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Biomedical subjects

V V Rogovin

Publications and source records attributed to V V Rogovin.

At least 19 recordsLinked to original sources
PubMed1982

[Complex electron microscopic cytochemical and stereological study of the action of clofibrate on peroperoxidasosome volume and count in the neutrophilic leukocytes of mouse bone marrow].

The distribution of peroxidase activity in maturing neutrophils of intact mice and of mice treated with clofibrate for a fortnight is studied. The product of peroxidase reaction in neutrophil promyelocytes in experimental and control animals is localized in the perinuclear cisternae, cisternae of RER and Golgi complexo and in primary granules. Peroxidases activity disappears from the secretory apparatus upon the neutrophil maturation. In the mature cells, the product of peroxidase reaction is seen only in the primary granules. Stereological method showed that the volume of peroxidase positive granules in intact and experimental animals decreased by 2.5 times. Clofibrate increases the volume of the primary granules by two times but exerts no effect on the quantity of these organelles.

Animals↗
PubMedDate not supplied

[The peroxisomes of eosinophilic leukocytes].

Functional properties of peroxidase-containing granules (peroxidasosomes) of eosinophiles are discussed. Findings are reported on the activities of peroxidase systems and of non-enzymic cationic proteins which occur in the eosinophilic peroxidasosomes in normal state and in various pathological states as well as their antimicrobial and antiparasitic activities.

Animals↗
PubMedDate not supplied

[The antimicrobial proteins and peptides of neutrophilic leukocytes].

Findings suggesting a vast variety of non-enzymic cationic proteins and peptides in human and animal leucocytes are reported. These cationic proteins and peptides demonstrate their antimicrobial and cytotoxic properties due to their detergent characteristics and their capacity to change the permeability of cellular wall and membrane by electrostatic interactions. Information on their homology with some serine proteases is presented.

Animals↗
PubMedDate not supplied

[Peroxisomes in human neutrophils].

Complex electronocytochemical and stereological methods showed that human neutrophil contained usually 442 +/- 14 peroxidasosomes, which occupied 7.8 +/- 0.2% of the cell cytoplasm volume (nuclear volume excluded). The mean diameter of the peroxidasosome was 406 +/- 14 nm and the volume--3.5 +/- 0.09 X 10(7) nm3. The EPR method exhibited that approximately 2.2 X 10(7) molecules of myeloperoxidase contained in each neutrophil, i.e. one peroxidasosome included about 5 X 10(4) molecules of myeloperoxidase.

Electron Spin Resonance Spectroscopy↗
PubMedDate not supplied

Electron cytochemistry of peroxidase activity in neutrophils of the bone marrow of the frog Rana temporaria.

The bone marrow of the frog was studied during the spring and winter periods. During the winter period, one type of large granules in the neutrophils of the frog proved to be peroxidase-positive. The remaining, smaller granules are peroxidase-negative. In the spring, immature and mature neutrophils are encountered in the frog. The mature neutrophils of the frog in the spring and winter periods are analogous. The immature neutrophils contain peroxidase activity in the perinuclear space, the endoplasmic reticulum and some of the granules. Some of the peroxidase-containing granules are directly associated with the canals of the endoplasmic reticulum. In the immature neutrophils, during the formation of the peroxidase-containing granules, peroxidase-negative granules smaller in size are already present in the cytoplasm. Thus, the sequence of granule formation usual for mammals is apparently not observed in the neutrophils of certain amphibia. "Annular" mitochondria, encompassing part of the cytoplasm were detected in the neutrophils. These apparently represent a section through a spherical mitochondrion enveloping and isolating a certain zone of the cell. It is proposed that the mitochondria in this way, differing from the lysosomal mode, participate in the catabolism of the cytoplasm.

Animals↗