Effect of water extracts of Rhizopus delemar on the stimulus coupled responses of neutrophils and their modulation by various protein kinase inhibitors
| Autor: | Katsuo Seto, Hiroyuki Kodama, Ikuo Ushikoshi, Setsuo Ushikoshi, Kazunori Sugahara, Jianying Zhang |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Neutrophils
Clinical Biochemistry Genistein Biochemistry chemistry.chemical_compound Superoxides medicine Humans Staurosporine Enzyme Inhibitors Protein kinase A Protein Kinase Inhibitors Protein kinase C Plant Extracts Superoxide Biochemistry (medical) Water General Medicine N-Formylmethionine Leucyl-Phenylalanine chemistry Phorbol Tetradecanoylphorbol Acetate Phosphorylation Tyrosine kinase Rhizopus medicine.drug |
| Zdroj: | Clinica Chimica Acta. 282:89-100 |
| ISSN: | 0009-8981 |
| DOI: | 10.1016/s0009-8981(99)00013-3 |
| Popis: | Human peripheral blood polymorphonuclear leukocytes were preincubated with water extracts from Rhizopus delemar. The water extracts significantly inhibited arachidonic acid induced superoxide generation, whereas enhanced superoxide generation induced by phorbol 12-myristate 13-acetate but not those induced by N-formyl-methionyl-leucyl-phenylalanine. Superoxide generation induced by water extracts was inhibited by staurosporine, an inhibitor of protein kinase C, and was enhanced by genistein, an inhibitor of tyrosine kinase. The water extracts incubated with phorbol 12-myristate 13-acetate markedly increased phosphorylation of serine residue of 28.5 kDa protein with time and the phosphorylation depended on the concentration of the water extracts, whereas the water extracts incubated with arachidonic acid decreased the phosphorylation of serine residue of 38 and 42 kDa proteins. The phosphorylation of 28.5 kDa protein induced by the water extracts was inhibited by staurosporine, an inhibitor of protein kinase C, but was not inhibited by genistein, an inhibitor of tyrosine kinase. |
| Databáze: | OpenAIRE |
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