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Nicotinamide Phosphoribosyltransferase in Human Diseases
Li Qin Zhang1, Daniel P Heruth, Shui Qing Ye
1Department of Pediatrics, Children's Mercy Hospitals and Clinics, University of Missouri School of Medicine, Kansas City, MO 64108, USA.
Journal of Bioanalysis & Biomedicine
|December 6, 2011
Summary
Nicotinamide phosphoribosyltransferase (NAMPT) is a versatile protein with roles in cell growth and inflammation. Its dysregulation is linked to numerous diseases, including cancer and diabetes, highlighting its pathological significance.
Area of Science:
- Biochemistry and Molecular Biology
- Cell Biology
- Pathophysiology
Background:
- Nicotinamide phosphoribosyltransferase (NAMPT) was initially identified as a pre-B-cell colony enhancing factor.
- Recent research reveals NAMPT as a pleiotropic protein with diverse functions, including roles as a growth factor, cytokine, enzyme, and visfatin.
- The official nomenclature has been standardized to NAMPT.
Purpose of the Study:
- To review the current understanding of NAMPT's structure and functions.
- To emphasize recent advancements in understanding the pathological roles of NAMPT in human diseases.
- To identify future research directions for exploring uncharted aspects of NAMPT.
Main Methods:
- Literature review of existing research on NAMPT.
- Synthesis of information regarding NAMPT's structure, functions, and disease associations.
- Analysis of recent findings on the pathological implications of NAMPT dysregulation.
Main Results:
- NAMPT exhibits multiple physiological functions, acting as a growth factor, cytokine, enzyme, and visfatin.
- Dysregulation of NAMPT is implicated in the pathogenesis of various human diseases, including acute lung injury, aging, atherosclerosis, cancer, diabetes, rheumatoid arthritis, and sepsis.
- Significant progress has been made in understanding NAMPT's role in disease.
Conclusions:
- NAMPT is a critical protein involved in numerous physiological processes.
- Aberrant NAMPT activity is a significant factor in the development of a wide range of human pathologies.
- Further research is warranted to fully elucidate NAMPT's complex roles and therapeutic potential.
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