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 Cloning of the Heat Shock Protein 70 (HSP70) Gene of Ehrlichia sennetsu and Differential Expression of HSP70 and HSP60 mRNA after Temperature Upshift

1998 ◽  
Vol 66 (7) ◽  
pp. 3106-3112 ◽  
Author(s):  
Yilan Zhang ◽  
Norio Ohashi ◽  
Yasuko Rikihisa
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Temperature Shift ◽  
Predicted Amino Acid Sequence ◽  
Mrna Levels ◽  
Hsp70 Gene ◽  
Hsp70 Mrna ◽  
E Coli ◽  
Mrna Induction

ABSTRACT Ehrlichia sennetsu is the causative agent of human Sennetsu ehrlichiosis. Heat shock protein 60 (HSP60) and HSP70 (DnaK) are two major bacterial HSPs, and their interaction modulates the stress response. Previously, we cloned and sequenced groEand expressed groEL of E. sennetsu. HSP60 (GroEL) was immunogenic and cross-reactive in Ehrlichiaspp. The present study was designed to (i) characterize the HSP70 gene of this organism and (ii) determine whether the expression of these two HSPs is inducible upon exposure to heat stress. A gene encoding an HSP70 homolog was isolated and sequenced from a gene library. The ehrlichial HSP70 gene encoded a 637-amino-acid protein, which had an approximate molecular mass of 68,354 Da and which was homologous to DnaK of Escherichia coli. A DNA sequence resembling −35 and −10 promoter sequences of E. coli dnaK was observed upstream of the ehrlichial HSP70 gene. Alignment of the predicted amino acid sequence with that of E. coli DnaK andBrucella, Salmonella, Borrelia,Chlamydia, and Mycobacterium HSP70s showed 63, 67, 63, 62, 58, and 53% identity, respectively. By reverse transcription-PCR analysis, the mRNA levels of ehrlichial HSP70 and HSP60 were examined after temperature shifts from 28 to 37°C and from 37 to 40°C. HSP70 mRNA induction levels were greater than those of HSP60 mRNA after a 37-to-40°C temperature shift, whereas the reverse was true after a 28-to-37°C temperature shift. Our data suggest that HSP60 and HSP70 may play different roles during transfer from vector temperature to human body temperature and during a febrile condition characteristic of ehrlichial disease. This study also provides a useful model system for examining mRNA expression in obligatory intracellular bacteria.

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.

scholarly journals Influence of detergents on determination of heat shock protein 70 by ELISA.

2002 ◽  
Vol 46 (4) ◽  
pp. 173-175
Author(s):  
Eiji Yoshihara ◽  
Takahiro Takimoto ◽  
Hayato Terayama ◽  
Yukako Shirato ◽  
Kazuhiko Iwahashi
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70

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.

Determination of the volume changes induced by ligand binding to heat shock protein 90 using high-pressure denaturation

2011 ◽  
Vol 413 (2) ◽  
pp. 171-178 ◽  
Author(s):  
Zigmantas Toleikis ◽  
Piotras Cimmperman ◽  
Vytautas Petrauskas ◽  
Daumantas Matulis
Keyword(s):  
High Pressure ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Ligand Binding ◽  
Heat Shock Protein 90 ◽  
Volume Changes

scholarly journals Selective renal overexpression of human heat shock protein 27 reduces renal ischemia-reperfusion injury in mice

2010 ◽  
Vol 299 (2) ◽  
pp. F347-F358 ◽  
Author(s):  
Minjae Kim ◽  
Sang Won Park ◽  
Mihwa Kim ◽  
Sean W. C. Chen ◽  
William T. Gerthoffer ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Fluorescent Protein ◽  
Ischemia Reperfusion Injury ◽  
Therapeutic Option ◽  
Ischemia Reperfusion ◽  
Heat Shock Protein 27 ◽  
Renal Ischemia ◽  
Specific Expression ◽  
Mrna Induction

We have previously shown that exogenous and endogenous A1 adenosine receptor (A1AR) activation protected against renal ischemia-reperfusion (IR) injury in mice by induction and phosphorylation of heat shock protein 27 (HSP27). With global overexpression of HSP27 in mice, however, there was a paradoxical increase in systemic inflammation with increased renal injury after an ischemic insult due to increased NK1.1 cytotoxicity. In this study, we hypothesized that selective renal expression of HSP27 in mice would improve renal function and reduce injury after IR. Mice were subjected to renal IR injury 2 days after intrarenal injection of saline or a lentiviral construct encoding enhanced green fluorescent protein (EGFP) or human HSP27 coexpressing EGFP (EGFP-huHSP27). Mice with kidney-specific reconstitution of huHSP27 had significantly lower plasma creatinine, renal necrosis, apoptosis, and inflammation as demonstrated by decreased proinflammatory cytokine mRNA induction and neutrophil infiltration. In addition, there was better preservation of the proximal tubule epithelial filamentous (F)-actin cytoskeleton in the huHSP27-reconstituted groups than in the control groups. Furthermore, huHSP27 overexpression led to increased colocalization with F-actin in renal proximal tubules. Taken together, these findings have important clinical implications, as they imply that kidney-specific expression of HSP27 through lentiviral delivery is a viable therapeutic option in attenuating the effects of renal IR.

Exogenous heat shock protein-70 inhibits cigarette smoke-induced intimal thickening

2008 ◽  
Vol 295 (4) ◽  
pp. R1320-R1327 ◽  
Author(s):  
Michiaki Matsumoto ◽  
Paul C. Dimayuga ◽  
Charles Wang ◽  
Jonathan Kirzner ◽  
Miha Cercek ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cigarette Smoke ◽  
Heat Shock Protein 70 ◽  
Nuclear Antigen ◽  
Cigarette Smoke Exposure ◽  
Hsp70 Expression ◽  
Intimal Thickening ◽  
Hsp70 Mrna ◽  
Recombinant Hsp70

Cigarette smoke is associated with increased carotid intimal thickening or stroke. Preliminary work showed that exposure to smoke resulted in a 4.5-fold reduction of heat shock protein-70 (HSP70) expression in spleens of mice using gene microarray analysis. In the current study, we investigated the role of extracellular HSP70 in carotid intimal thickening of mice exposed to cigarette smoke. Intimal thickening was induced by placement of a cuff around the right carotid artery of mice. Cuff injury resulted in increased HSP70 mRNA expression in carotid arteries that persisted for 21 days. Cigarette smoke exposure decreased arterial HSP70 expression and significantly increased intimal thickening compared with mice exposed to air. Treatment of mice exposed to cigarette smoke with intravenous recombinant HSP70 attenuated intimal thickening through reduced phosphorylated extracellular signal-regulated kinase (pERK) expression in the arterial wall. In vitro experiments with rat aortic smooth muscle cells confirmed that recombinant HSP70 decreases pERK and proliferating cell nuclear antigen (PCNA) expression in cells exposed to cigarette smoke extract and H2O2. Our study suggests that decreased expression of arterial HSP70 is an important mechanism by which exposure to cigarette smoke augments intimal thickening. The effects of recombinant HSP70 suggest a role for extracellular HSP70.

scholarly journals Heterozygous Single-Nucleotide Polymorphism Genotypes at Heat Shock Protein 70 Gene Potentially Influence Thermo-Tolerance Among Four Zebu Breeds of Nigeria

2021 ◽  
Vol 12 ◽  
Author(s):  
Gbolabo Olaitan Onasanya ◽  
George Mutani Msalya ◽  
Aranganoor Kannan Thiruvenkadan ◽  
Chirukandoth Sreekumar ◽  
Gopalan Krishnaswamy Tirumurugaan ◽  
...  
Keyword(s):  
Single Nucleotide Polymorphism ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Genetic Variants ◽  
Heat Shock Protein 70 ◽  
Genotypic Frequency ◽  
Nucleotide Polymorphism ◽  
Single Nucleotide ◽  
Unique Snps

Genetic variants at heat shock protein 70 gene and their influence on heat stress (HS) tolerance were studied among selected Nigeria zebu, namely, 25 White Fulani (WF), 21 Sokoto Gudali (SG), 21 Red Bororo (RB), and 23 Ambala (AM). Detection of single nucleotide polymorphism (SNP) followed by determination of genotype and genotypic frequency was made among the selected breeds. The heat tolerance coefficient (HTC) was determined from thermo-related parameters including body temperature, rectal temperature, and respiratory rate. Thermo-Tolerance was evaluated through the SNP–thermo-parameter relationship. Statistical analyses were done using the GLM procedure in SAS. A quantitative real-time/high-resolution melting-based assay detected twelve genetic variants. Five of these were common and shared across all breeds of cattle. Of the remaining seven variants, three were specifically identified in AM, two in SG, and two in RB. Also, SNPs were evaluated and four unique SNPs (C151T, C146T, G90A, and C219A) were identified. Heterozygous animals had lower HTC suggesting their potential to withstand HS than homozygous counterparts. The WF and RB animals had significantly lower values for all parameters (BT, RT, RR, and HTC) compared to AM and SG breeds. Thermo-related parameters were significantly different (P < 0.001), and it is recommended that screening of SNPs in zebu is needed to enable selection for improved thermo-tolerance.

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