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What lies ahead for the proprotein convertases?
1Laboratory of Biochemical Neuroendocrinology, Clinical Research Institute of Montreal, Montreal, Canada. seidahn@ircm.qc.ca
Annals of the New York Academy of Sciences
|March 11, 2011
Summary
Proprotein convertases (PCs) are essential enzymes that process secretory proteins, playing vital roles in both health and disease. These nine convertases regulate diverse physiological functions, from hormone production to cholesterol homeostasis.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- The proprotein convertase (PC) family comprises nine enzymes responsible for limited proteolysis of secretory proteins.
- These enzymes cleave proproteins at specific residues, influencing the maturation and function of numerous biologically active molecules.
Purpose of the Study:
- To provide a comprehensive overview of the proprotein convertase (PC) family.
- To highlight the diverse roles and functions of each PC member in physiological processes and disease states.
Main Methods:
- Review of existing literature on proprotein convertase function.
- Analysis of the substrate specificity and cellular localization of different PC enzymes.
Main Results:
- The PC family includes PC1/3, PC2, furin, PC4, PC5/6, PACE4, PC7, SKI-1/S1P, and PCSK9, each with distinct cleavage preferences and roles.
- Specific PCs like PC1/3 and PC2 regulate neuroendocrine functions, while others like furin process constitutively secreted proteins.
- Unique PCs, SKI-1/S1P and PCSK9, are crucial for cholesterol and lipid homeostasis, independent of basic residue cleavage sites.
Conclusions:
- Proprotein convertases are critical regulators of diverse biological processes, impacting hormone production, development, and metabolic homeostasis.
- Dysregulation of PC activity is implicated in various health and disease states, underscoring their therapeutic potential.
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