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Biomedical subjects

E E Fesenko

Publications and source records attributed to E E Fesenko.

At least 19 recordsLinked to original sources
PubMed1999

A novel 45 kDa secretory protein from rat olfactory epithelium: primary structure and localisation.

cDNA clones encoding the 45 kDa protein were isolated from a rat olfactory epithelium cDNA library and their inserts were sequenced. The reconstructed protein sequence comprises 400 amino acids with a calculated molecular mass of 46,026 Da. A homology was revealed between the amino acid sequence of the 45 kDa protein and the proteins involved in the transfer of hydrophobic ligands. Using in situ hybridisation, the 45 kDa protein mRNA expression was detected in the layer of supportive cells of olfactory epithelium, apical region of trachea, surface layer of the ciliated bronchial epithelium in lung and in skin epidermis.

Amino Acid Sequence↗
PubMed1999

Localization of 28-kDa peroxiredoxin in rat epithelial tissues and its antioxidant properties.

Peroxiredoxins are a novel family of antioxidant proteins that specifically prevent enzymes from metal-catalyzed oxidation. The localization of a member of the mono-cystein subfamily of peroxiredoxins, the 28-kDa protein, in different rat tissues and its antioxidant properties were investigated. By immunoblotting, the 28-kDa peroxiredoxin was found to be most highly concentrated in olfactory epithelium and present in all tissues tested (skin, lung, trachea, kidney, womb, and brain). Immunostaining with rabbit polyclonal antibody raised against the 28-kDa peroxiredoxin revealed the particularly high level of the 28-kDa peroxiredoxin immunoreactivity in air-contacting areas (apical regions and mucus of the olfactory and respiratory epithelium and skin epidermis), which are continually exposed to numerous air-borne reactive oxygen species. In the apical regions of the olfactory and respiratory epithelium, the 28-kDa-peroxiredoxin immunogold labeling outlined microvilli and cilia and was mainly located in sustentacular cells and in respiratory and goblet cells, as electron-microscopic analysis revealed. In skin epidermis, the 28-kDa peroxiredoxin immunoreactivity was confined to the granular layer and specifically concentrated in sebaceous glands of hair follicle. In situ hybridization with 33P-labeled antisense RNA probe revealed the expression of the 28-kDa peroxiredoxin mRNA in tissues with a high level of the 28-kDa peroxiredoxin immunoreactivity. Immunodepletion of the 28-kDa peroxiredoxin profoundly decreased the antioxidant activity of the olfactory tissue extract.

Animals↗
PubMed1999

Microwaves and cellular immunity. I. Effect of whole body microwave irradiation on tumor necrosis factor production in mouse cells.

Whole body microwave sinusoidal irradiation of male NMRI mice with 8.15-18 GHz (1 Hz within) at a power density of 1 microW/cm2 caused a significant enhancement of TNF production in peritoneal macrophages and splenic T lymphocytes. Microwave radiation affected T cells, facilitating their capacity to proliferate in response to mitogenic stimulation. The exposure duration necessary for the stimulation of cellular immunity ranged from 5 h to 3 days. Chronic irradiation of mice for 7 days produced the decreasing of TNF production in peritoneal macrophages. The exposure of mice for 24 h increased the TNF production and immune proliferative response, and these stimulatory effects persisted over 3 days after the termination of exposure. Microwave treatment increased the endogenously produced TNF more effectively than did lipopolysaccharide, one of the most potential stimuli of synthesis of this cytokine. The role of microwaves as a factor interfering with the process of cell immunity is discussed.

Animals↗
PubMed1999

Microwaves and cellular immunity. II. Immunostimulating effects of microwaves and naturally occurring antioxidant nutrients.

The effect of 8.15-18 GHz (1 Hz within) microwave radiation at a power density of 1 microW/cm2 on the tumor necrosis factor (TNF) production and immune response was tested. A single 5 h whole-body exposure induced a significant increase in TNF production in peritoneal macrophages and splenic T cells. The mitogenic response in T lymphocytes increased after microwave exposure. The activation of cellular immunity was observed within 3 days after exposure. The diet containing lipid-soluble nutrients (beta-carotene, alpha-tocopherol and ubiquinone Q9) increased the activity of macrophages and T cells from irradiated mice. These results demonstrate that irradiation with low-power density microwaves stimulates the immune potential of macrophages and T cells, and the antioxidant treatment enhances the effect of microwaves, in particular at later terms, when the effect of irradiation is reduced.

Animals↗
PubMed1998

Identification of a 28 kDa secretory protein from rat olfactory epithelium as a thiol-specific antioxidant.

The 28 kDa secretory protein is one of the abundant water-soluble proteins in olfactory epithelium of mammals. Analysis of partial amino acid sequence of the 28 kDa protein strongly suggested that it belongs to a new family of highly conserved antioxidant proteins requiring thiol for their antioxidant activity (TSA/AhpC family). In the present study, we found the 28 kDa protein to have thiol-dependent antioxidant activity, thereby protecting radical-sensitive proteins such as glutamine synthetase and hemoglobin from oxidative modification caused by thiol-dependent metal ion-catalyzed oxidation system. The purified 28 kDa protein did not possess catalase or glutathione peroxidase activities, and required thiols to exhibit its antioxidant activity. The 28 kDa protein is the first member of the family of thiol-specific antioxidants identified in olfactory epithelium and the first secretory protein shown to be thiol-specific antioxidant.

Animals↗
PubMed1998

[Study of structure of secretory 28 kDa protein from the rat olfactory epithelium].

Clone lambda a26.1 isolated from rat olfactory epithelium contains a full-length 28-kDa protein cDNA (1414 b.p.). The reconstructed protein sequence comprises 223 aa with a calculated molecular mass of 24,630 Da. A substantial homology was revealed between the amino acid sequence of the 28-kDa protein and those of thiol-specific antioxidants (peroxiredoxines). The 28-kDa protein belongs to the 1 Cys-subfamily of peroxiredoxines and is the first member of peroxiredoxines identified in the olfactory epithelium.

Amino Acid Sequence↗
PubMed1996

Novel 28-kDa secretory protein from rat olfactory epithelium.

We have isolated a novel secretory 28-kDa protein which is an abundant component of the rat olfactory mucosa. The partial sequence of the 28-kDa protein has been determined. The amino acid sequence of the 28-kDa protein is similar to that of non-selenium glutathione peroxidase from bovine ciliary body. The 28-kDa protein catalyzed decomposition of the hydrogen peroxide as well as organic hydroperoxides by reduced glutathione and seems to be a member of the glutathion peroxidase family.

Amino Acid Sequence↗
PubMed1996

45-kDa GTP-binding protein from rat olfactory epithelium: purification, characterization and localization.

The rat olfactory epithelium contains a specific water-soluble 45-kDa protein. This protein is recognized by anti-peptide antibodies which react with alpha-subunits of the known G-proteins. The 45-kDa protein has been isolated using DEAE-chromatography and gel-exclusion chromatography. The content of 45-kDa protein is about 2% of the total soluble proteins of the olfactory mucosa and it is located at the mucociliary surface. According to photo-affinity labeling, the 45-kDa protein possesses a high affinity to GTP and exhibits low GTP hydrolytic activity. The functions of the 45-kDa protein are discussed.

Affinity Labels↗
PubMed1995

Changes in the state of water, induced by radiofrequency electromagnetic fields.

Microwave irradiation (f = 36 GHz) changes the properties of distilled water within the first 1-10 min. The new state is retained for at least tens of minutes and manifests itself as changes in power density spectrum of periodic fading voltage fluctuations that are generated during discharge of a capacitor in which water is used as a dielectric. It is assumed that long-term changes in water properties mediate the effect of electromagnetic fields on biological systems.

Microwaves↗
PubMed1995

Preliminary microwave irradiation of water solutions changes their channel-modifying activity.

Earlier we have shown that millimetre microwaves (42.25 GHz) of non-thermal power, upon direct admittance into an experiment bath, greatly influence activation characteristics of single Ca(2+)-dependent K+ channels (in particular, the channel open state probability, Po). Here we present new data showing that similar changes in Po arise due to the substitution of a control bath solution for a preliminary microwave irradiated one of the same composition (100 mmol/l KCl with Ca2+ added), with irradiation time being 20-30 min. Therefore, due to the exposure to the field the solution acquires some new properties that are important for the channel activity. The irradiation terminated, the solution retains a new state for at least 10-20 min (solution memory). The data suggest that the effects of the field on the channels are mediated, at least partially, by changes in the solution properties.

Animals↗
PubMed1995

Dual effects of microwaves on single Ca(2+)-activated K+ channels in cultured kidney cells Vero.

Using the patch voltage-clamp method, possible effects of millimetre microwaves (42.25 GHz) on single Ca(2+)-activated K+ channels in cultured kidney cells (Vero) were investigated. It was found that exposure to the field of non-thermal power (about 100 microW/cm2) for 20-30 min greatly modifies both the Hill coefficient and an apparent affinity of the channels for Ca2+(i). The data suggest that the field alters both cooperativity and binding characteristics of the channel activation by internal Ca2+. The effects depend on initial sensitivity of the channels to Ca2+ and the Ca2+ concentration applied.

Animals↗
PubMed1994

Water-soluble GTP-binding protein from rat olfactory epithelium.

Rat olfactory epithelium and ciliar cytosol of olfactory cells contained the water-soluble 45 kDa protein which was revealed by antibodies against a peptide fragment of the alpha-subunits common to the G-proteins. No analogous proteins were found in other rat tissues. According to the photo-affinity labeling, the 45 kDa protein possessed a high affinity to GTP; it also exhibited a low GTP hydrolytic activity.

Amino Acid Sequence↗
PubMed1993

On the activation of phosphodiesterase by a 26 kDa protein.

The effects of a 26 kDa protein isolated from vertebrate retina rod outer segments (ROS) and its reconstituted analog on the phosphodiesterase (PDE) activity and cGMP-dependent conductance have been studied [Nature 313 (1985) 310-313]. Using the patch-clamp technique it was shown that the 26 kDa protein in concentrations up to 1 microM accelerates hydrolysis of cGMP by near-membrane PDE by 1-2 orders of magnitude. This process is suggested to be mediated by some intracellular agent. At the same concentrations the 26 kDa protein was shown to inhibit cGMP-dependent conductance of the photoreceptor membrane. A possible role of these effects in the processes of phototransduction and adaptation is discussed.

Animals↗
PubMed1992

Low molecular mass phosphoproteins from the frog rod outer segments form a complex with 48 kDa protein.

Upon separation of cAMP-dependent low molecular mass phosphoproteins [Components I and II; Polans et al. (1979) J. gen. Physiol. 74, 595-613] from the frog rod outer segments by gel-chromatography, isoelectric focusing, non-denaturating electrophoresis and ion-exchange chromatography, they behave like subunits of the oligomeric complex. Apparent molecular mass of the complex determined by gel-chromatography is 52-57 kDa and by non-denaturating gradient electrophoresis is 62-66 kDa. The isoelectric point of the complex is 5.5. The elution profile of Components I and II upon gel-chromatography and ion-exchange chromatography coincides with that of major rod outer segment 48 kDa protein. The isoelectric point for them also coincides with the isoelectric point of 48 kDa protein. The amount of low molecular mass phosphoproteins is sealed rods is equal to one molecule per 60 rhodopsin molecules and coincides with that of a 48 kDa protein. It is suggested that in solution Components I and II form an oligomeric complex with 48 kDa protein.

Animals↗
PubMed1991

Antiidiotypic antibodies against anti-cGMP polyclonal antibodies.

Affinity-purified polyclonal anti-cGMP antibodies were obtained from rabbit serum after immunization by succinyl derivative of cGMP coupled to bovine serum albumin. These antibodies were used to raise antiidiotypic antibodies in rats. Putative antiidiotypic serum inhibited the binding of [3H]cGMP to affinity-purified anti-cGMP antibodies. The influence of immunoglobulins isolated from antiidiotypic serum on the ion conductance of rod outer segment plasma membrane fragments from frog retina was studied in patch-clamp experiments. These immunoglobulins increased the conductance of ion channels acting like a natural agonist (cGMP). Preimmune immunoglobulins did not act. The data obtained suggest that antiidiotypic antibodies interact with regulatory cGMP-binding sites of the plasma membrane channels.

Animals↗
PubMed1991

Antiidiotypic antibodies interacting with cGMP-dependent channels of frog retinal rod outer segments.

Antiidiotypic approach was used to obtain antibodies interacting with cGMP-binding site of the cGMP-activated channel of the photoreceptor cell. Monoclonal anti-BrcGMP antibodies having characteristics of binding of agonist and its analogs close to those for a natural receptor have been obtained. These antibodies were used to raise polyclonal antiidiotypic antibodies capable of interacting with a natural cGMP-receptor. Application of immunoglobulins, isolated from antiidiotypic serum, to inside-out fragments of the rod plasma membrane led to an irreversible increase of the conductance of cGMP-dependent channels.

Animals↗
PubMed1990

[An analysis of the supramolecular organization of the olfactory neuroepithelium in the rat by freeze etching with rotary platinum-carbon shadow-casting].

The rat olfactory epithelium was analysed by freeze-deep etching and Pt/C rotary replication. Ultrathin sections and freeze-etching findings of proximal (dendrite) and distal (axon) parts of bipolar olfactory neurons are examined. The supramolecular organization of neuron membranes and intracellular cytoskeleton structure is studied. The role of the Schwann cells in formation of isolated axon bundles is discussed. Methods of the whole neuroepithelium preparation for freeze-etching and different easy approaches of obtaining the Pt/C rotary shadowing replicas with high resolution (15-20A) are presented.

Animals↗