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Proteases for processing proneuropeptides into peptide neurotransmitters and hormones
Vivian Hook1, Lydiane Funkelstein, Douglas Lu
1Skaggs School of Pharmacy and Pharmaceutical Sciences, and Department of Neuroscience, Pharmacology, and Medicine, School of Medicine, University of California-San Diego, La Jolla, CA 92093-0744, USA. vhook@ucsd.edu
Annual Review of Pharmacology and Toxicology
|January 11, 2008
Summary
Neuropeptides, crucial for cell communication, are processed by two main protease pathways: cathepsin L and subtilisin-like proprotein convertases. Understanding these pathways aids neuropeptide drug development.
Area of Science:
- Biochemistry
- Neuroscience
- Endocrinology
Background:
- Neuropeptides are vital for cell-cell communication in neurotransmission and endocrine regulation.
- Their synthesis involves proteolytic processing of proneuropeptides within secretory vesicles.
Purpose of the Study:
- To review interdisciplinary strategies elucidating neuropeptide biosynthesis pathways.
- To highlight current and future directions in biomedical neuropeptide research.
Main Methods:
- Elucidation of two primary protease pathways: secretory vesicle cathepsin L and subtilisin-like proprotein convertases.
- Integration of peptidomics and proteomics for systems biology approaches.
Main Results:
- Identified two key protease pathways essential for neuropeptide biosynthesis.
- Discussed structural interactions between proneuropeptides and proteases.
Conclusions:
- In-depth understanding of protease mechanisms is crucial for developing pharmacological strategies targeting neuropeptide functions.
- Neuropeptide research holds potential for novel therapeutics in various health conditions.
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