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Expression and function of protein kinase C isozymes
K P Huang1, F L Huang, H Nakabayashi
1Section on Metabolic Regulation, National Institute of Child Health and Human Development, Bethesda, Maryland.
Acta Endocrinologica
|September 1, 1989
Summary
This study identifies three protein kinase C (PKC) isozymes (I, II, III) and their tissue-specific expression patterns. Differential regulation of PKC isozymes suggests distinct cellular functions.
Area of Science:
- Molecular Biology
- Neuroscience
- Biochemistry
Background:
- Three major protein kinase C (PKC) isozymes (I, II, III) are key Ca2+/phospholipid-stimulated kinases in animal tissues.
- Immunochemical analysis reveals distinct genetic encoding: PKC I (gamma cDNA), PKC II (beta I/II cDNAs), and PKC III (alpha cDNA).
Purpose of the Study:
- To investigate the tissue-specific and developmental expression of PKC isozymes.
- To explore the distinct functional roles of PKC isozymes in cellular regulation.
Main Methods:
- Immunochemical analysis to determine cDNA encoding for PKC isozymes.
- Analysis of tissue-specific and developmental expression patterns in the central and peripheral nervous systems.
- Treatment of rat basophilic leukemia cells with phorbol ester to study differential enzyme down-regulation.
Main Results:
- High expression of all three PKC isozymes in the central nervous system; PKC II and III predominantly in peripheral tissues.
- PKC I expression correlates with synaptogenesis during brain development; PKC II and III increase postnatally.
- Phorbol ester treatment induced faster degradation of PKC II than PKC III, indicating differential regulation.
Conclusions:
- Each PKC isozyme exhibits distinct tissue distribution and developmental regulation.
- Differential down-regulation by phorbol ester suggests unique functional roles for PKC II and III.
- These findings support the hypothesis that each PKC isozyme plays a specific role in cellular process regulation.