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Indoleamine 2,3-dioxygenase 1 (IDO-1) and interferon-gamma (IFN-γ) are proteins that play a significant role in inflammatory conditions and tumor development. The detection of IDO1 and IFN-γ is crucial for understanding their interplay in immune responses. This study introduced a novel method for the simultaneous quantitative determination of IDO-1 and IFN-γ in different biological samples/materials. The method is based on an optical biosensor, with surface plasmon resonance detection carried out by the imaging version of the sensor (SPRi). Biotinylated antibodies immobilized on the surfaces of the linker and carboxymethylated dextran served as the recognition elements for the developed biosensor. Relevant studies were conducted to optimize the activities of the biosensor by employing appropriate reagent concentrations. Validation was performed for each protein separately; low detection and quantification limits were obtained (for IDO-1 LOD = 0.27 ng/mL, LOQ = 0.81 ng/mL; for IFN-γ LOD = 1.76 pg/mL and LOQ = 5.29 pg/mL). The sensor operating ranges were 0.001-10 ng/mL for IDO-1 and 0.1-1000 pg/mL for IFN-γ. The constructed biosensor demonstrated its sensitivity and precision when the appropriate analytical parameters were determined, based on the proposed method. It can also selectively capture IDO-1 and IFN-γ from a large sample matrix. The biosensor efficiency was confirmed by the determination of IDO-1 and IFN-γ in simultaneous measurements of the plasma and urine samples of patients diagnosed with bladder cancer and the control group. The outcomes were compared to those obtained using a certified ELISA test, demonstrating convergence between the two methodologies. The preliminary findings demonstrate the biosensor's efficacy and suitability for comprehensive analyses of the examined biological samples.
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http://dx.doi.org/10.3390/bios15070444 | DOI Listing |
J Am Heart Assoc
August 2025
Department of Cardiology Erasmus MC, University Medical Center Rotterdam The Netherlands.
Background: Activation of the plasma kynurenine pathway (KP) may contribute to the progression of pulmonary arterial hypertension (PAH). We investigated the functional role and molecular mechanisms of KP activation in PAH.
Methods: KP activity was measured in the lungs and plasma of humans and rodents with pulmonary hypertension (PH).
Front Immunol
July 2025
Instituto Leônidas e Maria Deane (ILMD), Fiocruz Amazônia, Manaus, Amazonas, Brazil.
Introduction: Malaria remains a significant public health challenge in Brazil, where () is the predominant species. Dysregulated immune responses contribute substantially to malaria pathogenesis. Indoleamine 2,3-dioxygenase (IDO) mediates the catabolism of tryptophan (TRP) into kynurenine (KYN), an immunosuppressive metabolite implicated in immune tolerance.
View Article and Find Full Text PDFBiosensors (Basel)
July 2025
Bioanalysis Laboratory, Faculty of Chemistry, University of Bialystok, Ciolkowskiego 1K, 15-245 Bialystok, Poland.
Indoleamine 2,3-dioxygenase 1 (IDO-1) and interferon-gamma (IFN-γ) are proteins that play a significant role in inflammatory conditions and tumor development. The detection of IDO1 and IFN-γ is crucial for understanding their interplay in immune responses. This study introduced a novel method for the simultaneous quantitative determination of IDO-1 and IFN-γ in different biological samples/materials.
View Article and Find Full Text PDFInflammopharmacology
July 2025
Molecular Immunology Research Center, Tehran University of Medical Sciences, P. O. Box: 1419733151, Tehran, Iran.
Introduction: The COVID-19 pandemic with various clinical symptoms has posed significant challenges to the healthcare system. The aryl-hydrocarbon receptor (AhR), a transcription factor that can be activated by both external and internal ligands, may play a role in the regulation of pro-inflammatory cytokines, including interleukin (IL)-6. Additionally, indoleamine-2,3-dioxygenase (IDO)-1 is thought to have an immunomodulatory role and provides kynurenine, an AhR agonist.
View Article and Find Full Text PDFFront Immunol
June 2025
Center for Thoracic Oncology, Tisch Cancer Institute, Mount Sinai Health System, New York, NY, United States.
Background: Indoleamine 2,3-dioxygenase-1 (IDO-1) is a cytosolic enzyme involved in the catabolism of tryptophan. IDO-1-related immune suppression is due to decreased tryptophan availability and to the generation of tryptophan metabolites, culminating in substantial suppression of T-lymphocytes. Here we investigate IDO-1 expression in 2 cohorts of non-small-cell lung cancer (NSCLC) specimens, both in tumor cells and in immune infiltrate, with correlation of IDO-1 to PD-L1 expression, clinical patient demographics and outcomes.
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