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Updated: Feb 26, 2026

Quantification of Monocyte Chemotactic Activity In Vivo and Characterization of Blood Monocyte Derived Macrophages
Published on: August 12, 2019
Cysteine-Containing Peptides Stimulate Monocyte Migration through NADPH-Oxidase Activation.
T L Krasnikova1, T I Arefieva2, E A Pylaeva2
1Russian Cardiology Research and Production Complex, Ministry of Health of the Russian Federation, Moscow, Russia. tlkrasnikova@gmail.com.
Cysteine-containing peptides stimulate monocyte migration via NADPH oxidase, specifically Nox4. Apocinin and MEK/ERK blockers completely inhibited this migration, suggesting a key role for this pathway.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Monocyte migration is crucial for immune responses.
- Chemokines like MCP-1 and fractalkine regulate monocyte trafficking.
- NADPH oxidases, particularly Nox4, are implicated in cellular processes.
Purpose of the Study:
- To investigate the role of NADPH oxidase, specifically Nox4, in monocyte migration.
- To determine the effect of apocinin and PD98059 on chemokine-induced monocyte migration.
Main Methods:
- Monocyte migration assays were performed.
- Apocinin (NADPH inhibitor) and PD98059 (MEK/ERK blocker) were used.
- Chemokine fragments (MCP-1, fractalkine) were employed as stimuli.
Main Results:
- Apocinin completely inhibited monocyte migration stimulated by cysteine-containing peptides.
- PD98059 also completely inhibited this migration.
- These findings implicate the NADPH oxidase system, particularly Nox4, in the observed monocyte migration.
Conclusions:
- Cysteine-containing peptides stimulate monocyte migration through the NADPH oxidase system.
- Nox4 is likely the key NADPH oxidase isoform involved.
- Inhibiting NADPH oxidase or MEK/ERK signaling effectively blocks this specific type of monocyte migration.
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