Eosinopenia of Acute Infection

Bass, David; Gonwa, Thomas A.; Szejda, Pamela; Cousart, M S; DeChatelet, Lawrence R.; McCall, Charles E.

doi:10.1172/jci109789

Cited by 148 publications

(61 citation statements)

References 26 publications

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“…DCFH is trapped inside the cells and oxidized to the highly fluorescent DCF by a variety of reactive species such as HO • and ROO • [24] and also by RNS like • NO and ONOO − [18]. In 1983, Bass et al [46] used, for the first time, the probe DCFH to measure H 2 O 2 in neutrophils. Later, it was reported that the oxidation of DCFH by H 2 O 2 is an indirect reaction since it depends on the peroxidase activity [47,48].…”

Section: 7 -Dichlorodihydrofluorescein (Dcfh)mentioning

confidence: 99%

Optical probes for detection and quantification of neutrophils’ oxidative burst. A review

Freitas

Lima

Fernandes

2009

Analytica Chimica Acta

149

115

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Section: 7 -Dichlorodihydrofluorescein (Dcfh)mentioning

confidence: 99%

Optical probes for detection and quantification of neutrophils’ oxidative burst. A review

Freitas

Lima

Fernandes

2009

Analytica Chimica Acta

149

115

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“…To demonstrate this in human breast carcinoma MCF-7 cells, these cells were incubated with the non¯uorescent probe, 2',7'-dichloro¯uorescin, (DCFH-DA) (Bass et al, 1983). This probe enters the cells and can be oxidized in the presence of ROS, generating the¯uorescent compound, 2',7', dichloro¯uorescein (DCF).…”

Section: Hypoxia Increases Mitochondrial Generation Of Reactive Oxygementioning

confidence: 99%

Redox regulation of p53 during hypoxia

et al. 2000

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The transcription factor p53 can induce growth arrest or death in cells. Tumor cells that develop mutations in p53 demonstrate a diminished apoptotic potential, which may contribute to growth and tumor metastasis. Cellular levels of p53 are stabilized during hypoxia. The present study tested the hypothesis that reactive oxygen species (ROS) released from mitochondria regulate the cytosolic redox state and are required for the stabilization of p53 protein levels in response to hypoxia. Our results indicate that hypoxia (1.5% O 2 ) increases mitochondrial ROS generation and increases p53 protein levels in human breast carcinoma MCF-7 cells and in normal human diploid ®broblast IMR-90 cells. MCF-7 cells depleted of their mitochondrial DNA (r8 cells) failed to stabilize p53 protein levels during hypoxia. The antioxidant Nacetylcysteine and the Cu/Zn superoxide dismutase inhibitor diethyldithiocarbamic acid abolished the hypoxia-induced increases in ROS and p53 levels. Rotenone, an inhibitor of mitochondrial complex I, and 4,4'-diisothiocyanato-stilbene-2,2'-disulfonate, a mitochondrial anion channel inhibitor, also abolished the increase in ROS signal and p53 levels during hypoxia. The p53-dependent gene p21 WAF1/CIP1 was also induced by hypoxia in both MCF-7 and IMR-90 cells without aecting the growth rate of either cell line. In contrast, both cell lines exhibited increases in p21 WAF1/CIP1 expression and growth arrest after gamma irradiation. Primary chick cardiac myocytes and murine embryonic ®broblasts also showed an increase in p53 protein levels in response to hypoxia without cell death or growth arrest. These results indicate that mitochondria regulate p53 protein levels during hypoxia through a redox-dependent mechanism involving ROS. Despite p53-induction, hypoxia alone does not cause either growth arrest or cell death.

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“…AcetylTyrFluo taken up by neutrophils is deacetylated by cytosolic esterases [29]. As shown by confocal laser scanning microscopy, the ensuing deacetylated TyrFluo product was present throughout the cells after PMA-stimulation (Fig.…”

Section: Protein Tyrosylation In Pma-activated Neutrophilsmentioning

confidence: 78%

Identification of proteins in activated human neutrophils susceptible to tyrosyl radical attack. A proteomic study using a tyrosylating fluorophore

et al. 2004

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Tyrosyl radicals cross-linked to protein tyrosine residues (tyrosylated proteins) represent hallmarks of neutrophil-mediated injury at the inflammatory locus. Yet the proteins targeted by tyrosyl radicals in an intact cellular system remain to be elucidated. Here, we show that tyrosyl radicals generated by human neutrophils after activation by phorbol 12-myristate 13-acetate (PMA), interferon-g (IFN-g) or TNF-a could act in an autocrine manner by cross-linking to endogenous proteins. We have identified the tyrosylated proteins by using a membraneimpermeable tyrosine analogue, tyramine coupled to fluorescein (TyrFluo), in combination with proteomics techniques. Confocal microscopy images indicated that initially the tyrosylated proteins were localized in patches at the cell surface to become internalized subsequently. In the neutrophil membrane-associated proteome, lactoferrin was the prime target of tyrosylation. Out of three isoforms identified, an 80 kDa neutral isoform was tyrosylated more extensively than the 85 kD basic isoform, particularly after PMA activation. Although all three stimuli induced tyrosylation of the filamentous component vimentin, additional tyrosylated vimentin fragments were detected after IFN-g-and TNF-a-stimulation. Moreover, upon activation the bulk of vimentin behaved as a dimer (M r 120 kDa) being slightly tyrosylated, yet phosphorylated at Thr-425 possibly as a requirement for its externalization. Unexpectedly, bovine catalase added to end tyrosyl radicals formation was detected as a highly tyrosylated neutrophil-associated protein. A moderate stimulus-dependent tyrosylation of ATP synthaseb, a-enolase, glyceraldehyde 3-phosphate dehydrogenase, cytokeratin-10, filamin-A, and annexin-I was also observed. When the membrane-permeable probe (acetylTyrFluo) was used, protein tyrosylation was not observed indicating that the intracellular proteins were well protected against oxidative attack. This study shows that human neutrophils can modulate their proteome via a tyrosine oxidation pathway induced by pro-inflammatory mediators.

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Eosinopenia of Acute Infection

Cited by 148 publications

References 26 publications

Optical probes for detection and quantification of neutrophils’ oxidative burst. A review

Optical probes for detection and quantification of neutrophils’ oxidative burst. A review

Redox regulation of p53 during hypoxia

Identification of proteins in activated human neutrophils susceptible to tyrosyl radical attack. A proteomic study using a tyrosylating fluorophore

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