Cleavage of the third component of complement (C3) by mannose-binding protein-associated serine protease (MASP) with subsequent complement activation

Immunobiology. 1995 Nov;194(4-5):443-48. doi: 10.1016/S0171-2985(11)80110-5.

Abstract

We have previously shown that a novel C1s-like serine protease termed MBP-associated serine protease (MASP) is responsible for activation of the complement cascade initiated by mannose-binding protein (MBP). In this communication, we report that MASP is unique in having the proteolytic capacity to cleave C3 with subsequent activation of the alternative pathway, a capacity which C1s lacks.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / immunology
  • Carrier Proteins / pharmacology*
  • Complement Activation / drug effects*
  • Complement C1s / pharmacology
  • Complement C3 / metabolism*
  • Humans
  • Hydrolysis / drug effects
  • Lectins / immunology*
  • Mannose*
  • Mannose-Binding Lectins
  • Mannose-Binding Protein-Associated Serine Proteases
  • Serine Endopeptidases / immunology
  • Serine Endopeptidases / pharmacology*

Substances

  • Carrier Proteins
  • Complement C3
  • Lectins
  • Mannose-Binding Lectins
  • Mannose-Binding Protein-Associated Serine Proteases
  • Serine Endopeptidases
  • Complement C1s
  • Mannose