A potential second messenger role for arachidonic acid: activation of Ca2+-dependent protein kinase.
Trans Assoc Am Physicians
; 97: 222-31, 1984.
Article
em En
| MEDLINE
| ID: mdl-6242084
ABSTRACT
A widely distributed Ca2+- and phospholipid-dependent protein kinase, protein kinase C, may play a major role in cellular regulation. We now report that arachidonate can directly activate protein kinase C from human neutrophils. Activation was Ca2+-dependent and was enhanced by diolein, but did not require phosphatidylserine. Arachidonate enhanced the apparent affinity of the kinase for Ca2+ in the presence of phosphatidylserine. Other unsaturated, but not saturated, fatty acids also activated protein kinase C. These results suggest a novel means of leukocyte activation and cellular regulation arachidonate, which is released by ligand-receptor interactions in neutrophils and many other cell types, could function as a second messenger via activation and modulation of protein kinase C.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Quinases
/
Ácidos Araquidônicos
/
Cálcio
/
Neutrófilos
Idioma:
En
Revista:
Trans Assoc Am Physicians
Ano de publicação:
1984
Tipo de documento:
Article