Arrangement of the respiratory burst oxidase in the plasma membrane of the neutrophil.

Babior, G L; Rosin, Richard E.; McMurrich, B. Jane; Peters, W A; Babior, Bernard M.

doi:10.1172/jci110210

Cited by 135 publications

(37 citation statements)

References 21 publications

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“…Here we confirm with bovine PMN permeabilized by deoxycholate that added NADPH is readily oxidi7ed with generation of 0; and that NADH is virtually incffective. The fact that deoxycholate makes the 0; -generating oxidase readily accessible to added NADPH is in accordance with the specifjc oxidase being located in the plasma membrane and with its NADPH-binding site exposed to the interior of the cell [45]. In this context, the lack of effect of deoxycholate on the oxidase activity of phagocytic vacuoles harvested from an homogenate of bovine PMN after phagocytosis of PMh-coated latex particles may be explained by assuming thal in phagocytic vacuoles the NADPH binding site of the O:-generating oxidase is inside-out and therefore exposed to the medium.…”

Section: O~n Z Y M C Spc'clfi'city Of the Respiratory Burstmentioning

confidence: 59%

The respiratory burst of bovine neutrophilis

Morel¹,

Doussière²,

Stasia³

et al. 1985

European Journal of Biochemistry

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1.A new method of preparation of bovine polymorphonuclear leukocytes (PMN) is described. The subcellular distribution of cytochrome b in resting and activated bovine PMN was compared to that of the 0;-generating oxidase (assessed as NADPH cytochrome c reductase inhibited by superoxide dismutase). In resting PMN and in PMN activated by phorbol myristate acetate (PMA), cytochrome b was located into two membrane fractions, one of which was enriched in plasma membrane and cosediinented with alkaline phosphatase, while the other consisted of a denser material cosedimenting with markers of the specific and azurophil granules, i.c. the vitamin-BIZ-binding protein and myeloperoxidase respectively. During activation of PMN by PMA, 15 -20% cytochrome b migrated from dense granules to the plasma membrane.2. The distribution of the 0; generating oxidase and cytochrome h in subcellular particles was studied during the course of phagocytosis of PMA-coated latex beads by bovine PMN. At the onset of the respiratory burst, the phagocytic vacuoles arising from internalization of the plasma membrane were enriched in oxidase and alkaline phosphatase, but their specific content of cytochrome h was limited; in contrast, cytochrome h was predominant in denser membrane fractions cosedimenting with myeloperoxidase and the vitamin-BI ,-binding protein. After a few minutes of phagocytosis, a fraction of light vacuoles, slightly denser than the phagocytic vacuoles, became enriched in 0;-generating oxidase, cytochrome b, the vitamin-B,,-binding protein and myeloperoxidase. These vacuoles probably arose from the fusion of the phagocytic vacuoles with dense granules.3. In bovine P M N supplemented with glucose and maintained in anaerobiosis, activation by PMA induced slow reduction of cytochrome b (60-70% in 15 min at 37°C). Similar results were obtained with cytoplasts after activation by PMA (30% reduction in 3 niin at 37°C). Cytochrome h in a particulate fraction obtained by centrifugation at I00000 x g of an homogenate of PMA-activated PMN, was slowly reduced upon addition of NADPH under anaerobiosis (less 20% in 20 min at 37 'C). N o reduction occurred in the 100000 x g fraction prepared from non-activated PMN. The Soret band of cytochrome h reduced by dithionite was displaced by C 0 only by 1 -2 nm. At subsaturating concentrations, CO had no effect on the rate of O2 uptake by activated bovine PMN. 4. The specificity for NADPH and NADH of the 0;-generating oxidase was assayed in the 100000xg fraction obtained from PMA-activated bovine PMN and in the phagocytic vacuoles prepared after phagocytosis of PMA-coated latex beads. In both types of particles, the preferential substrate was NADPH. On the other hand, NADH was a better electron donor for a superoxide-dismutase insensitive cytochrome <' reductase (diaphorase). Deoxycholate enhanced the NADPH-dependent Or-generating oxidase of the 100000 x g fraction, but not that of the phagocytic vacuoles, indicating free access of NADPH to its binding site on the oxidase in the latter case, but n...

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Section: O~n Z Y M C Spc'clfi'city Of the Respiratory Burstmentioning

confidence: 59%

The respiratory burst of bovine neutrophilis

Morel¹,

Doussière²,

Stasia³

et al. 1985

European Journal of Biochemistry

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“…Neutrophil function was measured using the luminol-enhanced chemiluminescence (CL) response as the parameter of function (Allred et al, 1980;Babior et al, 1981). The data presented here show that PMN function is suppressed in vitro when exposed to purified FeLV-pl5E and UV-FeLV.…”

Section: Introductionmentioning

confidence: 89%

Suppression of in vitro Neutrophil Function by Feline Leukaemia Virus (FeLV) and Purified FeLV-p15E

Lafrado¹,

Lewis²,

Mathes

et al. 1987

Journal of General Virology

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“…CL is the result of the oxidative metabolic burst associated with the membranes of phagocytic cells and is measured by a light release assay (Babior et al, 1981 ;Klebanoff, 1980). The CL response associated with particle uptake by PMN has been directly associated with their microbiocidal activity (Horan et al, 1982).…”

Section: Introductionmentioning

confidence: 99%

Polymorphonuclear Leukocyte Dysfunction Associated with Feline Leukaemia Virus Infection

Lewis¹,

Duska²,

Stiff³

et al. 1986

Journal of General Virology

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SUMMARYThe chemiluminescent characteristics of enriched (>95%) peripheral blood polymorphonuclear leukocyte populations (PMN) from normal and feline leukaemia virus (FeLV)-infected cats were investigated. FeLV-infected cats demonstrated a significantly lower (P < 0.001) PMN chemiluminescent response when compared to the response of normal age-matched controls. Normal PMN treated with FeLVinfected cat serum exhibited a depressed response in comparison to control cells. A titration of serum from infected cats supplemented with normal serum revealed a titratable suppression of chemiluminescence with increasing concentration of serum from the infected cats. However, PMN from FeLV-infected cats treated with normal serum displayed a slight increase in chemiluminescence over the same cells in autologous serum. The addition of inactivated FeLV to normal PMN caused a titratable decrease in chemiluminescence.

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Arrangement of the respiratory burst oxidase in the plasma membrane of the neutrophil.

Cited by 135 publications

References 21 publications

The respiratory burst of bovine neutrophilis

The respiratory burst of bovine neutrophilis

Suppression of in vitro Neutrophil Function by Feline Leukaemia Virus (FeLV) and Purified FeLV-p15E

Polymorphonuclear Leukocyte Dysfunction Associated with Feline Leukaemia Virus Infection

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