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Subcellular localization of diacylglycerol kinase activity in stimulated and unstimulated human peripheral blood lymphocytes and neutrophils
Author(s) -
Hurttia Helena,
Leino Lasse
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201163
Subject(s) - diacylglycerol kinase , phytohaemagglutinin , biochemistry , cytosol , kinase , biology , protein kinase c , enzyme , microbiology and biotechnology , chemistry , in vitro
The diacylglycerol (DAG) kinase activity was determined in crude cytosol and membrane fractions in human peripheral blood lymphocytes and neutrophils. In neutrophils the basal lipid kinase activity was indentical in the two subcellular fractions whereas in lymphocytes the basal enzyme activity was 1.6‐fold higher in the membrane fraction. In general, the DAG kinase activity in lymphocyte fractions was 10‐ to 20‐fold higher than in neutrophil fractions. When lymphocytes were stimulated with phytohaemagglutinin for 4 hours, a significant decrease in the DAG kinase activity in the membrane fraction was detected. By contrast, a 30‐min activation with N‐formyl‐methionyl‐leucyl‐phenylalanine markedly increased the lipid kinase activity in both subcellular fractions in neutrophils. This activity was partially inhibited by the compound R59022. These results suggest that the DAG kinase is widely distributed in human leukocytes, but the enzyme's activity and regulation may vary in different leukocyte types.