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At least 973 records · Page 54Linked to original sources
PubMed2004

Development of a multiplex PCR (m-PCR) test for rapid identification of genes encoding heat-labile (LTI) and heat-stable (STI and STII) toxins of enterotoxigenic Escherichia coli (ETEC) with internal control of amplification.

A multiplex PCR system was developed for specific identification of genes encoding heat-labile (LTI) and heat-stable (STI and STII) toxins of enterotoxigenic Escherichia coli (ETEC) strains. In addition, primers specific for the E. coli gene coding for 16S rRNA were used as an internal control of the DNA amplification. The specificity of the method was validated by single PCR tests performed with reference to E. coli strains as well as pig-isolated bacteria and 100% correlation was observed. The developed multiplex PCR allowed rapid and specific identification of enterotoxin-positive E. coli and may be used as a sensitive and specific method for a direct determination of ETEC and to differentiate them from other E. coli isolates.

Bacterial Toxins↗
PubMed2003

[The fusion and expression of genes encoding heat-stable and heat-labile enterotoxins of escherichia coli from porcine origin].

The genes encoding precursor heat-stabile (pro-ST) and mature peptide of B unit of heat-labile (LT) enterotoxins of Escherichia coli from piglet were amplified by polymerase chain reaction (PCR). The 3' terminus of gene encoding pro-ST was genetically fused to the 5' terminus of the LTB subunit gene in nest-PCR. The fusion genes encoding pro-ST and LTB were cloned into pGEM-T vector and subcloned into the pQE30. The recombinant plasmid was expressed in E. coli by IPTG induction. The fusion protein possessed both ST and LTB antigenicity, as well as it had lost the biological toxicity of ST or LT toxin.

Amino Acid Sequence↗
PubMed2006

[Research on relationship of syndrome type and parameters of hemorheology and platelet activation in patients with acute gout arthritis of dampness-heat blockage type and stasis-heat accumulate type].

OBJECTIVE: To study the relationship between syndrome type and the parameters of hemorrheology and platelet activation in patients with acute gout arthritis of dampness-heat blockage (DHB) type and stasis-heat accumulation (SHA) type. METHODS: Forty patients with acute gouty arthritis were divided into 2 groups according to TCM syndrome differentiation, the DHB group (n=24) and the SHA group (n=16), and 20 healthy people were taken as the control group. Hemorrheological parameters, platelet activating factor (PAC-1) and P-selection (CD62p) in them were detected. RESULTS: Plasma viscosity, outcome of erythrocyte sedimentation and K value of its equation, levels of PAC-1 and CD62p were higher, erythrocyte electrophoresis index was significantly lower in gout patients of both types than those in the control group (all P < 0.01), and the levels of PAC-1 and CD62p in the SHA group were higher than those in the DHB group (P < 0.05). CONCLUSION: DHB type and SHA syndrome type of acute gout arthritis are correlated with parameters of hemorrheology and platelet activation, and the different levels of these pameters showed in the two types, may be the internal factors for their genesis.

Acute Disease↗
PubMedDate not supplied

Noninvasive measurement of arterial oxyhemoglobin saturation with a heated and a non-heated skin reflectance pulse oximeter sensor.

The feasibility of measuring arterial oxyhemoglobin saturation (SaO2) noninvasively using a skin reflectance pulse oximeter sensor attached to the scalp, neck, and thigh regions of anesthetized swine was investigated. The optical reflectance sensor used consisted of a pair of red and infrared light-emitting diodes and a concentric array of six identical photodiodes. Two prototype sensor assemblies were evaluated: one assembly housed only the optical sensor, whereas the other also included a miniature heater. Measurements made from the scalp and neck regions were obtained with the non-heated skin reflectance sensor, and measurements from the thigh were made with the heated prototype. Each sensor was interfaced to a commercial transmittance pulse oximeter adapted to perform as a reflectance pulse oximeter. SaO2 values obtained by the reflectance pulse oximeters (SpO2(r) were compared simultaneously with SaO2 values obtained from arterial blood samples and analyzed in vitro with a CO-oximeter. The equations for the best-fitted linear regression lines describing the relationships between SpO2(r) and SaO2 values in the range between 30 and 100% were: SpO2(r) = 10.7 + 0.90 (SaO2), n = 321, r = 0.97; SpO2(r) = 16.72 + 0.82 (SaO2), n = 217, r = 0.95; and SpO2(r) = 20.21 + 0.77 (SaO2), n = 37, r = 0.97 for the neck, thigh, and scalp measurements, respectively. The regression analysis revealed significant correlation and a relatively small standard error of estimate (SEE = 4.05% for the neck, 4.79% for the thigh, and 3.50% for the scalp measurements). This study demonstrated the feasibility of measuring SaO2 noninvasively over a wide range of values utilizing the principle of reflectance pulse oximetry.

Animals↗
PubMed1985

Stability, heat stability and heat sensitivity of proteins: thermodynamic considerations.

The heat sensitivity and stability of a protein should be characterized by the Arrhenius parameters of the irreversible denaturation. The terms "thermostability" or "activation enthalpy" and "activation entropy" of denaturation as "thermodynamic parameters of protein stability" are misleading. The terms "measure of heat sensitivity" and "measure of stability" should be used as comparative data for protein structure.

Hot Temperature↗
PubMedDate not supplied

[The role of external respiration and blood circulation in heat emission during exposure of Taurotragus oryx canna antelopes to solar heat].

Experiments have been made on 4 elands at the age of 3--4 months, mean body weight 78 kg. At ambient temperature 31.5degrees combined with solar radiation, polypnoe was observed in the animals. Under these conditions, only small changes in the body temperature were observed, although skin temperature became 4--6degrees higher than in the morning. Heat production was 10% lower than that at 22.5degrees. The animals eliminated about 8% of metabolic heat through respiration in the morning and about 7%--in the afternoon.

Animals↗
PubMed1994

A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins.

MAPK-activated protein kinase-2 (MAPKAP kinase-2) is activated in vitro by the p42 and p44 isoforms of MAPK (p42/p44MAPK). In several cell lines, however, MAPKAP kinase-2 is activated by sodium arsenite, heat shock, or osmotic stress and not by agonists that activate p42/p44MAPK. We have identified a MAPK-like enzyme that acts as a MAPKAP kinase-2 reactivating kinase (RK). RK is recognized by an antiserum raised against a Xenopus MAPK (Mpk2), which is most similar to HOG1 from S. cerevisiae. We also identified a RK kinase (RKK) on the basis of its ability to activate either RK or a GST-Mpk2 fusion protein. The RKK, RK, and MAPKAP kinase-2 constitute a new stress-activated signal transduction pathway in vertebrates that is distinct from the classical MAPK cascade.

Amino Acid Sequence↗
PubMed1994

High calcium induces heat shock proteins 72 and 60 in cultured human keratinocytes: comparative study with heat shock and sunlamp light irradiation.

Expression/induction of the 72 and 60 kDa heat shock proteins (HSPS 72 and 60) in cultured human keratinocytes by high calcium was studied with immunofluorescent staining and the flow cytometric method. Normal human keratinocytes cultured in serum free, low calcium medium (Ca2+, 0.1 mM) at 3-passage weakly expressed HSP 60, but not HSP 72, as fine granules in the cytoplasm. HSP 72 was induced in the perinuclear cytosomal area and then in the nucleus after transferring the cells in high calcium medium (Ca2+, 1.8 mM). Whereas the nuclear accumulation began to decrease 24 h after the treatment, the perinuclear cytosomal staining continued. High calcium also augmented the expression of HSP 60 as coarse granules in the cytoplasm. Flow cytometric analyses quantitatively revealed the induction of HSP 72 and the upregulation of HSP 60 by high calcium treatment. Our results clearly demonstrated that extracellular calcium concentration modifies the level of expression of HSP 72 and 60 in normal human keratinocytes, indicating the importance of the careful attention to medium condition in evaluating the expression of HSPS 72 and 60 in cultured keratinocytes.

Calcium↗
PubMed2003

Organization and nucleotide sequence of the European flat oyster Ostrea edulis heat shock cognate 70 (hsc70) and heat shock protein 70 (hsp70) genes.

The heat shock protein 70 family is composed of both environmentally inducible (Hsp) and constitutively expressed (Hsc) members. We sequenced two genes encoding Hsp70 and Hsc70 in the European flat oyster Ostrea edulis. The Oehsc70 gene contained introns, while the Oehsp70 gene did not. The corresponding amino acid sequences contained the characteristic motifs of the HSP70 family.

Amino Acid Sequence↗
PubMed2001

Heat shock protein 27 shows a distinctive widespread spatial and temporal pattern of induction in CNS glial and neuronal cells compared to heat shock protein 70 and caspase 3 following kainate administration.

Kainate-induced status epilepticus is associated with both apoptotic and necrotic cell death and induction of heat shock proteins (HSPs) in hippocampal and cortical regions of the rodent brain. In the present study we have examined the temporal, spatial and cellular expression patterns of mRNAs for the highly inducible HSPs, HSP70 and HSP27, together with the apoptotic marker, caspase 3 (CPP32) in rat brain after systemic administration of kainate. HSP70 mRNA was transiently induced in the forebrain by kainate, principally in the CA1, CA3 and hilar cells of the hippocampal formation, in piriform cortex and discrete thalamic nuclei. Maximal expression was seen at 8 h after kainate which then declined to background levels by 7 days. Labelling was predominantly neuronal. In contrast, HSP27 mRNA expression was more widespread. Intense labelling was observed in CA1, CA3 and the hilar region at 8 h after kainate but the expression profile for HSP27 mRNA expanded considerably with intense signals seen in corpus callosum, cortex and thalamus at 24 h post kainate. Emulsion autoradiographs indicated a predominantly glial localisation for HSP27 mRNA. In the hilus, a distinct subpopulation of interneurones were found to express HSP27 mRNA. CPP32 mRNA was upregulated in CA1, CA3 and hilus of the hippocampal formation and in piriform cortex. CPP32 mRNA expression was more restricted and similar in distribution to HSP70 mRNA being localised to neurones. The present study demonstrates the unique early expression of HSP27 mRNA by glial cells and distinct populations of neurones which extends beyond those in which HSP70 and CPP32 induction occurs with subsequent cell loss.

Animals↗
PubMed1997

Heat shock protein 80 of Neurospora crassa, a cytosolic molecular chaperone of the eukaryotic stress 90 family, interacts directly with heat shock protein 70.

The subunit structure of Hsp80, the most abundant heat-shock protein of Neurospora crassa, was examined by chemical cross-linking of the purified protein in vitro. Resolution of glutaraldehyde-treated Hsp80 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis SDS-PAGE suggests that the native state of this protein is a tetramer; the relative proportion of cross-linked species, estimated by the fraction of protein recovered in each category, is consistent with a dimer-of-dimer structure. Upon interaction with nucleotides, higher order cross-linked oligomers were detected, indicating ligand-induced conformational changes. The effect of nucleotides was also monitored by following tryptophan fluorescence: CTP, UTP, and NAD led to fluorescence quenching, the effect of CTP being the most pronounced. As individual molecular chaperones often act in concert with cochaperones, interaction between the two major cytosolic stress proteins--Hsp80 and Hsp70--was examined. Purified Hsp70 was immobilized on ATP-agarose and purified Hsp80 was applied to the Hsp70-saturated matrix; while Hsp80 did not bind to ATP-agarose by itself, it was bound strongly by immobilized Hsp70. The [Hsp70-Hsp80] complex was eluted with ATP and coelution of both proteins was confirmed by Western blot analysis, using specific polyclonal antibodies raised against each protein. The physical association of stress-inducible Hsp70 and Hsp80 was verified by interprotein cross-linking in vitro followed by immunoblot analysis and by immunoprecipitation.

Cross-Linking Reagents↗
PubMed2002

Heat shock protein 70 and heat shock protein 90 expression in light- and dark-adapted adult octopus retinas.

Light- and dark-adaptation leads to changes in rhabdom morphology and photopigment distribution in the octopus retina. Molecular chaperones, including heat shock proteins (Hsps), may be involved in specific signaling pathways that cause changes in photoreceptor actin- and tubulin-based cytoskeletons and movement of the photopigments, rhodopsin and retinochrome. In this study, we used immunoblotting, in situ RT-PCR, immunofluorescence and confocal microscopy to localize the inducible form of Hsp70 and the larger Hsp90 in light- and dark-adapted and dorsal and ventral halves of adult octopus retinas. The Hsps showed differences in distribution between the light and dark and in dorsal vs. ventral position in the retina. Double labeling confocal microscopy co-localized Hsp70 with actin and tubulin, and Hsp90 with the photopigment, retinochrome. Our results demonstrate the presence of Hsp70 and Hsp90 in otherwise non-stressed light- and dark-adapted octopus retinas. These Hsps may help stabilize the cytoskeleton, important for rhabdom structure, and are perhaps involved in the redistribution of retinochrome in conditions of light and dark.

Adaptation, Ocular↗
PubMed1997

Heat shock and proinflammatory stressors induce differential localization of heat shock proteins in human monocytes.

Heat shock (HS) proteins (HSP) are a family of molecular chaperones induced by environmental stresses such as oxidative injury, and contribute to protection from and adaptation to cellular stress. We investigated in human monocytes the expression and subcellular distribution of hsp70 and hsc70 after HS and inflammation-related stresses leading to generation of reactive oxygen species by these cells, such as the phorbol ester PMA and erythrophagocytosis (E phi). By combining immunofluorescent staining and Western blot on subcellular fractions, we found that all three stress factors resulted in an increased hsp70 expression, however the subcellular distribution pattern was different depending on the type of stress. While HS induced a rapid translocation of hsp70 into the nucleus, no nuclear translocation of hsp70 was observed after PMA or E phi. Neither of the examined stresses induced membrane expression of hsp70. The observed differences in subcellular distribution pattern might relate to distinct regulation and specific functions of hsp70 in inflammation.

Biological Transport↗
PubMed2004

Heat-shock protein 70 and heat-shock protein 90 associate with Toll-like receptor 4 in response to bacterial lipopolysaccharide.

Mammalian responses to bacterial LPS (lipopolysaccharide) from the outer membrane of Gram-negative bacteria can lead to an uncontrolled inflammatory response that can be deadly for the host. It has been shown that the innate immune system employs at least three cell surface receptors, CD14, TLR4 (Toll-like receptor 4) and MD-2, in order to recognize bacterial LPS. In our previous work we have found that Hsps (heat-shock proteins) are also involved in the innate recognition of bacterial products. Their presence on the cell surface, as well as their involvement in the innate recognition process, are poorly understood. In the present study we have investigated the association of TLR4 with Hsp70 and Hsp90 following LPS stimulation, both on the cell surface and intracellularly. Our results show that Hsp70 and Hsp90 form a cluster with TLR4 within lipid microdomains following LPS stimulation. In addition, Hsp70 and Hsp90 seem to be involved in TLR4/LPS trafficking and targeting to the Golgi apparatus, since upon LPS stimulation we found that both Hsps are targeted to the Golgi along with TLR4. The present study sheds new light into the involvement of Hsps in the innate immune response.

Cell Line↗
PubMed2000

A non-toxic heat shock protein 70 inducer, geranyl-geranyl-acetone, restores the heat shock response in gastric mucosa of protein-malnourished rats.

Acute gastric mucosal lesions caused by stress or noxious stimuli are important to consider in the management of critically or chronically ill patients. Protein malnutrition has been implicated as a risk factor for stress ulcer and subsequent complications in those patients. When male Wistar rats fed a 5% or 20% casein diet for 3 weeks were exposed to restraint and water-immersion stress, the low-protein diet significantly increased the ulcer index. The low-protein diet did not change the level of heat shock factor 1 (HSF1) in gastric mucosa but it did attenuate the HSF1 activation after exposure to the stress, resulting in the inhibition of HSP70 mRNA expression and HSP70 induction in gastric mucosa. HSP70 is crucial for the maintenance of cell integrity during pathophysiologic conditions; therefore the impaired HSP70 induction appeared to at least in part aggravate stress ulcer. We also tested whether a non-toxic HSP70 inducer, geranyl-geranyl-acetone (GGA), effectively improved the mucosal integrity by stimulating HSP70 induction under protein malnutrition. Intragastric administration of GGA (200 mg/kg twice a day) to the protein-malnourished rats for up to 1 week failed to stimulate the HSP70 induction. However, the administration of GGA (200 mg/kg twice a day) for 3 weeks restored HSP70 induction and induced higher resistance against stress ulcer as compared with results in vehicle-treated, normally nourished rats. Our results suggest that GGA may have a potential benefit for the prevention of stress ulcer in chronically or critically ill patients with protein malnutrition.

Animals↗
PubMed1998

Heat stress affects the glucocorticoid receptor interaction with heat shock protein Hsp70 in the rat liver.

The association of glucocorticoid hormones receptor (GR) with heat shock protein Hsp70 in the liver cytosol of rats exposed to 41 degrees C whole body hyperthermic stress was examined by quantitative immunoblotting of the two proteins within immunopurified untransformed GR multiprotein complexes. The presence of Hsp70 in the rat liver GR heterocomplexes was confirmed, and 2-fold increase in the Hsp70 relative to the steroid binding protein content within the complexes was recorded 2 and 12 h after the stress. This increase exceeded the stress-induced elevation in the total cytoplasmic Hsp70 level, but could not be seen 24 h after the stress, when cytoplasmic Hsp70 returned to basal level. The results suggest that hyperthermic stress alters the composition of the rat liver untransformed GR heterocomplexes increasing the Hsp70 share.

Animals↗
PubMed2005

Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells.

Dengue virus requires the presence of an unidentified cellular receptor on the surface of the host cell. By using a recently published affinity chromatography approach, an 84-kDa molecule, identified as heat shock protein 90 (HSP90) by matrix-assisted laser desorption ionization-time of flight mass spectrometry, was isolated from neuroblastoma and U937 cells. Based on the ability of HSP90 (84 kDa) to interact with HSP70 (74 kDa) on the surface of monocytes during lipopolysaccharide (LPS) signaling and evidence that LPS inhibits dengue virus infection, the presence of HSP70 was demonstrated in affinity chromatography eluates and by pull-down experiments. Infection inhibition assays support the conclusion that HSP90 and HSP70 participate in dengue virus entry as a receptor complex in human cell lines as well as in monocytes/macrophages. Additionally, our results indicate that both HSPs are associated with membrane microdomains (lipid rafts) in response to dengue virus infection. Moreover, methyl-beta-cyclodextrin, a raft-disrupting drug, inhibits dengue virus infection, supporting the idea that cholesterol-rich membrane fractions are important in dengue virus entry.

Cell Line, Tumor↗