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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.
The Journal of Biological Chemistry
|January 30, 2014
Summary
Meprin metalloproteases degrade the inflammatory cytokine interleukin-6 (IL-6), reducing its activity. This suggests meprins modulate inflammation by inactivating IL-6.
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.
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