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Proteolytic processing of galectin-3 by meprin metalloproteases is crucial for host-microbiome homeostasis

Cynthia Bülck1, Elisabeth E L Nyström1, Tomas Koudelka2

  • 1Institute of Biochemistry, University of Kiel, 24118 Kiel, Germany.

Science Advances
|March 31, 2023
PubMed

Insights

Meprin α/β heterodimers, crucial for gut health, process galectin-3. This cleavage regulates bacterial interactions, maintaining colon host-microbiome homeostasis, especially during inflammation.

Area of Science:

  • Gastroenterology
  • Proteomics
  • Microbiome research

Background:

  • Meprin α and meprin β metalloproteases are vital for gut mucosal homeostasis.
  • Their expression decreases in inflammatory bowel disease, suggesting a protective role.
  • In the colon, these proteases form membrane-tethered heterodimers with dual proteolytic activity.

Purpose of the Study:

  • To investigate the function of meprin α/β heterodimers in the gut.
  • To identify key substrates of meprin α/β heterodimers.
  • To understand the role of meprin α/β-galectin-3 interaction in host-microbiome homeostasis.

Main Methods:

  • N-terminomics to identify meprin α/β substrates.
  • Comparative analysis of wild-type, galectin-3-deficient, and meprin α/β double knockout mice.
  • Assessment of galectin-3 processing and bacterial agglutination in different mouse models.

Main Results:

  • Galectin-3 was identified as the primary intestinal substrate for meprin α/β heterodimers.
  • Mice lacking galectin-3 or meprin α/β exhibited similar microbiome alterations.
  • Meprin α/β heterodimers differentially process galectin-3, affecting its bacterial agglutination properties.

Conclusions:

  • Meprin α/β heterodimers constitutively cleave galectin-3 in the colon.
  • This processing is critical for regulating bacterial agglutination and maintaining host-microbiome homeostasis.
  • The meprin α/β-galectin-3 axis represents a key factor in colon mucosal health.

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