Regulation of TNF-α Receptor Expression on Human Neutrophils by Various Cell Activating Factors

Solomkin, Joseph S.; Tindal, Carolyn J.; Cave, Cynthia M.; Zemlan, Frank P.

doi:10.1006/jsre.1994.1041

Cited by 4 publications

(3 citation statements)

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“…In association with an increased number of Hobs, is a subsequent increase in receptor sites for hTNF-a [39][40][41]. Therefore, any produced and released hTNF-a would quickly bind to available receptor sites, resulting in an inhibition of Hobs activity on the surfaces.…”

Section: Article In Pressmentioning

confidence: 97%

The inflammatory potential of biphasic calcium phosphate granules in osteoblast/macrophage co-culture

2005

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Section: Article In Pressmentioning

confidence: 97%

The inflammatory potential of biphasic calcium phosphate granules in osteoblast/macrophage co-culture

2005

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“…Blood cells were separated by Dextran (Pharmacia) sedimentation and Ficoll-Hypaque density centrifugation as previously described (28,29). Neutrophil preparations were routinely greater than 95% pure with greater than 95% viability as assessed by trypan blue exclusion.…”

Section: Peripheral Blood Neutrophil Isolation and Pretreatment With mentioning

confidence: 99%

Interleukin 8 Dimerization as a Mechanism for Regulation of Neutrophil Adherence-Dependent Oxidant Production

Williams

Cave²,

Quaid³

et al. 2005

Shock

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Interleukin 8 (IL-8), a member of the CXC subfamily of chemoattractant cytokines, induces a range of functional responses in human neutrophils via its interactions with two high-affinity cell-surface receptors, CXCR1 and CXCR2. Like other CXC chemokines, IL-8 forms homodimers at physiologic concentrations. Monomers and dimers bind to CXC receptors with high affinity and induce various functions. Binding to glycosaminoglycans decreases the dimerization constant, enhancing surface-bound dimer formation. However, a specific role for IL-8 dimerization has not been identified. We explored the hypothesis that certain neutrophil responses to IL-8 were induced primarily by the IL-8 dimers. To this end, two dimerization-deficient IL-8 mutant proteins, M3 and M4, were used in various functional assays. In contrast to native IL-8, these proteins existed primarily as monomers at micromolar concentrations. The mutants retained high-affinity binding to both CXC receptors and potently induced neutrophil calcium flux, chemotaxis, and elastase release. In contrast to native IL-8, neither mutant inhibited tumor necrosis factor alpha-induced oxidant production. Additionally, M4 was less effective than native IL-8 at desensitizing neutrophil migration. These data suggest that although IL-8 dimers or monomers are sufficient for several neutrophil functions, dimers may participate in suppression of specific surface-dependent neutrophil responses.

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“…Blood cells were separated by dextran (Pharmacia, Columbus, Ohio) sedimentation and Ficoll histopaque (Ficoll-Hypaque; Sigma-Aldrich Corporation) density centrifugation as previously described. 30,31 Neutrophil preparations were routinely greater than 95% pure with greater than 95% viability as assessed by trypan blue exclusion. For assays involving chemokine pretreatment, PMNs were pretreated at 1 ϫ 10 7 cells/mL in indicated concentrations of chemokines for 15 minutes at 37°C before subjection to various assays.…”

Section: Peripheral Blood Neutrophil Isolation and Pretreatment With mentioning

confidence: 99%

Chemokine Regulation of Neutrophil Function in Surgical Inflammation

Williams

Cave²,

Quaid³

et al. 1999

Arch Surg

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Background: Morbidity and even mortality correlate closely with major injury that causes a systemic inflammatory response. Cytokines and bioactive molecules present at the inflammatory site induce this response and regulate neutrophil proinflammatory responses. The CXC chemokines, important for neutrophil recruitment and activation, include interleukin 8 (IL-8), granulocyte chemotactic protein 2 (GCP-2), and epithelial cell-derived neutrophil attractant 78 (ENA-78). They induce neutrophil responses via 2 cell-surface receptors, CXCR-1 and CXCR-2. All 3 chemokines bind CXCR-2 with high affinity. Only IL-8 and GCP-2 bind CXCR-1 with high affinity. Hypothesis: The CXC chemokines regulate neutrophil responses differently. Methods: Pretreatment of neutrophils from healthy volunteers with IL-8, GCP-2, or ENA-78; measured IL-8induced migration; and tumor necrosis factor ␣ (TNF-␣)-induced peroxide production. Results: Flow cytometry and radioligand binding data indicate that IL-8, GCP-2, and ENA-78 equivalently reduced CXCR-1 and CXCR-2 cell surface expression by 34% to 54%. All treatments decreased affinity of both receptors 1.5-to 2-fold. However, only IL-8 pretreatment inhibited chemotaxis to 10-nmol/L IL-8 (mean ± SE inhibition, 62% ± 6%). Although IL-8 and GCP-2, but not ENA-78, suppressed TNF-␣-induced oxidant production (mean ± SE inhibition, 42% ± 8% and 40% ± 23%, respectively), only GCP-2 inhibited the oxidative response to complement fragment C5a, and to the bacterial cell wall peptide N-formyl-methionyl-leucylphenylalanine. Conclusions: The CXC chemokines regulate neutrophil proinflammatory functions differently. A thorough understanding of mechanisms for modulating neutrophil responses in inflammation will aid the development of interventions that reduce morbidity and mortality associated with severe trauma and sepsis.

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Regulation of TNF-α Receptor Expression on Human Neutrophils by Various Cell Activating Factors

Cited by 4 publications

References 0 publications

The inflammatory potential of biphasic calcium phosphate granules in osteoblast/macrophage co-culture

The inflammatory potential of biphasic calcium phosphate granules in osteoblast/macrophage co-culture

Interleukin 8 Dimerization as a Mechanism for Regulation of Neutrophil Adherence-Dependent Oxidant Production

Chemokine Regulation of Neutrophil Function in Surgical Inflammation

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