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Blood inflammatory response to inhaled endotoxin in normal subjects (1995)

MICHEL, O. ; DUCHATEAU, J. ; PLAT, G. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Clinical & experimental allergy 25 (1995), S. 0

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ISSN: 1365-2222

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: Previously we have reported that in asthmatics an inhalation of 20 μg lipopolysaccharide (LPS) produces a bronchial obstruction associated with an inflammatory blood response. The aim of the present study was to evaluate this response in normal subjects. Eight normal non-atopic subjects were challenged by inhalation of a solution containing 20 μg LPS (from Escherichia coli 026:B6) a week after bronchial challenge with control solution. The lung function response was evaluated by the changes in forced expiratory volume in one second (FEV1), in specific conductance and in airway resistance while the blood inflammatory response was evaluated by serial measures of total white blood cells (WBC) and polymorphonuclear neutrophils (PMN) count, luminol enhanced-chemiluminescence (luminol-CL, as a marker of the PMN degree of activation), C-reactive protein (CRP), haptoglobin, complement fraction C3, tumour necrosis factor-α (TNF-α) and adrenocorticotropic hormone (ACTH). No response in lung function was observed for 6 h after the LPS inhalation. The count in WBC and PMN increased 300 (P 〈 0.01) and 360 (P 〈 0.01) min after the LPS challenge associated with an increase in the level of luminol-CL (P 〈 0.001). This rise in luminol-CL level was significant at 120 min (P 〈 0.05) before any change in the PMN count. After 24 and 48 h the acute-phase protein CRP raised significantly (P 〈 0.01), the other proteins C3 and haptoglobin being unchanged. A slight increase in ACTH was observed 240 and 360 min (P 〈 0.05) after the LPS challenge while the TNFα detectable level was not modified. In conclusion, in normal subjects, inhalation of a pro-inflammatory agent is able to induce a systemic inflammatory response in the absence of any effect on lung mechanics, while in asthmatics the same bronchial challenge has been reported to induce a similar blood inflammation associated with a significant response in lung function.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1365-2222.1995.tb01005.x

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Characterization of glyoxysomes in yeasts and their transformation into peroxisomes in response to changes in environmental conditions (1983)

Zwart, K. B. ; Veenhuis, M. ; Plat, G. ; [et al.]

Springer

Archives of microbiology 136 (1983), S. 28-38

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ISSN: 1432-072X

Keywords: Yeasts ; Candida utilis ; Hansenula polymorpha ; Microbodies ; Peroxisomes ; Glyoxysomes ; Cell fractionation ; Cytochemistry ; Catalase ; Glyoxylate cycle ; Oxidase

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract During growth of the yeasts Candida utilis and Hansenula polymorpha in mineral media containing ethanol as a carbon source and ammonium sulphate as a nitrogen source, the specific activities of isocitrate lyase and malate synthase were significantly increased when compared to glucose/ammonium sulphate-grown cells. In addition to the enhanced levels of these glyoxylate cycle enzymes, an increase in the specific activities of d-amino acid oxidase, amine oxidase or urate oxidase was observed when ammonium sulphate in the ethanol medium was replaced by d-alanine, methyl- or ethylamine, or uric acid. The subcellular localization of these enzymes was investigated by cell fractionation studies involving homogenization of protoplasts followed by differential and sucrose gradient centrifugation. In ethanol/ammonium sulphate-grown cells, isocitrate lyase and malate synthase cosedimented in a fraction together with catalase and part of the malate dehydrogenase. Electron microscopy revealed that this fraction consisted of microbodies which must be regarded as glyoxysomes. Two other glyoxylate cycle enzymes, citrate synthase and aconitase together with the other part of malate dehydrogenase, cosedimented with cytochrome c oxidase, a mitochondrial marker enzyme. In ethanol/d-alanine-, ethanol/methylamine- or ethanol/ethylamine-grown C. utilis and ethanol/uric acid-grown H. polymorpha, a peroxisomal enzyme, i.e. d-amino acid oxidase, amine oxidase or uric acid oxidase cosedimented with the glyoxysomal key enzymes. Cytochemical staining experiments demonstrated that in these variously-grown cells the activities of the oxidases were confined to the microbodymatrix; this also contained malate synthase activity. Transfer of C. utilis cells from glucose/ammonium sulphate- into ethanol/ammonium sulphate-containing media resulted in an increase in the original size and volume fraction of the microbodies. A further increase was observed when ammonium sulphate was replaced by methylamine. Essentially similar results were obtained with H. polymorpha cells. In neither of the two organisms indications of de novo synthesis of microbodies was obtained during transfer experiments. Invariably the microbodies developing in cells placed in the new environment originated from organelles already present in the inoculum cells by import of the substratespecific enzyme protein(s). The combined results of biochemical, cytochemical and electron microscopical experiments showed that in the yeasts studied under appropriate conditions glyoxysomal and peroxisomal enzyme activities were localized in one and the same microbody, rather than in separate organelles.