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Proprotein Convertases and the Complement System.

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Summary

Proprotein convertases (PCs) are crucial for complement system function. While some complement proteins are processed intracellularly, others like MASP-3 are activated extracellularly by PCs, highlighting their essential role.

Keywords:
MASP-3alternative pathwayclassical pathwaycomplement systemlectin pathwayproprotein convertaseprotein secretion and processing

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Area of Science:

  • Biochemistry
  • Immunology
  • Proteolysis

Background:

  • Proteins for secretion undergo proteolytic processing by proprotein convertases (PCs).
  • The complement system is a vital blood proteolytic cascade for defense and immune homeostasis.
  • Several complement components (C3, C4, C5, Factor I) are multi-chain proteins processed intracellularly by PCs, likely including furin.

Purpose of the Study:

  • To review the critical role of proprotein convertases (PCs) in the proper functioning of the complement system.
  • To highlight novel findings on extracellular complement protein processing by PCs.

Main Methods:

  • Literature review of known proprotein convertase functions.
  • Analysis of complement protein processing pathways.
  • Identification of specific PCs involved in complement component activation.

Main Results:

  • Intracellular processing of complement components C3, C4, C5, and Factor I by PCs is established.
  • Extracellular processing and activation of Mannan-binding lectin-associated serine protease-3 (MASP-3) by PCSK6 (PACE4) has been discovered.
  • Extracellular activation of corin by PCSK6 is also documented.

Conclusions:

  • The complement system's proper functioning is intimately dependent on proprotein convertase activity.
  • PCs activate both non-enzymatic complement components and complement proteases (Factor I, MASP-3) intracellularly and extracellularly.
  • The alternative pathway's activity is indirectly reliant on blood-borne PCs via MASP-3 activation of pro-factor D.