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Increased protein kinase C activity in low density eosinophils
M E Bates1, P J Bertics, W J Calhoun
1Department of Medicine, University of Wisconsin Medical School, Madison 53792.
Journal of Immunology (Baltimore, Md. : 1950)
|May 15, 1993
Summary
Human eosinophil function differences may stem from Protein Kinase C (PKC) activity. Eosinophil PKC activity, mainly from the beta isozyme, correlates with cell density and may influence function.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Eosinophil heterogeneity in density, receptors, and function is known.
- Increased eosinophil functional activities correlate with decreased sedimentation density.
- Cellular mechanisms for eosinophil function up-regulation remain underexplored.
Purpose of the Study:
- To investigate the role of Protein Kinase C (PKC) in human eosinophil function.
- To determine if PKC activity differences explain functional heterogeneity.
- To identify PKC isozymes present in eosinophils.
Main Methods:
- Measured PKC activity in human granulocyte lysate supernatants.
- Assayed PKC activity in blood eosinophils of varying densities.
- Analyzed PKC activity in bronchoalveolar lavage (BAL) eosinophils post-antigen challenge.
- Utilized Western blotting to detect PKC isozymes in eosinophils.
Main Results:
- Eosinophils showed a higher percentage of phosphatidyl serine-dependent PKC activity than neutrophils.
- Low-density blood eosinophils exhibited higher PKC activity than high-density cells.
- BAL eosinophil PKC activity was comparable to blood eosinophils of similar density.
- The beta isozyme of PKC was detected in eosinophils, but not alpha or gamma.
Conclusions:
- Eosinophil PKC activity is primarily mediated by the beta isozyme.
- PKC activity in blood eosinophils is linked to cell density.
- PKC activity may play a role in eosinophil function and heterogeneity.