PKC epsilon is involved in granulocyte-macrophage colony-stimulating factor signal transduction: evidence from microphysiometry and antisense oligonucleotide experiments
| Autor: | G T Baxter, Wada Hg, D.L. Miller, John C. Owicki, Kuo Rc |
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| Rok vydání: | 1992 |
| Předmět: |
Cations
Divalent medicine.medical_treatment Blotting Western Molecular Sequence Data Biology PKC alpha Biochemistry Choline Alkaloids Western blot medicine Phospholipase D Animals Humans Protein kinase C Protein Kinase C medicine.diagnostic_test Base Sequence Granulocyte-Macrophage Colony-Stimulating Factor Oligonucleotides Antisense Staurosporine Molecular biology Rats Enzyme Activation Isoenzymes Cytokine Granulocyte macrophage colony-stimulating factor Cell culture Calcium Signal transduction medicine.drug Signal Transduction |
| Zdroj: | Biochemistry. 31(45) |
| ISSN: | 0006-2960 |
| Popis: | We have used microphysiometry and antisense methodology to show that the epsilon isoenzyme of protein kinase C (PKC) is involved in the signal transduction pathway of granulocyte-macrophage colony-stimulating factor (GM-CSF) in a human bone marrow cell line, TF-1. These cells require GM-CSF or a related cytokine for proliferation. When the cells are appropriately exposed to GM-CSF, they exhibit a burst of metabolic activity that can be detected on the time scale of minutes in the microphysiometer, a biosensor-based instrument that measures the rate at which cells excrete protons. These cells express PKC alpha and -epsilon, as determined by Western blot analysis. Treatment with isoenzyme-specific antisense oligonucleotides inhibits expression appropriately, but only inhibition of PKC epsilon appreciably diminishes the burst of metabolic activity induced by GM-CSF. Consistent with the involvement of PKC epsilon, GM-CSF appears to activate phospholipase D and does not cause a detectable increase in cytosolic [Ca2+]. |
| Databáze: | OpenAIRE |
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