Secretagogues for lysosomal enzyme release as stimulants of arachidonyl phosphatidylinositol turnover in rabbit neutrophils

• Published in: Biochemical and biophysical research communications Vol. 90; no. 4; pp. 1364 - 1370
• Main Authors: Rubin, R.P., Sink, L.E., Schrey, M.P., Day, A.R., Liao, C.S., Freer, R.J.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 29.10.1979
• Subjects: Animals; Arachidonic Acids - metabolism; Calcimycin - pharmacology; Cytochalasin B - pharmacology; Kinetics; Lysosomes - drug effects; Lysosomes - metabolism; Neutrophils - drug effects; Neutrophils - metabolism; Oligopeptides - pharmacology; Palmitic Acids - metabolism; Phosphatidylinositols - metabolism; Rabbits; Structure-Activity Relationship; ACTH; PI; F-Met-Leu-Phe; Met-Leu-Phe
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(79)91186-0

[ 14C]arachidonic acid incorporation into phosphatidylinositol from rabbit neutrophils pretreated with cytochalasin B was increased within 2 min by the synthetic peptide formyl-methionyl-leucyl-phenylalanine and the Ca 2+ ionophore A23187. A high concentration of the peptide elicited only a small increase in phosphatidylinositol turnover when [ 14C]palmitic acid was employed as precursor. These data coincide with our earlier studies which identified a Ca 2+-dependent increase in arachidonyl phosphatidylinositol turnover during adrenocorticotropin and A23187-induced activation of steroid production and release in adrenocortical cells. It is concluded that an increase in arachidonyl phosphatidylinositol turnover mediated by a Ca 2+-dependent phospholipase A 2 may be a general mechanism for altering membrane function during secretory activity.