a concentration of 10 ng/ml. We observed an intensive longitudinal growth of neurites, an increase in their amount per unit area, a considerable intensification of ramification, and formation of strong anastomoses, numerous dense plexuses, and arcades. Fasciculi of neurites covered with glia are formed. The cerebral neurite-stimulating protein is evidently one of the neuron-growth factors regulating development of the nervous system in the body.

Animals↗
PubMedDate not supplied

[Effect of brain and thymus cationic proteins on membrane permeability].

Cationic proteins of brain lysosomes (LCP), myelin (MCP) and nuclear histone fractions from calf thymus (T) and rat brain (B) are shown to increase at different degree the permeability of brain lysosomes and neutrophiles for acid RNAase, acid phosphatase, catepsin D and beta-galactosidase. According to the effectivity, basic proteins can be listed in the following order: for lysosomes-f2aT, F3B, f3T greater than total histones B, f2bT greater than f2B greater than LCP, MCP greater than flT, flB; for neutriphiles-f3T larger than or equal to total histones B larger than or equal to f3b MCP larger than or equal to f2aT, f2bT greater than f2B greater than LCP greater than flB greater than flT. Fractions f2a and f3 considerably increased the release of acid RNAase from lysosomes in very low concentrations beginning from 0,2 mug/ml, while the release of catepsine and acid phosphatase took place beginning from 5-10 mug/ml. The effect of lysosome and myelin cationic proteins on the release of hydrolases occurred at concentrations ten to hundred times higher.

Acid Phosphatase↗