{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNAMPT is best known for its critical intracellular role as the rate‐limiting enzyme in the NAD⁺ salvage pathway, a function pivotal for maintaining cellular energy and redox homeostasis. By catalyzing the conversion of nicotinamide to nicotinamide mononucleotide (NMN), NAMPT supports NAD⁺ production required for the activity of NAD⁺‐dependent enzymes such as sirtuins, which are important for metabolism, mitochondrial integrity, stress resistance, and longevity. Fasting‐induced increases in NAMPT expression help preserve mitochondrial NAD⁺ levels and protect cells from genotoxic stress, while extracellular vesicle–mediated delivery of NAMPT contributes to systemic NAD⁺ biosynthesis and anti‐aging effects."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its intracellular enzymatic activity, NAMPT is also found in the extracellular milieu under the names visfatin or pre‐B cell colony–enhancing factor (PBEF). As an adipokine and proinflammatory cytokine, extracellular NAMPT influences immune cell function and inflammatory responses, stimulates cytokine production, and modulates insulin signaling. These actions appear to contribute to the pathophysiology of obesity, insulin resistance, and various inflammatory diseases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nNAMPT’s contributions extend to the regulation of cell survival, proliferation, and stress responses in pathological states such as cancer. Upregulation of NAMPT has been linked to enhanced tumor cell growth, improved resistance to oxidative stress, and the promotion of cancer stem cell–like properties—all of which may occur via NAD⁺–dependent modulation of factors like SIRT1 and p53. These findings underscore its potential as both a prognostic marker and a therapeutic target across a range of malignancies."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in metabolism and cancer, NAMPT also modulates immune cell function and contributes to vascular, inflammatory, and stress‐related responses. Inhibition of NAMPT has been shown to deplete NAD⁺, impairing T lymphocyte activation and cytokine secretion, which highlights its relevance in immune–mediated disorders. In cardiovascular cells and in lung injury models, aberrant NAMPT expression is linked to altered inflammatory signaling and endothelial dysfunction. These diverse effects reflect a broader involvement of NAMPT in regulating bioenergetics, cell survival pathways, and inflammation under stress conditions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "22", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent reviews and additional studies have further highlighted the multifaceted nature of NAMPT. Structural analyses have provided insights into its catalytic mechanism and substrate specificity, while clinical investigations link its expression to disease severity in conditions ranging from astrocytomas and metabolic syndrome to osteoarthritis. As both a functional enzyme regulating intracellular NAD⁺ levels and an extracellular signaling molecule, NAMPT emerges as a metabokine that can modulate cellular metabolism, inflammation, and tissue regeneration—thereby representing a promising target for therapeutic intervention and a potential biomarker for diverse pathologies."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "32"}, {"type": "fg_f", "ref": "6"}, {"type": "fg_fs", "start_ref": "33", "end_ref": "39"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Hongying Yang, Tianle Yang, Joseph A Baur, et al. 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