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Calpain and kininogen mediated inflammation.
M Sasaki1, M Kunimatsu, T Tada
1Department of Biochemistry, Nagoya City University Medical School, Japan.
Biomedica Biochimica Acta
|January 1, 1991
Summary
Researchers explored peptides derived from calpains, identifying specific N-acetylated and unmodified peptides with neutrophil chemotactic activity. These findings suggest the calpain-kininogen system
Area of Science:
- Biochemistry
- Immunology
- Molecular Biology
Background:
- Previous research indicated N-acetyl nonapeptide from human calpain I large subunit exhibits neutrophil chemotactic activity.
- Calpains are calcium-dependent cysteine proteases involved in various cellular processes.
Purpose of the Study:
- To synthesize and evaluate the chemotactic activity of various N-acetylated and unmodified peptides from calpain I and II large and small subunits.
- To investigate the interaction between calpain and kininogens and its effect on kinin liberation and calpain activity.
Main Methods:
- Synthesis of over 30 N-acetylated and unmodified peptides based on calpain subunit sequences.
- Estimation of chemotactic activity of synthesized peptides for neutrophils.
- Incubation of calpain with high and low molecular weight kininogen to assess kinin liberation and calpain inhibition.
Main Results:
- Several synthesized peptides, including an N-acetyl nonapeptide from calpain I large subunit and an unmodified nonapeptide from calpain II large subunit, demonstrated chemotactic activity.
- N-acetylated peptides of varying lengths from the calpain small subunit also exhibited chemotactic properties.
- Calpain incubation with kininogens resulted in kinin liberation and simultaneous calpain inhibition by kininogen.
Conclusions:
- Specific peptides derived from calpain subunits possess neutrophil chemotactic activity.
- The calpain-kininogen system generates chemical mediators that may influence neutrophil migration and accumulation at inflammatory sites.