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Meprin metalloproteases inactivate interleukin 6.

Timothy R Keiffer1, Judith S Bond

  • 1From the Department of Biochemistry and Molecular Biology, Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033.

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|January 30, 2014
PubMed
Summary

Meprin metalloproteases degrade the inflammatory cytokine interleukin-6 (IL-6), reducing its activity. This suggests meprins modulate inflammation by inactivating IL-6.

Keywords:
Cell CultureCytokineInflammationInterleukinMeprinsMetalloproteaseProtease

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Area of Science:

  • Biochemistry
  • Immunology
  • Enzymology

Background:

  • Meprins are implicated in inflammatory diseases like inflammatory bowel disease.
  • Interleukin-6 (IL-6) is a key cytokine in inflammation, with elevated levels in meprin knockout models of inflammatory bowel disease.

Purpose of the Study:

  • To investigate the interaction between meprins and IL-6.
  • To determine if meprins can degrade or inactivate IL-6.

Main Methods:

  • Assessed cleavage of human and rodent IL-6 by purified meprin A and B.
  • Quantified kinetic parameters (Km, kcat/Km) for IL-6 cleavage.
  • Utilized Madin-Darby canine kidney cells expressing meprin constructs to study IL-6 cleavage.
  • Measured the biological activity of cleaved IL-6 by assessing B9 cell proliferation.

Main Results:

  • Meprin A and B efficiently cleave IL-6, removing 3-5 amino acids from the C terminus.
  • High catalytic efficiencies (kcat/Km) were observed for IL-6 cleavage by meprins.
  • Cleavage by meprins inactivates IL-6, reducing its ability to stimulate B9 cell proliferation.

Conclusions:

  • Meprin metalloproteases inactivate IL-6 through proteolytic cleavage.
  • This inactivation mechanism suggests a role for meprins in modulating inflammatory responses by degrading key cytokines.