Cleavage of Kininogen and Subsequent Bradykinin Release by the Complement Component: Mannose-Binding Lectin-Associated Serine Protease (MASP)-1
2011

How a Protein Cleaves Kininogen to Release Bradykinin

publication Evidence: moderate

Author Information

Author(s): Dobó József, Major Balázs, Kékesi Katalin A., Szabó István, Megyeri Márton, Hajela Krishnan, Juhász Gábor, Závodszky Péter, Gál Péter

Primary Institution: Institute of Enzymology, Hungarian Academy of Sciences, Budapest, Hungary

Hypothesis

Activated MASPs can digest kininogen to release bradykinin.

Conclusion

MASP-1 can cleave high-molecular-weight kininogen to produce bradykinin, while MASP-2 can cleave kininogen but does not release bradykinin.

Supporting Evidence

  • MASP-1 was shown to cleave high-molecular-weight kininogen resulting in bradykinin production.
  • MASP-2 could cleave kininogen but did not release bradykinin.
  • The catalytic efficiency of MASP-1 was significantly higher than that of MASP-2.

Takeaway

There are proteins in our blood that can cut up other proteins to make a substance called bradykinin, which can cause swelling. One of these proteins, called MASP-1, is really good at this job.

Methodology

The study used differential gel electrophoresis and HPLC to analyze the cleavage of kininogen by MASP-1 and MASP-2.

Limitations

The study did not explore the in vivo implications of MASP-1 activity on bradykinin levels in patients with hereditary angioedema.

Digital Object Identifier (DOI)

10.1371/journal.pone.0020036

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