Displaying publications 1 - 20 of 113 in total

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  1. Induction and characterization of heat shock proteins of Salmonella typhi and their reactivity with sera from patients with typhoid fever
    Tang SW, Abubakar S, Devi S, Puthucheary S, Pang T
    Infect Immun, 1997 Jul;65(7):2983-6.
    PMID: 9199477
    The heat shock protein (HSP) response of Salmonella typhi following exposure to elevated growth temperatures was studied. Three major proteins with molecular sizes of 58, 68, and 88 kDa were abundantly expressed when S. typhi cells were shifted from 37 to 45 degrees C and to 55 degrees C. These proteins were also constitutively expressed at 37 degrees C. Western blotting and immunoprecipitation studies with anti-HSP monoclonal antibodies revealed that the 58- and 68-kDa proteins were analogous to the GroEL and DnaK proteins, respectively, of Escherichia coli. These HSPs are also abundantly present in the outer membrane fraction of disrupted cells and, to a lesser extent, in the cytosol. Immunoblotting experiments with sera from patients with a culture-positive diagnosis of typhoid fever showed the presence of antibodies to these HSPs. Nine of twelve sera reacted with the 58-, 68-, and 88-kDa proteins, while three sera reacted only with the 68- and 88-kDa proteins. All 10 sera from healthy individuals showed no binding to these HSPs. In light of the well-documented roles of HSPs in the pathogenesis of microbial infections and as immunodominant antigens, these findings may be relevant for a better understanding of disease processes and for the future development of diagnostic and preventive strategies.
    Matched MeSH terms: Heat-Shock Proteins/analysis*; Heat-Shock Proteins/immunology*; HSP70 Heat-Shock Proteins/immunology
  2. Effect of a carotene concentrate on the growth of human breast cancer cells and pS2 gene expression
    Nesaretnam K, Jin Lim E, Reimann K, Lai LC
    Toxicology, 2000 Oct 26;151(1-3):117-26.
    PMID: 11074306
    Breast cancer is the most common cancer in women worldwide. The growth of breast cancer cells is either hormone-dependent or hormone-independent. Both types are represented in vitro by the estrogen-receptor positive (ER+) MCF-7 and the estrogen-receptor negative (ER-) MDA-MB-231 cell lines, respectively. The pS2 gene is an estrogen-regulated gene and serves as a marker for the ER+ tumours. Carotenoids are pigments with anti-cancer properties besides having pro-vitamin A, antioxidant and free-radical quenching effects. This study was designed firstly, to compare the effect of palm oil carotene concentrate with retinoic acid on the growth of the ER+ MCF-7 and the ER- MDA-MB-231 cells; and secondly to evaluate the effect of the palm oil carotene concentrate on the regulation of pS2 mRNA. The growth experiments were performed with monolayer cells seeded in phenol red free RPMI 1640 culture media and subsequently treated with varying concentrations of either retinoic acid or palm oil carotenoids. The cell numbers were determined at the start of each experiment and then at successive time intervals. The results showed that the palm oil carotene concentrate caused dose-dependent inhibition of estradiol-stimulated growth of MCF-7 cells but did not affect the proliferation of MDA-MB-231 cells. Retinoic acid caused similar, albeit more potent effects, as significant inhibition was observed at lower concentrations than the palm oil carotenoids. In the pS2 gene expression experiment, cell monolayers were treated with the carotene concentrate (10(-6) M), either with or without supplemented estradiol (10(-8) M), and subsequently the RNA was extracted. Northern blotting was performed and the regulation of pS2 mRNA determined using a 32P-labelled pS2 cDNA probe. The results showed that the palm oil carotene concentrate did not affect the expression of pS2 mRNA and are therefore independent of the estrogen-regulated pathway.
    Matched MeSH terms: Heat-Shock Proteins/biosynthesis; Heat-Shock Proteins/genetics
  3. The effect of early-age food restriction on heat shock protein 70 response in heat-stressed female broiler chickens
    Zulkifli I, Che Norma MT, Israf DA, Omar AR
    Br Poult Sci, 2002 Mar;43(1):141-5.
    PMID: 12003331
    1. This study was conducted to determine the effect of early-age food restriction on heat shock protein (hsp) 70 synthesis in the brains of female broiler chickens exposed to high ambient temperatures. 2. Chicks were brooded for 3 weeks and then maintained at 24+/-1 degrees C. 3. On d 0, chicks were assigned to one of 4 feeding regimens; each regimen was applied to 4 cages of chicks. The regimens were: (1) ad libitum feeding (AL); (2) 80% food restriction at 4, 5 and 6 d of age (F80); (3) 60% food restriction at 4, 5, and 6 d of age (F60); and (4) 40% food restriction at 4, 5 and 6 d of age (F40). From d 35 to d 41, all chicks were subjected to 38+/-1 degrees C for 2 h/d. 4. One day following food restriction (d 7), hsp 70 expression in the brain samples of F60 and F40 chicks was augmented but not those fed AL and F80. 5. Prior to the heat challenge (d 35), all chicks had similar hsp 70 response. Irrespective of feeding regimen, there was a marked increase in hsp 70 expression after 4 d of heat treatment (d 38). Following 7 d of heat exposure (d 41), except for the F60 chicks, the augmented hsp 70 expression in the brains of AL, F80 and F40 birds was not maintained. 6. Enhancement of hsp 70 expression was noted in birds subjected to F60, but not AL, F80 or F40, throughout the period of heat exposure.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/biosynthesis*
  4. Effects of early age feed restriction and heat conditioning on heat shock protein 70 expression, resistance to infectious bursal disease, and growth in male broiler chickens subjected to heat stress
    Liew PK, Zulkifli I, Hair-Bejo M, Omar AR, Israf DA
    Poult Sci, 2003 Dec;82(12):1879-85.
    PMID: 14717545
    The effects of early age feed restriction and heat conditioning on heat shock protein (HSP) 70 expression, antibody production, resistance to infectious bursal disease (IBD), and growth of heat-stressed male broiler chickens were investigated. Chicks were divided into 4 groups: 60% feed restriction on d 4,5, and 6 (FR); exposure to 36 +/- 1 degrees C for 1 h from d 1 to 21 (HT); combination of FR and HT (FRHT); and control. From d 35 to 50, heat stress was induced by exposing birds to 38 +/- 1 degrees C and 80% RH for 2 h/d. On d 36, each bird was administered 10 times the normal dose of live IBD vaccine. After heat exposure, the FRHT birds had higher HSP 70 density (d 41) and weight gain (from d 35 to 49) and lower bursal histological score (BHS) (d 51) than their HT and control counterparts. The HSP 70 expression and BHS of FR birds were not significantly different from those of the other 3 groups during the heat exposure period. Heat shock protein 70 and BHS data were negatively correlated (r = -0.33, P = 0.0008). We concluded that FRHT could improve weight gain and resistance to IBD in male broiler chickens under heat stress conditions. The improved heat tolerance and disease resistance in FRHT birds could be attributed to better HSP 70 response.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/analysis*
  5. Mimotopes of heat shock proteins of Salmonella enterica serovar Typhi identified from phage-displayed peptide library
    Yuen HL, Shamala D, Thong KL
    J Infect Dev Ctries, 2008 Aug 30;2(4):313-23.
    PMID: 19741295
    BACKGROUND: Heat shock proteins (HSPs) are known to be involved in the pathogenesis of Salmonella enterica serovar Typhi (S. Typhi), the causative agent of typhoid fever. The objective of this study was to apply a phage display library to identify mimotopes of two HSPs, HSP90 and DnaK in S. Typhi.

    METHODOLOGY: A 12-mer random peptide library expressed on the surface of the filamentous phage, M13, was used to select the mimotopes of two S. Typhi heat shock proteins by biopanning with monoclonal antibodies (mAbs), DnaK and HSP90. The immunogenicity of the selected peptides was determined through binding affinity with polyclonal antibodies from pooled typhoid-confirmed patients' sera and purified HSPs mAb using Western blotting and ELISA.

    RESULTS: Five rounds of biopanning resulted in enrichment of phage clones expressing the binding motifs TDxSTRP and FPSHYWLYPPPT, respectively. The selected peptides showed strong immunoreactivity with patients' sera. Thus, monoclonal antibodies against HSP and patient sera can select common mimotopes from the random peptide library.

    CONCLUSION: These findings may provide fundamental information for further studies on diagnostic application or vaccine design against this aetiologic agent of typhoid fever.

    Matched MeSH terms: HSP90 Heat-Shock Proteins/immunology*; HSP90 Heat-Shock Proteins/isolation & purification*
  6. Fulltext Crating and heat stress influence blood parameters and heat shock protein 70 expression in broiler chickens showing short or long tonic immobility reactions
    Zulkifli I, Al-Aqil A, Omar AR, Sazili AQ, Rajion MA
    Poult Sci, 2009 Mar;88(3):471-6.
    PMID: 19211514 DOI: 10.3382/ps.2008-00287
    Two hundred thirty-five 1-d-old broiler chickens showing short or long tonic immobility responses were classified as low fear (LF) or high fear (HF) responders, respectively. On d 41, they were subjected to either crating or heat challenge (34 +/- 1 degrees C) for 3 h and its effect on plasma corticosterone concentration, heterophil/lymphocyte ratios, and heat shock protein (HSP) 70 expression in brain tissue were determined. Crating and heat exposure elevated heterophil/lymphocyte ratios in both LF and HF birds. Circulating corticosterone, however, was greater in HF than LF birds after crating and heat challenge. Although differences between fear responder group for HSP 70 were negligible before heat challenge, after 3 h of heat exposure, the response was greater for the HF than the LF group. Both LF and HF showed similar increases in HSP 70 after crating.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/genetics; HSP70 Heat-Shock Proteins/metabolism*
  7. Fulltext Changes in heat shock protein 70 expression and blood characteristics in transported broiler chickens as affected by housing and early age feed restriction
    Al-Aqil A, Zulkifli I
    Poult Sci, 2009 Jul;88(7):1358-64.
    PMID: 19531704 DOI: 10.3382/ps.2008-00554
    An experiment was conducted to determine the effects of 2 types of housing systems and early age feed restriction on heat shock protein (hsp) 70 expression and blood parameters in broiler chickens subjected to road transportation. On d 1, female chicks were housed either in windowless environmentally controlled chambers (temperature was set at 32 degrees C on d 1 and gradually reduced to 23 degrees C by d 21; CH) or in conventional open-sided houses (OH) with cyclic temperatures (minimum, 24 degrees C; maximum, 34 degrees C). Equal number of chicks from each housing system were subjected to either ad libitum feeding or 60% feed restriction on d 4, 5, and 6 (FR). On d 42, all of the birds were crated and transported for 6 h. Birds raised in OH had smaller increases in heterophil:lymphocyte ratios and plasma corticosterone concentrations than those of CH. Subjecting birds to FR dampened heterophil:lymphocyte ratios and corticosterone reactions to transportation. After 4 h of transportation, the OH birds had greater hsp 70 expression than their CH counterparts. Within the CH, the FR chicks showed higher hsp 70 density than those of the ad libitum-fed group. Except for glucose, housing system had a negligible effect on serum levels of cholesterol, potassium, and chloride. Collectively, the results suggest that the improved tolerance to transport stress in OH and FR chicks could be associated with better hsp 70 expression.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/genetics; HSP70 Heat-Shock Proteins/metabolism*
  8. Feeding Artemia franciscana (Kellogg) larvae with bacterial heat shock protein, protects from Vibrio campbellii infection
    Sung YY, Ashame MF, Chen S, Macrae TH, Sorgeloos P, Bossier P
    J Fish Dis, 2009 Aug;32(8):675-85.
    PMID: 19515074 DOI: 10.1111/j.1365-2761.2009.01046.x
    Among their numerous physiological effects, heat shock proteins (Hsps) are potent immunomodulators, a characteristic reflecting their potential as therapeutic agents and which led to their application in combating infection. As an example, the up-regulation of endogenous Hsp70 in the branchiopod crustacean Artemia franciscana (Kellogg) is concurrent with shielding against bacterial infection. To better understand this protective mechanism, gnotobiotic Artemia were fed with Escherichia coli treated to over-produce different prokaryotic Hsps. This was shown to increase larval resistance to experimental Vibrio campbellii exposure. Immunoprobing of Western blots showed that the enhanced resistance to V. campbellii correlated with DnaK production in E coli. A definitive role for DnaK was then demonstrated by feeding Artemia larvae with transformed bacteria over-producing only this protein, although other Hsps such as DnaJ and grpE also provided tolerance against Vibrio infection. Feeding of bacteria synthesizing selected Hsps is therefore suggested as an alternative to antibiotic use as a means of enhancing resistance of Artemia larvae to bacterial infection, which may have potential applications in aquaculture.
    Matched MeSH terms: Heat-Shock Proteins/administration & dosage*; HSP70 Heat-Shock Proteins/metabolism
  9. Fulltext Ingestion of bacteria overproducing DnaK attenuates Vibrio infection of Artemia franciscana larvae
    Sung YY, Dhaene T, Defoirdt T, Boon N, MacRae TH, Sorgeloos P, et al.
    Cell Stress Chaperones, 2009 Nov;14(6):603-9.
    PMID: 19373565 DOI: 10.1007/s12192-009-0112-2
    Feeding of bacterially encapsulated heat shock proteins (Hsps) to invertebrates is a novel way to limit Vibrio infection. As an example, ingestion of Escherichia coli overproducing prokaryotic Hsps significantly improves survival of gnotobiotically cultured Artemia larvae upon challenge with pathogenic Vibrio campbellii. The relationship between Hsp accumulation and enhanced resistance to infection may involve DnaK, the prokaryotic equivalent to Hsp70, a major molecular chaperone in eukaryotic cells. In support of this proposal, heat-stressed bacterial strains LVS 2 (Bacillus sp.), LVS 3 (Aeromonas hydrophila), LVS 8 (Vibrio sp.), GR 8 (Cytophaga sp.), and GR 10 (Roseobacter sp.) were shown in this work to be more effective than nonheated bacteria in protecting gnotobiotic Artemia larvae against V. campbellii challenge. Immunoprobing of Western blots and quantification by enzyme-linked immunosorbent assay revealed that the amount of DnaK in bacteria and their ability to enhance larval resistance to infection by V. campbellii are correlated. Although the function of DnaK is uncertain, it may improve tolerance to V. campbellii via immune stimulation, a possibility of significance from a fundamental perspective and also because it could be applied in aquaculture, a major method of food production.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/biosynthesis; HSP70 Heat-Shock Proteins/immunology
  10. Fulltext Physiological responses of 3 chicken breeds to acute heat stress
    Soleimani AF, Zulkifli I, Omar AR, Raha AR
    Poult Sci, 2011 Jul;90(7):1435-40.
    PMID: 21673158 DOI: 10.3382/ps.2011-01381
    Domestic animals have been modified by selecting individuals exhibiting desirable traits and culling the others. To investigate the alterations introduced by domestication and selective breeding in heat stress response, 2 experiments were conducted using Red Jungle Fowl (RJF), village fowl (VF), and commercial broilers (CB). In experiment 1, RJF, VF, and CB of a common chronological age (30 d old) were exposed to 36 ± 1°C for 3 h. In experiment 2, RJF, VF, and CB of common BW (930 ± 15 g) were subjected to similar procedures as in experiment 1. Heat treatment significantly increased body temperature, heterophil:lymphocyte ratio, and plasma corticosterone concentration in CB but not in VF and RJF. In both experiments and irrespective of stage of heat treatment, RJF showed lower heterophil:lymphocyte ratio, higher plasma corticosterone concentration, and higher heat shock protein 70 expression than VF and CB. It can be concluded that selective breeding for phenotypic traits in the domestication process has resulted in alterations in the physiology of CB and concomitantly the ability to withstand high ambient temperature compared with RJF and VF. In other words, domestication and selective breeding are leading to individuals that are more susceptible to stress rather than resistant. It is also apparent that genetic differences in body size and age per se may not determine breed or strain variations in response to heat stress.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/metabolism
  11. Fulltext Neonatal feed restriction modulates circulating levels of corticosterone and expression of glucocorticoid receptor and heat shock protein 70 in aged Japanese quail exposed to acute heat stress
    Soleimani AF, Zulkifli I, Omar AR, Raha AR
    Poult Sci, 2011 Jul;90(7):1427-34.
    PMID: 21673157 DOI: 10.3382/ps.2011-01403
    This study aimed to determine the effect of neonatal feed restriction on plasma corticosterone concentration (CORT), hippocampal glucocorticoid receptor (GR) expression, and heat shock protein (Hsp) 70 expression in aged male Japanese quail subjected to acute heat stress. Equal numbers of chicks were subjected to either ad libitum feeding (AL) or 60% feed restriction on d 4, 5, and 6 (FR). At 21 (young) and 270 (aged) d of age, birds were exposed to 43 ± 1°C for 1 h. Blood and hippocampus samples were collected to determine CORT and Hsp 70 and GR expressions before heat stress and following 1 h of heat stress, 1 h of post-heat stress recovery, and 2 h of post-heat stress recovery. With the use of real-time PCR and enzyme immunoassay, we examined the hippocampal expression of GR and Hsp 70 and CORT. The GR expression of the young birds increased following heat stress and remained consistent throughout the period of recovery. Conversely, no significant changes were noted on GR expression of aged birds. Although both young and aged birds had similar CORT before and during heat stress, the latter exhibited greater values following 1 and 2 h of recovery. Within the young group, feeding regimens had no significant effect on Hsp 70 expression. However, neonatal feed restriction improved Hsp 70 expression in aged birds. Neonatal feed restriction, compared with the AL group, resulted in higher CORT on d 21 but the converse was noted on d 270. Neonatal feed restriction appears to set a robust reactive hypothalamo-pituitary-adrenal response allowing the development of adaptive, healthy, and resilient phenotypes in aged quail as measured by a higher hippocampal Hsp 70 expression along with lower CORT.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/biosynthesis*; HSP70 Heat-Shock Proteins/genetics
  12. Eurycomanone suppresses expression of lung cancer cell tumor markers, prohibitin, annexin 1 and endoplasmic reticulum protein 28
    Wong PF, Cheong WF, Shu MH, Teh CH, Chan KL, AbuBakar S
    Phytomedicine, 2012 Jan 15;19(2):138-44.
    PMID: 21903368 DOI: 10.1016/j.phymed.2011.07.001
    Bioactive compounds from the medicinal plant, Eurycoma longifolia Jack have been shown to promote anti-proliferative effects on various cancer cell lines. Here we examined the effects of purified eurycomanone, a quassinoid found in Eurycoma longifolia Jack extract, on the expression of selected genes of the A549 lung cancer cells. Eurycomanone inhibited A549 lung cancer cell proliferation in a dose-dependent manner at concentrations ranging from 5 to 20 μg/ml. The concentration that inhibited 50% of cell growth (GI(50)) was 5.1 μg/ml. The anti-proliferative effects were not fully reversible following the removal of eurycomanone, in which 30% of cell inhibition still remained (p<0.0001, T-test). At 8 μg/ml (GI(70)), eurycomanone suppressed anchorage-independent growth of A549 cells by >25% (p<0.05, T-test, n=8) as determined using soft agar colony formation assay. Cisplatin, a chemotherapy drug used for the treatment of non small cell lung cancer on the other hand, inhibited A549 cells proliferation at concentrations ranging from 0.2 μg/ml to 15 μg/ml with a GI(50) of 0.58 μg/ml. The treatment with eurycomanone reduced the abundance expression of the lung cancer markers, heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1, p53 tumor suppressor protein and other cancer-associated genes including prohibitin (PHB), annexin 1 (ANX1) and endoplasmic reticulum protein 28 (ERp28) but not the house keeping genes. The mRNA expressions of all genes with the exception of PHB were significantly downregulated, 72 h after treatment (p<0.05, T-test, n=9). These findings suggest that eurycomanone at viable therapeutic concentrations of 5-20 μg/ml exhibited significant anti-proliferative and anti-clonogenic cell growth effects on A549 lung cancer cells. The treatment also resulted in suppression of the lung cancer cell tumor markers and several known cancer cell growth-associated genes.
    Matched MeSH terms: Heat-Shock Proteins/chemistry*
  13. Fulltext The role of heat shock protein 70 in resistance to Salmonella enteritidis in broiler chickens subjected to neonatal feed restriction and thermal stress
    Soleimani AF, Zulkifli I, Hair-Bejo M, Omar AR, Raha AR
    Poult Sci, 2012 Feb;91(2):340-5.
    PMID: 22252346 DOI: 10.3382/ps.2011-01703
    Environmental stressors may influence chicken performance and susceptibility to pathogens, such as Salmonella enteritidis. This study was conducted to determine the effects of heat shock protein (Hsp)70 expression on resistance to Salmonella enteritidis infection in broiler chickens subjected to heat exposure. Chicks were divided into 3 feeding regimens: ad libitum feeding (control); 60% feed restriction on d 4, 5, and 6 (FR60); and 60% feed restriction on d 4, 5, and 6 plus 1,500 mg/kg of quercetin (FR60Q). On d 35, all of the chickens were individually inoculated with 1 mL of Salmonella enteritidis (1.5 × 10(8) cfu/bird) and exposed to an ambient temperature of 37 ± 1°C and 70% RH for 3 h/d. The FR60 and FR60Q chickens had significantly lower Salmonella enteritidis colonization and lower Hsp70 expression than that of the control chickens following the heat exposure period. The least colonization was observed in the FR60Q group (1.38 log(10) cfu/g in the spleen and 1.96 log(10) cfu/g in the cecal content) and the highest was in the control group (2.1 log(10) cfu/g in the spleen and 4.42 log(10) cfu/g in the cecal content). It appears that neonatal feed restriction can enhance resistance to Salmonella enteritidis colonization in heat-stressed broiler chicks, and the underlying mechanism could be associated with the lower expression of Hsp70.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/genetics; HSP70 Heat-Shock Proteins/metabolism*
  14. The relationship between adrenocortical function and Hsp70 expression in socially isolated Japanese quail
    Soleimani AF, Zulkifli I, Omar AR, Raha AR
    Comp Biochem Physiol A Mol Integr Physiol, 2012 Feb;161(2):140-4.
    PMID: 22036750 DOI: 10.1016/j.cbpa.2011.10.003
    Physiological responses to social isolation stress were compared in 56-day-old male Japanese quail. Birds were fed pretreated diets for 3 days as follows: (i) Basal diet (control); (ii) Basal diet+1500 mg/kg metyrapone (BM); (iii) Basal diet+30 mg/kg corticosterone (BCO); (iv) Basal diet+250 mg/kg ascorbic acid (BC); (v) Basal diet+250 mg/kg α-tocopherol (BE); (vi) Basal diet+250 mg/kg ascorbic acid and 250 mg/kg α-tocopherol (BCE). The birds were subsequently socially isolated in individual opaque brown paper box for 2 hours. Plasma corticosterone (CORT) concentration and heart and brain heat shock protein 70 (Hsp 70) expressions were determined before stress and immediately after stress. Two hours of isolation stress elevated CORT concentration significantly in the control and BE birds but not in the BC, BCE and BM birds. There was a significant reduction in CORT concentration after isolation stress in the BCO group. Isolation stress increased Hsp 70 expression in the brain and heart of control and BM birds. However, brain and heart Hsp 70 expressions were not significantly altered in the isolated BC, BCE and BE birds. Although, the CORT concentration of BM birds was not affected by isolation stress, Hsp70 expression in both brain and heart were significantly increased. Moreover, exogenous corticosterone supplementation did not result in elevation of Hsp 70 expression. It can be concluded that, although Hsp 70 induction had not been directly affected by CORT concentration, it may be modulated by the HPA axis function via activation of ACTH.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/metabolism*
  15. Gene expression and functional studies of small heat shock protein 37 (MrHSP37) from Macrobrachium rosenbergii challenged with infectious hypodermal and hematopoietic necrosis virus (IHHNV)
    Arockiaraj J, Vanaraja P, Easwvaran S, Singh A, Othman RY, Bhassu S
    Mol Biol Rep, 2012 Jun;39(6):6671-82.
    PMID: 22290288 DOI: 10.1007/s11033-012-1473-7
    In this study, we have reported a full length of small heat shock protein 37 (designated MrHSP37) gene, identified from the transcriptome database of freshwater prawn Macrobrachium rosenbergii. The complete gene sequence of the MrHSP37 is 2,425 base pairs in length, and encodes 338 amino acids. MrHSP37 contains a long heat shock protein family profile in the amino acid sequence between 205 and 288. The mRNA expressions of MrHSP37 in healthy and the infectious hypodermal and hematopoietic necrosis virus (IHHNV) challenged M. rosenbergii were examined using quantitative real time polymerase chain reaction (qRT-PCR). MrHSP37 is highly expressed in hepatopancreas and all the other tissues (walking leg, gills, muscle, stomach, haemocyte, intestine, pleopods, brain and eye stalk) of M. rosenbergii taken for analysis. The expression is strongly up-regulated after IHHNV challenge. To understand its biological activity, the recombinant MrHSP37 gene was constructed and expressed in Escherichia coli BL21 (DE3). The results of ATPase assay showed that the recombinant MrHSP37 protein exhibited apparent ATPase activity which increased with the concentration of the protein. And also the purified recombinant MrHSP37 protein was used for thermal aggregation assay (chaperone activity). It showed that the recombinant MrHSP37 protein is an active chaperone in this assay. Taken together, these results suggest that MrHSP37 is potentially involved in the immune responses against IHHNV challenge in M. rosenbergii.
    Matched MeSH terms: Heat-Shock Proteins, Small/genetics*; Heat-Shock Proteins, Small/metabolism; Heat-Shock Proteins, Small/chemistry
  16. Enhancement of Hsp70 synthesis protects common carp, Cyprinus carpio L., against lethal ammonia toxicity
    Sung YY, Roberts RJ, Bossier P
    J Fish Dis, 2012 Aug;35(8):563-8.
    PMID: 22724455 DOI: 10.1111/j.1365-2761.2012.01397.x
    Exposure to TEX-OE®, a patented extract of the prickly pear cactus (Opuntia ficus indica) containing chaperone-stimulating factor, was shown to protect common carp, Cyprinus carpio L., fingerlings against acute ammonia stress. Survival was enhanced twofold from 50% to 95% after exposure to 5.92 mg L(-1) NH(3) , a level determined in the ammonia challenge bioassay as the 1-h LD50 concentration for this species. Survival of TEX-OE®-pre-exposed fish was enhanced by 20% over non-exposed controls during lethal ammonia challenge (14.21 mg L(-1)  NH(3) ). Increase in the levels of gill and muscle Hsp70 was evident in TEX-OE®-pre-exposed fish but not in the unexposed controls, indicating that application of TEX-OE® accelerated carp endogenous Hsp70 synthesis during ammonia perturbation. Protection against ammonia was correlated with Hsp70 accretion.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/genetics*; HSP70 Heat-Shock Proteins/metabolism*
  17. Epigenetic modification: possible approach to reduce Salmonella enterica serovar enteritidis susceptibility under stress conditions
    Soleimani AF, Zulkifli I, Hair-Bejo M, Ebrahimi M, Jazayeri SD, Hashemi SR, et al.
    Avian Pathol, 2012;41(4):351-4.
    PMID: 22834548 DOI: 10.1080/03079457.2012.691155
    Stressors may influence chicken susceptibility to pathogens such as Salmonella enterica. Feed withdrawal stress can cause changes in normal intestinal epithelial structure and may lead to increased attachment and colonization of Salmonella. This study aimed to investigate modulatory effects of epigenetic modification by feed restriction on S. enterica serovar Enteritidis colonization in broiler chickens subjected to feed withdrawal stress. Chicks were divided into four groups: ad libitum feeding; ad libitum feeding with 24-h feed withdrawal on day 42; 60% feed restriction on days 4, 5, and 6; and 60% feed restriction on days 4, 5, and 6 with 24-h feed withdrawal on day 42. Attachment of S. Enteritidis to ileal tissue was determined using an ex vivo ileal loop assay, and heat shock protein 70 (Hsp70) expression was evaluated using sodium dodecyl sulphate-polyacrylamide gel electrophoresis and western blotting. Feed withdrawal stress increased S. Enteritidis attachment to ileal tissue. However, following feed withdrawal the epigenetically modified chickens had significantly lower attachment of S. Enteritidis than their control counterparts. A similar trend with a very positive correlation was observed for Hsp70 expression. It appears that epigenetic modification can enhance resistance to S. Enteritidis colonization later in life in chickens under stress conditions. The underlying mechanism could be associated with the lower Hsp70 expression in the epigenetically modified chickens.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/metabolism
  18. Fulltext Acute toxicity and gastroprotection studies of a new schiff base derived copper (II) complex against ethanol-induced acute gastric lesions in rats
    Hajrezaie M, Golbabapour S, Hassandarvish P, Gwaram NS, A Hadi AH, Mohd Ali H, et al.
    PLoS One, 2012;7(12):e51537.
    PMID: 23251568 DOI: 10.1371/journal.pone.0051537
    BACKGROUND: Copper is an essential element in various metabolisms. The investigation was carried out to evaluate acute gastroprotective effects of the Copper (II) complex against ethanol-induced superficial hemorrhagic mucosal lesions in rats.

    METHODOLOGY/PRINCIPAL FINDINGS: Rats were divided into 7 groups. Groups 1 and 2 were orally administered with Tween 20 (10% v/v). Group 3 was orally administered with 20 mg/kg omeprazole (10% Tween 20). Groups 4-7 received 10, 20, 40, and 80 mg/kg of the complex (10% Tween 20), respectively. Tween 20 (10% v/v) was given orally to group 1 and absolute ethanol was given orally to groups 2-7, respectively. Rats were sacrificed after 1 h. Group 2 exhibited severe superficial hemorrhagic mucosal lesions. Gastric wall mucus was significantly preserved by the pre-treatment complex. The results showed a significant increase in glutathione (GSH), superoxide dismutase (SOD), nitric oxide (NO), and Prostaglandin E2 (PGE(2)) activities and a decrease in malondialdehyde (MDA) level. Histology showed marked reduction of hemorrhagic mucosal lesions in groups 4-7. Immunohistochemical staining showed up-regulation of Hsp70 and down-regulation of Bax proteins. PAS staining of groups 4-7 showed intense stain uptake of gastric mucosa. The acute toxicity revealed the non-toxic nature of the compound.

    CONCLUSIONS/SIGNIFICANCE: The gastroprotective effect of the Copper (II) complex may possibly be due to preservation of gastric wall mucus; increase in PGE(2) synthesis; GSH, SOD, and NO up-regulation of Hsp70 protein; decrease in MDA level; and down-regulation of Bax protein.

    Matched MeSH terms: HSP70 Heat-Shock Proteins/metabolism
  19. Fulltext Changes in heat shock protein 70, blood parameters, and fear-related behavior in broiler chickens as affected by pleasant and unpleasant human contact
    Al-Aqil A, Zulkifli I, Hair Bejo M, Sazili AQ, Rajion MA, Somchit MN
    Poult Sci, 2013 Jan;92(1):33-40.
    PMID: 23243228 DOI: 10.3382/ps.2012-02446
    An experiment was conducted to determine the effects of combining both pleasant and unpleasant contacts with human beings on physiology and behavior of broiler chickens. Birds were subjected to the following treatments: (i) received no physical or visual contact with humans (control); (ii) from d 1 to 28, chicks were individually stroked gently for 30 s once daily (PL); (iii) from d 1 to 28, chicks were picked up individually, suspended by both legs, exposed to recorded noise, and swung gently for 15 s once daily (UNPL); (iv) from d 1 to 14 and from d 15 to 28, chicks were subjected to PL and UNPL, respectively (PL-UNPL); and (v) from d 1 to 14 and from d 15 to 28, chicks were subjected to UNPL and PL, respectively (UNPL-PL). On d 42, birds from each treatment group were road-transported for 3 h. Heat shock protein (hsp) 70 expression, plasma levels of corticosterone, serum creatine kinase concentration, heterophil/lymphocyte ratios (HLR), and tonic immobility duration were determined pre- and posttransit. There were significant (P < 0.05) duration of transportation × human contact treatment interactions for HLR and hsp 70 density. Following transit, the PL chicks had significantly (P < 0.05) lower HLR and greater hsp 70 density than the other groups. The corticosterone of PL and UNPL chicks were lower than their control, PL-UNPL, and UNPL-PL counterparts. The PL and PL-UNPL treatments were effective in shortening tonic immobility duration significantly (P < 0.05). Except for UNPL-PL, the serum creatine kinase activity of PL was significantly lower than the other groups. In conclusion, subjecting birds to pleasant human contact reduced stress and fear reactions to transportation by enhancing the ability to express hsp 70 in the brain. Unpleasant human contact had adverse effect on the birds' response to transportation. Early age pleasant experience with humans failed to negate the adverse effects of subsequent unpleasant contact.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/genetics; HSP70 Heat-Shock Proteins/metabolism*
  20. Regulation of G protein signaling by the 70kDa heat shock protein
    Lim WK, Kanelakis KC, Neubig RR
    Cell Signal, 2013 Feb;25(2):389-96.
    PMID: 23153586 DOI: 10.1016/j.cellsig.2012.11.002
    G protein-coupled receptors (GPCRs) transduce extracellular signals to the interior of the cell by activating membrane-bound guanine nucleotide-binding regulatory proteins (G proteins). An increasing number of proteins have been reported to bind to and regulate GPCRs. We report a novel regulation of the alpha(2A) adrenergic receptor (α(2A)-R) by the ubiquitous stress-inducible 70kDa heat shock protein, hsp70. Hsp70, but not hsp90, attenuated G protein-dependent high affinity agonist binding to the α(2A)-R in Sf9 membranes. Antagonist binding was unchanged, suggesting that hsp70 uncouples G proteins from the receptor. As hsp70 did not bind G proteins but complexed with the α(2A)-R in intact cells, a direct interaction with the receptor seems likely. In the presence of hsp70, α(2A)-R-catalyzed [(35)S]GTPγS binding was reduced by approximately 70%. In contrast, approximately 50-fold higher concentrations of hsp70 were required to reduce agonist binding to the stress-inducible 5-hydroxytryptamine(1A) receptor (5-HT(1A)-R). In heat-stressed CHO cells, the α(2A)-R was significantly uncoupled from G proteins, coincident with an increased localization of hsp70 at the membrane. The contrasting effect of hsp70 on the α(2A)-R compared to the 5-HT(1A)-R suggests that during stress, upregulation of hsp70 may attenuate signaling from specific GPCRs as part of the stress response to foster survival.
    Matched MeSH terms: HSP70 Heat-Shock Proteins/metabolism; HSP70 Heat-Shock Proteins/pharmacology*
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