Specific signaling by nicotinamide adenine dinucleotide oxidases – Role of their site of action

Abstract

Nicotinamide adenine dinucleotide (NADPH) oxidases, known for their role in generating reactive oxygen species (ROS) have emerged as key regulators of specific cellular signaling pathways. While their primary function is ROS production, recent research has highlighted the significance of their site-specific activity in governing distinct cellular signaling events.

NADPH oxidases (Nox) are found in various cell types, and both their expression and activities are tightly regulated. The generated ROS, such as superoxide anions and hydrogen peroxide, function as secondary messengers that modulate various signaling molecules, including protein kinases, transcription factors, and phosphatases.

The site-specific action of NADPH oxidases in different cellular compartments, such as the plasma membrane, endosomes, and endoplasmic reticulum, allows for precise control over specific signaling pathways. Understanding the complex interplay of NADPH oxidases in cellular signaling is essential for deciphering their roles in health and disease. Dysregulation of these enzymes can lead to oxidative stress and inflammation, making them potential therapeutic targets in various pathological conditions. Ongoing research into NADPH oxidase activation and site-specific signaling promises to unveil new insights into cellular physiology and potential treatment strategies.