Antiapoptotic function of Bcl-2 in mast cells is dependent on its association with heat shock protein 90β

Blood ◽  
2006 ◽  
Vol 107 (4) ◽  
pp. 1413-1420 ◽  
Author(s):  
Cellina Cohen-Saidon ◽  
Irit Carmi ◽  
Avishai Keren ◽  
Ehud Razin
Keyword(s):  
Mast Cell ◽  
Rna Interference ◽  
Mast Cells ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Caspase 3 ◽  
Caspase 7 ◽  
Antiapoptotic Activity ◽  
Novel Strategy ◽  
First Time

In the present study, we demonstrated that the antiapoptotic function of Bcl-2 in mast cells is significantly dependent on its association with the heat shock protein 90β (Hsp90β). Dissociation of these 2 proteins inhibits the antiapoptotic activity of Bcl-2 by initiating the release of cytochrome c from mitochondria into cytosol and increasing the activity of caspase 3 and caspase 7, resulting in mast-cell apoptosis. The antiapoptotic activity of Bcl-2 was greatly affected by knocking-out specifically Hsp90β using the RNA interference approach. Thus, for the first time, it has been shown that Hsp90β might modulate the antiapoptotic activity of Bcl-2 at least in mast cells. These findings could have implications for a novel strategy of regulating apoptosis in patients with mastocytosis and other mast cell–associated diseases.

Isolation and Structure Determination of a Heat Shock Protein Inducer, Asparagus-Derived Proline-Containing 3-Alkyldiketopiperazines (Asparaprolines), From a Standardized Extract of Asparagus officinalis Stem

2020 ◽  
Vol 15 (3) ◽  
pp. 1934578X2091468
Author(s):  
Shoichiro Inoue ◽  
Jun Takanari ◽  
Keima Abe ◽  
Ayako Nagayama ◽  
Yukinobu Ikeya ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Spectroscopic Data ◽  
Asparagus Officinalis ◽  
Hsp70 Mrna ◽  
Mrna Induction ◽  
Natural Amino Acids ◽  
First Time ◽  
Hsp70 Induction

ETAS® has been developed from the stems of Asparagus officinalis L. as a functional ingredient for nutraceuticals. ETAS possesses heat shock protein 70 (HSP70) induction activity and may contribute to maintenance and improvement of health. Here, 3 compounds (1, 2, 3) were isolated from ETAS. The structures of 1, 2, and 3 were deduced by HREIMS and NMR spectroscopic data, and the compounds were identified as cyclo(l-Phe-l-Pro), cyclo(l-Tyr-l-Pro), and cyclo(l-Leu-l-Pro), respectively. Each compound contained a diketopiperazine ring derived from proline with an alkyl group at C-3; thus, we termed them asparagus-derived proline-containing 3-alkyldiketopiperazines (Asparaprolines). In an HSP70 mRNA induction assay in HL-60 cells, Asparaprolines significantly enhanced the expression of HSP70 mRNA compared with a control. To our knowledge, these results demonstrate for the first time that proline-containing diketopiperazines derived from natural amino acids exhibit HSP70 mRNA induction activity.

scholarly journals Knockdown of the small heat-shock protein p26 by RNA interference modifies the diapause proteome of Artemia franciscana

2019 ◽  
Vol 97 (4) ◽  
pp. 471-479
Author(s):  
Hajer Salem Malitan ◽  
Alejandro M. Cohen ◽  
Thomas H. MacRae
Keyword(s):  
Rna Interference ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Stress Tolerance ◽  
Small Heat Shock Protein ◽  
Isotopic Labeling ◽  
Artemia Franciscana ◽  
Signal Transducers ◽  
Translation Factors

Embryos of the crustacean Artemia franciscana may arrest as gastrulae, forming cysts that enter diapause, which is a state of reduced metabolism and enhanced stress tolerance. Diapausing cysts survive physiological stresses for years due, in part, to molecular chaperones. p26, a small heat-shock protein, is an abundant diapause-specific molecular chaperone in cysts, and it affects embryo development and stress tolerance. p26 is therefore thought to influence many proteins in cysts, and this study was undertaken to determine how the loss of p26 by RNA interference (RNAi) affects the diapause proteome of A. franciscana. The proteome was analyzed by shot-gun proteomics coupled to differential isotopic labeling and tandem mass spectrometry. Proteins in the diapause proteome included metabolic enzymes, antioxidants, binding proteins, structural proteins, transporters, translation factors, receptors, and signal transducers. Proteins within the diapause proteome either disappeared or were reduced in amount when p26 was knocked down, or conversely, proteins appeared or increased in amount. Those proteins that disappeared may be p26 substrates, whereas the synthesis of those proteins that appeared or increased may be regulated by p26. This study provides the first global characterization of the diapause proteome of A. franciscana and demonstrates that the sHsp p26 influences proteome composition.

scholarly journals Detection of 70 kDa heat shock protein in the saliva of dairy cows

2017 ◽  
Vol 84 (3) ◽  
pp. 280-282 ◽  
Author(s):  
Elsa Lamy ◽  
Viktor Jurkovich ◽  
Lénia Rodrigues ◽  
Ana Geraldo ◽  
Liliana Cachucho ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Dairy Cows ◽  
Cellular Response ◽  
Holstein Friesian ◽  
Elisa Technique ◽  
Animal Growth ◽  
Cattle Blood ◽  
Shock Proteins ◽  
First Time

This Research Communication describes, for the first time, the detection of HSP70 in saliva of dairy cows. Thermal stress is a major environmental stress that limits animal growth, metabolism, and productivity. The cellular response to heat stress involves the synthesis of heat shock proteins (HSPs), presumably to protect the functional stability of cells at increasing temperatures. HSP70 has been found to be present in cattle blood serum and may also be present in other secretory fluids, such as saliva, as already observed in humans. The aim of this study was to detect heat shock protein HSP70 in bovine saliva. Saliva samples were taken from higher- (n = 5) and lower milk producing (n = 5) Holstein-Friesian cows in summer and in winter for the detection of HSP70. HSP70 concentrations were assayed using the ELISA technique. Salivary HSP70 concentrations ranged from 0·524 to 12·174 ng/ml in cows. Higher salivary HSP70 concentrations were significantly associated with higher milk production and higher environmental temperature, but not with rectal temperature.

scholarly journals Altered Expression of Heat Shock Protein-27 and Monocyte Chemoattractant Protein-1 after Acute Spinal Cord Injury: A Pilot Study

2019 ◽  
Vol 10 (03) ◽  
pp. 452-458
Author(s):  
Vidyasagar Boraiah ◽  
Shweta Modgil ◽  
Kaushal Sharma ◽  
Vivek Podder ◽  
Madhava Sai Sivapuram ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Spinal Cord Injury ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Caspase 3 ◽  
Monocyte Chemoattractant Protein 1 ◽  
Monocyte Chemoattractant ◽  
Monocyte Chemoattractant Protein ◽  
Hsp 27 ◽  
Cord Injury

Abstract Background Spinal cord injury (SCI) leads to serious complications involving primary trauma and progressive loss due to inflammation, local ischemia, or infection. Despite a worldwide annual incidence of 15 to 40 cases per million, methylprednisolone is the only treatment available to alleviate neurologic dysfunction; therefore, research is currently focused on identifying novel targets by biochemical and molecular studies. Purpose Here, we investigated the expression of various molecular markers at the messenger ribonucleic acid (mRNA) and protein level at day 0 and day 30 post-SCI. Methods Enzyme-linked immunosorbent assay (ELISA) was performed to determine the expression of CASPASE-3 and heat shock protein-27 (HSP-27) in serum samples. Real-time polymerase chain reaction (RT-PCR) was performed to determine the level of mRNA expression of vascular endothelial growth factor receptor-1 (VEGFR-1), VEGFR-2, HSP-27, monocyte chemoattractant protein-1 (MCP-1), and CASPASE-3. Results HSP-27 expression at day 30, as compared with day 0, showed significant downregulation. In contrast, there was elevated expression of MCP-1. ELISA analysis showed no significant change in the expression of CASPASE-3 or HSP-27. Conclusion There may be possible opposing role of HSP-27 and MCP-1 governing SCI. Their association can be studied by designing in vitro studies.

Thermal stress induces heat shock protein 70 and apoptosis during embryo development in a Neotropical freshwater fish

2019 ◽  
Vol 31 (3) ◽  
pp. 547 ◽  
Author(s):  
Camila F. Sales ◽  
Flavia S. Lemos ◽  
Roberto D. V. S. Morais ◽  
Ralph G. Thomé ◽  
Helio B. Santos ◽  
...  
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Embryo Development ◽  
Caspase 3 ◽  
Control Group ◽  
Tunel Reaction ◽  
Group 3 ◽  
Group 2 ◽  
Group 1

Fish embryos are particularly vulnerable to temperature changes, with the effects varying with developmental stage. The major aim of the present study was to analyse the relationship between apoptosis and heat shock protein (HSP) 70 during embryo development under thermal stress conditions. To this end, Prochilodus lineatus embryos at the blastopore closure stage were subjected to one of three thermal treatments for 1h (Group 1, 25°C (control); Group 2, 20°C; Group 3, 30°C) and then examined at 0, 4 and 8h posttreatment (h.p.t.). The viability of embryos was highest in Group 1 (81.33±16.65%), followed by Group 3 and Group 2 (75.33±12.10% and 68.67±16.86% respectively), with significant difference between Groups 1 and 2 (P<0.05). At 0h.p.t., embryos subjected to thermal stress (Group 3) had a significantly higher number of terminal deoxyribonucleotidyl transferase-mediated dUTP–digoxigenin nick end-labelling (TUNEL)- and caspase-3-labelled cells, and a lower number of HSP70-positive cells than those in the control group. At 4h.p.t., there was a decrease in the TUNEL reaction and an increase in HSP70 in embryos in Group 3. At 8h.p.t., the size of Group 3 embryos was significantly smaller than that of Group 1 embryos. The results indicate a cytoprotective role for HSP70, regulating caspase-3-mediated apoptosis during embryo development of P. lineatus; however, this mechanism is not effective in controlling embryo viability and larval malformations.

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