Hyperthermia stimulates nitric oxide formation: electron paramagnetic resonance detection of .NO-heme in blood

Hall, David; Buettner, Garry R.; Matthes, R. D.; Gisolfi, C. V.

doi:10.1152/jappl.1994.77.2.548

Cited by 136 publications

(107 citation statements)

References 25 publications

Supporting

Mentioning

100

Contrasting

Unclassified

Order By: Relevance

“…The increased levels of NO immediately subsequent to the insult would cause the observed increases in CBF, CBV and the absent CBVR (this response would already be saturated with NO). Hypothermia is cerebroprotective in our piglet model ; intriguingly hyperthermia has recently been shown to stimulate NO production in i o (Hall et al 1994). Also, the close links recently shown between nitric oxide, mitochondrial damage and apoptosis are also consistent with our model (Shimaoka et al 1995 ;Liu et al 1996).…”

Section: (B) Neonatal Hypoxia-ischaemiasupporting

confidence: 85%

Measurement of cytochrome oxidase and mitochondrial energetics by near–infrared spectroscopy

Cooper

Springett

1997

Phil. Trans. R. Soc. Lond. B

139

111

View full text Add to dashboard Cite

SUMMARYCytochrome oxidase is the terminal electron acceptor of the mitochondrial respiratory chain. It is responsible for the vast majority of oxygen consumption in the body and essential for the efficient generation of cellular ATP. The enzyme contains four redox active metal centres ; one of these, the binuclear Cu A centre, has a strong absorbance in the near-infrared that enables it to be detectable in i o by near-infrared spectroscopy. However, the fact that the concentration of this centre is less than 10 % of that of haemoglobin means that its detection is not a trivial matter.Unlike the case with deoxyhaemoglobin and oxyhaemoglobin, concentration changes of the total cytochrome oxidase protein occur very slowly (over days) and are therefore not easily detectable by nearinfrared spectroscopy. However, the copper centre rapidly accepts and donates an electron, and can thus change its redox state quickly ; this redox change is detectable by near-infrared spectroscopy. Many factors can affect the Cu A redox state in i o , but the most significant is likely to be the molecular oxygen concentration (at low oxygen tensions, electrons build up on Cu A as reduction of oxygen by the enzyme starts to limit the steady-state rate of electron transfer).The factors underlying haemoglobin oxygenation, deoxygenation and blood volume changes are, in general, well understood by the clinicians and physiologists who perform near-infrared spectroscopy measurements. In contrast, the factors that control the steady-state redox level of Cu A in cytochrome oxidase are still a matter of active debate, even amongst biochemists studying the isolated enzyme and mitochondria. Coupled with the difficulties of accurate in i o measurements it is perhaps not surprising that the field of cytochrome oxidase near-infrared spectroscopy has a somewhat chequered past. Too often papers have been written with insufficient information to enable the measurements to be repeated and few attempts have been made to test the algorithms in i o.In recent years a number of research groups and commercial spectrometer manufacturers have made a concerted attempt to not only say how they are attempting to measure cytochrome oxidase by nearinfrared spectroscopy but also to demonstrate that they are really doing so. We applaud these attempts, which in general fall into three areas : first, modelling of data can be performed to determine what problems are likely to derail cytochrome oxidase detection algorithms (Matcher et al. 1995) ; secondly haemoglobin concentration changes can be made by haemodilution (using saline or artificial blood substitutes) in animals (Tamura 1993) or patients (Skov & Greisen 1994) ; and thirdly, the cytochrome oxidase redox state can be fixed by the use of mitochondrial inhibitors and then attempts made to cause spurious cytochrome changes by dramatically varying haemoglobin oxygenation, haemoglobin concentration and light scattering (Cooper et al. 1997).We have previously written reviews covering the difficulties of measuring the cyt...

show abstract

Section: (B) Neonatal Hypoxia-ischaemiasupporting

confidence: 85%

Measurement of cytochrome oxidase and mitochondrial energetics by near–infrared spectroscopy

Cooper

Springett

1997

Phil. Trans. R. Soc. Lond. B

139

111

View full text Add to dashboard Cite

show abstract

“…For instance, lipopolysaccharides, classic inducers of NO synthesis [8], also activate HSP70 synthesis [9]. On the other hand, HS, which is a conventional factor inducing HSP synthesis [1,2,10], is attended by an increase in nitrosyl heme content in blood [11]. Our own experiments have demonstrated that adaptation of the organism to stress both activates HSP70 synthesis [7] and potentiates NO generation in the same organs [12].…”

Section: Introductionmentioning

confidence: 99%

Nitric oxide donor induces HSP70 accumulation in the heart and in cultured cells

et al. 1996

View full text Add to dashboard Cite

As our group has shown, the NO-synthase inhibitor L-NNA decreased 2-3 times heat shock-induced synthesis of the heat shock protein HSP70 (FEBS Lett. 370 (1995) 159-162). It was suggested that NO is involved in such induction. In the present study, it was found that (1) injection of the NO donor dinitrosyl iron complex (DNIC) into rats results in accumulation of HSP70 in the heart; (2) heat shock is accompanied by increased generation of NO (EPR assay) and HSP70 accumulation in cultured cells; (3) DNIC induces HSP70 accumulation in cultured cells not exposed to heat shock.Taken together the data suggest that NO may contribute to the activation of HSP70 synthesis. The goal of the present study was to verify this hypothesis. We studied: (1) the effect of NO donor injection into rats on HSP70 accumulation in the heart; (2) the effect of HS on NO production in cultured cells, and (3) the effect of the NO donor on HSP70 accumulation in cultured cells. Materials and methods

show abstract

“…In intact rats, it is demonstrated that high hyperthermic conditions increased formation of ROS in the portal circulation (Hall et al, 1994;Lin et al, 2006). In broiler chickens, high ambient temperature increased plasma MDA which indicated an oxidant/antioxidant equilibrium disturbance leading to oxidative stress (Lin et al, Abbreviations: BHT, butylated hydroxytoluene; Zn, zinc; PHE300, purslane hydroextract 300 mg kg −1 of diet; PHE600, purslane hydroextract 600 mg kg −1 of diet; ZPHE300, zinc 100 mg kg −1 diet + purslane hydroextract 300 mg kg −1 of diet; ZPHE600, zinc 100 mg kg −1 diet + purslane hydroextract 600 mg kg −1 of diet; MDA, malondialdehyde; TAC, total antioxidant capacity; CAT, catalase; SRBC, sheep red blood cells; HA, hemagglutination assay; SEM, standard error of means; values are means ± SEM.…”

Section: Discussionmentioning

confidence: 99%

The effect of purslane hydroextract and zinc on performance, antioxidant capacity and immunity of broiler chickens during summer conditions

2018

View full text Add to dashboard Cite

Abstract. Due to negative effects of high ambient temperature, the present study was conducted to investigate the effects of Portulaca oleracea hydroextract (PHE) and zinc (Zn) on the growth performance and immunity of broiler chickens reared under high summer ambient temperature conditions. A total of 420 day-old male broiler chickens (Ross 308) were randomly allocated to seven dietary treatments each replicated four times with 15 birds per replicate. The basal diet as the control diet was supplemented with 100 mg kg −1 butylated hydroxytoluene (BHT), or 300 and 600 mg kg −1 of PHE, 100 mg kg −1 of zinc and 100 mg kg −1 of zinc plus 300 or 600 mg kg −1 of PHE (ZP300 and ZP600). The result of the present study showed that Zn, PHE and their combination did not alter daily feed intake and feed conversion ratio. Although there was a tendency toward an increase in broiler body weight at 24 and 44 days of age (P = 0.059 and P = 0.061), the body weight of birds fed the basal diet supplemented with Zn reduced at day 10. The birds fed diets supplemented with BHT or ZP600 showed lower aspartate aminotransferase (ASAT) and lactate dehydrogenase activity at 24 days of age (P < 0.05), but it remains lower in the ZP600 group only for ASAT activity level at day 44. The results of the present study suggest that dietary PHE and Zn supplementation partially improved body weight and serum antioxidant capacity, superoxide dismutase activity and antibody titer against sheep red blood cells and Newcastle diseases in the broiler chickens during summer conditions.

show abstract

Hyperthermia stimulates nitric oxide formation: electron paramagnetic resonance detection of .NO-heme in blood

Cited by 136 publications

References 25 publications

Measurement of cytochrome oxidase and mitochondrial energetics by near–infrared spectroscopy

Measurement of cytochrome oxidase and mitochondrial energetics by near–infrared spectroscopy

Nitric oxide donor induces HSP70 accumulation in the heart and in cultured cells

The effect of purslane hydroextract and zinc on performance, antioxidant capacity and immunity of broiler chickens during summer conditions

Contact Info

Product

Resources

About