Abstract
The effect of AlF4- on the degranulation process in human neutrophils was investigated. In intact neutrophils, AlF4- induced degranulation, whereas in electropermeabilized neutrophils AlF4- did not stimulate degranulation. In electropermeabilized neutrophils, fluoride ions proved to be inhibitory for the degranulation induced by addition of Ca2+ and/or GTP-gamma-S. Another phosphatase inhibitor, okadaic acid, inhibited degranulation induced by Ca2+ or by GTP-gamma-S but not degranulation induced by the combination of Ca2+ plus GTP-gamma-S. It is concluded that under suboptimal conditions of stimulation with Ca2+ or GTP-gamma-S, protein dephosphorylation plays an important role in the degranulation response in human neutrophils.
| Original language | English |
|---|---|
| Pages (from-to) | 489-95 |
| Number of pages | 7 |
| Journal | Journal of leukocyte biology |
| Volume | 55 |
| Issue number | 4 |
| Publication status | Published - Apr 1994 |
Keywords
- Antigens, CD
- Antigens, Neoplasm
- Cell Adhesion Molecules
- Cell Degranulation
- Ethers, Cyclic
- Fluorides
- GTP-Binding Proteins
- Guanosine 5'-O-(3-Thiotriphosphate)
- Humans
- Journal Article
- Membrane Glycoproteins
- Neutrophils
- Okadaic Acid
- Permeability
- Platelet Membrane Glycoproteins
- Research Support, Non-U.S. Gov't
- Tetraspanin 30