Enhancement of Neutrophil Function as a Result of Prior Exposure to Chemotactic Factor

Epps, Dennis E. Van; Garcia, M. R.

doi:10.1172/jci109841

Cited by 153 publications

(44 citation statements)

References 22 publications

(19 reference statements)

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“…The ability of arachidonate to activate in the neutrophil particulate fraction after priming is similar to the elicited macrophage system described by Bromberg and Pick (7). Thus, it is possible that the exposure of macrophages in vivo to an eliciting agent is analogous to the priming of neutrophils in vitro, and evidence for in vivo priming of neutrophils by elicitation to the peritoneum has been described (14). Alternatively, the macrophage may have somewhat different regulatory mechanisms for oxidase activation than those in the neutrophil.…”

Section: Resultssupporting

confidence: 61%

Activation of the respiratory burst enzyme from human neutrophils in a cell-free system. Evidence for a soluble cofactor.

McPhail¹,

Shirley²,

Clayton³

et al. 1985

J. Clin. Invest.

324

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Activation of the respiratory burst in phagocytic cells, an important host defense process, is not yet well understood. We now report the development of a cell-free system for activation of NADPH oxidase, the respiratory burst enzyme, in human neutrophils. Activation was achieved by the addition of arachidonic acid to a postnuclear supernatant (500 g) from disrupted unstimulated cells (no arachidonate, 0.2; with arachidonate, 3.4 nmol superoxide anion/min per mg) and was dependent on both the concentration of arachidonate and on the amount of cellular material present. Activity stimulated by arachidonate appeared to be NADPH oxidase based on a Michaelis constant for NADPH of 32 jzM and a pH optimum of 7.0-75. Separation of the 500-g supernatant by high speed centrifugation revealed a requirement for both soluble and particulate cofactors. Activation of NADPH oxidase by arachidonate did not occur in the high speed pellet fraction from unstimulated cells but could be restored by the addition of the high speed supernatant. In addition, priming of intact neutrophils with low concentrations of the chemoattractant N-formyl-methionyl-leucyl-phenylhlanine or the tumor promoter phorbol myristate acetate replaced the soluble factor requirement for NADPH oxidase activation by arachidonate in the high speed pellet. This cell-free system can now be used to provide further insight into the biochemical basis of priming and the terminal mechanisms involved in the activation of NADPH oxidase.

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Section: Resultssupporting

confidence: 61%

Activation of the respiratory burst enzyme from human neutrophils in a cell-free system. Evidence for a soluble cofactor.

McPhail¹,

Shirley²,

Clayton³

et al. 1985

J. Clin. Invest.

324

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“…It has been observed previously that PMNL modify their functional characteristics by sequential stimulation [16,[21][22][23][24].…”

Section: Discussionmentioning

confidence: 99%

The Role of Formylpeptide Receptors, C5a Receptors, and Cytosolic-Free Calcium in Neutrophil Priming

Zimmerli

Reber²,

Dahinden³

1990

Journal of Infectious Diseases

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“…The identical time elapsed between the onset of these protracted stimuli (tissue cages or glycogen), the cytology of the two exudates, and the results of histopathologic examination of the two surrounding tissues suggest the presence of cell populations of the same age. This issue, however, can be resolved unambiguously only by future experiments involving comparison of pulselabeled PMNLs; for the time being, comparison of PMNLs from blood and exudate has been considered as an adequate procedure in similar experiments [40]. (2) The observed phagocytic bactericidal defect in PMNLs from tissue cages is all the more striking because Van Epps and Garcia have demonstrated that PMNLs from peritoneal exudates of guinea pigs elicited by a soluble stimulus actually show increased, rather than decreased, metabolic activity [40].…”

Section: Discussionmentioning

confidence: 99%

Pathogenesis of Foreign Body Infection: Description and Characteristics of an Animal Model

Zimmerli

Waldvogel

Vaudaux

et al. 1982

Journal of Infectious Diseases

576

383

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An animal model involving the subcutaneous implantation of tissue cages into guinea pigs and subsequent infection with Staphylococcus aureus was used to study factors pertinent to foreign body infection. Whereas 10 8 colony-forming units (cfu) of S. aureus strain Wood 46 did not produce any abscesses in the absence of foreign material, 10 2 cfu was sufficient to infect 95070 of the tissue cages despite the presence of polymorphonuclear leukocytes (PMNLs) in sterile tissue cage fluid. Opsonization of S. aureus by tissue cage fluid was adequate during the first hour of infection, but opsonic coating of the organisms decreased at 20 hr after the induction of infection. PMNLs from sterile tissue cage fluid showed decreased phagocytic and bactericidal activities when compared with PMNLs from either blood or peritoneal exudate obtained after short-or long-term stimulation (P < 0.001).The enhanced risk of bacterial infections in the vicinity of a foreign body -such as sutures and metallic or polymeric implants -has been repeatedly documented in cardiovascular [1][2][3], orthopedic [4][5][6], plastic reconstructive [7], and general [8] surgery. Staphylococcus aureus, Staphylococcus epidermidis, and Escherichia coli are most frequently implicated as the etiologic agents [9]. Foreign body infection proceeds by two possible routes: early infection, due to local bacterial contamination during surgery [4], and late infection, after occasional seeding of microorganisms by the hematogenous route [6]. Both types of infections, once established, rarely heal, and excision of the foreign body remains the only effective treatment.

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Enhancement of Neutrophil Function as a Result of Prior Exposure to Chemotactic Factor

Cited by 153 publications

References 22 publications

Activation of the respiratory burst enzyme from human neutrophils in a cell-free system. Evidence for a soluble cofactor.

Activation of the respiratory burst enzyme from human neutrophils in a cell-free system. Evidence for a soluble cofactor.

The Role of Formylpeptide Receptors, C5a Receptors, and Cytosolic-Free Calcium in Neutrophil Priming

Pathogenesis of Foreign Body Infection: Description and Characteristics of an Animal Model

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