8 research outputs found

    Category Features of Toast as Small Speech Genre

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    Toasts logically fit into modern cultural space, including folklore. Folklore as a field of artistic creativity is widely spread in a variety of forms and types in modern reality. This phenomenon is dynamic, evolving, and quickly transformable; within humanitarian knowledge it interacts with such concise concepts as post-folklore, subculture; it reflects quality changes of public and everyday life of our era. Conceptually, the subject field of urban folklore is fairly well understood and even developed despite its specifics and complexity

    Category Features of Toast as Small Speech Genre

    No full text
    Toasts logically fit into modern cultural space, including folklore. Folklore as a field of artistic creativity is widely spread in a variety of forms and types in modern reality. This phenomenon is dynamic, evolving, and quickly transformable; within humanitarian knowledge it interacts with such concise concepts as post-folklore, subculture; it reflects quality changes of public and everyday life of our era. Conceptually, the subject field of urban folklore is fairly well understood and even developed despite its specifics and complexity

    Distribution, phosphorylation, and activities of Hsp25 in heat-stressed H9c2 myoblasts: a functional link to cytoprotection

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    The behavior of the endogenous heat shock protein 25 (Hsp25) in heat-stressed rat H9c2 myoblasts was studied. After mild or severe heating, this protein became less extractable with Triton X-100 and displayed characteristic immunofluorescence patterns, namely (1) granules in the nucleus, and (2) association with F-actin bundles in the cytoplasm. The intranuclear granulation of Hsp25 and its association with F-actin were sensitive to drugs affecting Hsp25 phosphorylation (cantharidin, sodium orthovanadate, SB203580, SB202190). Isoform analysis of Hsp25 translocated to the nucleus-free cytoskeletal fraction revealed only mono- and biphosphorylated Hsp25 and no unphosphorylated Hsp25. Transfected luciferase with initial localization in the nucleosol became colocalized with the Hsp25-containing granules after a heat shock treatment that denatured the enzyme in the cells. The association of Hsp25 with actin filaments after a mild heat stress conferred protection from subsequent F-actin–damaging treatments with cytochalasins (D and B) or severe heat stress. We hypothesize that (1) the binding of heat-denatured nucleosolic proteins to the Hsp25 contained in specific granular structures may serve for the subsequent chaperoning or degradation of the bound proteins, and (2) the actin cytoskeleton is stabilized by the direct targeting of phosphorylated Hsp25 to microfilament bundles

    Pilot studies of age-related changes in blood perfusion in two different types of skin

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    Abstract Laser Doppler flowmetry (LDF) was utilized to assess age-related changes in the blood microcirculation at the skin sites with different morphology and regulation. The LDF signals obtained from the glabrous skin of the middle finger pad and nonglabrous skin on the dorsal wrist surface were analyzed. Statistically higher baseline perfusion was observed in the zone with glabrous skin in the older group of volunteers compared to younger participants. Observed site-specific and age-related differences in perfusion can be used in the future experimental design for the studies of the blood microcirculation system in patients with different pathologies

    Regulation of stress-induced intracellular sorting and chaperone function of Hsp27 (HspB1) in mammalian cells

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    In vitro, small Hsps (heat-shock proteins) have been shown to have chaperone function capable of keeping unfolded proteins in a form competent for Hsp70-dependent refolding. However, this has never been confirmed in living mammalian cells. In the present study, we show that Hsp27 (HspB1) translocates into the nucleus upon heat shock, where it forms granules that co-localize with IGCs (interchromatin granule clusters). Although heat-induced changes in the oligomerization status of Hsp27 correlate with its phosphorylation and nuclear translocation, Hsp27 phosphorylation alone is not sufficient for effective nuclear translocation of HspB1. Using firefly luciferase as a heat-sensitive reporter protein, we demonstrate that HspB1 expression in HspB1-deficient fibroblasts enhances protein refolding after heat shock. The positive effect of HspB1 on refolding is completely diminished by overexpression of Bag-1 (Bcl-2-associated athanogene), the negative regulator of Hsp70, consistent with the idea of HspB1 being the substrate holder for Hsp70. Although HspB1 and luciferase both accumulate in nuclear granules after heat shock, our results suggest that this is not related to the refolding activity of HspB1. Rather, granular accumulation may reflect a situation of failed refolding where the substrate is stored for subsequent degradation. Consistently, we found 20S proteasomes concentrated in nuclear granules of HspB1 after heat shock. We conclude that HspB1 contributes to an increased chaperone capacity of cells by binding unfolded proteins that are hereby kept competent for refolding by Hsp70 or that are sorted to nuclear granules if such refolding fails
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