Interferon-γ-mediated pathways and in vitro PBMC proliferation in HIV-infected patients
-
Katharina Schroecksnadel
Abstract
HIV infection is characterized by progressive immunodeficiency: HIV-infected peripheral blood mononuclear cells (PBMCs) cannot properly react to stimulation with allo-antigens and mitogens. In this study, we examined interferon-γ (IFN-γ)-mediated pathways and the proliferative response of mitogen-stimulated HIV-infected PBMCs in vitro. PBMCs of 30 HIV-infected patients were stimulated with the mitogens concanavalin A (Con A), phytohemagglutinin (PHA), and pokeweed mitogen (PWM). Mitogen stimulation induced expression of IFN-γ, GTP cyclohydrolase I (GCH-I), and indoleamine (2,3)-dioxygenase (IDO) resulting in enhanced neopterin formation and tryptophan degradation by HIV-infected and control PBMCs. IFN-γ concentrations correlated with neopterin levels and tryptophan degradation. Proliferative responses to PHA and PWM cytokine were lower in HIV patients, with IFN-γ formation predicting proliferative responses. Higher mRNA expression of IFN-γ, GCH-I and IDO after 6 h was related to better proliferative responses in HIV-infected PBMCs. In conclusion, induction of IFN-γ and subsequent enzymes appears to importantly influence the proliferative response of HIV-infected PBMCs in vitro, suggesting a prominent role of the cytokine in the development of immunodeficiency.
©2009 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Minireview
- Functional genetic mouse models: promising tools for investigation of the proteolytic internet
- Protein Structure and Function
- Primary sequence, together with other factors, influence peptide deimination by peptidylarginine deiminase-4
- Mercury and cadmium trigger expression of the copper importer Ctr1B, which enables Drosophila to thrive on heavy metal-loaded food
- Cell Biology and Signaling
- Interferon-γ-mediated pathways and in vitro PBMC proliferation in HIV-infected patients
- Exploring the pathogenesis of renal cell carcinoma: pathway and bioinformatics analysis of dysregulated genes and proteins
- Aptamers selected against the unglycosylated EGFRvIII ectodomain and delivered intracellularly reduce membrane-bound EGFRvIII and induce apoptosis
- Involvement of heparan sulfate proteoglycans in cellular uptake of high molecular weight kininogen
- Overexpression of Pygopus2 protects HeLa cells from vinblastine-induced apoptosis
- Proteolysis
- Selectivity of propeptide-enzyme interaction in cathepsin L-like cysteine proteases
- Murine and human cathepsin B exhibit similar properties: possible implications for drug discovery
- Novel Techniques
- Isotope tracing enhancement of chemiluminescence assays for nitric oxide research
Articles in the same Issue
- Minireview
- Functional genetic mouse models: promising tools for investigation of the proteolytic internet
- Protein Structure and Function
- Primary sequence, together with other factors, influence peptide deimination by peptidylarginine deiminase-4
- Mercury and cadmium trigger expression of the copper importer Ctr1B, which enables Drosophila to thrive on heavy metal-loaded food
- Cell Biology and Signaling
- Interferon-γ-mediated pathways and in vitro PBMC proliferation in HIV-infected patients
- Exploring the pathogenesis of renal cell carcinoma: pathway and bioinformatics analysis of dysregulated genes and proteins
- Aptamers selected against the unglycosylated EGFRvIII ectodomain and delivered intracellularly reduce membrane-bound EGFRvIII and induce apoptosis
- Involvement of heparan sulfate proteoglycans in cellular uptake of high molecular weight kininogen
- Overexpression of Pygopus2 protects HeLa cells from vinblastine-induced apoptosis
- Proteolysis
- Selectivity of propeptide-enzyme interaction in cathepsin L-like cysteine proteases
- Murine and human cathepsin B exhibit similar properties: possible implications for drug discovery
- Novel Techniques
- Isotope tracing enhancement of chemiluminescence assays for nitric oxide research