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G M Shevchenko

Publications and source records attributed to G M Shevchenko.

12 recordsLinked to original sources
PubMed1988

[Identification and characteristics of concanavalin A-binding neurospecific glycoproteins in human brain and brain tumors].

Soluble and membrane-bound neurospecific Con A-binding glycoproteins from human brain and tumours were identified and characterized, using a procedure which included stepwise extraction with low and high ionic strength buffers, buffered. Triton X-100 and sodium deoxycholate followed by ConA-Sepharose column chromatography, SDS-PAAG electrophoresis and immunoblotting. Adsorbed antisera against different types of neurospecific glycoproteins were used. The bulk of neurospecific glycoproteins (11 and 13) were revealed in protein fractions extracted with low ionic strength buffers and Triton X-100. In astrocytomas and glyoblastomas, some neurospecific glycoproteins were absent. Some glycoproteins were found in tumours, but were absent in brain tissue. Soluble, 77 kD glycoprotein, 11 and 16 kD glycoproteins solubilized with high ionic strength buffers and intrinsic membrane-bound 51, 57, 61, 74 and 77 kD glycoproteins can be viewed as stable neurospecific markers in malignant brain tumours.

Brain Chemistry↗
PubMed1987

[Neurospecific proteins: potentials and prospects for their use in morphological research on tumors].

Data on the application of neurospecific proteins S-100, GFAP, D2 glycoprotein and neuron-specific enolase (NSE) in the differential tumor diagnosis are reviewed. S-100 protein and GFAP are found in well differentiated astroglial tumors. S-100 protein can be used as melanoma and Schwannoma specific marker. In malignant CNS tumors there is a decrease of S-100 protein content up to its complete disappearance, while the content of GFAP is variable. D2 glycoprotein is detected in gliomas and medulloblastomas, being absent in other brain tumors. NSE is invariably present in apudomas and was also found in the majority of investigated astrocytomas, ependymomas, glioblastomas and in some medulloblastomas.

Animals↗
PubMed1985

[Neurospecific proteins in human malignant brain tumors].

The content of neurospecific proteins S-100, GFA and D2 was measured in malignant cerebral tumors by electrophoresis with the use of monospecific antisera. Concomitant measurement of proteins S-100 and GFA is a more reliable diagnostic criterion as to the tumor histogenesis than study of each protein alone. D2 protein appeared to be the most stable specific marker.

Biopsy↗
PubMed1981

[Neutral proteinase from brain, hydrolyzing serum albumin].

The regional, cellular and subcellular distribution of neutral proteinase hydrolyzing serum albumin in the brain was studied. The enzyme was detected in soluble cell fraction. The neutral proteinase activity in the neuron cell enriched fraction from the cat cortex was 4 times as high as that in the glia. Neutral proteinase was isolated and purified from bovine cerebellum by ammonium sulfate precipitation, dialysis, gel chromatography and affinity chromatography on albumin-Biogel P-300. Two peaks of neutral proteinase activity were observed. The degree of purification was 3400 and 7700, respectively; the recovery was 6 and 4%, respectively. The enzyme was activated by 2-mercaptoethanol and was inhibited by EDTA and p-chloromercurybenzoate. Phenylmethylsulfonylfluoride and pepstatin had no effect on the enzyme activity. The inhibitory analysis demonstrated that the enzyme probably contains some proteinases capable to bind to immobilized serum albumin.

Animals↗
PubMedDate not supplied

[The distribution of glial fibrillary acidic protein and protein S-100 in experimental brain tumors in rats].

The methods of quantitative immunoelectrophoresis and indirect immunofluorescence were used study the content of glial fibrillary acid protein in 10 serially reinoculated rat gliomas induced primarily by ethylnitrosourea (a total of 135 tumors). It was found that the GFAP content reduced with increase of malignancy. However, wide scattering of the GFAP content in some of the tumors was characteristic of all strains. In the group of slowly growing glial tumors (2 malignant astrocytomas and one malignant oligoastrocytoma) the GFAP content ranged from 50 to 600% and exceeded the normal content two-to threefold on the average. In the group of highly malignant gliomas (4 malignant ependymomas, 2 malignant gliomas, and one glioblastoma) the GFAP content was within the limits of 65-120%. In most cases the GFAP level was below normal or could not be determined at all. At the same time, tumors with a high GFAP content were encountered. The GFAP-positive cells were unevenly distributed in the gliomas: separately, in foci, and around the vessels. Their number increased in the direction of the periphery of the tumor. Intensive fluorescence was noted on the tumor--brain borderline. The content of protein S-100 in the experimental gliomas was always below normal.

Animals↗
PubMedDate not supplied

[Characteristics of concanavalin A-binding neurospecific glycoproteins from various regions of the rat brain during experimental neurosis].

The polypeptide composition of neurospecific glycoproteins in different areas of the rat brain under experimental neurosis is characterized using SDS-PAG-electrophoresis followed by electroblot and immunofixation on nitrocellulose membranes. The soluble and membrane-bound glycoproteins are purified by Con A-Sepharose column chromatography. Changes in the glycoprotein polypeptide composition in different areas of the rat brain under experimental neurosis are qualitative. Soluble glycopolypeptide 27 kDa and membrane glycopolypeptide 32 kDa are not revealed in the midbrain and corpus striatum. Soluble polypeptide 47 kDa is absent in the cerebral cortex and hippocampus. It is suggested that the above mentioned glycopolypeptides are important for the CNS physiological functioning.

Animals↗
PubMedDate not supplied

[Neurospecific cytoskeletal proteins].

Data available in literature on neurospecific proteins of cytoskeletal structures--microtubules, microfilaments and intermediate filaments are generalized. Properties of tissue-specific cytoskeletal proteins which are typical of nerve cells are summarized. The structure, physicochemical properties, cell localization, metabolism and function of cytoskeletal proteins are characterized. The coexpression and interaction of different cytoskeletal structures are considered. An analysis of neurospecific cytoskeletal proteins is of great practical importance for neurobiology, neurooncology, neurosurgery. The proteins can be used as markers of different pathologies in the nervous system.

Animals↗