Inhibition of phorbol ester-induced neutrophil chemiluminescence by FeLV

Dezzutti, Charlene S.; Lafrado, Louis J.; Lewis, Mark G.; Olsen, Richard G.

doi:10.1007/bf01310506

Cited by 9 publications

(3 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Previous studies have demonstrated that FeLV infection affects neutrophil function and their response to different stimuli (Kiehl et al, 1987;Dezzutti et al, 1989Dezzutti et al, , 1990Hoffmann-Jagielska et al, 2005). Thus, neutrophils from FeLV + experimentally infected and clinically ill cats show a reduced chemotactic response in vitro in comparison with neutrophils from FeLV 2 cats (Kiehl et al, 1987).…”

Section: Neutrophil Phagocytosismentioning

confidence: 99%

“…Thus, exogenous H 2 O 2 generated from NADPH oxidase induced NET release in mammals and release of heterophil extracellular traps in chickens (Fuchs et al, 2007;Chuammitri et al, 2009). FeLV infection inhibits neutrophil activation by inhibition of protein kinase C and a decrease in ROS production Lewis et al, 1986;Lafrado et al, 1987;Dezzutti et al, 1989Dezzutti et al, , 1990Hoffmann-Jagielska et al, 2005).…”

Section: Characterization Of Feline Netsmentioning

confidence: 99%

“…Likewise, neutrophils from FeLV 2 animals were not activated by opsonized particles with serum obtained from FeLV + cats (Lewis et al, 1986). Dezzutti et al (1989Dezzutti et al ( , 1990 demonstrated that neutrophils from experimentally viraemic cats presented reduced protein kinase C activation when stimulated by phorbol myristate acetate (PMA). Similarly, neutrophils from healthy cats exposed to inactivated FeLV or purified p15E FeLV protein resulted in a diminished response to Ca + ionophore (Lafrado et al, 1987).…”

Section: Net Release and Myeloperoxidase (Mpo) Activitymentioning

confidence: 99%

See 2 more Smart Citations

Characterization of neutrophil extracellular traps in cats naturally infected with feline leukemia virus

Wardini

Guimarães-Costa

Nascimento

et al. 2009

Journal of General Virology

107

View full text Add to dashboard Cite

Feline leukemia virus (FeLV), a common, naturally occurring gammaretrovirus in domestic cats, is associated with degenerative diseases of the haematopoietic system, immunodeficiency and neoplasia. FeLV infection causes an important suppression of neutrophil function, leading to opportunistic infections. Recently, a new microbicidal mechanism named NETosis was described in human, bovine and fish neutrophils, as well as in chicken heterophils. The purpose of the present study was to characterize NETosis in feline neutrophils, as well as to evaluate neutrophil function in FeLV naturally infected symptomatic and asymptomatic cats through the phagocytosis process, release of neutrophil extracellular traps (NETs) and myeloperoxidase (MPO) activity. The results showed that feline neutrophils stimulated with protozoa parasites released structures comprising DNA and histones, which were characterized as NETs by immunofluorescence. Quantification of NETs after neutrophil stimulation showed a significant increase in NET release by neutrophils from FeLV " and FeLV + asymptomatic cats compared with FeLV + symptomatic cats.Moreover, the number of released NETs and MPO activity in unstimulated neutrophils of FeLV + symptomatic cats were higher than those in unstimulated neutrophils from FeLV " and FeLV + asymptomatic cats. This study reports, for the first time, NET release by feline neutrophils, along with the fact that NET induction may be modulated by a viral infection. The results indicate that the NET mechanism appears to be overactivated in FeLV + cats and that this feature could be considered a marker of disease progression in FeLV infection.

show abstract

Section: Neutrophil Phagocytosismentioning

confidence: 99%

Section: Characterization Of Feline Netsmentioning

confidence: 99%

Section: Net Release and Myeloperoxidase (Mpo) Activitymentioning

confidence: 99%

See 1 more Smart Citation

Characterization of neutrophil extracellular traps in cats naturally infected with feline leukemia virus

Wardini

Guimarães-Costa

Nascimento

et al. 2009

Journal of General Virology

107

View full text Add to dashboard Cite

show abstract

Synthetic hexapeptides derived from the transmembrane envelope proteins of retroviruses suppress N-formylpeptide–induced monocyte polarization

Oostendorp

Schaaper²,

Post³

et al. 1992

Journal of Leukocyte Biology

View full text Add to dashboard Cite

Retroviral infections are frequently associated with immunosuppression. Retroviral transmembrane envelope proteins (TM proteins) play an important role in this phenomenon. CKS-17, a synthetic heptadecapeptide, represents the immunosuppressive site of these retroviral TM proteins. Here we support on the further delineation of this immunosuppressive site using CKS-17-derived hexapeptides. The N-formyl-methionyl-leucyl-phenylalanine-induced monocyte polarization assay was used throughout this study because this monocyte function has been shown to be highly sensitive to TM protein p15E-related immunosuppression. We found that in addition to CKS-17 one CKS-17-derived hexapeptide, LDLLFL, reversibly inhibited monocyte polarization, with 50% inhibitory concentrations of 20 and 2 microM respectively. LDLLFL-mediated inhibition was sequence specific because the reverse peptide LFLLDL and scrambled peptides were not inhibitory. Hexapeptides corresponding to LDLLFL, but derived from various retroviruses other than murine leukemia virus, also inhibited monocyte polarization. Peptides most homologous to LDLLFL-LDILFL (feline leukemia virus) and LDLLFW (human T lymphotropic virus types I and II)--were the most potent inhibitors. Peptides homologous to primate and human endogenous proviruses were not suppressive. LDLLFL and some of its homologous also inhibited polarization of neutrophilic granulocytes. These findings lend further support to the view that conserved retroviral TM protein-related peptides can play an important role in suppression of inflammatory cell function as encountered in retrovirus-associated immunosuppression.

show abstract

Hepatitis C Virus Core Protein Inhibits Interleukin 12 and Nitric Oxide Production from Activated Macrophages

et al. 2001

View full text Add to dashboard Cite

A characteristic feature of hepatitis C virus (HCV) infection is a high frequency of persistence and the progression to chronic liver diseases. Recent data suggest that prevalent T helper (Th) 2 immunity as well as weak HCV-specific T-cell response is associated with viral persistence. Here, we showed that the production of interleukin 12 (IL-12) and nitric oxide (NO) that is critical for the induction of Th1 and innate immunity, but not that of tumor necrosis factor alpha (TNF-alpha), was significantly suppressed in both HCV core-expressing macrophage cell lines and mouse peritoneal macrophages treated with recombinant core protein. In addition, IL-12 p40 promoter activity was repressed by the presence of HCV core in macrophages stimulated with lipopolysaccharride (LPS) following IFN-gamma treatment, indicating that IL-12 production may be downregulated at the transcriptional level. We also found that proliferation of T cells and IFN-gamma production in mixed lymphocyte reactions (MLR) with core-expressing cells were inhibited. Taken together, our results suggest that HCV core protein could play roles in suppressing the induction of Th1 immunity through inhibition of IL-12 and NO production.

show abstract

Inhibition of phorbol ester-induced neutrophil chemiluminescence by FeLV

Cited by 9 publications

References 38 publications

Characterization of neutrophil extracellular traps in cats naturally infected with feline leukemia virus

Characterization of neutrophil extracellular traps in cats naturally infected with feline leukemia virus

Synthetic hexapeptides derived from the transmembrane envelope proteins of retroviruses suppress N-formylpeptide–induced monocyte polarization

Hepatitis C Virus Core Protein Inhibits Interleukin 12 and Nitric Oxide Production from Activated Macrophages

Contact Info

Product

Resources

About