scholarly journals INFLUENCE OF PHENYLHYDRAZINE ON THE SENSITIVITY OF MAMMALIAN ERYTHROCYTES TO HYPERTONIC SHOCK

2018 ◽  
Vol 4.3 (141) ◽  
pp. 394 ◽  
Author(s):  
E. E. Nipot ◽  
N. A. Ershova ◽  
O. A. Shapkina ◽  
O. A. Lohinova ◽  
S. S. Ershov
Keyword(s):  
Hypertonic Shock

Comparative study of sensitivity of bovine and ram erythrocytes to post-hypertonic shock

2017 ◽  
Vol 19 (2) ◽  
pp. 64-69
Author(s):  
A. A. Mazur ◽  
◽  
E. Ye. Nipot ◽  
N. V. Orlova ◽  
N. M. Shpakova ◽  
...  
Keyword(s):  
Comparative Study ◽  
Hypertonic Shock

scholarly journals Bacteriorhodopsin induces a light-scattering change in Halobacterium halobium.

1978 ◽  
Vol 79 (3) ◽  
pp. 657-662 ◽  
Author(s):  
C L Wey ◽  
P L Ahl ◽  
R A Cone
Keyword(s):  
Absorption Spectrum ◽  
Light Scattering ◽  
Near Infrared ◽  
Action Spectrum ◽  
Bright Light ◽  
Infrared Region ◽  
Halobacterium Halobium ◽  
Scattering Response ◽  
Near Infrared Region ◽  
Hypertonic Shock

When suspensions of Halobacterium halobium are exposed to bright light, the light-scattering properties of the bacteria change. This light-scattering response can produce a transmission decrease of about 1% throughout the red and near-infrared region. The action spectrum for the light-scattering response appropriately matches the absorption spectrum of bacteriorhodopsin. The response is eliminated by cyanide p-trifluoro-methoxyphenylhydrazone, a proton ionophore, and by triphenylmethylphosphonium, a membrane permanent cation. A mild hypertonic shock induces a similar light-scattering change, suggesting that bright light causes the bacteria to shrink about 1% in volume, thereby producing the light-scattering response.

scholarly journals Glycerol Impact on Human and Bovine Erythrocytes Under Hypertonic Shock

2019 ◽  
Vol 29 (3) ◽  
pp. 199-205
Author(s):  
Olena Nipot ◽  
◽  
Natalya Yershova ◽  
Olga Shapkina ◽  
Sergiy Yershov ◽  
...  
Keyword(s):  
Hypertonic Shock ◽  
Bovine Erythrocytes

Stimulation of tubulin gene transcription by deciliation of sea urchin embryos

1987 ◽  
Vol 7 (12) ◽  
pp. 4238-4246
Author(s):  
Z Y Gong ◽  
B P Brandhorst
Keyword(s):  
Gene Transcription ◽  
Sea Urchin ◽  
Elevated Level ◽  
Elevated Concentration ◽  
Tubulin Gene ◽  
Lytechinus Pictus ◽  
Tubulin Genes ◽  
Tubulin Mrna ◽  
Hypertonic Shock ◽  
Stimulation Of

Deciliation by hypertonic shock of embryos of the sea urchin Lytechinus pictus resulted in an increase in synthesis of alpha- and beta-tubulins, the consequence of an increased concentration of RNA encoding the tubulins. RNA run-on assays in isolated nuclei indicated that this response is due to a transient increase in the rate of synthesis of tubulin RNA beginning within 5 min of deciliation. This enhancement of tubulin gene transcription also occurred in deciliated embryos treated with the microtubule-depolymerizing agent colcemid; thus the reaction to deciliation is not a response to a reduction in concentration of unpolymerized tubulin utilized for ciliogenesis. In deciliated embryos treated with colcemid, the elevated level of tubulin RNA declined rapidly, due to its destabilization by the elevated concentration of unpolymerized tubulin. The increased transcription of tubulin genes is a response to the loss of cilia, not to the hypertonic shock, and occurs even when cilium regeneration is prevented. Inhibition of protein synthesis with puromycin or emetine did not prevent the transcriptional enhancement but stabilized tubulin mRNA, resulting in increased accumulation of tubulin mRNA after deciliation.

Measurement of changes in cell volume based on fluorescence quenching

1997 ◽  
Vol 272 (4) ◽  
pp. C1405-C1414 ◽  
Author(s):  
S. P. Srinivas ◽  
J. A. Bonanno
Keyword(s):  
Fluorescence Quenching ◽  
Cell Volume ◽  
Signal To Noise Ratio ◽  
Regulatory Volume Decrease ◽  
Ringer Solution ◽  
Simple Relationship ◽  
Quenching Probe ◽  
Hypertonic Shock ◽  
Rate Limiting ◽  
Intracellular Fluorescence

The intracellular fluorescence of 6-methoxy-N-(3-sulfopropyl)-quinolinium (SPQ), a Cl(-) -sensitive fluorescent dye, is quenched by intracellular organic anions and proteins of unknown identity. The concentration of these intracellular quenchers (ICQs), however, is dependent on cell volume. In the absence of Cl-, changes in the observed SPQ fluorescence may therefore reflect changes in cell volume. This concept has been applied to determine relative changes in cell volume of cultured corneal endothelium in response to anisosmotic shocks, using NO3- as the Cl- substituent. SPQ fluorescence increased with decreasing osmolarity and vice versa. A 20 mosM hypertonic shock was needed to detect a change in SPQ fluorescence with a signal-to-noise ratio of >25. Assuming dynamic quenching by ICQs, we applied an extension of the Stern-Volmer equation to develop a simple relationship between the measured SPQ fluorescence and relative changes in cell volume. For large hyposmotic shocks, regulatory volume decrease (RVD) was observed. The rate of RVD could be enhanced by exposure to 0.5 microM gramicidin in low-Na+ Ringer solution (i.e., K+-NO3- efflux), indicating that K+ conductance is rate limiting for RVD. These results demonstrate the principle of using fluorescence quenching to measure changes in cell volume in real time. Because SPQ is sensitive to Cl-, its usefulness as a quenching probe is limited. However, a structure-activity study can be expected to yield useful Cl(-)-insensitive analogs.

scholarly journals Perturbation of the Nucleus: A Novel Hog1p-independent, Pkc1p-dependent Consequence of Hypertonic Shock in Yeast

2001 ◽  
Vol 12 (6) ◽  
pp. 1835-1841 ◽  
Author(s):  
Jayasri Nanduri ◽  
Alan M. Tartakoff
Keyword(s):  
Map Kinase ◽  
Rna Synthesis ◽  
Kinase Activity ◽  
Nuclear Proteins ◽  
Cell Integrity ◽  
Kinase C ◽  
Nucleolar Proteins ◽  
Map Kinase Cascade ◽  
Kinase Cascade ◽  
Hypertonic Shock

Hypertonic shock of Saccharomyces cerevisiaeactivates the Hog1p MAP kinase cascade. In contrast, protein kinase C (Pkc1p) and the “cell integrity” MAP kinase cascade are critical for the response to hypotonic shock. We observed that hypertonic shock transiently relocated many, but not all, nuclear and nucleolar proteins to the cytoplasm. We hypothesized that the relocation of nuclear proteins was due to activation of the Hog1p kinase cascade, yet, surprisingly, Hog1p was not required for these effects. In contrast, Pkc1p kinase activity was required, although the Pkc1p MAP kinase cascade and several factors known to lie upstream and downstream of Pkc1p were not. Moreover, sudden induction of a hyperactive form of Pkc1p was sufficient to relocate nuclear proteins. Taken together, these observations show that the scope of involvement of Pkc1p in the organization of the nucleus considerably exceeds what has been characterized previously. The relocation of nuclear proteins is likely to account for the profound inhibition of RNA synthesis that was observed during hypertonic shock.

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