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At least 937 records · Page 52Linked to original sources
PubMed1987

Influence of prior heat treatment on the effects of heat alone or combined with X-rays on mouse stromal tissue.

The tumour bed effect assay was used to study the sensitivity of mouse stromal tissue to heat applied alone or combined with irradiation. Prior heat treatment, 30 min at 43 degrees C, of the tumour bed led to thermotolerance. After priming, thermotolerance developed fully within 24 h and it had disappeared completely after about 10 days. The kinetics of development and decay of thermotolerance in this slowly dividing tissue is similar to that which we had observed previously in skin. When decay rates of several normal tissues with different proliferation characteristics are compared, it is obvious that there is not a clear relationship between proliferation rate of the presumed target cells in the tissue and thermotolerance decay rate.

Acclimatization↗
PubMed1987

Biological observations from feeding heated corn oil and heated peanut oil to rats.

Five groups of male weanling rats were provided purified diets containing 15% by weight of either fresh or laboratory-heated corn oil (FCO, HCO) or fresh, laboratory-heated, or commercial pressure deep-fry peanut oil (FPO, HPO, PPO). Total weight gain, feed consumption, and feed efficiency were consistently greater for the FCO, FPO, and PPO groups. Although relative heart weights were unaffected, the HCO and HPO produced elevated liver and kidney weights. The dietary fats had no effect on the hematological status of the animals or the proportions of cells comprising the total leukocytes of the blood. Physical, chemical, and microscopic evaluation of the urine detected no pathologic conditions. Rats fed diets containing HCO or HPO demonstrated toxicity of thermally oxidized fats by the appearance of diarrhea, dermatitis, seborrhea, and hair loss. Histological examinations revealed injury of the thymus by all fat samples except the FCO; the liver was damaged by the HCO, HPO, and PPO, and the testes and epididymides by HPO and PPO. In the latter case there was complete cessation of spermatogenesis.

Animals↗
PubMed1983

Vaccine for enterotoxigenic Escherichia coli based on synthetic heat-stable toxin crossed-linked to the B subunit of heat-labile toxin.

Synthetically produced Escherichia coli heat-stable toxin (ST) was conjugated to the nontoxic B subunit of the heat-labile toxin (LT) by the carbodiimide reaction. Modifying the molar ratio of toxins mixed and the ratio of carbodiimide added to the toxins permitted synthesis of conjugates with any desired degree of proportional antigenicity for each toxin component. Immunization of rats by the parenteral/peroral routes with cross-linked vaccine containing 39% ST and 61% B subunit antigenicity, with 0.06% residual ST toxicity, evoked fourfold to sevenfold increases over control values of serum IgG and mucosal secretory IgA antitoxin titers to each of the component toxins, thus providing significant (P less than 0.001) protection against challenge with either LT or ST or with viable heterologous strains which produce these toxins. These observations show that cross-linking synthetic ST to the B subunit results in a nontoxic vaccine that provides protection against all types of enterotoxigenic E. coli.

Animals↗
PubMed1993

In vitro comparison of heated saline-blood admixture with a heat exchanger for rapid warming of red blood cells.

We compared the rapidity of rewarming and infusing red blood cells (RBCs) mixed with 24 degrees C, 50 degrees C, and 60 degrees C saline with the rapidity of administering undiluted RBCs through a heat exchanger. We measured flow rate, final temperature, and hemolysis in matched 41-45-day-old pooled AS-1 RBCs infused through high-flow tubing via a 14-gauge catheter under the influence of gravity. Undiluted RBCs were tested as controls. The final temperature of the 60 degrees C admixture technique was lower than that with the heat exchanger (28.5 +/- 0.2 degrees C vs. 32.7 +/- 0.2 degrees C), but the flow rate was higher (258 +/- 8 mL/min vs. 61 +/- 4 mL/min). Admixture with 60 degrees C saline resulted in no increase in hemolysis. This technique appears to be a simple, inexpensive method for rapid rewarming and infusion of RBCs and may be valuable for administration of RBCs simultaneously through multiple sites during resuscitation.

Erythrocyte Transfusion↗
PubMed1995

Comparison of thermocoagulation effects of low power, slow heating versus high power, rapid heating Nd: YAG laser regimens in a canine prostate model.

We compared the thermocoagulation effects of low power, slow heating (15 W x 180 seconds) versus high power, rapid heating (50 W x 60 seconds) laser regimens in the canine prostate. The study was performed in 20 mongrel canines. On each prostate, the low power regimen was delivered at the 2 and 4 o'clock positions, and the high power at the 8 and 10 o'clock positions. The laser power was measured at the fiber tip. Seven dogs (acute group) were sacrificed 1 hour after the procedure. The other 13 dogs (chronic group) were sacrificed at different time intervals from 3 days to 9 weeks after the procedure. The average depth of coagulation was significantly greater in lesions treated at low power (acute: 10.7 mm., chronic: 13.3 mm.) than in those treated at high power (acute: 8.5 mm., chronic: 11.6 mm.). Another potential benefit of the low power regimen observed in the study was preservation of the integrity and efficiency of the laser probe.

Animals↗
PubMed2000

Ion heating and high-energy-particle production by ion-cyclotron heating in the large helical device

Ion-cyclotron heating was applied to the Large Helical Device. When the proton-cyclotron resonance was near the saddle point of the magnetic field-strength plane, strong ion-cyclotron damping occurred. Under these conditions efficient plasma heating was achieved for more than one minute. A high-energy ion tail was observed, and the effective tail temperature was determined by a balance between the wave acceleration and the electron-drag relaxation. There was no apparent sign of particle orbit loss effect in the investigated density range of 0.8-1.3x10(19) m(-3).

Journal Article↗
PubMed1985

Determination of the heat resistance of spores using a solid heating block system.

A simple and accurate technique for the determination of the heat resistance of spores is described. The technique combines a modified capillary tube method with a solid heating block. The come-up time of spore suspensions was found to be short and simple and accurate technique is suggested for the correction of the come-up times. Experimental results are presented for the destruction of spores of Bacillus stearothermophilus at 120 degrees which indicates the accuracy and reproducibility of the new method.

Geobacillus stearothermophilus↗
PubMed1985

The release of dipicolinic acid during heating and its relation to the heat destruction of Bacillus stearothermophilus spores.

The rates of dipicolinic acid (Dpa) release and the rates of death were studied for spores of five strains of Bacillus stearothermophilus. It was observed that a highly significant relationship exists between the rate of Dpa release and rate of spore death for the four out of five strains tested and for all test temperatures. At 115 degrees C the rate of Dpa release was found to be faster than the rate of death, equal at 120 degrees C and slower at 125 degrees C. The role of Dpa in heat resistance was considered and a theory is proposed to explain the mechanism by which the heat resistance of bacterial spores is overcome.

Geobacillus stearothermophilus↗
PubMed1990

Export and processing analysis of a fusion between the extracellular heat-stable enterotoxin and the periplasmic B subunit of the heat-labile enterotoxin in Escherichia coli.

As an initial approach in the study of the mechanism of secretion of the extracellular heat-stable enterotoxin of Escherichia coli (STA), and in order to use this polypeptide as an extracellular carrier we previously constructed a fusion between the complete STA toxin (pre-pro-STA) and the mature B subunit of the periplasmic heat-labile enterotoxin (LTB); the resulting STA-LTB hybrid was not secreted to the extracellular environment, and cells expressing the hybrid lysed at temperatures above 35 degrees C. In this work we have established that the hybrid is initially detected as pre-pro-STA-LTB and converted to pro-STA-LTB, which lacks the 19 amino acids that share the properties of a signal peptide; the sequenced 17 amino-terminal residues of pro-STA-LTB defined the processing site of pre-pro-STA-LTB at pro-3phe-2ala-1 decreases gln+1. This process was sensitive to an energy uncoupler (CCCP) and was correlated with translocation of pro-STA-LTB across the inner membrane. Additionally, we are able to show that although pre-pro-STA-LTB is processed at 37 degrees C and 29 degrees C, it is more efficiently processed at the latter temperature. At 37 degrees C, pro-STA-LTB was poorly released into the periplasm, resulting in accumulation of this protein, pre-pro-STA-LTB, and pre-beta-lactamase in the inner membrane, and in cell lysis. In contrast, at 29 degrees C pro-STA-LTB was localized in the periplasm and in the inner membrane, and pre-pro-STA-LTB and pre-beta-lactamase did not accumulate; however, translocation of periplasmic pro-STA-LTB across the outer membrane still did not occur, and a second processing step that would eliminate the pro segment from pro-STA-LTB was never observed. Thus, the fusion of pre-pro-STA and LTB resulted in a polypeptide that, while incompatible with secretion to the extracellular medium, is exported to the periplasm in a temperature-conditional fashion. This latter observation is consistent with an STA secretion pathway whereby pre-pro-STA is first processed to periplasmic pro-STA by the removal of a 19-amino-acid signal peptide.

Amino Acid Sequence↗
PubMed1984

Determination of skin blood flow by 133Xe washout and by heat flux from a heated tc-PO2 electrode.

133Xe washout measurements were used to determine cutaneous and subcutaneous blood flow beneath a specially designed double-thermostat tc-PO2 electrode. The skin blood flow was determined using thermal methods based on reduced heat dissipation during blood flow cessation. A total of 20 measurements were performed on two healthy volunteers, using the volar side of the right forearm as the experimental area. Cutaneous as well as subcutaneous blood flow increased with increasing electrode temperature. The cutaneous blood flow increased from 12.3 +/- 1.3 ml (100 g)-1 X min-1 (37 degrees C) to 49.1 +/- 5.4 ml (100 g)-1 X min-1 (45 degrees C) and the subcutaneous values from 20.9 +/- 0.2 ml (100 g)-1 X min-1 to 57.3 +/- 0.5 ml (100 g)-1 X min-1. Preheating of the measuring area or injection of papaverine as blood flow accelerator did not increase the maximum blood flow values. A considerable inter-individual difference between cutaneous and subcutaneous blood flow was observed, but in spite of that a good overall correlation between the 133Xe washout measurements and the two thermal flow measurements was found (r = 0.932 and 0.945, respectively). It is concluded that in some cases, but not always, measurements of tc-PO2 at electrode temperatures of 45 degrees C take place on a maximally perfused skin and that it is possible to determine skin blood flow by means of determinations of the heat dissipated from the tc-PO2 electrode to the underlying skin.

Adult↗
PubMed1991

Unusual Drosophila virilis stress-puff at 20CD: cytological localization of a heat sensitive locus and some peculiarities of the heat shock response.

Using a series of chromosome aberrations a heat shock (hs) inducible site of the Drosophila virilis heat shock puff 20CD has been cytologically localized in the distal 20C subdivision: the hs puff was not observable in chromosome 2 carrying the Df(2)ebTG-52 deficiency; the bands in the proximal 20D subdivision could not autonomously be activated by hs in aberrant chromosomes that have this deficiency or the In(2)ebPC-19 inversion. An electron microscopy (EM) analysis of the successive stages of puff development in the 20CD and 20F regions shows that the 20CD puff is intially formed from the right part of the 20C6-7 band. In the maximally developed puff, the neighboring bands of the 20C and 20D regions are only partially decondensed; they are seen as discrete compact chromatin clumps. Specific differences in the ultrastructural organization and in response to hs have been found between the D. virilis "unusual" 20CD and typical 20F hs puffs.

Animals↗
PubMed2006

Significance of heat-stable and heat-labile enterotoxins in porcine colibacillosis in an additive model for pathogenicity studies.

Although heat-stable (ST) and heat-labile (LT) enterotoxins produced by enterotoxigenic Escherichia coli (ETEC) have been documented as important factors associated with diarrheal diseases, investigations assessing the contributions of individual enterotoxins to the pathogenesis of E. coli infection have been limited. To address the individual roles of enterotoxins in the diarrheal disease caused by K88-positive ETEC in young pigs, enterotoxin-positive and -negative isogenic E. coli strains were constructed by using pBR322 to clone and express LT and STb. Four strains, K88+ astA, K88+ astA/pBR322, K88+ astA STb+, and K88+ astA LT+, were constructed and subsequently included in gnotobiotic piglet challenge studies, and their pathogenesis was assessed. The results indicated that all K88+ isogenic strains were able to colonize the small intestines of piglets exhibiting the K88 receptor. However, only LT- and STb-positive strains caused appreciable diarrhea. Piglets inoculated with the K88+ astA LT+ strain became dehydrated within 18 h, while those inoculated with the K88+ astA STb+ strain did not, although diarrhea developed in several piglets. The changes in the blood packed-cell volume and plasma total protein of gnotobiotic piglets inoculated with the LT-positive strains were significantly greater than those of pigs inoculated with the K88 astA/pBR322 strain (P = 0.012, P = 0.002). Immunochemistry image analysis also suggested that LT enhanced bacterial colonization in a gnotobiotic piglet model. This investigation suggested that LT is a major contributor to the virulence of K88+ ETEC and that isogenic constructs are a useful tool for studying the pathogenesis of ETEC infection.

Animals↗
PubMed1981

Immunological properties of Escherichia coli heat-stable enterotoxins: development of a radioimmunoassay specific for heat-stable enterotoxins with suckling mouse activity.

Antiserum was raised against the purified heat-stable enterotoxin (ST) produced by enterotoxigenic Escherichia coli strain 431, a class II porcine enteropathogen. The antiserum was used to examine the antigenic determinants of STs produced by enterotoxigenic strains of different host origins and develop a sensitive radioimmunoassay specific for ST having biological activity in suckling mice and piglets (STA). The antiserum neutralized one effective dose of toxin at a dilution of 1:5,000 and neutralized approximately 40 microgram of toxin per ml of serum. In the radioimmunoassay, protein A-bearing staphylococci was used as the primary solid-phase adsorbent. The purified STs produced by a class I enteropathogen (strain 667) and by a bovine enterotoxigenic strain (B-41) exhibited patterns of competitive inhibition identical to those of homologous unlabeled strain 431 ST in the radioimmunoassay when specific antibody to strain 431 ST was used. The levels of ST in culture supernatants determined by the suckling mouse assay correlated with the concentrations of toxin measured by the radioimmunoassay. The antiserum was specific for STA produced by enterotoxigenic E. coli of porcine, bovine, and human origins and did not react with heat-labile enterotoxin or with ST that had biological activity in piglets but not in suckling mice (STB). These results suggest that STA molecules having different host origins share at least one antigenic determinant.

Animals↗
PubMed1982

Development of a vaccine of cross-linked heat-stable and heat-labile enterotoxins that protects against Escherichia coli producing either enterotoxin.

A vaccine of cross-linked heat-stable (ST) and heat-labile (LT) toxins that protects against heterologous serotypes of strains of Escherichia coli which produce either the LT or ST enterotoxin was developed by conjugating ST to LT by the carbodiimide reaction. Three interrelated factors were found to affect the composition and properties of the final conjugate: (i) the amount of carbodiimide added to the toxins, (ii) the initial ratio of ST to LT, and (iii) the duration of the conjugation reaction. Optimal conjugation conditions were identified as a carbodiimide-to-toxin ratio of 10:1 by weight, an initial molar ratio of ST to LT of 100:1, and a conjugation reaction time of 96 h. This approach yielded a conjugate that contained 96% by moles and 36% by weight pure ST, determined with radioiodinated pure ST, and 34% by weight semi-pure ST, determined by the Lowry protein method. The retained antigenicities of the conjugated toxins, as determined by enzyme-linked immunosorbent assays, was greater than or equal to 82%, and their toxicities, as determined by the Y1 adrenal cell assay for LT and by the suckling mouse assay for ST, were reduced to less than or equal to 0.15%. Immunization of rats with this cross-linked ST-LT vaccine provided strong protection against challenge with either the LT or the ST toxin or with viable heterologous strains which produce these toxins, either singly or together. These observations indicate that conjugation of ST to LT results in a unique new immunogen in that ST acquires immunogenicity as a function of the reaction, LT retains most of its antigenicity, and the toxic properties of each individual toxin are greatly reduced.

Animals↗
PubMed1983

Plasmid coding for drug resistance and production of heat-labile and heat-stable toxins harbored by an Escherichia coli strain of human origin.

In a study of enterotoxigenic strains of Escherichia coli isolated from children with diarrhea in São Paulo, Brazil, a new enterotoxin and antibiotic resistance plasmid that carries heat-labile toxin, heat-stable toxin, and drug resistance genes was found. This is the first such plasmid to be found in a human strain of E. coli. The plasmid is nonconjugative, has a molecular weight of at least 54 x 10(6), and is mobilized by the R plasmid present in the host strain.

Anti-Bacterial Agents↗
PubMed1983

Characterization of the gene encoding heat-stable toxin II and preliminary molecular epidemiological studies of enterotoxigenic Escherichia coli heat-stable toxin II producers.

The gene encoding heat-stable toxin II (STII) was cloned into an Escherichia coli K-12 strain, and its nucleotide sequence was determined. The deduced amino acid sequence indicates that STII is synthesized within the cell as a 71-amino-acid protein and that neither the DNA nor amino acid sequence bears any similarity to that of heat-stable toxin I. A DNA fragment containing the STII gene was used to probe enterotoxigenic E. coli clinical isolates with various toxin phenotypes and was shown to be useful in detecting all STII and only STII producers.

Amino Acid Sequence↗
PubMed1986

Plasmids coding for colonization factor antigens I and II, heat-labile enterotoxin, and heat-stable enterotoxin A2 in Escherichia coli.

Colonization factor antigens I and II (CFA/I and CFA/II) are important in the pathogenesis of diarrhea in humans caused by some enterotoxigenic Escherichia coli (ETEC). Plasmid DNA from 16 CFA/I+ and five CFA/II+ ETEC were examined by Southern blot analysis with enterotoxin gene probes and were compared with plasmid DNA from derivatives of the same ETEC that had lost the ability to produce these colonization factors. Among the 16 CFA/I+ ETEC strains, the loss of CFA/I was accompanied by the loss of a plasmid of between 34 and 68 megadaltons (MDa) coding for heat-stable enterotoxin A2 (ST-A2) in 12 strains, by the loss of a 60-MDa plasmid coding for heat-labile enterotoxin (LT) and ST-A2 in one strain, or by deletions of a segment of DNA encoding for ST-A2 in three strains. Among five CFA/II+ ETEC strains, the loss of CFA/II was associated with the loss of a plasmid of 75 MDa coding for LT and ST-A2 in three strains, with the loss of genes coding for LT and ST-A2 from a 68-MDa plasmid in one strain, or with no discernible loss of a plasmid or DNA sequences coding for enterotoxins in the remaining strain. The loss of CFA/I and CFA/II production was associated with the loss of DNA sequences encoding for ST-A2 in 20 of 21 ETEC examined.

Antigens, Bacterial↗
PubMed1990

Construction of a nontoxic fusion peptide for immunization against Escherichia coli strains that produce heat-labile and heat-stable enterotoxins.

The 5' terminus of the gene that codes for the heat-stable enterotoxin of Escherichia coli (ST) was genetically fused to the 3' terminus of the gene that codes for the binding subunit of the heat-labile enterotoxin of E. coli (LT-B). The ST-encoding gene used for these studies was constructed synthetically with appropriate restriction sites to permit in-frame, downstream insertion of the oligomer. For this construction, maximum expression of ST antigenicity was obtained when a seven-amino-acid, proline-containing linker was included between the LT-B and ST moieties. The LT-B-ST fusion peptide was purified by affinity chromatography and consisted of a single polypeptide chain with an apparent molecular weight of 18,000 when examined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. There was no evidence of multimer formation and no change in the mobility of the fusion peptide when it was boiled in SDS or in SDS with dithiothreitol. The LT-B-ST fusion peptide was nontoxic, and immunologic determinants of both LT and ST were recognized by antibodies to the native toxins. More importantly, the LT-B-ST fusion peptide was immunogenic. Animals immunized with crude or purified preparations containing the hybrid molecule produced antibodies that were able to recognize native toxin in vitro. Significantly, these antibodies were able to neutralize the biological activity of native ST.

Amino Acid Sequence↗