Publications by authors named "Yan Yu Komissarchik"

We studied the ultrastructure of human histiocytic lymphoma U-937cells after apoptosis induction with two external agents, hypertonic shock and etoposide. Appearance of aggregates of particles of nuclear origin within the nuclei and cytoplasm of the induced cells was the first and the most prominent morphological sign of apoptosis. These aggregates were not coated by a membrane, had variable shape, density and size.

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α-Crystallin-type small heat shock proteins (sHsps) are expressed in many bacteria, animals, plants, and archaea. Among mycoplasmas (Mollicutes), predicted sHsp homologues so far were found only in the Acholeplasmataceae family. In this report, we describe the cloning and functional characterization of a novel sHsp orthologue, IbpA protein, present in Acholeplasma laidlawii.

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Immunoelectron microscopy was used to locate the proteins BASP1 and MARCKS in the post-meiotic spermatids of male rat testis. It was shown that in early spermatids, BASP1 and MARCKS accumulate in chromatoid bodies, which are characteristic organelles for these cells. During spermatogenesis, while the spermatid nucleus is still active, the chromatoid body periodically moves to the cell nucleus and absorbs the precursors of definite mRNAs and small RNAs.

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Earlier, we have shown that spontaneously isolated non-pathogenic bacteria Serratia grimesii and Serratia proteamaculans invade eukaryotic cells, provided that they synthesize thermolysin-like metalloproteases ECP32/grimelysin or protealysin characterized by high specificity towards actin. To address the question of whether the proteases are active players in entry of these bacteria into host cells, in this work, human larynx carcinoma Hep-2 cells were infected with recombinant Escherichia coli expressing grimelysin or protealysin. Using confocal and electron microscopy, we have found that the recombinant bacteria, whose extracts limitedly cleaved actin, were internalized within the eukaryotic cells residing both in vacuoles and free in cytoplasm.

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Microsporidia are obligatory intracellular parasites, most species of which live in the host cell cytosol. They synthesize and then transport secretory proteins from the endoplasmic reticulum to the plasma membrane for formation of the spore wall and the polar tube for cell invasion. However, microsporidia do not have a typical Golgi complex.

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