Effects of heat and freeze on isolated erythrocyte submembrane skeletons

Ivanov, Ivan T.; Paarvanova, Boyana; Ivanov, V. N.; Smuda, Kathrin; Bäumler, Hans; Georgieva, Radostina

doi:10.4149/gpb_2016046

Cited by 11 publications

(9 citation statements)

References 34 publications

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“…Under natural conditions, temperature greatly influences insect growth and development, their basic behavior, and evolutionary path (Lee and Denlinger, 1991 ). Lee ( 1989 ) defined cold tolerance as the survival ability of a living creature exposed to low temperature, for a long or short time, according to seasonal environmental changes, genetic factors, nutritional status, and the length of exposure to low temperature. Insects have evolved a variety of cold-resistance measures (Jing and Kang, 2002 ), mainly including ecological (or behavior) and physiological aspects.…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning and Induced Expression of Six Small Heat Shock Proteins Mediating Cold-Hardiness in Harmonia axyridis (Coleoptera: Coccinellidae)

et al. 2017

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The main function of small heat shock proteins (sHSPs) as molecular chaperones is to protect proteins from denaturation under adverse conditions. Molecular and physiological data were used to examine the sHSPs underlying cold-hardiness in Harmonia axyridis. Complementary DNA sequences were obtained for six H. axyridis sHSPs based on its transcriptome, and the expression of the genes coding for these sHSPs was evaluated by quantitative real-time PCR (qRT-PCR) in several developmental stages, under short-term cooling or heating conditions, and in black and yellow females of experimental and overwintering populations under low-temperature storage. In addition, we measured water content and the super cooling and freezing points (SCP and FP, respectively) of H. axyridis individuals from experimental and overwintering populations. The average water content was not significantly different between adults of both populations, but the SCP and FP of the overwintering population were significantly lower than that of the experimental population. Overall, the six sHSPs genes showed different expression patterns among developmental stages. In the short-term cooling treatment, Hsp16.25 and Hsp21.00 expressions first increased and then decreased, while Hsp10.87 and Hsp21.56 expressions increased during the entire process. Under short-term heating, the expressions of Hsp21.00, Hsp21.62, Hsp10.87, and Hsp16.25 showed an increasing trend, whereas Hsp36.77 first decreased and then increased. Under low-temperature storage conditions, the expression of Hsp36.77 decreased, while the expressions of Hsp21.00 and Hsp21.62 were higher than that of the control group in the experimental population. The expression of Hsp36.77 first increased and then decreased, whereas Hsp21.56 expression was always higher than that of the control group in the overwintering population. Thus, differences in sHSPs gene expression were correlated with the H. axyridis forms, suggesting that the mechanism of cold resistance might differ among them. Although, Hsp36.77, Hsp16.25, Hsp21.00, and Hsp21.62 regulated cold- hardiness, the only significant differences between overwintering and experimental populations were found for Hsp16.25 and Hsp21.00.

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Section: Introductionmentioning

confidence: 99%

Molecular Cloning and Induced Expression of Six Small Heat Shock Proteins Mediating Cold-Hardiness in Harmonia axyridis (Coleoptera: Coccinellidae)

et al. 2017

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“…This is the temperature of spectrin denaturation [29]. Total damage to spectrin filaments can lead to alterations in the spectrin matrix as a whole, in turn leading to changes in RBC morphology.…”

Section: Resultsmentioning

confidence: 99%

“…Special attention was given to temperature in the range of 49–50°C, at which spectrin denaturation occurs [29]. This leads to the RBC membrane in vitro to lose its stability [29].…”

Section: Discussionmentioning

confidence: 99%

Conformational Distortions of the Red Blood Cell Spectrin Matrix Nanostructure in Response to Temperature Changes In Vitro

et al. 2019

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The spectrin matrix is a structural element of red blood cells (RBCs). As such, it affects RBC morphology, membrane deformability, nanostructure, stiffness, and, ultimately, the rheological properties of blood. However, little is known about how temperature affects the spectrin matrix. In this study, the nanostructure of the spectrin network was recorded by atomic force microscopy. We describe how the nanostructure of the RBC spectrin matrix changes from a regular network to a chaotic pattern following an increase in temperature from 20 to 50°C. At 20–37°С, the spectrin network formed a regular structure with dimensions of typically 150±60 nm. At 42–43°С, 83% of the spectrin network assumed an irregular structure. Finally, at 49–50°С the chaotic pattern was observed, and no quantitative estimates of the spectrin structure’s parameters could be made. These results can be useful for biophysical studies on the destruction of the spectrin network under pathological conditions, as well as for investigating cell morphology and blood rheology in different diseases.

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“…Нагрівання еритроцитів до температур вище +45 °С широко використовується для вивчення явища термічного гемолізу, функці ональних якостей крові після опіків, а також як структурна модифікація клітин і їх мембран для проведення будь-якого подальшого дослі дження [4,11]. Використання модифікуючих властивостей температури ґрунтується на ві домих фактах термічної денатурації протеїнів цитоскелету, зокрема спектрину і анкирину.…”

Section: результати й обговоренняunclassified

“…Використання модифікуючих властивостей температури ґрунтується на ві домих фактах термічної денатурації протеїнів цитоскелету, зокрема спектрину і анкирину. Для еритроцитів людини темрература +49 °С відповідає тепловому переходу спектрину, для щурів -анкирину [4,13]. У роботі [13] було показано, що термоінактіваційні температури для більшості мембранних білків в людських і щурячих еритроцитах дуже різні, що свід чить про суттєві відмінності в розташуванні їх мембранних каркасів.…”

Section: результати й обговоренняunclassified