Association of Hsp60 expression with damage to rat myocardial cells exposed to heat stress in vivo and in vitro

Mortalin/mtHsp70 (mitochondrial Hsp70) and HSP60 (heat-shock protein 60) are heat-shock proteins that reside in multiple subcellular compartments, with mitochondria being the predominant one. In the present study, we demonstrate that the two proteins interact both in vivo and in vitro, and that the N-terminal region of mortalin is involved in these interactions. Suppression of HSP60 expression by shRNA (short hairpin RNA) plasmids caused the growth arrest of cancer cells similar to that obtained by suppression of mortalin expression by ribozymes. An overexpression of mortalin, but not of HSP60, extended the in vitro lifespan of normal fibroblasts (TIG-1). Taken together, this study for the first time delineates: (i) molecular interactions of HSP60 with mortalin; (ii) their co- and exclusive localizations in vivo; (iii) their involvement in tumorigenesis; and (iv) their functional distinction in pathways involved in senescence.

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In vitro evaluation of aspirin-induced HspB1 against heat stress damage in chicken myocardial cells

Cell Stress and Chaperones ◽

10.1007/s12192-016-0666-8 ◽

2016 ◽

Vol 21 (3) ◽

pp. 405-413 ◽

Cited By ~ 18

Author(s):

Di Wu ◽

Miao Zhang ◽

Jiao Xu ◽

Erbao Song ◽

Yinjun Lv ◽

...

Keyword(s):

Heat Stress ◽

Myocardial Cells ◽

In Vitro Evaluation ◽

Stress Damage

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319 The protective effects of ButipearlTM Z during heat stress as measured through in vitro studies with swine intestinal epithelial cells and an in vivo swine trial

Journal of Animal Science ◽

10.2527/msasas2016-319 ◽

2016 ◽

Vol 94 (suppl_2) ◽

pp. 150-150

Author(s):

V. Mani ◽

J. K. Rubach ◽

D. A. Koltes ◽

N. K. Gabler ◽

M. J. Poss

Keyword(s):

Heat Stress ◽

Epithelial Cells ◽

Intestinal Epithelial Cells ◽

In Vitro Studies ◽

Protective Effects ◽

Intestinal Epithelial

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Responses of tobacco pollen to high humidity and heat stress: viability and germinability in vitro and in vivo

Sexual Plant Reproduction ◽

10.1007/bf00196495 ◽

1991 ◽

Vol 4 (2) ◽

Cited By ~ 37

Author(s):

K.R. Shivanna ◽

H.F. Linskens ◽

M. Cresti

Keyword(s):

Heat Stress ◽

High Humidity ◽

Tobacco Pollen

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Interplay of Structural Disorder and Short Binding Elements in the Cellular Chaperone Function of Plant Dehydrin ERD14

Cells ◽

10.3390/cells9081856 ◽

2020 ◽

Vol 9 (8) ◽

pp. 1856

Author(s):

Nikoletta Murvai ◽

Lajos Kalmar ◽

Bianka Szalaine Agoston ◽

Beata Szabo ◽

Agnes Tantos ◽

...

Keyword(s):

Heat Stress ◽

Intrinsically Disordered Proteins ◽

Stress Protein ◽

Structural Disorder ◽

Disordered Proteins ◽

Sequence Motifs ◽

E Coli ◽

Intrinsically Disordered

Details of the functional mechanisms of intrinsically disordered proteins (IDPs) in living cells is an area not frequently investigated. Here, we dissect the molecular mechanism of action of an IDP in cells by detailed structural analyses based on an in-cell nuclear magnetic resonance experiment. We show that the ID stress protein (IDSP) A. thaliana Early Response to Dehydration (ERD14) is capable of protecting E. coli cells under heat stress. The overexpression of ERD14 increases the viability of E. coli cells from 38.9% to 73.9% following heat stress (50 °C × 15 min). We also provide evidence that the protection is mainly achieved by protecting the proteome of the cells. In-cell NMR experiments performed in E. coli cells show that the protective activity is associated with a largely disordered structural state with conserved, short sequence motifs (K- and H-segments), which transiently sample helical conformations in vitro and engage in partner binding in vivo. Other regions of the protein, such as its S segment and its regions linking and flanking the binding motifs, remain unbound and disordered in the cell. Our data suggest that the cellular function of ERD14 is compatible with its residual structural disorder in vivo.

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In VitroImmune Competence of Buffaloes (Bubalus bubalis) of Different Production Potential: Effect of Heat Stress and Cortisol

Veterinary Medicine International ◽

10.4061/2011/860252 ◽

2011 ◽

Vol 2011 ◽

pp. 1-5 ◽

Cited By ~ 2

Author(s):

Joydip Mukherjee ◽

Sujata Pandita ◽

Ruokuobeinuo Huozha ◽

Manju Ashutosh

Keyword(s):

Heat Stress ◽

Stimulation Index ◽

Bubalus Bubalis ◽

Potential Effect ◽

Production Level ◽

Cell Mediated Immunity ◽

Lymphocyte Proliferation Response ◽

Proliferation Response

Twelve healthy lactating Murrah buffaloes of similar parity (3rd) between 90 and 120 days of lactation, selected from the herd of National Dairy Research Institute (Karnal, India) and maintained at managemental practices as followed at the Institute they were included in this experiment. The animals were divided into two groups based on their production level in previous lactation. The average milk production level of group 1 and II was 9.3 and 6 lit/day, respectively. Blood was collected from these buffaloes on three occasions 10 days apart. The lymphocytes were separated and cultured in RPMI 1640 medium with PHA-P for 24 h at 37°C in a humidified CO2incubator (95% air and 5% CO2). The lymphocyte responsiveness was also evaluated in response to thein vivoheat stress andin vitrocortisol. Mitogen-induced stimulation index was not affected by production level (). Stimulation index was significantly reduced () in both the groups when cortisol was added at 2.0 ng level in the culture. However, in heat-stressed buffaloes stimulation index did not vary despite increasing levels of cortisol, thus indicating that lymphocyte may become cortisol resistant during periods of acute heat stress. The results showed that lymphocyte proliferation response can be effectively used to study buffalo cell-mediated immunityin vitro.

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